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      <references>
        <reference>
          <otype>Reference</otype>
          <mtid>69894893</mtid>
          <link>/api/reference/69894893</link>
          <label>1. Valentao 2020: Endoplasmic reticulum stress signaling in cancer and neurodegenerative disorders: Tools and strategies to understand its complexity., Pharmacol. Res., 155, p. 104702, DOI: 10.1016/j.phrs.2020.104702</label>
          <listPosition>1</listPosition>
          <doi>10.1016/j.phrs.2020.104702</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894894</mtid>
          <link>/api/reference/69894894</link>
          <label>2. Schwarz 2016: The endoplasmic reticulum: Structure, function and response to cellular signaling., Cell. Mol. Life Sci., 73, p. 79, DOI: 10.1007/s00018-015-2052-6</label>
          <listPosition>2</listPosition>
          <doi>10.1007/s00018-015-2052-6</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894895</mtid>
          <link>/api/reference/69894895</link>
          <label>3. Chen 2023: Endoplasmic reticulum stress: Molecular mechanism and therapeutic targets., Signal Transduct. Target. Ther., 8, p. 352, DOI: 10.1038/s41392-023-01570-w</label>
          <listPosition>3</listPosition>
          <doi>10.1038/s41392-023-01570-w</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894896</mtid>
          <link>/api/reference/69894896</link>
          <label>4. Gorlach 2006: The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control., Antioxid. Redox Signal., 8, p. 1391, DOI: 10.1089/ars.2006.8.1391</label>
          <listPosition>4</listPosition>
          <doi>10.1089/ars.2006.8.1391</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894897</mtid>
          <link>/api/reference/69894897</link>
          <label>5. Qi 2019: Endoplasmic Reticulum Stress and Autophagy., Adv. Exp. Med. Biol., 1206, p. 167, DOI: 10.1007/978-981-15-0602-4_8</label>
          <listPosition>5</listPosition>
          <doi>10.1007/978-981-15-0602-4_8</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894898</mtid>
          <link>/api/reference/69894898</link>
          <label>6. Ogata 2006: Autophagy is activated for cell survival after endoplasmic reticulum stress., Mol. Cell. Biol., 26, p. 9220, DOI: 10.1128/MCB.01453-06</label>
          <listPosition>6</listPosition>
          <doi>10.1128/MCB.01453-06</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894899</mtid>
          <link>/api/reference/69894899</link>
          <label>7. Tabas 2011: Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress., Nat. Cell Biol., 13, p. 184, DOI: 10.1038/ncb0311-184</label>
          <listPosition>7</listPosition>
          <doi>10.1038/ncb0311-184</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894900</mtid>
          <link>/api/reference/69894900</link>
          <label>8. Spencer 2020: The Role of Endoplasmic Reticulum Stress in Cell Survival and Death., J. Comp. Pathol., 181, p. 86, DOI: 10.1016/j.jcpa.2020.10.006</label>
          <listPosition>8</listPosition>
          <doi>10.1016/j.jcpa.2020.10.006</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894901</mtid>
          <link>/api/reference/69894901</link>
          <label>9. Jaattela 2007: Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium., Cell Death Differ., 14, p. 1576, DOI: 10.1038/sj.cdd.4402200</label>
          <listPosition>9</listPosition>
          <doi>10.1038/sj.cdd.4402200</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894902</mtid>
          <link>/api/reference/69894902</link>
          <label>10. Koksal 2021: Endoplasmic reticulum stress in biological processing and disease., J. Investig. Med., 69, p. 309, DOI: 10.1136/jim-2020-001570</label>
          <listPosition>10</listPosition>
          <doi>10.1136/jim-2020-001570</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894903</mtid>
          <link>/api/reference/69894903</link>
          <label>11. Kaneko 2017: ER Stress and Disease: Toward Prevention and Treatment., Biol. Pharm. Bull., 40, p. 1337, DOI: 10.1248/bpb.b17-00342</label>
          <listPosition>11</listPosition>
