<?xml version="1.0" encoding="UTF-8"?>
<?xml-stylesheet type="text/xsl" href="https://m2.mtmt.hu/xsl/gui3.xsl" ?>
<myciteResult>
  <serverUrl>https://m2.mtmt.hu/</serverUrl>
  <labelLang>hun</labelLang>
  <responseDate>2026-09-22 12:40</responseDate>
  <content>
    <publication>
      <otype>JournalArticle</otype>
      <mtid>32040119</mtid>
      <status>VALIDATED</status>
      <published>true</published>
      <comment>Department of Medical Biochemistry, Semmelweis University, Budapest, 1085, Hungary            
            MTA-SE Lendület Ion Channel Research Group, Semmelweis University, Budapest, 1085, Hungary            
            HCEMM-SE Molecular Channelopathies Research Group, Semmelweis University, Budapest, 1085, Hungary            
            Cited By :2            
            Export Date: 9 March 2022            
            Correspondence Address: Szollosi, A.; Department of Medical Biochemistry, Hungary; email: szollosi.andras@med.semmelweis-univ.hu            
            Funding details: 739593            
            Funding details: LP2017-14/2017            
            Funding text 1: Supported by MTA Lend?let grant LP2017-14/2017 and EU Horizon 2020 Research and Innovation Program grant 739593.            
            Funding text 2: Funding: Supported by MTA Lendület grant LP2017-14/2017 and EU Horizon 2020 Research and Innovation Program grant 739593.</comment>
      <unhandledTickets>0</unhandledTickets>
      <deleted>false</deleted>
      <lastRefresh>2026-06-12T16:06:38.164+0000</lastRefresh>
      <lastModified>2026-04-22T07:12:56.252+0000</lastModified>
      <created>2021-05-28T11:27:32.560+0000</created>
      <creator>
        <snippet>true</snippet>
        <mtid>10074913</mtid>
        <familyName>Sághi-Keszthelyi</familyName>
        <givenName>Anna</givenName>
        <link>/api/admin/10074913</link>
        <otype>Admin</otype>
        <label>Sághi-Keszthelyi Anna (SE_KK_Admin5_SKA, admin)</label>
        <published>true</published>
      </creator>
      <lastDuplumOK>2026-05-22T11:44:33.271+0000</lastDuplumOK>
      <lastDuplumSearch>2026-05-22T11:44:33.271+0000</lastDuplumSearch>
      <validated>2022-02-24T10:11:51.354+0000</validated>
      <validator>
        <snippet>true</snippet>
        <mtid>10062250</mtid>
        <familyName>Molnár-Taga</familyName>
        <givenName>Márta</givenName>
        <link>/api/admin/10062250</link>
        <otype>Admin</otype>
        <label>Molnár-Taga Márta (SE 4-es admin)</label>
        <published>true</published>
        <oldId>10062250</oldId>
      </validator>
      <core>true</core>
      <publicationPending>false</publicationPending>
      <type>
        <snippet>true</snippet>
        <mtid>24</mtid>
        <code>24</code>
        <link>/api/publicationtype/24</link>
        <otype>PublicationType</otype>
        <label>Folyóiratcikk</label>
        <listPosition>1</listPosition>
        <published>true</published>
        <oldId>24</oldId>
        <otypeName>JournalArticle</otypeName>
      </type>
      <subType>
        <snippet>true</snippet>
        <mtid>1134514</mtid>
        <nameEng>Survey paper</nameEng>
        <docType>
          <snippet>true</snippet>
          <mtid>24</mtid>
          <code>24</code>
          <link>/api/publicationtype/24</link>
          <otype>PublicationType</otype>
          <label>Folyóiratcikk</label>
          <listPosition>1</listPosition>
          <published>true</published>
          <oldId>24</oldId>
          <otypeName>JournalArticle</otypeName>
        </docType>
        <link>/api/subtype/1134514</link>
        <name>Összefoglaló cikk</name>
        <otype>SubType</otype>
        <label>Összefoglaló cikk (Folyóiratcikk)</label>
        <listPosition>102</listPosition>
        <published>true</published>
        <oldId>1134514</oldId>
      </subType>
      <category>
        <snippet>true</snippet>
        <mtid>1</mtid>
        <link>/api/category/1</link>
        <otype>Category</otype>
        <label>Tudományos</label>
        <published>true</published>
        <oldId>1</oldId>
      </category>
      <firstAuthor>Szollosi, A.</firstAuthor>
      <title>Two decades of evolution of our understanding of the transient receptor potential melastatin 2 (Trpm2) cation channel</title>
      <journal>
        <snippet>true</snippet>
        <sciIndexed>true</sciIndexed>
        <link>/api/journal/10024487</link>
        <reviewType>REVIEWED</reviewType>
        <label>LIFE-BASEL 2075-1729</label>
        <published>true</published>
        <hungarian>false</hungarian>
        <oldId>10024487</oldId>
        <noIF>false</noIF>
        <mtid>10024487</mtid>
        <scopusIndexed>true</scopusIndexed>
        <eIssn>2075-1729</eIssn>
        <otype>Journal</otype>
        <lang>FOREIGN</lang>
      </journal>
      <volume>11</volume>
      <issue>5</issue>
      <internalId>397</internalId>
      <firstPageOrInternalIdForSort>397</firstPageOrInternalIdForSort>
      <pageLength>23</pageLength>
      <publishedYear>2021</publishedYear>
      <abstractText>The transient receptor potential melastatin (TRPM) family belongs to the superfamily of TRP ion channels. It consists of eight family members that are involved in a plethora of cellular functions. TRPM2 is a homotetrameric Ca2+-permeable cation channel activated upon oxidative stress and is important, among others, for body heat control, immune cell activation and insulin secretion. Invertebrate TRPM2 proteins are channel enzymes; they hydrolyze the activating ligand, ADP-ribose, which is likely important for functional regulation. Since its cloning in 1998, the understanding of the biophysical properties of the channel has greatly advanced due to a vast number of structure– function studies. The physiological regulators of the channel have been identified and characterized in cell-free systems. In the wake of the recent structural biochemistry revolution, several TRPM2 cryo-EM structures have been published. These structures have helped to understand the general features of the channel, but at the same time have revealed unexplained mechanistic differences among channel orthologues. The present review aims at depicting the major research lines in TRPM2 structure-function. It discusses biophysical properties of the pore and the mode of action of direct channel effectors, and interprets these functional properties on the basis of recent three-dimensional structural models. © 2021 by the author. Licensee MDPI, Basel, Switzerland.</abstractText>
      <fundings>
        <funding>
          <otype>Funding</otype>
          <mtid>2010102</mtid>
          <link>/api/funding/2010102</link>
          <label>(LP2017-14/2017)</label>
          <published>false</published>
          <snippet>true</snippet>
        </funding>
        <funding>
          <otype>Funding</otype>
          <mtid>2010103</mtid>
          <link>/api/funding/2010103</link>
          <label>(739593) Támogató: Horizon 2020</label>
          <published>false</published>
          <snippet>true</snippet>
        </funding>
      </fundings>
      <digital>true</digital>
      <printed/>
      <sourceYear>2021</sourceYear>
      <foreignEdition>true</foreignEdition>
      <foreignLanguage>true</foreignLanguage>
      <fullPublication>true</fullPublication>
      <conferencePublication>false</conferencePublication>
      <nationalOrigin>true</nationalOrigin>
      <missingAuthor>false</missingAuthor>
      <oaType>GOLD</oaType>
      <oaCheckDate>2026-06-12</oaCheckDate>
      <oaFree>true</oaFree>
      <oaLink>https://doi.org/10.3390/life11050397</oaLink>
      <citationCount>27</citationCount>
      <citationCountUnpublished>0</citationCountUnpublished>
      <citationCountWoOther>27</citationCountWoOther>
      <independentCitCountWoOther>25</independentCitCountWoOther>
      <nationalOriginCitationCount>6</nationalOriginCitationCount>
      <foreignEditionCitationCount>27</foreignEditionCitationCount>
      <doiCitationCount>27</doiCitationCount>
      <wosCitationCount>24</wosCitationCount>
      <scopusCitationCount>26</scopusCitationCount>
      <wosScopusCitationCount>27</wosScopusCitationCount>
      <wosScopusCitationCountWoOther>27</wosScopusCitationCountWoOther>
      <wosScopusIndependentCitationCount>25</wosScopusIndependentCitationCount>
      <wosScopusIndependentCitationCountWoOther>25</wosScopusIndependentCitationCountWoOther>
      <independentCitationCount>25</independentCitationCount>
      <selfCitationCount>2</selfCitationCount>
      <unhandledCitationCount>0</unhandledCitationCount>
      <citingPubCount>27</citingPubCount>
      <independentCitingPubCount>25</independentCitingPubCount>
      <citingPubCountWoOther>27</citingPubCountWoOther>
      <independentCitingPubCountWoOther>25</independentCitingPubCountWoOther>
      <unhandledCitingPubCount>0</unhandledCitingPubCount>
      <citedPubCount>11</citedPubCount>
      <citedCount>11</citedCount>
      <pubStats>
        <types>
          <type>Folyóiratcikk</type>
          <typeEng>Journal Article</typeEng>
          <code>24</code>
          <count>27</count>
        </types>
        <types>
          <type>Könyvrészlet</type>
          <typeEng>Chapter in Book</typeEng>
          <code>25</code>
          <count>0</count>
        </types>
        <types>
          <type>Könyv</type>
          <typeEng>Book</typeEng>
          <code>23</code>
          <count>0</count>
        </types>
        <types>
          <type>Egyéb konferenciaközlemény</type>
          <typeEng>Conference paper</typeEng>
          <code>31</code>
          <count>0</count>
        </types>
        <types>
          <type>Egyéb konferenciakötet</type>
          <typeEng>Conference proceedings</typeEng>
          <code>32</code>
          <count>0</count>
        </types>
        <types>
          <type>Oltalmi formák</type>
          <typeEng>Protection forms</typeEng>
          <code>26</code>
          <count>0</count>
        </types>
        <types>
          <type>Disszertáció</type>
          <typeEng>Thesis</typeEng>
          <code>28</code>
          <count>0</count>
        </types>
        <types>
          <type>Egyéb</type>
          <typeEng>Miscellaneous</typeEng>
          <code>29</code>
          <count>0</count>
        </types>
        <types>
          <type>Alkotás</type>
          <typeEng>Achievement</typeEng>
          <code>22</code>
          <count>0</count>
        </types>
        <types>
          <type>Kutatási adat</type>
          <typeEng>Research data</typeEng>
          <code>33</code>
          <count>0</count>
        </types>
        <citationTypes>
          <type>Folyóiratcikk</type>
          <typeEng>Journal Article</typeEng>
          <code>24</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Könyvrészlet</type>
          <typeEng>Chapter in Book</typeEng>
          <code>25</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Könyv</type>
          <typeEng>Book</typeEng>
          <code>23</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Egyéb konferenciaközlemény</type>
          <typeEng>Conference paper</typeEng>
          <code>31</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Egyéb konferenciakötet</type>
          <typeEng>Conference proceedings</typeEng>
          <code>32</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Oltalmi formák</type>
          <typeEng>Protection forms</typeEng>
          <code>26</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Disszertáció</type>
          <typeEng>Thesis</typeEng>
          <code>28</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Egyéb</type>
          <typeEng>Miscellaneous</typeEng>
          <code>29</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Alkotás</type>
          <typeEng>Achievement</typeEng>
          <code>22</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <citationTypes>
          <type>Kutatási adat</type>
          <typeEng>Research data</typeEng>
          <code>33</code>
          <countUnknown>0</countUnknown>
          <countIndependent>0</countIndependent>
          <countSelfCitation>0</countSelfCitation>
        </citationTypes>
        <years>
          <year>2021</year>
          <publicationCount>0</publicationCount>
          <citationCount>1</citationCount>
          <independentCitationCount>1</independentCitationCount>
          <citingPubCount>1</citingPubCount>
          <independentCitingPubCount>1</independentCitingPubCount>
          <oaStats/>
          <oaStats2/>
        </years>
        <years>
          <year>2022</year>
          <publicationCount>0</publicationCount>
          <citationCount>2</citationCount>
          <independentCitationCount>2</independentCitationCount>
          <citingPubCount>2</citingPubCount>
          <independentCitingPubCount>2</independentCitingPubCount>
          <oaStats/>
          <oaStats2/>
        </years>
        <years>
          <year>2023</year>
          <publicationCount>0</publicationCount>
          <citationCount>6</citationCount>
          <independentCitationCount>5</independentCitationCount>
          <citingPubCount>6</citingPubCount>
          <independentCitingPubCount>5</independentCitingPubCount>
          <oaStats/>
          <oaStats2/>
        </years>
        <years>
          <year>2024</year>
          <publicationCount>0</publicationCount>
          <citationCount>6</citationCount>