          <doi>10.1248/bpb.b17-00342</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894904</mtid>
          <link>/api/reference/69894904</link>
          <label>12. Wu 2018: Tunicamycin specifically aggravates ER stress and overcomes chemoresistance in multidrug-resistant gastric cancer cells by inhibiting N-glycosylation., J. Exp. Clin. Cancer Res., 37, p. 272, DOI: 10.1186/s13046-018-0935-8</label>
          <listPosition>12</listPosition>
          <doi>10.1186/s13046-018-0935-8</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894905</mtid>
          <link>/api/reference/69894905</link>
          <label>13. Yoo 2018: GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation., Nat. Struct. Mol. Biol., 25, p. 217, DOI: 10.1038/s41594-018-0031-y</label>
          <listPosition>13</listPosition>
          <doi>10.1038/s41594-018-0031-y</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894906</mtid>
          <link>/api/reference/69894906</link>
          <label>14. Andersen 2015: Thapsigargin–from Thapsia L. to mipsagargin., Molecules, 20, p. 6113, DOI: 10.3390/molecules20046113</label>
          <listPosition>14</listPosition>
          <doi>10.3390/molecules20046113</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894907</mtid>
          <link>/api/reference/69894907</link>
          <label>15. Oslowski 2011: Measuring ER stress and the unfolded protein response using mammalian tissue culture system., Methods Enzymol., 490, p. 71, DOI: 10.1016/B978-0-12-385114-7.00004-0</label>
          <listPosition>15</listPosition>
          <doi>10.1016/B978-0-12-385114-7.00004-0</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894908</mtid>
          <link>/api/reference/69894908</link>
          <label>16. Kapuy 2013: A cellular stress-directed bistable switch controls the crosstalk between autophagy and apoptosis., Mol. Biosyst., 9, p. 296, DOI: 10.1039/C2MB25261A</label>
          <listPosition>16</listPosition>
          <doi>10.1039/C2MB25261A</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894909</mtid>
          <link>/api/reference/69894909</link>
          <label>17. Yamamoto 1999: BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M., Mol. Cell. Biol., 19, p. 8469, DOI: 10.1128/MCB.19.12.8469</label>
          <listPosition>17</listPosition>
          <doi>10.1128/MCB.19.12.8469</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894910</mtid>
          <link>/api/reference/69894910</link>
          <label>18. Siddiqui 2015: The mystery of BCL2 family: Bcl-2 proteins and apoptosis: An update., Arch. Toxicol., 89, p. 289, DOI: 10.1007/s00204-014-1448-7</label>
          <listPosition>18</listPosition>
          <doi>10.1007/s00204-014-1448-7</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894911</mtid>
          <link>/api/reference/69894911</link>
          <label>19. Riedl 2004: Molecular mechanisms of caspase regulation during apoptosis., Nat. Rev. Mol. Cell Biol., 5, p. 897, DOI: 10.1038/nrm1496</label>
          <listPosition>19</listPosition>
          <doi>10.1038/nrm1496</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894912</mtid>
          <link>/api/reference/69894912</link>
          <label>20. Pattingre 2005: Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy., Cell, 122, p. 927, DOI: 10.1016/j.cell.2005.07.002</label>
          <listPosition>20</listPosition>
          <doi>10.1016/j.cell.2005.07.002</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894913</mtid>
          <link>/api/reference/69894913</link>
          <label>21. Lindqvist 2014: Prosurvival Bcl-2 family members affect autophagy only indirectly, by inhibiting Bax and Bak., Proc. Natl. Acad. Sci. USA, 111, p. 8512, DOI: 10.1073/pnas.1406425111</label>
          <listPosition>21</listPosition>
          <doi>10.1073/pnas.1406425111</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894914</mtid>
          <link>/api/reference/69894914</link>
          <label>22. Szegezdi 2006: Mediators of endoplasmic reticulum stress-induced apoptosis., EMBO Rep., 7, p. 880, DOI: 10.1038/sj.embor.7400779</label>
          <listPosition>22</listPosition>