          <independentCitationCount>6</independentCitationCount>
          <citingPubCount>6</citingPubCount>
          <independentCitingPubCount>6</independentCitingPubCount>
          <oaStats/>
          <oaStats2/>
        </years>
        <years>
          <year>2025</year>
          <publicationCount>0</publicationCount>
          <citationCount>10</citationCount>
          <independentCitationCount>9</independentCitationCount>
          <citingPubCount>10</citingPubCount>
          <independentCitingPubCount>9</independentCitingPubCount>
          <oaStats/>
          <oaStats2/>
        </years>
        <years>
          <year>2026</year>
          <publicationCount>0</publicationCount>
          <citationCount>2</citationCount>
          <independentCitationCount>2</independentCitationCount>
          <citingPubCount>2</citingPubCount>
          <independentCitingPubCount>2</independentCitingPubCount>
          <oaStats/>
          <oaStats2/>
        </years>
      </pubStats>
      <ratingsForSort>Q2</ratingsForSort>
      <hasCitationDuplums>false</hasCitationDuplums>
      <inSelectedPubs>10020191</inSelectedPubs>
      <importDuplum>false</importDuplum>
      <importOverwritten>false</importOverwritten>
      <importSkipped>false</importSkipped>
      <userChangeableUntil>2021-05-27T11:33:04.633+0000</userChangeableUntil>
      <directInstitutesForSort>Biokémiai Tanszék (SE / AOK / I / BMBI); HCEMM-SE Molekuláris Csatornabetegségek Kutatóc... (SE / AOK / I / BMBI / BT); MTA-SE Lendület Ioncsatorna Kutatócsoport (SE / AOK / I / BMBI / BT)</directInstitutesForSort>
      <ownerAuthorCount>1</ownerAuthorCount>
      <ownerInstituteCount>10</ownerInstituteCount>
      <directInstituteCount>3</directInstituteCount>
      <authorCount>1</authorCount>
      <contributorCount>0</contributorCount>
      <hasQualityFactor>true</hasQualityFactor>
      <languages>
        <language>
          <otype>Language</otype>
          <mtid>10002</mtid>
          <link>/api/language/10002</link>
          <label>Angol</label>
          <name>Angol</name>
          <nameEng>English</nameEng>
          <published>true</published>
          <oldId>2</oldId>
          <snippet>true</snippet>
        </language>
      </languages>
      <authorships>
        <authorship>
          <otype>PersonAuthorship</otype>
          <mtid>96445875</mtid>
          <link>/api/authorship/96445875</link>
          <label>Szollosi, A. ✉ [Szöllősi, András (Biokémia), szerző] MTA-SE Lendület Ioncsatorna Kutatócsoport (SE / AOK / I / BMBI / BT); Biokémiai Tanszék (SE / AOK / I / BMBI); HCEMM-SE Molekuláris Csatornabetegségek Kutatóc... (SE / AOK / I / BMBI / BT)</label>
          <listPosition>1</listPosition>
          <share>1.0</share>
          <first>true</first>
          <last>false</last>
          <corresponding>true</corresponding>
          <author>
            <otype>Author</otype>
            <mtid>10020191</mtid>
            <link>/api/author/10020191</link>
            <label>Szöllősi András (Biokémia)</label>
            <familyName>Szöllősi</familyName>
            <givenName>András</givenName>
            <published>true</published>
            <oldId>10020191</oldId>
            <snippet>true</snippet>
          </author>
          <familyName>Szollosi</familyName>
          <givenName>A.</givenName>
          <authorTyped>true</authorTyped>
          <editorTyped>false</editorTyped>
          <otherTyped>false</otherTyped>
          <type>
            <otype>AuthorshipType</otype>
            <mtid>1</mtid>
            <link>/api/authorshiptype/1</link>
            <label>Szerző</label>
            <code>0</code>
            <published>true</published>
            <oldId>0</oldId>
            <snippet>true</snippet>
          </type>
          <published>false</published>
          <snippet>true</snippet>
        </authorship>
      </authorships>
      <identifiers>
        <identifier>
          <otype>PublicationIdentifier</otype>
          <mtid>18846969</mtid>
          <link>/api/publicationidentifier/18846969</link>
          <label>DOI: 10.3390/life11050397</label>
          <source>
            <otype>PlainSource</otype>
            <mtid>6</mtid>
            <link>/api/publicationsource/6</link>
            <label>DOI</label>
            <type>
              <otype>PublicationSourceType</otype>
              <mtid>10001</mtid>
              <link>/api/publicationsourcetype/10001</link>
              <label>DOI</label>
              <mayHaveOa>true</mayHaveOa>
              <published>true</published>
              <snippet>true</snippet>
            </type>
            <name>DOI</name>
            <nameEng>DOI</nameEng>
            <linkPattern>https://doi.org/@@@</linkPattern>
            <publiclyVisible>true</publiclyVisible>
            <published>true</published>
            <oldId>6</oldId>
            <snippet>true</snippet>
          </source>
          <oaType>GOLD</oaType>
          <oaFree>true</oaFree>
          <validState>IDENTICAL</validState>
          <idValue>10.3390/life11050397</idValue>
          <realUrl>https://doi.org/10.3390/life11050397</realUrl>
          <published>false</published>
          <snippet>true</snippet>
        </identifier>
        <identifier>
          <otype>PublicationIdentifier</otype>
          <mtid>18926098</mtid>
          <link>/api/publicationidentifier/18926098</link>
          <label>WoS: 000654116000001</label>
          <source>
            <otype>PlainSource</otype>
            <mtid>1</mtid>
            <link>/api/publicationsource/1</link>
            <label>WoS</label>
            <type>
              <otype>PublicationSourceType</otype>
              <mtid>10003</mtid>
              <link>/api/publicationsourcetype/10003</link>
              <label>Indexelő adatbázis</label>
              <mayHaveOa>false</mayHaveOa>
              <published>true</published>
              <snippet>true</snippet>
            </type>
            <name>WoS</name>
            <nameEng>WoS</nameEng>
            <linkPattern>https://www.webofscience.com/wos/woscc/full-record/@@@</linkPattern>
            <publiclyVisible>true</publiclyVisible>
            <published>true</published>
            <oldId>1</oldId>
            <snippet>true</snippet>
          </source>
          <validState>IDENTICAL</validState>
          <idValue>000654116000001</idValue>
          <realUrl>https://www.webofscience.com/wos/woscc/full-record/000654116000001</realUrl>
          <published>true</published>
          <snippet>true</snippet>
        </identifier>
        <identifier>
          <otype>PublicationIdentifier</otype>
          <mtid>18846968</mtid>
          <link>/api/publicationidentifier/18846968</link>
          <label>Scopus: 85105782082</label>
          <source>
            <otype>PlainSource</otype>
            <mtid>3</mtid>
            <link>/api/publicationsource/3</link>
            <label>Scopus</label>
            <type>
              <otype>PublicationSourceType</otype>
              <mtid>10003</mtid>
              <link>/api/publicationsourcetype/10003</link>
              <label>Indexelő adatbázis</label>
              <mayHaveOa>false</mayHaveOa>
              <published>true</published>
              <snippet>true</snippet>
            </type>
            <name>Scopus</name>
            <nameEng>Scopus</nameEng>
            <linkPattern>http://www.scopus.com/record/display.url?origin=inward&amp;eid=2-s2.0-@@@</linkPattern>
            <publiclyVisible>true</publiclyVisible>
            <published>true</published>
            <oldId>3</oldId>
            <snippet>true</snippet>
          </source>
          <validState>IDENTICAL</validState>
          <idValue>85105782082</idValue>
          <realUrl>http://www.scopus.com/record/display.url?origin=inward&amp;eid=2-s2.0-85105782082</realUrl>
          <published>false</published>
          <snippet>true</snippet>
        </identifier>
        <identifier>
          <otype>PublicationIdentifier</otype>
          <mtid>18926107</mtid>
          <link>/api/publicationidentifier/18926107</link>
          <label>PubMed: 33925466</label>
          <source>
            <otype>PlainSource</otype>
            <mtid>17</mtid>
            <link>/api/publicationsource/17</link>
            <label>PubMed</label>
            <type>
              <otype>PublicationSourceType</otype>
              <mtid>10003</mtid>
              <link>/api/publicationsourcetype/10003</link>
              <label>Indexelő adatbázis</label>
              <mayHaveOa>false</mayHaveOa>
              <published>true</published>
              <snippet>true</snippet>
            </type>
            <name>PubMed</name>
            <nameEng>PubMed</nameEng>
            <linkPattern>http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;list_uids=@@@&amp;dopt=Abstract</linkPattern>
            <publiclyVisible>true</publiclyVisible>
            <published>true</published>
            <oldId>17</oldId>
            <snippet>true</snippet>
          </source>
          <validState>IDENTICAL</validState>
          <idValue>33925466</idValue>
          <realUrl>http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;list_uids=33925466&amp;dopt=Abstract</realUrl>
          <published>false</published>
          <snippet>true</snippet>
        </identifier>
        <identifier>
          <otype>PublicationIdentifier</otype>
          <mtid>31874235</mtid>
          <link>/api/publicationidentifier/31874235</link>
          <label>Egyéb URL: https://www.scopus.com/pages/publications/85105782082?origin=resultslist</label>
          <source>
            <otype>PlainSource</otype>
            <mtid>40</mtid>
            <link>/api/publicationsource/40</link>
            <label>Egyéb URL</label>
            <type>
              <otype>PublicationSourceType</otype>
              <mtid>10006</mtid>
              <link>/api/publicationsourcetype/10006</link>
              <label>Link</label>
              <mayHaveOa>true</mayHaveOa>
              <published>true</published>
              <snippet>true</snippet>
            </type>
            <name>Egyéb URL</name>
            <nameEng>Other URL</nameEng>
            <linkPattern>@@@</linkPattern>
            <publiclyVisible>true</publiclyVisible>
            <published>true</published>
            <oldId>40</oldId>
            <snippet>true</snippet>
          </source>
          <oaType>NONE</oaType>
          <validState>IDENTICAL</validState>
          <idValue>https://www.scopus.com/pages/publications/85105782082?origin=resultslist</idValue>
          <realUrl>https://www.scopus.com/pages/publications/85105782082?origin=resultslist</realUrl>
          <published>false</published>
          <snippet>true</snippet>
        </identifier>
      </identifiers>
      <keywords>
        <keyword>
          <otype>Keyword</otype>
          <mtid>2282</mtid>
          <link>/api/keyword/2282</link>
          <label>ION CHANNELS</label>
          <published>true</published>
          <oldId>2282</oldId>
          <snippet>true</snippet>
        </keyword>
        <keyword>
          <otype>Keyword</otype>
          <mtid>1014845</mtid>
          <link>/api/keyword/1014845</link>
          <label>ADP-ribose</label>
          <published>true</published>
          <oldId>1014845</oldId>
          <snippet>true</snippet>
        </keyword>
        <keyword>
          <otype>Keyword</otype>
          <mtid>1507502</mtid>
          <link>/api/keyword/1507502</link>
          <label>Single particle cryo-EM</label>
          <published>true</published>
          <snippet>true</snippet>
        </keyword>
        <keyword>
          <otype>Keyword</otype>
          <mtid>1533642</mtid>
          <link>/api/keyword/1533642</link>
          <label>TRPM2</label>
          <published>true</published>
          <snippet>true</snippet>
        </keyword>
        <keyword>
          <otype>Keyword</otype>
          <mtid>1711741</mtid>
          <link>/api/keyword/1711741</link>
          <label>Nudix hydrolase</label>
          <published>true</published>
          <snippet>true</snippet>
        </keyword>
      </keywords>
      <ratings>
        <rating>
          <otype>SjrRating</otype>
          <mtid>11195856</mtid>
          <link>/api/sjrrating/11195856</link>
          <label>sjr:Q2 (2021) Scopus - Biochemistry, Genetics and Molecular Biology (miscellaneous) LIFE-BASEL 2075-1729</label>
          <listPos>102</listPos>
          <rankValue>0.49</rankValue>
          <type>journal</type>
          <ratingType>
            <otype>RatingType</otype>
            <mtid>10002</mtid>
            <link>/api/ratingtype/10002</link>
            <label>sjr</label>
            <code>sjr</code>
            <published>true</published>
            <snippet>true</snippet>
          </ratingType>
          <subject>
            <otype>ClassificationExternal</otype>
            <mtid>1301</mtid>
            <link>/api/classificationexternal/1301</link>
            <label>Scopus - Biochemistry, Genetics and Molecular Biology (miscellaneous)</label>
            <published>true</published>
            <oldId>1301</oldId>
            <snippet>true</snippet>
          </subject>
          <ranking>Q2</ranking>
          <calculation>DIRECT</calculation>
          <published>true</published>
          <snippet>true</snippet>
        </rating>