          <doi>10.1038/sj.embor.7400779</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894915</mtid>
          <link>/api/reference/69894915</link>
          <label>23. Yang, B., Liu, Q., and Bi, Y. (2019). Autophagy and apoptosis are regulated by stress on Bcl2 by AMBRA1 in the endoplasmic reticulum and mitochondria. Theor. Biol. Med. Model., 16., DOI: 10.1186/s12976-019-0113-5</label>
          <listPosition>23</listPosition>
          <doi>10.1186/s12976-019-0113-5</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894916</mtid>
          <link>/api/reference/69894916</link>
          <label>24. Strappazzon 2011: Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy., EMBO J., 30, p. 1195, DOI: 10.1038/emboj.2011.49</label>
          <listPosition>24</listPosition>
          <doi>10.1038/emboj.2011.49</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894917</mtid>
          <link>/api/reference/69894917</link>
          <label>25. Fimia 2013: Ambra1 at the crossroad between autophagy and cell death., Oncogene, 32, p. 3311, DOI: 10.1038/onc.2012.455</label>
          <listPosition>25</listPosition>
          <doi>10.1038/onc.2012.455</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894918</mtid>
          <link>/api/reference/69894918</link>
          <label>26. Ma 2013: Interaction of Bcl-2 with the autophagy-related GABAA receptor-associated protein (GABARAP): Biophysical characterization and functional implications., J. Biol. Chem., 288, p. 37204, DOI: 10.1074/jbc.M113.528067</label>
          <listPosition>26</listPosition>
          <doi>10.1074/jbc.M113.528067</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894919</mtid>
          <link>/api/reference/69894919</link>
          <label>27. Siddiqui 2015: RNase L Cleavage Products Promote Switch from Autophagy to Apoptosis by Caspase-Mediated Cleavage of Beclin-1., Int. J. Mol. Sci., 16, p. 17611, DOI: 10.3390/ijms160817611</label>
          <listPosition>27</listPosition>
          <doi>10.3390/ijms160817611</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894920</mtid>
          <link>/api/reference/69894920</link>
          <label>28. Strappazzon 2016: Prosurvival AMBRA1 turns into a proapoptotic BH3-like protein during mitochondrial apoptosis., Autophagy, 12, p. 963, DOI: 10.1080/15548627.2016.1164359</label>
          <listPosition>28</listPosition>
          <doi>10.1080/15548627.2016.1164359</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894921</mtid>
          <link>/api/reference/69894921</link>
          <label>29. Gordy 2012: The crosstalk between autophagy and apoptosis: Where does this lead?., Protein Cell, 3, p. 17, DOI: 10.1007/s13238-011-1127-x</label>
          <listPosition>29</listPosition>
          <doi>10.1007/s13238-011-1127-x</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894922</mtid>
          <link>/api/reference/69894922</link>
          <label>30. Zhu 2010: Beclin 1 cleavage by caspase-3 inactivates autophagy and promotes apoptosis., Protein Cell, 1, p. 468, DOI: 10.1007/s13238-010-0048-4</label>
          <listPosition>30</listPosition>
          <doi>10.1007/s13238-010-0048-4</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894923</mtid>
          <link>/api/reference/69894923</link>
          <label>31. Kirsch 1999: Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c., J. Biol. Chem., 274, p. 21155, DOI: 10.1074/jbc.274.30.21155</label>
          <listPosition>31</listPosition>
          <doi>10.1074/jbc.274.30.21155</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894924</mtid>
          <link>/api/reference/69894924</link>
          <label>32. Zhu 2007: Bcl-2 cleavages at two adjacent sites by different caspases promote cisplatin-induced apoptosis., Cell Res., 17, p. 441, DOI: 10.1038/cr.2007.36</label>
          <listPosition>32</listPosition>
          <doi>10.1038/cr.2007.36</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894925</mtid>
          <link>/api/reference/69894925</link>
          <label>33. Banerjee, S., Ansari, A.A., Upadhyay, S.P., Mettman, D.J., Hibdon, J.R., Quadir, M., Ghosh, P., Kambhampati, A., and Banerjee, S.K. (2024). Benefits and Pitfalls of a Glycosylation Inhibitor Tunicamycin in the Therapeutic Implication of Cancers. Cells, 13., DOI: 10.20944/preprints202401.1900.v1</label>
          <listPosition>33</listPosition>
          <doi>10.20944/preprints202401.1900.v1</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894926</mtid>
          <link>/api/reference/69894926</link>
          <label>34. Wu 2020: The endoplasmic reticulum stress induced by tunicamycin affects the viability and autophagy activity of chondrocytes., J. Clin. Lab. Anal., 34, p. e23437, DOI: 10.1002/jcla.23437</label>
          <listPosition>34</listPosition>
          <doi>10.1002/jcla.23437</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894927</mtid>
          <link>/api/reference/69894927</link>
          <label>35. Holczer, M., Marton, M., Kurucz, A., Banhegyi, G., and Kapuy, O. (2015). A Comprehensive Systems Biological Study of Autophagy-Apoptosis Crosstalk during Endoplasmic Reticulum Stress. BioMed Res. Int., 2015., DOI: 10.1155/2015/319589</label>
          <listPosition>35</listPosition>
          <doi>10.1155/2015/319589</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894928</mtid>
          <link>/api/reference/69894928</link>
          <label>36. Bastholm 2007: Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2., Mol. Cell, 25, p. 193, DOI: 10.1016/j.molcel.2006.12.009</label>
          <listPosition>36</listPosition>
          <doi>10.1016/j.molcel.2006.12.009</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894929</mtid>
          <link>/api/reference/69894929</link>
          <label>37. Grotemeier 2010: AMPK-independent induction of autophagy by cytosolic Ca2+ increase., Cell Signal., 22, p. 914, DOI: 10.1016/j.cellsig.2010.01.015</label>
          <listPosition>37</listPosition>
          <doi>10.1016/j.cellsig.2010.01.015</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894930</mtid>
          <link>/api/reference/69894930</link>
          <label>38. Wang 2016: Thapsigargin induces apoptosis when autophagy is inhibited in HepG2 cells and both processes are regulated by ROS-dependent pathway., Environ. Toxicol. Pharmacol., 41, p. 167, DOI: 10.1016/j.etap.2015.11.020</label>
          <listPosition>38</listPosition>
          <doi>10.1016/j.etap.2015.11.020</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894931</mtid>
          <link>/api/reference/69894931</link>
          <label>39. Lindner 2020: Cell death induced by the ER stressor thapsigargin involves death receptor 5, a non-autophagic function of MAP1LC3B, and distinct contributions from unfolded protein response components., Cell Commun. Signal., 18, p. 12, DOI: 10.1186/s12964-019-0499-z</label>
          <listPosition>39</listPosition>
          <doi>10.1186/s12964-019-0499-z</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894932</mtid>
          <link>/api/reference/69894932</link>
          <label>40. Jaskulska, A., Janecka, A.E., and Gach-Janczak, K. (2020). Thapsigargin-From Traditional Medicine to Anticancer Drug. Int. J. Mol. Sci., 22., DOI: 10.3390/ijms22010004</label>
          <listPosition>40</listPosition>
          <doi>10.3390/ijms22010004</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894933</mtid>
          <link>/api/reference/69894933</link>
          <label>41. Holczer, M., Banhegyi, G., and Kapuy, O. (2016). GADD34 Keeps the mTOR Pathway Inactivated in Endoplasmic Reticulum Stress Related Autophagy. PLoS ONE, 11., DOI: 10.1371/journal.pone.0168359</label>
          <listPosition>41</listPosition>
          <doi>10.1371/journal.pone.0168359</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894934</mtid>
          <link>/api/reference/69894934</link>
          <label>42. Holczer, M., Besze, B., Lehel, A., and Kapuy, O. (2024). The Dual Role of Sulforaphane-Induced Cellular Stress-A Systems Biological Study. Int. J. Mol. Sci., 25., DOI: 10.3390/ijms25021220</label>
          <listPosition>42</listPosition>
          <doi>10.3390/ijms25021220</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894935</mtid>
          <link>/api/reference/69894935</link>