      </ratings>
      <references>
        <reference>
          <otype>Reference</otype>
          <mtid>20866278</mtid>
          <link>/api/reference/20866278</link>
          <label>1. Kühn, F.J.P., Watt, J.M., Potter, B.V.L., Lückhoff, A., Different substrate specificities of the two ADPR binding sites in TRPM2 channels of Nematostella vectensis and the role of IDPR (2019) Sci. Rep, 9, p. 4985. , [CrossRef]</label>
          <listPosition>1</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866277</mtid>
          <link>/api/reference/20866277</link>
          <label>2. Zubcevic, L., Hsu, A.L., Borgnia, M.J., Lee, S.-Y., Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes (2019) eLife, 8, p. 8. , [CrossRef]</label>
          <listPosition>2</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866276</mtid>
          <link>/api/reference/20866276</link>
          <label>3. Zubcevic, L., Herzik, M.A., Wu, M., Borschel, W.F., Hirschi, M., Song, A.S., Lander, G.C., Lee, S.-Y., Conformational ensemble of the human TRPV3 ion channel (2018) Nat. Commun, 9, pp. 1-12. , [CrossRef]</label>
          <listPosition>3</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866275</mtid>
          <link>/api/reference/20866275</link>
          <label>4. Yoo, J., Wu, M., Yin, Y., Herzik, M.A., Lander, G.C., Lee, S.-Y., Cryo-EM structure of a mitochondrial calcium uniporter (2018) Science, 361, pp. 506-511. , [CrossRef] [PubMed]</label>
          <listPosition>4</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866274</mtid>
          <link>/api/reference/20866274</link>
          <label>5. Nguyen, N.X., Armache, J.-P., Lee, C., Yang, Y., Zeng, W., Mootha, V.K., Cheng, Y., Jiang, Y., Cryo-EM structure of a fungal mitochondrial calcium uniporter (2018) Nat. Cell Biol, 559, pp. 570-574. , [CrossRef] [PubMed]</label>
          <listPosition>5</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866273</mtid>
          <link>/api/reference/20866273</link>
          <label>6. Matthies, D., Dalmas, O., Borgnia, M.J., Dominik, P.K., Merk, A., Rao, P., Reddy, B.G., Perozo, E., Cryo-EM Structures of the Magnesium Channel CorA Reveal Symmetry Break upon Gating (2016) Cell, 164, pp. 747-756. , [CrossRef] [PubMed]</label>
          <listPosition>6</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866272</mtid>
          <link>/api/reference/20866272</link>
          <label>7. Fan, C., Fan, M., Orlando, B.J., Fastman, N.M., Zhang, J., Xu, Y., Chambers, M.G., Liao, M., X-ray and cryo-EM structures of the mitochondrial calcium uniporter (2018) Nat. Cell Biol, 559, pp. 575-579. , [CrossRef]</label>
          <listPosition>7</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866271</mtid>
          <link>/api/reference/20866271</link>
          <label>8. Baradaran, R., Wang, C., Siliciano, A.F., Long, S.B., Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters (2018) Nat. Cell Biol, 559, pp. 580-584. , [CrossRef]</label>
          <listPosition>8</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866270</mtid>
          <link>/api/reference/20866270</link>
          <label>9. Yin, Y., Le, S.C., Hsu, A.L., Borgnia, M.J., Yang, H., Lee, S.-Y., Structural basis of cooling agent and lipid sensing by the cold-activated TRPM8 channel (2019) Science, 363, p. eaav9334. , [CrossRef]</label>
          <listPosition>9</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866269</mtid>
          <link>/api/reference/20866269</link>
          <label>10. Jin, P., Bulkley, D., Guo, Y., Zhang, W., Guo, Z., Huynh, W., Wu, S., Jan, L.Y., Electron cryo-microscopy structure of the mechanotransduction channel NOMPC (2017) Nature, 547, pp. 118-122. , [CrossRef]</label>
          <listPosition>10</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866268</mtid>
          <link>/api/reference/20866268</link>
          <label>11. Duan, J., Li, J., Zeng, B., Chen, G.-L., Peng, X., Zhang, Y., Wang, J., Zhang, J., Structure of the mouse TRPC4 ion channel (2018) Nat. Commun, 9, pp. 1-10. , [CrossRef]</label>
          <listPosition>11</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866267</mtid>
          <link>/api/reference/20866267</link>
          <label>12. Sun, J., MacKinnon, R., Structural Basis of Human KCNQ1 Modulation and Gating (2020) Cell, 180, pp. 340-347. , e9. [CrossRef]</label>
          <listPosition>12</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866266</mtid>
          <link>/api/reference/20866266</link>
          <label>13. Hughes, T.E.T., Pumroy, R.A., Yazici, A.T., Kasimova, M.A., Fluck, E.C., Huynh, K.W., Samanta, A., Carnevale, V., Structural insights on TRPV5 gating by endogenous modulators (2018) Nat. Commun, 9, pp. 1-11. , [CrossRef]</label>
          <listPosition>13</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866265</mtid>
          <link>/api/reference/20866265</link>
          <label>14. Gao, Y., Cao, E., Julius, Y.G.E.C.D., Cheng, Y.G.Y., TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action (2016) Nature, 534, pp. 347-351. , [CrossRef]</label>
          <listPosition>14</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866264</mtid>
          <link>/api/reference/20866264</link>
          <label>15. Yudin, Y., Lukacs, V., Cao, C., Rohacs, T., Decrease in phosphatidylinositol 4,5-bisphosphate levels mediates desensitization of the cold sensor TRPM8 channels (2011) J. Physiol, 589, pp. 6007-6027. , [CrossRef]</label>
          <listPosition>15</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866263</mtid>
          <link>/api/reference/20866263</link>
          <label>16. Rohacs, T., Nilius, B., Regulation of transient receptor potential (TRP) channels by phosphoinositides (2007) Pflügers Arch. Eur. J. Physiol, 455, pp. 157-168. , [CrossRef]</label>
          <listPosition>16</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866262</mtid>
          <link>/api/reference/20866262</link>
          <label>17. Yin, Y., Wu, M., Hsu, A.L., Borschel, W.F., Borgnia, M.J., Lander, G.C., Lee, S.-Y., Visualizing structural transitions of ligand-dependent gating of the TRPM2 channel (2019) Nat. Commun, 10, pp. 1-14. , [CrossRef]</label>
          <listPosition>17</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866261</mtid>
          <link>/api/reference/20866261</link>
          <label>18. Mei, Z.-Z., Mao, H.-J., Jiang, L.-H., Conserved cysteine residues in the pore region are obligatory for human TRPM2 channel function (2006) Am. J. Physiol. Physiol, 291, pp. C1022-C1028. , [CrossRef]</label>
          <listPosition>18</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866260</mtid>
          <link>/api/reference/20866260</link>
          <label>19. Huffer, K.E., Aleksandrova, A.A., Jara-Oseguera, A., Forrest, L.R., Swartz, K.J., Global alignment and assessment of TRP channel transmembrane domain structures to explore func-tional mechanisms (2020) eLife, 9, p. e58660. , [CrossRef]</label>
          <listPosition>19</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866259</mtid>
          <link>/api/reference/20866259</link>
          <label>20. Xia, R., Mei, Z.-Z., Mao, H.-J., Yang, W., Dong, L., Bradley, H., Beech, D.J., Jiang, L.-H., Identification of Pore Residues Engaged in Determining Divalent Cationic Permeation in Transient Receptor Potential Melastatin Subtype Channel 2* (2008) J. Biol. Chem, 283, pp. 27426-27432. , [CrossRef]</label>
          <listPosition>20</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866258</mtid>
          <link>/api/reference/20866258</link>
          <label>21. Voets, T., Nilius, B., Hoefs, S., van der Kemp, A.W., Droogmans, G., Bindels, R.J., Hoenderop, J.G., TRPM6 Forms the Mg2+ Influx Channel Involved in Intestinal and Renal Mg2+ Absorption (2004) J. Biol. Chem, 279, pp. 19-25. , [CrossRef]</label>
          <listPosition>21</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866257</mtid>
          <link>/api/reference/20866257</link>
          <label>22. Lambert, S., Drews, A., Rizun, O., Wagner, T.F.J., Lis, A., Mannebach, S., Plant, S., Philipp, S.E., Transient receptor potential melastatin 1 (TRPM1) is an ion-conducting plasma membrane channel in-hibited by zinc ions (2011) J. Biol. Chem, 286, pp. 12221-12233. , [CrossRef]</label>
          <listPosition>22</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866256</mtid>
          <link>/api/reference/20866256</link>
          <label>23. Grimm, C., Kraft, R., Sauerbruch, S., Schultz, G., Harteneck, C., Molecular and Functional Characterization of the Melastatin-related Cation Channel TRPM3 (2003) J. Biol. Chem, 278, pp. 21493-21501. , [CrossRef]</label>
          <listPosition>23</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866255</mtid>
          <link>/api/reference/20866255</link>
          <label>24. Winkler, P.A., Huang, Y., Sun, W., Du, J., Lü, W., Electron cryo-microscopy structure of a human TRPM4 channel (2017) Nat. Cell Biol, 552, pp. 200-204. , [CrossRef]</label>
          <listPosition>24</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866254</mtid>
          <link>/api/reference/20866254</link>
          <label>25. Autzen, H.E., Myasnikov, A.G., Campbell, M.G., Asarnow, D., Julius, D., Cheng, Y., Structure of the human TRPM4 ion channel in a lipid nanodisc (2018) Science, 359, pp. 228-232. , [CrossRef]</label>
          <listPosition>25</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866253</mtid>
          <link>/api/reference/20866253</link>
          <label>26. Zhou, Y., Morais-Cabral, J.H., Kaufman, A., MacKinnon, R., Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution (2001) Nat. Cell Biol, 414, pp. 43-48. , [CrossRef]</label>
          <listPosition>26</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866252</mtid>
          <link>/api/reference/20866252</link>
          <label>27. Doyle, D.A., Cabral, J.M., Pfuetzner, R.A., Kuo, A., Gulbis, J.M., Cohen, S.L., Chait, B.T., MacKinnon, R., The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity (1998) Science, 280, pp. 69-77. , [CrossRef]</label>
          <listPosition>27</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866251</mtid>
          <link>/api/reference/20866251</link>
          <label>28. Wang, L., Fu, T.-M., Zhou, Y., Xia, S., Greka, A., Wu, H., Structures and gating mechanism of human TRPM2 (2018) Science, 362, p. eaav4809. , [CrossRef]</label>
          <listPosition>28</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866250</mtid>
          <link>/api/reference/20866250</link>
          <label>29. Paulsen, C.E., Armache, J.-P., Gao, Y., Cheng, Y., Julius, D., Structure of the TRPA1 ion channel suggests regulatory mechanisms (2015) Nature, 520, pp. 511-517. , [CrossRef]</label>
          <listPosition>29</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866249</mtid>
          <link>/api/reference/20866249</link>
          <label>30. Liao, M., Cao, E., Julius, D., Cheng, Y., Structure of the TRPV1 ion channel determined by electron cryo-microscopy (2013) Nature, 504, pp. 107-112. , [CrossRef]</label>
          <listPosition>30</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866248</mtid>
          <link>/api/reference/20866248</link>
          <label>31. Guo, J., She, J., Zeng, W., Chen, Q., Bai, X.-C., Jiang, Y., Structures of the calcium-activated, non-selective cation channel TRPM4 (2017) Nature, 552, pp. 205-209. , [CrossRef]</label>
          <listPosition>31</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866247</mtid>
          <link>/api/reference/20866247</link>
          <label>32. Frank, J., Penczek, P., Grassucci, R., Srivastava, S., Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: The distribution of ribosomal RNA (1991) J. Cell Biol, 115, pp. 597-605. , [CrossRef]</label>
          <listPosition>32</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866246</mtid>
          <link>/api/reference/20866246</link>
          <label>33. Frank, J., Van Heel, M., Correspondence analysis of aligned images of biological particles (1982) J. Mol. Biol, 161, pp. 134-137. , [CrossRef]</label>
          <listPosition>33</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866245</mtid>
          <link>/api/reference/20866245</link>
          <label>34. Dubochet, J., Adrian, M., Chang, J.-J., Homo, J.-C., Lepault, J., McDowall, A.W., Schultz, P., Cryo-electron microscopy of vitrified specimens (1988) Q. Rev. Biophys, 21, pp. 129-228. , [CrossRef] [PubMed]</label>
          <listPosition>34</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866244</mtid>
          <link>/api/reference/20866244</link>
          <label>35. Glaeser, R.M., Limitations to significant information in biological electron microscopy as a result of radiation damage (1971) J. Ultrastruct. Res, 36, pp. 466-482. , [CrossRef]</label>
          <listPosition>35</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866243</mtid>
          <link>/api/reference/20866243</link>
          <label>36. Henderson, R., Baldwin, J., Downing, K., Lepault, J., Zemlin, F., Structure of purple membrane from halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution (1986) Ultramicroscopy, 19, pp. 147-178. , [CrossRef]</label>
          <listPosition>36</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866242</mtid>
          <link>/api/reference/20866242</link>
          <label>37. Henderson, R., From Electron Crystallography to Single Particle CryoEM (Nobel Lecture) (2018) Angew. Chem. Int. Ed, 57, pp. 10804-10825. , [CrossRef]</label>