          <label>43. Holczer 2018: Epigallocatechin-3-Gallate (EGCG) Promotes Autophagy-Dependent Survival via Influencing the Balance of mTOR-AMPK Pathways upon Endoplasmic Reticulum Stress., Oxid. Med. Cell. Longev., 2018, p. 6721530, DOI: 10.1155/2018/6721530</label>
          <listPosition>43</listPosition>
          <doi>10.1155/2018/6721530</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894936</mtid>
          <link>/api/reference/69894936</link>
          <label>44. Sehgal 2017: Inhibition of the sarco/endoplasmic reticulum (ER) Ca2+-ATPase by thapsigargin analogs induces cell death via ER Ca2+ depletion and the unfolded protein response., J. Biol. Chem., 292, p. 19656, DOI: 10.1074/jbc.M117.796920</label>
          <listPosition>44</listPosition>
          <doi>10.1074/jbc.M117.796920</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894937</mtid>
          <link>/api/reference/69894937</link>
          <label>45. Lytton 1991: Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps., J. Biol. Chem., 266, p. 17067, DOI: 10.1016/S0021-9258(19)47340-7</label>
          <listPosition>45</listPosition>
          <doi>10.1016/S0021-9258(19)47340-7</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894938</mtid>
          <link>/api/reference/69894938</link>
          <label>46. Grabel 1983: Tunicamycin reversibly inhibits the terminal differentiation of teratocarcinoma stem cells to endoderm., Dev. Biol., 95, p. 115, DOI: 10.1016/0012-1606(83)90011-8</label>
          <listPosition>46</listPosition>
          <doi>10.1016/0012-1606(83)90011-8</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894939</mtid>
          <link>/api/reference/69894939</link>
          <label>47. Engedal 2013: Modulation of intracellular calcium homeostasis blocks autophagosome formation., Autophagy, 9, p. 1475, DOI: 10.4161/auto.25900</label>
          <listPosition>47</listPosition>
          <doi>10.4161/auto.25900</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894940</mtid>
          <link>/api/reference/69894940</link>
          <label>48. Ganley 2011: Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest., Mol. Cell, 42, p. 731, DOI: 10.1016/j.molcel.2011.04.024</label>
          <listPosition>48</listPosition>
          <doi>10.1016/j.molcel.2011.04.024</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894941</mtid>
          <link>/api/reference/69894941</link>
          <label>49. Dubois 2020: Co-targeting Mitochondrial Ca2+ Homeostasis and Autophagy Enhances Cancer Cells’ Chemosensitivity., iScience, 23, p. 101263, DOI: 10.1016/j.isci.2020.101263</label>
          <listPosition>49</listPosition>
          <doi>10.1016/j.isci.2020.101263</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894942</mtid>
          <link>/api/reference/69894942</link>
          <label>50. Williams 2008: Novel targets for Huntington’s disease in an mTOR-independent autophagy pathway., Nat. Chem. Biol., 4, p. 295, DOI: 10.1038/nchembio.79</label>
          <listPosition>50</listPosition>
          <doi>10.1038/nchembio.79</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894943</mtid>
          <link>/api/reference/69894943</link>
          <label>51. Gordon 1993: Dependence of hepatocytic autophagy on intracellularly sequestered calcium., J. Biol. Chem., 268, p. 26107, DOI: 10.1016/S0021-9258(19)74287-2</label>
          <listPosition>51</listPosition>
          <doi>10.1016/S0021-9258(19)74287-2</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894944</mtid>
          <link>/api/reference/69894944</link>
          <label>52. Mbara 2024: Endoplasmic reticulum stress in pancreatic beta-cell dysfunction: The potential therapeutic role of dietary flavonoids., Curr. Res. Pharmacol. Drug Discov., 6, p. 100184, DOI: 10.1016/j.crphar.2024.100184</label>
          <listPosition>52</listPosition>
          <doi>10.1016/j.crphar.2024.100184</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894945</mtid>
          <link>/api/reference/69894945</link>
          <label>53. Nizami 2024: Phytochemical-mediated modulation of autophagy and endoplasmic reticulum stress as a cancer therapeutic approach., Phytother. Res., 38, p. 4353, DOI: 10.1002/ptr.8283</label>
          <listPosition>53</listPosition>