          <listPosition>37</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866241</mtid>
          <link>/api/reference/20866241</link>
          <label>38. Huang, Y., Winkler, P.A., Sun, W., Lü, W., Du, J., Architecture of the TRPM2 channel and its activation mechanism by ADP-ribose and calcium (2018) Nat. Cell Biol, 562, pp. 145-149. , [CrossRef]</label>
          <listPosition>38</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866240</mtid>
          <link>/api/reference/20866240</link>
          <label>39. Huang, Y., Roth, B., Lü, W., Du, J., Ligand recognition and gating mechanism through three ligand-binding sites of human TRPM2 channel (2019) eLife, 8, p. 8. , [CrossRef]</label>
          <listPosition>39</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866239</mtid>
          <link>/api/reference/20866239</link>
          <label>40. Tóth, B., Iordanov, I., Csanády, L., Selective profiling of N-and C-terminal nucleotide-binding sites in a TRPM2 channel (2020) J. Gen. Physiol, 152. , [CrossRef]</label>
          <listPosition>40</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866238</mtid>
          <link>/api/reference/20866238</link>
          <label>41. Kühn, F.J.P., Kühn, C., Winking, M., Hoffmann, D.C., Lückhoff, A., ADP-Ribose Activates the TRPM2 Channel from the Sea Anemone Nematostella vectensis Independently of the NUDT9H Domain (2016) PLoS ONE, 11, p. e0158060. , [CrossRef]</label>
          <listPosition>41</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866237</mtid>
          <link>/api/reference/20866237</link>
          <label>42. Waterhouse, A.M., Procter, J.B., Martin, D.M.A., Clamp, M., Barton, G.J., Jalview Version 2–a multiple sequence alignment editor and analysis workbench (2009) Bioinformatics, 25, pp. 1189-1191. , [CrossRef]</label>
          <listPosition>42</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866236</mtid>
          <link>/api/reference/20866236</link>
          <label>43. Li, W., Cowley, A., Uludag, M., Gur, T., McWilliam, H., Squizzato, S., Park, Y.M., Lopez, R., The EMBL-EBI bioinformatics web and programmatic tools framework (2015) Nucleic Acids Res, 43, pp. W580-W584. , [CrossRef] [PubMed]</label>
          <listPosition>43</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866235</mtid>
          <link>/api/reference/20866235</link>
          <label>44. Pankiewicz, K.W., Lesiak, K., Watanabe, K.A., Efficient Synthesis of Methylenebis(phosphonate) Analogues of P1, P2-Disubstituted Pyrophosphates of Biological Interest. A Novel Plausible Mechanism (1997) J. Am. Chem. Soc, 119, pp. 3691-3695. , [CrossRef]</label>
          <listPosition>44</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866234</mtid>
          <link>/api/reference/20866234</link>
          <label>45. Tóth, B., Iordanov, I., Csanády, L., Putative chanzyme activity of TRPM2 cation channel is Unrelated to pore gating (2014) Proc. Natl. Acad. Sci. USA, 111, pp. 16949-16954. , [CrossRef]</label>
          <listPosition>45</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866233</mtid>
          <link>/api/reference/20866233</link>
          <label>46. Rafty, L.A., Schmidt, M.T., Perraud, A.-L., Scharenberg, A.M., Denu, J.M., Analysis of O-Acetyl-ADP-ribose as a Target for Nudix ADP-ribose Hydrolases (2002) J. Biol. Chem, 277, pp. 47114-47122. , [CrossRef]</label>
          <listPosition>46</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866232</mtid>
          <link>/api/reference/20866232</link>
          <label>47. Ames, B.N., Dubin, D.T., The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid (1960) J. Biol. Chem, 235, pp. 769-775. , [CrossRef]</label>
          <listPosition>47</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866231</mtid>
          <link>/api/reference/20866231</link>
          <label>48. Kühn, F.J.P., Lückhoff, A., Sites of the NUDT9-H Domain Critical for ADP-ribose Activation of the Cation Channel TRPM2 (2004) J. Biol. Chem, 279, pp. 46431-46437. , [CrossRef]</label>
          <listPosition>48</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866230</mtid>
          <link>/api/reference/20866230</link>
          <label>49. Krapivinsky, G., Krapivinsky, L., Manasian, Y., Clapham, D.E., The TRPM7 Chanzyme Is Cleaved to Release a Chromatin-Modifying Kinase (2014) Cell, 157, pp. 1061-1072. , [CrossRef] [PubMed]</label>
          <listPosition>49</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866229</mtid>
          <link>/api/reference/20866229</link>
          <label>50. Csanády, L., Vergani, P., Gadsby, D.C., Structure, Gating, and Regulation of the CFTR Anion Channel (2019) Physiol. Rev, 99, pp. 707-738. , [CrossRef] [PubMed]</label>
          <listPosition>50</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866228</mtid>
          <link>/api/reference/20866228</link>
          <label>51. Csanady, L., Vergani, P., Gadsby, D.C., Strict coupling between CFTR’s catalytic cycle and gating of its Cl-ion pore revealed by distributions of open channel burst durations (2010) Proc. Natl. Acad. Sci. USA, 107, pp. 1241-1246. , [CrossRef]</label>
          <listPosition>51</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866227</mtid>
          <link>/api/reference/20866227</link>
          <label>52. Moreau, C., Kirchberger, T., Swarbrick, J.M., Bartlett, S.J., Fliegert, R., Yorgan, T., Bauche, A., Potter, B.V.L., Structure-activity relationship of adenosine 5’-diphosphoribose at the transient receptor potential me-lastatin 2 (TRPM2) channel: Rational design of antagonists (2013) J. Med. Chem, 56, pp. 10079-10102. , [CrossRef]</label>
          <listPosition>52</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866226</mtid>
          <link>/api/reference/20866226</link>
          <label>53. Fliegert, R., Bauche, A., Pérez, A.M.W., Watt, J.M., Rozewitz, M.D., Winzer, R., Janus, M., Harneit, A., 2’-Deoxyadenosine 5’-diphosphoribose is an endogenous TRPM2 superagonist (2017) Nat. Chem. Biol, 13, pp. 1036-1044. , [CrossRef]</label>
          <listPosition>53</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866225</mtid>
          <link>/api/reference/20866225</link>
          <label>54. Tóth, B., Iordanov, I., Csanády, L., Ruling out pyridine dinucleotides as true TRPM2 channel activators reveals novel direct agonist ADP-ribose-2′-phosphate (2015) J. Gen. Physiol, 145, pp. 419-430. , [CrossRef]</label>
          <listPosition>54</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866224</mtid>
          <link>/api/reference/20866224</link>
          <label>55. Heiner, I., Eisfeld, J., Warnstedt, M.U., Radukina, N., Jüngling, E., Lückhoff, A., Endogenous ADP-ribose enables calcium-regulated cation currents through TRPM2 channels in neutrophil granulocytes (2006) Biochem. J, 398, pp. 225-232. , [CrossRef]</label>
          <listPosition>55</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866223</mtid>
          <link>/api/reference/20866223</link>
          <label>56. Yu, P., Liu, Z., Yu, X., Ye, P., Liu, H., Xue, X., Yang, L., Fang, C., Direct Gating of the TRPM2 Channel by cADPR via Specific Interactions with the ADPR Binding Pocket (2019) Cell Rep, 27, pp. 3684-3695. , e4. [CrossRef]</label>
          <listPosition>56</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866222</mtid>
          <link>/api/reference/20866222</link>
          <label>57. Lange, I., Penner, R., Fleig, A., Beck, A., Synergistic regulation of endogenous TRPM2 channels by adenine dinucleotides in primary human neu-trophils (2008) Cell Calcium, 44, pp. 604-615. , [CrossRef]</label>
          <listPosition>57</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866221</mtid>
          <link>/api/reference/20866221</link>
          <label>58. Beck, A., Kolisek, M., Bagley, L.A., Fleig, A., Penner, R., Nicotinic acid adenine dinucleotide phosphate and cyclic ADP-ribose regulate TRPM2 channels in T lymphocytes (2006) FASEB J, 20, pp. 962-964. , [CrossRef]</label>
          <listPosition>58</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866220</mtid>
          <link>/api/reference/20866220</link>
          <label>59. Kim, H., Jacobson, E.L., Jacobson, M.K., Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases (1993) Science, 261, pp. 1330-1333. , [CrossRef]</label>
          <listPosition>59</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866219</mtid>
          <link>/api/reference/20866219</link>
          <label>60. Perraud, A.-L., Takanishi, C.L., Shen, B., Kang, S., Smith, M.K., Schmitz, C., Knowles, H.M., Zhang, J., Accumulation of Free ADP-ribose from Mitochondria Mediates Oxidative Stress-induced Gating of TRPM2 Cation Channels (2005) J. Biol. Chem, 280, pp. 6138-6148. , [CrossRef]</label>
          <listPosition>60</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866218</mtid>
          <link>/api/reference/20866218</link>
          <label>61. Tóth, B., Csanády, L., Pore collapse underlies irreversible inactivation of TRPM2 cation channel currents (2012) Proc. Natl. Acad. Sci. USA, 109, pp. 13440-13445. , [CrossRef]</label>
          <listPosition>61</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866217</mtid>
          <link>/api/reference/20866217</link>
          <label>62. Iordanov, I., Mihályi, C., Tóth, B., Csanády, L., The proposed channel-enzyme transient receptor potential melastatin 2 does not possess ADP ribose hydrolase activity (2016) eLife, 5, p. e17600. , [CrossRef]</label>
          <listPosition>62</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866216</mtid>
          <link>/api/reference/20866216</link>
          <label>63. Iordanov, I., Tóth, B., Szollosi, A., Csanády, L., Enzyme activity and selectivity filter stability of ancient TRPM2 channels were simultaneously lost in early vertebrates (2019) eLife, 8, p. 8. , [CrossRef]</label>
          <listPosition>63</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866215</mtid>
          <link>/api/reference/20866215</link>
          <label>64. Zhang, Z., Tóth, B., Szollosi, A., Chen, J., Csanády, L., Structure of a TRPM2 channel in complex with Ca2+ explains unique gating regulation (2018) eLife, 7, p. e36409. , [CrossRef]</label>
          <listPosition>64</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866214</mtid>
          <link>/api/reference/20866214</link>
          <label>65. Tong, Q., Zhang, W., Conrad, K., Mostoller, K., Cheung, J.Y., Peterson, B.Z., Miller, B.A., Regulation of the Transient Receptor Potential Channel TRPM2 by the Ca2+ Sensor Calmodulin (2006) J. Biol. Chem, 281, pp. 9076-9085. , [CrossRef]</label>
          <listPosition>65</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866213</mtid>
          <link>/api/reference/20866213</link>
          <label>66. Tóth, B., Csanády, L., Identification of Direct and Indirect Effectors of the Transient Receptor Potential Melastatin 2 (TRPM2) Cation Channel* (2010) J. Biol. Chem, 285, pp. 30091-30102. , [CrossRef]</label>
          <listPosition>66</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866212</mtid>
          <link>/api/reference/20866212</link>
          <label>67. Csanady, L., Torocsik, B., Four Ca2+ ions activate TRPM2 channels by binding in deep crevices near the pore but in-tracellularly of the gate (2009) J. Gen Physiol, 133, pp. 189-203. , [CrossRef]</label>
          <listPosition>67</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866211</mtid>
          <link>/api/reference/20866211</link>
          <label>68. Starkus, J., Beck, A., Fleig, A., Penner, R., Regulation of TRPM2 by Extra-and Intracellular Calcium (2007) J. Gen. Physiol, 130, pp. 427-440. , [CrossRef]</label>
          <listPosition>68</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866210</mtid>
          <link>/api/reference/20866210</link>
          <label>69. Sano, Y., Inamura, K., Miyake, A., Mochizuki, S., Yokoi, H., Matsushime, H., Furuichi, K., Immunocyte Ca2+ Influx System Mediated by LTRPC2 (2001) Science, 293, pp. 1327-1330. , [CrossRef]</label>
          <listPosition>69</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866209</mtid>
          <link>/api/reference/20866209</link>
          <label>70. McHugh, D., Flemming, R., Xu, S.-Z., Perraud, A.-L., Beech, D.J., Critical Intracellular Ca2+ Dependence of Transient Receptor Potential Melastatin 2 (TRPM2) Cation Channel Activation (2003) J. Biol. Chem, 278, pp. 11002-11006. , [CrossRef]</label>
          <listPosition>70</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866208</mtid>
          <link>/api/reference/20866208</link>
          <label>71. Kolisek, M., Beck, A., Fleig, A., Penner, R., Cyclic ADP-Ribose and Hydrogen Peroxide Synergize with ADP-Ribose in the Activation of TRPM2 Channels (2005) Mol. Cell, 18, pp. 61-69. , [CrossRef]</label>
          <listPosition>71</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866207</mtid>
          <link>/api/reference/20866207</link>
          <label>72. Nagamine, K., Kudoh, J., Minoshima, S., Kawasaki, K., Asakawa, S., Ito, F., Shimizu, N., Molecular cloning of a novel putative Ca2+ channel protein (TRPC7) highly expressed in brain (1998) Genomics, 54, pp. 124-131. , [CrossRef]</label>
          <listPosition>72</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866206</mtid>
          <link>/api/reference/20866206</link>
          <label>73. Grubisha, O., Rafty, L.A., Takanishi, C.L., Xu, X., Tong, L., Perraud, A.-L., Scharenberg, A.M., Denu, J.M., Metabolite of SIR2 Reaction Modulates TRPM2 Ion Channel (2006) J. Biol. Chem, 281, pp. 14057-14065. , [CrossRef]</label>
          <listPosition>73</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866205</mtid>
          <link>/api/reference/20866205</link>
          <label>74. Tong, L., Denu, J.M., Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose (2010) Biochim. Biophys. Acta (BBA) Proteins Proteom, 1804, pp. 1617-1625. , [CrossRef] [PubMed]</label>
          <listPosition>74</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866204</mtid>
          <link>/api/reference/20866204</link>
          <label>75. Shen, B.W., Perraud, A.L., Scharenberg, A., Stoddard, B.L., The Crystal Structure and Mutational Analysis of Human NUDT9 (2003) J. Mol. Biol, 332, pp. 385-398. , [CrossRef]</label>
          <listPosition>75</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866203</mtid>
          <link>/api/reference/20866203</link>
          <label>76. Legler, P.M., Massiah, M.A., Mildvan, A.S., Mutational, Kinetic, and NMR Studies of the Mechanism ofE. coliGDP-Mannose Mannosyl Hydrolase, an Unusual Nudix Enzyme† (2002) Biochemistry, 41, pp. 10834-10848. , [CrossRef] [PubMed]</label>
          <listPosition>76</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866202</mtid>
          <link>/api/reference/20866202</link>
          <label>77. Gabelli, S.B., Bianchet, A.M., Ohnishi, Y., Ichikawa, Y., Bessman, M.J., Amzel, L.M., Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase (2002) Biochemistry, 41, pp. 9279-9285. , [CrossRef]</label>
          <listPosition>77</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866201</mtid>
          <link>/api/reference/20866201</link>
          <label>78. Harris, T.K., Wu, G., Massiah, M.A., Mildvan, A.S., Mutational, Kinetic, and NMR Studies of the Roles of Conserved Glutamate Residues and of Lysine-39 in the Mechanism of the MutT Pyrophosphohydrolase† (2000) Biochemistry, 39, pp. 1655-1674. , [CrossRef]</label>
          <listPosition>78</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866200</mtid>
          <link>/api/reference/20866200</link>
          <label>79. Perraud, A.-L., Shen, B., Dunn, C.A., Rippe, K., Smith, M.K., Bessman, M.J., Stoddard, B.L., Scharenberg, A.M., NUDT9, a Member of the Nudix Hydrolase Family, Is an Evolutionarily Conserved Mitochondrial ADP-ribose Pyrophosphatase (2003) J. Biol. Chem, 278, pp. 1794-1801. , [CrossRef]</label>
          <listPosition>79</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866199</mtid>
          <link>/api/reference/20866199</link>
          <label>80. Mildvan, A., Xia, Z., Azurmendi, H., Saraswat, V., Legler, P., Massiah, M., Gabelli, S., Amzel, L., Structures and mechanisms of Nudix hydrolases (2005) Arch. Biochem. Biophys, 433, pp. 129-143. , [CrossRef]</label>
          <listPosition>80</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866198</mtid>
          <link>/api/reference/20866198</link>
          <label>81. Long, S.B., Campbell, E.B., MacKinnon, R., Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling (2005) Science, 309, pp. 903-908. , [CrossRef]</label>
          <listPosition>81</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866197</mtid>
          <link>/api/reference/20866197</link>
          <label>82. Long, S.B., Campbell, E.B., MacKinnon, R., Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K+ Channel (2005) Science, 309, pp. 897-903. , [CrossRef]</label>
          <listPosition>82</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866196</mtid>
          <link>/api/reference/20866196</link>
          <label>83. Kaneko, S., Kawakami, S., Hara, Y., Wakamori, M., Itoh, E., Minami, T., Takada, Y., Mori, Y., A Critical Role of TRPM2 in Neuronal Cell Death by Hydrogen Peroxide (2006) J. Pharmacol. Sci, 101, pp. 66-76. , [CrossRef]</label>
          <listPosition>83</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866195</mtid>
          <link>/api/reference/20866195</link>
          <label>84. Hermosura, M.C., Cui, A.M., Go, R.C.V., Davenport, B., Shetler, C.M., Heizer, J.W., Schmitz, C., Perraud, A.-L., Altered functional properties of a TRPM2 variant in Guamanian ALS and PD (2008) Proc. Natl. Acad. Sci. USA, 105, pp. 18029-18034. , [CrossRef]</label>
          <listPosition>84</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866194</mtid>
          <link>/api/reference/20866194</link>
          <label>85. Fonfria, E., Marshall, I.C.B., Boyfield, I., Skaper, S.D., Hughes, J.P., E Owen, D., Zhang, W., McNulty, E.S., Amyloid beta-peptide (1–42) and hydrogen peroxide-induced toxicity are mediated by TRPM2 in rat primary striatal cultures (2005) J. Neurochem, 95, pp. 715-723. , [CrossRef]</label>
          <listPosition>85</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866193</mtid>
          <link>/api/reference/20866193</link>
          <label>86. Nilius, B., Owsianik, G., Voets, T., Peters, J.A., Transient Receptor Potential Cation Channels in Disease (2007) Physiol. Rev, 87, pp. 165-217. , [CrossRef]</label>
          <listPosition>86</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866192</mtid>
          <link>/api/reference/20866192</link>
          <label>87. Song, K., Wang, H., Kamm, G.B., Pohle, J., Reis, F.D.C., Heppenstall, P., Wende, H., Siemens, J., The TRPM2 channel is a hypothalamic heat sensor that limits fever and can drive hypothermia (2016) Science, 353, pp. 1393-1398. , [CrossRef]</label>
          <listPosition>87</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866191</mtid>
          <link>/api/reference/20866191</link>
          <label>88. Yamamoto, S., Shimizu, S., Kiyonaka, S., Takahashi, N., Wajima, T., Hara, Y., Negoro, T., Okada, T., TRPM2-mediated Ca2+ influx induces chemokine production in monocytes that aggravates inflam-matory neutrophil infiltration (2008) Nat. Med, 14, pp. 738-747. , [CrossRef]</label>
          <listPosition>88</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866190</mtid>
          <link>/api/reference/20866190</link>
          <label>89. Uchida, K., Tominaga, M., The role of thermosensitive TRP (transient receptor potential) channels in insulin secretion (2011) Endocr. J, 58, pp. 1021-1028. , [CrossRef]</label>
          <listPosition>89</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866189</mtid>
          <link>/api/reference/20866189</link>
          <label>90. Perraud, A.-L., Fleig, A., Dunn, C.A., Bagley, L.A., Launay, P., Schmitz, C., Stokes, A.J., Penner, R., ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology (2001) Nat. Cell Biol, 411, pp. 595-599. , [CrossRef]</label>
          <listPosition>90</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866188</mtid>
          <link>/api/reference/20866188</link>
          <label>91. Kühn, F.J., Structure-Function Relationship of TRPM2: Recent Advances, Contradictions, and Open Questions (2020) Int. J. Mol. Sci, 21, p. 6481. , [CrossRef]</label>
          <listPosition>91</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866187</mtid>
          <link>/api/reference/20866187</link>
          <label>92. Hara, Y., Wakamori, M., Ishii, M., Maeno, E., Nishida, M., Yoshida, T., Yamada, H., Kudoh, J., LTRPC2 Ca2+-Permeable Channel Activated by Changes in Redox Status Confers Susceptibility to Cell Death (2002) Mol. Cell, 9, pp. 163-173. , [CrossRef]</label>
          <listPosition>92</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866186</mtid>
          <link>/api/reference/20866186</link>
          <label>93. Liu, D., Liman, E.R., Intracellular Ca2+ and the phospholipid PIP2 regulate the taste transduction ion channel TRPM5 (2003) Proc. Natl. Acad. Sci. USA, 100, pp. 15160-15165. , [CrossRef] [PubMed]</label>
          <listPosition>93</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866185</mtid>
          <link>/api/reference/20866185</link>
          <label>94. Launay, P., Fleig, A., Perraud, A.-L., Scharenberg, A.M., Penner, R., Kinet, J.-P., TRPM4 is a Ca2+-activated nonselective cation channel mediating cell membrane depolarization (2002) Cell, 109, pp. 397-407. , [CrossRef]</label>
          <listPosition>94</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866184</mtid>
          <link>/api/reference/20866184</link>
          <label>95. Huang, Y., Fliegert, R., Guse, A.H., Lü, W., Du, J., A structural overview of the ion channels of the TRPM family (2020) Cell Calcium, 85, p. 102111. , [CrossRef]</label>
          <listPosition>95</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>20866183</mtid>
          <link>/api/reference/20866183</link>
          <label>96. Wang, H., Siemens, J., TRP ion channels in thermosensation, thermoregulation and metabolism (2015) Temperature, 2, pp. 178-187. , [CrossRef] [PubMed]</label>
          <listPosition>96</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
      </references>
      <link>/api/publication/32040119</link>
      <label>Szollosi A.. Two decades of evolution of our understanding of the transient receptor potential melastatin 2 (Trpm2) cation channel. (2021) LIFE-BASEL 2075-1729 11 5</label><template>&lt;div class=&quot;JournalArticle Publication short-list&quot;&gt; &lt;div class=&quot;authors&quot;&gt; &lt;span class=&quot;author-name&quot; mtid=&quot;10020191&quot;&gt; &lt;a href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10020191&quot; target=&quot;_blank&quot;&gt;Szollosi, A. ✉&lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;author-type&quot;&gt; &lt;/span&gt; &lt;/div &gt;&lt;div class=&quot;title&quot;&gt;&lt;a href=&quot;/gui2/?mode=browse&amp;params=publication;32040119&quot; mtid=&quot;32040119&quot; target=&quot;_blank&quot;&gt;Two decades of evolution of our understanding of the transient receptor potential melastatin 2 (Trpm2) cation channel&lt;/a&gt;&lt;/div&gt; &lt;div class=&quot;pub-info&quot;&gt; &lt;span class=&quot;journal-title&quot;&gt;LIFE-BASEL&lt;/span&gt; &lt;span class=&quot;journal-volume&quot;&gt;11&lt;/span&gt; : &lt;span class=&quot;journal-issue&quot;&gt;5&lt;/span&gt; &lt;span class=&quot;page&quot;&gt; Paper: 397 , 23 p. &lt;/span&gt; &lt;span class=&quot;year&quot;&gt;(2021)&lt;/span&gt; &lt;/div&gt; &lt;div class=&quot;pub-end&quot;&gt;&lt;div class=&quot;identifier-list&quot;&gt; &lt;span class=&quot;identifiers&quot;&gt; &lt;span class=&quot;id identifier oa_GOLD&quot; title=&quot; Gold &quot;&gt; &lt;a style=&quot;color:blue&quot; title=&quot;10.3390/life11050397&quot; target=&quot;_blank&quot; href=&quot;https://doi.org/10.3390/life11050397&quot;&gt; DOI &lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;id identifier oa_none&quot; title=&quot;none&quot;&gt; &lt;a style=&quot;color:blue&quot; title=&quot;000654116000001&quot; target=&quot;_blank&quot; href=&quot;https://www.webofscience.com/wos/woscc/full-record/000654116000001&quot;&gt; WoS &lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;id identifier oa_none&quot; title=&quot;none&quot;&gt; &lt;a style=&quot;color:blue&quot; title=&quot;85105782082&quot; target=&quot;_blank&quot; href=&quot;http://www.scopus.com/record/display.url?origin=inward&amp;eid=2-s2.0-85105782082&quot;&gt; Scopus &lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;id identifier oa_none&quot; title=&quot;none&quot;&gt; &lt;a style=&quot;color:blue&quot; title=&quot;33925466&quot; target=&quot;_blank&quot; href=&quot;http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;list_uids=33925466&amp;dopt=Abstract&quot;&gt; PubMed &lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;id identifier oa_NONE&quot; title=&quot; Nincs &quot;&gt; &lt;a style=&quot;color:blue&quot; title=&quot;https://www.scopus.com/pages/publications/85105782082?origin=resultslist&quot; target=&quot;_blank&quot; href=&quot;https://www.scopus.com/pages/publications/85105782082?origin=resultslist&quot;&gt; Egyéb URL &lt;/a&gt; &lt;/span&gt; &lt;/span&gt; &lt;/div&gt; &lt;div class=&quot;short-pub-prop-list&quot;&gt; &lt;span class=&quot;short-pub-mtid&quot;&gt; Közlemény:32040119 &lt;/span&gt; &lt;span class=&quot;status-holder&quot;&gt;&lt;span class=&quot;status-data status-VALIDATED&quot;&gt; Egyeztetett &lt;/span&gt;&lt;/span&gt; &lt;span class=&quot;pub-core&quot;&gt;Forrás Idéző &lt;/span&gt; &lt;span class=&quot;pub-type&quot;&gt;Folyóiratcikk (Összefoglaló cikk ) &lt;/span&gt; &lt;!-- &amp;&amp; !record.category.scientific --&gt; &lt;span class=&quot;pub-category&quot;&gt;Tudományos&lt;/span&gt; &lt;div class=&quot;publication-citation&quot; style=&quot;margin-left: 0.5cm;&quot;&gt; &lt;span title=&quot;Nyilvános idézőközlemények összesen, említések nélkül&quot; class=&quot;citingPub-count&quot;&gt;Nyilvános idéző összesen: 27&lt;/span&gt; | Független: 25 | Függő: 2 | Nem jelölt: 0 | WoS jelölt: 24 | Scopus jelölt:&amp;nbsp;26 | WoS/Scopus jelölt:&amp;nbsp;27 | DOI jelölt:&amp;nbsp;27 &lt;/div&gt; &lt;/div&gt; &lt;/div&gt; &lt;/div&gt;</template><template2>&lt;div class=&quot;JournalArticle Publication long-list&quot;&gt;
&lt;div class=&quot;authors&quot;&gt;
	&lt;img title=&quot;Forrásközlemény&quot; style=&quot;float: left&quot; src=&quot;/frontend/resources/grid/publication-core-icon.png&quot;&gt;
	&lt;img title=&quot;Idézőközlemény&quot; style=&quot;float: left&quot; src=&quot;/frontend/resources/grid/publication-citation-icon.png&quot;&gt;