          <doi>10.1002/ptr.8283</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894946</mtid>
          <link>/api/reference/69894946</link>
          <label>54. Hajimohammadi 2024: Exploring the therapeutic effects of sulforaphane: An in-depth review on endoplasmic reticulum stress modulation across different disease contexts., Inflammopharmacology, 32, p. 2185, DOI: 10.1007/s10787-024-01506-y</label>
          <listPosition>54</listPosition>
          <doi>10.1007/s10787-024-01506-y</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894947</mtid>
          <link>/api/reference/69894947</link>
          <label>55. Mansour 2022: Modulation of endoplasmic reticulum stress via sulforaphane-mediated AMPK upregulation against nonalcoholic fatty liver disease in rats., Cell Stress Chaperones, 27, p. 499, DOI: 10.1007/s12192-022-01286-w</label>
          <listPosition>55</listPosition>
          <doi>10.1007/s12192-022-01286-w</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894948</mtid>
          <link>/api/reference/69894948</link>
          <label>56. Dana 2022: Role of sulforaphane in endoplasmic reticulum homeostasis through regulation of the antioxidant response., Life Sci., 299, p. 120554, DOI: 10.1016/j.lfs.2022.120554</label>
          <listPosition>56</listPosition>
          <doi>10.1016/j.lfs.2022.120554</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894949</mtid>
          <link>/api/reference/69894949</link>
          <label>57. Ding, S., Jiang, J., Zhang, G., Bu, Y., Zhang, G., and Zhao, X. (2017). Resveratrol and caloric restriction prevent hepatic steatosis by regulating SIRT1-autophagy pathway and alleviating endoplasmic reticulum stress in high-fat diet-fed rats. PLoS ONE, 12., DOI: 10.1371/journal.pone.0183541</label>
          <listPosition>57</listPosition>
          <doi>10.1371/journal.pone.0183541</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894950</mtid>
          <link>/api/reference/69894950</link>
          <label>58. Gowd 2020: Resveratrol: Evidence for Its Nephroprotective Effect in Diabetic Nephropathy., Adv. Nutr., 11, p. 1555, DOI: 10.1093/advances/nmaa075</label>
          <listPosition>58</listPosition>
          <doi>10.1093/advances/nmaa075</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894951</mtid>
          <link>/api/reference/69894951</link>
          <label>59. Yuan 2018: Protective effect of resveratrol on kidney in rats with diabetic nephropathy and its effect on endoplasmic reticulum stress., Eur. Rev. Med. Pharmacol. Sci., 22, p. 1485</label>
          <listPosition>59</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894952</mtid>
          <link>/api/reference/69894952</link>
          <label>60. Xiang 2016: Inhibition of autophagic flux by ROS promotes apoptosis during DTT-induced ER/oxidative stress in HeLa cells., Oncol. Rep., 35, p. 3471, DOI: 10.3892/or.2016.4725</label>
          <listPosition>60</listPosition>
          <doi>10.3892/or.2016.4725</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894953</mtid>
          <link>/api/reference/69894953</link>
          <label>61. Tsai 2010: Synergistic cytotoxic effects of arsenic trioxide plus dithiothreitol on mice oral cancer cells., Anticancer Res., 30, p. 3655</label>
          <listPosition>61</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894954</mtid>
          <link>/api/reference/69894954</link>
          <label>62. Khurram 2024: Thapsigargin and its prodrug derivatives: Exploring novel approaches for targeted cancer therapy through calcium signaling disruption., Med. Oncol., 42, p. 7, DOI: 10.1007/s12032-024-02541-z</label>
          <listPosition>62</listPosition>
          <doi>10.1007/s12032-024-02541-z</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894955</mtid>
          <link>/api/reference/69894955</link>
          <label>63. Suresh 2024: Thapsigargin: A promising natural product with diverse medicinal potential - a review of synthetic approaches and total syntheses., Org. Biomol. Chem., 22, p. 8551, DOI: 10.1039/D4OB01239A</label>
          <listPosition>63</listPosition>