		&lt;div class=&quot;autype autype0&quot;&gt;				&lt;span class=&quot;author-name&quot; mtid=&quot;10020191&quot;&gt;&lt;a 
																				   href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10020191&quot; target=&quot;_blank&quot;&gt;Szollosi A. ✉
            (&lt;span class=&quot;authorship-author-name&quot;&gt;Szöllősi András&lt;/span&gt;
            &lt;span class=&quot;authorAux-mtmt&quot;&gt; Biokémia&lt;/span&gt;)
			&lt;/a&gt;
    &lt;/span&gt;
&lt;span class=&quot;author-affil&quot;&gt;&lt;span title=&quot;Semmelweis Egyetem&quot;&gt;SE&lt;/span&gt;/&lt;span title=&quot;Általános Orvostudományi Kar&quot;&gt;AOK&lt;/span&gt;/&lt;span title=&quot;Intézet&quot;&gt;I&lt;/span&gt;/&lt;span title=&quot;Biokémiai és Molekuláris Biológiai Intézet&quot;&gt;BMBI&lt;/span&gt;/&lt;span title=&quot;Biokémiai Tanszék&quot;&gt;BT&lt;/span&gt;/MTA-SE Lendület Ioncsatorna Kutatócsoport; &lt;span title=&quot;Semmelweis Egyetem&quot;&gt;SE&lt;/span&gt;/&lt;span title=&quot;Általános Orvostudományi Kar&quot;&gt;AOK&lt;/span&gt;/&lt;span title=&quot;Intézet&quot;&gt;I&lt;/span&gt;/&lt;span title=&quot;Biokémiai és Molekuláris Biológiai Intézet&quot;&gt;BMBI&lt;/span&gt;/Biokémiai Tanszék; &lt;span title=&quot;Semmelweis Egyetem&quot;&gt;SE&lt;/span&gt;/&lt;span title=&quot;Általános Orvostudományi Kar&quot;&gt;AOK&lt;/span&gt;/&lt;span title=&quot;Intézet&quot;&gt;I&lt;/span&gt;/&lt;span title=&quot;Biokémiai és Molekuláris Biológiai Intézet&quot;&gt;BMBI&lt;/span&gt;/&lt;span title=&quot;Biokémiai Tanszék&quot;&gt;BT&lt;/span&gt;/HCEMM-SE Molekuláris Csatornabetegségek Kutatócsoport&lt;/span&gt;

				    &lt;/div&gt;
&lt;/div&gt;
&lt;div class=&quot;title&quot;&gt;&lt;a href=&quot;/gui2/?mode=browse&amp;params=publication;32040119&quot; target=&quot;_blank&quot;&gt;Two decades of evolution of our understanding of the transient receptor potential melastatin 2 (Trpm2) cation channel&lt;/a&gt;&lt;/div&gt;    &lt;div&gt;		&lt;span class=&quot;journal-title&quot;&gt;LIFE-BASEL&lt;/span&gt;

        &lt;span class=&quot;journal-issn&quot;&gt;( &lt;a target=&quot;_blank&quot; href=&quot;https://portal.issn.org/resource/ISSN/2075-1729&quot;&gt;2075-1729&lt;/a&gt;)&lt;/span&gt;:
		&lt;span class=&quot;journal-volume&quot;&gt;11&lt;/span&gt; &lt;span class=&quot;journal-issue&quot;&gt;5&lt;/span&gt;
&lt;span class=&quot;page&quot;&gt;
		Paper 397.
	 23 p. 
&lt;/span&gt;		 &lt;span class=&quot;year&quot;&gt;(2021)&lt;/span&gt;  
    &lt;/div&gt;
&lt;div class=&quot;pub-footer&quot;&gt;
    

	&lt;span class=&quot;language&quot; xmlns=&quot;http://www.w3.org/1999/html&quot;&gt;Nyelv:
			Angol
		 |  &lt;/span&gt;

	&lt;span class=&quot;identifiers&quot;&gt;
						&lt;span class=&quot;id identifier oa_GOLD&quot; title=&quot;	Gold
&quot;&gt;
							
							&lt;a style=&quot;color:blue&quot; title=&quot;10.3390/life11050397&quot; target=&quot;_blank&quot; href=&quot;https://doi.org/10.3390/life11050397&quot;&gt;
									DOI
							&lt;/a&gt;
						&lt;/span&gt;
						&lt;span class=&quot;id identifier oa_none&quot; title=&quot;none&quot;&gt;
							
							&lt;a style=&quot;color:blue&quot; title=&quot;000654116000001&quot; target=&quot;_blank&quot; href=&quot;https://www.webofscience.com/wos/woscc/full-record/000654116000001&quot;&gt;
									WoS
							&lt;/a&gt;
						&lt;/span&gt;
						&lt;span class=&quot;id identifier oa_none&quot; title=&quot;none&quot;&gt;
							
							&lt;a style=&quot;color:blue&quot; title=&quot;85105782082&quot; target=&quot;_blank&quot; href=&quot;http://www.scopus.com/record/display.url?origin=inward&amp;eid=2-s2.0-85105782082&quot;&gt;
									Scopus
							&lt;/a&gt;
						&lt;/span&gt;
						&lt;span class=&quot;id identifier oa_none&quot; title=&quot;none&quot;&gt;
							
							&lt;a style=&quot;color:blue&quot; title=&quot;33925466&quot; target=&quot;_blank&quot; href=&quot;http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;list_uids=33925466&amp;dopt=Abstract&quot;&gt;
									PubMed
							&lt;/a&gt;
						&lt;/span&gt;
						&lt;span class=&quot;id identifier oa_NONE&quot; title=&quot;	Nincs
&quot;&gt;
							
							&lt;a style=&quot;color:blue&quot; title=&quot;https://www.scopus.com/pages/publications/85105782082?origin=resultslist&quot; target=&quot;_blank&quot; href=&quot;https://www.scopus.com/pages/publications/85105782082?origin=resultslist&quot;&gt;
									Egyéb URL
							&lt;/a&gt;
						&lt;/span&gt;
	&lt;/span&gt;


	&lt;OnlyViewableByAuthor&gt;&lt;div class=&quot;ratings&quot;&gt;
				&lt;div class=&quot;journal-subject&quot;&gt;Folyóirat szakterülete: Scopus - Biochemistry, Genetics and Molecular Biology (miscellaneous)&amp;nbsp;&amp;nbsp;&amp;nbsp;SJR indikátor:&amp;nbsp;Q2&lt;/div&gt;
				&lt;div class=&quot;journal-subject&quot;&gt;Folyóirat szakterülete: Scopus - Ecology, Evolution, Behavior and Systematics&amp;nbsp;&amp;nbsp;&amp;nbsp;SJR indikátor:&amp;nbsp;Q2&lt;/div&gt;
				&lt;div class=&quot;journal-subject&quot;&gt;Folyóirat szakterülete: Scopus - Paleontology&amp;nbsp;&amp;nbsp;&amp;nbsp;SJR indikátor:&amp;nbsp;Q2&lt;/div&gt;
				&lt;div class=&quot;journal-subject&quot;&gt;Folyóirat szakterülete: Scopus - Space and Planetary Science&amp;nbsp;&amp;nbsp;&amp;nbsp;SJR indikátor:&amp;nbsp;Q3&lt;/div&gt;
    &lt;/div&gt;&lt;/OnlyViewableByAuthor&gt;


	&lt;div class=&quot;publication-citation&quot; style=&quot;margin-left: 0.5cm;&quot;&gt;
		&lt;span title=&quot;Nyilvános idézőközlemények összesen, említések nélkül&quot; class=&quot;citingPub-count&quot;&gt;Nyilvános idéző összesen: 27&lt;/span&gt;
		| Független: 25
		| Függő: 2
		| Nem jelölt: 0
		| WoS jelölt: 24 
		|  Scopus jelölt:&amp;nbsp;26 
		|  WoS/Scopus jelölt:&amp;nbsp;27 
		|  DOI jelölt:&amp;nbsp;27 
		
	&lt;/div&gt;
    
    
	&lt;div class=&quot;publication-citation&quot;&gt;
		&lt;a target=&quot;_blank&quot; href=&quot;/api/publication?cond=citations.related;eq;32040119&amp;sort=publishedYear,desc&amp;sort=title&quot;&gt;
			Idézett közlemények száma: 11
		&lt;/a&gt;
	&lt;/div&gt;



    &lt;div class=&quot;mtid&quot;&gt;&lt;span class=&quot;long-pub-mtid&quot;&gt;Közlemény: 32040119&lt;/span&gt;
    | &lt;span class=&quot;status-data status-VALIDATED&quot;&gt; 	Egyeztetett
  &lt;/span&gt;
        
	
	
Forrás	 Idéző
	
	
    | &lt;span class=&quot;type-subtype&quot;&gt;Folyóiratcikk
			( Összefoglaló cikk
			
			)
		&lt;/span&gt;
      		| &lt;span class=&quot;pub-category&quot;&gt;Tudományos&lt;/span&gt;
	| &lt;span class=&quot;publication-sourceOfData&quot;&gt;Scopus&lt;/span&gt;
&lt;/div&gt;

&lt;div class=&quot;funder&quot;&gt; (LP2017-14/2017),    HCEMM(739593) Támogató: Horizon 2020   &lt;/div&gt;
&lt;div class=&quot;lastModified&quot;&gt;Utolsó módosítás: 2026.04.22. 09:12 Kajtár Virág Anna (SE_AOK_Biokemia_Admin5_KV, admin)
&lt;/div&gt;




	&lt;pre class=&quot;comment&quot; style=&quot;margin-top: 0; margin-bottom: 0;&quot;&gt;&lt;u&gt;Megjegyzés&lt;/u&gt;: Department of Medical Biochemistry, Semmelweis University, Budapest, 1085, Hungary            
            MTA-SE Lendület Ion Channel Research Group, Semmelweis University, Budapest, 1085, Hungary            
            HCEMM-SE Molecular Channelopathies Research Group, Semmelweis University, Budapest, 1085, Hungary            
            Cited By :2            
            Export Date: 9 Ma...&lt;/pre&gt;

&lt;/div&gt;&lt;/div&gt;</template2>
    </publication>
  </content>
</myciteResult>