          <doi>10.1039/D4OB01239A</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894956</mtid>
          <link>/api/reference/69894956</link>
          <label>64. Christensen 2021: From Plant to Patient: Thapsigargin, a Tool for Understanding Natural Product Chemistry, Total Syntheses, Biosynthesis, Taxonomy, ATPases, Cell Death, and Drug Development., Prog. Chem. Org. Nat. Prod., 115, p. 59</label>
          <listPosition>64</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894957</mtid>
          <link>/api/reference/69894957</link>
          <label>65. Tyson 2003: Sniffers, buzzers, toggles and blinkers: Dynamics of regulatory and signaling pathways in the cell., Curr. Opin. Cell Biol., 15, p. 221, DOI: 10.1016/S0955-0674(03)00017-6</label>
          <listPosition>65</listPosition>
          <doi>10.1016/S0955-0674(03)00017-6</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894958</mtid>
          <link>/api/reference/69894958</link>
          <label>66. Tyson 2002: The dynamics of cell cycle regulation., BioEssays, 24, p. 1095, DOI: 10.1002/bies.10191</label>
          <listPosition>66</listPosition>
          <doi>10.1002/bies.10191</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894959</mtid>
          <link>/api/reference/69894959</link>
          <label>67. Ferrell 1996: Tripping the switch fantastic: How a protein kinase cascade can convert graded inputs into switch-like outputs., Trends Biochem. Sci., 21, p. 460, DOI: 10.1016/S0968-0004(96)20026-X</label>
          <listPosition>67</listPosition>
          <doi>10.1016/S0968-0004(96)20026-X</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894960</mtid>
          <link>/api/reference/69894960</link>
          <label>68. Kapuy 2009: Bistability by multiple phosphorylation of regulatory proteins., Prog. Biophys. Mol. Biol., 100, p. 47, DOI: 10.1016/j.pbiomolbio.2009.06.004</label>
          <listPosition>68</listPosition>
          <doi>10.1016/j.pbiomolbio.2009.06.004</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894961</mtid>
          <link>/api/reference/69894961</link>
          <label>69. Bassik 2004: Phosphorylation of BCL-2 regulates ER Ca2+ homeostasis and apoptosis., EMBO J., 23, p. 1207, DOI: 10.1038/sj.emboj.7600104</label>
          <listPosition>69</listPosition>
          <doi>10.1038/sj.emboj.7600104</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894962</mtid>
          <link>/api/reference/69894962</link>
          <label>70. Bhatt 2008: Effects of targeted Bcl-2 expression in mitochondria or endoplasmic reticulum on renal tubular cell apoptosis., Am. J. Physiol. Renal Physiol., 294, p. F499, DOI: 10.1152/ajprenal.00415.2007</label>
          <listPosition>70</listPosition>
          <doi>10.1152/ajprenal.00415.2007</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894963</mtid>
          <link>/api/reference/69894963</link>
          <label>71. Brahmbhatt 2015: Molecular Pathways: Leveraging the BCL-2 Interactome to Kill Cancer Cells–Mitochondrial Outer Membrane Permeabilization and Beyond., Clin. Cancer Res., 21, p. 2671, DOI: 10.1158/1078-0432.CCR-14-0959</label>
          <listPosition>71</listPosition>
          <doi>10.1158/1078-0432.CCR-14-0959</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894964</mtid>
          <link>/api/reference/69894964</link>
          <label>72. Chandrika, B.B., Yang, C., Ou, Y., Feng, X., Muhoza, D., Holmes, A.F., Theus, S., Deshmukh, S., Haun, R.S., and Kaushal, G.P. (2015). Endoplasmic Reticulum Stress-Induced Autophagy Provides Cytoprotection from Chemical Hypoxia and Oxidant Injury and Ameliorates Renal Ischemia-Reperfusion Injury. PLoS ONE, 10., DOI: 10.1371/journal.pone.0140025</label>
          <listPosition>72</listPosition>
          <doi>10.1371/journal.pone.0140025</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894965</mtid>
          <link>/api/reference/69894965</link>
          <label>73. Chang 2010: Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1., EMBO J., 29, p. 606, DOI: 10.1038/emboj.2009.369</label>
          <listPosition>73</listPosition>
          <doi>10.1038/emboj.2009.369</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894966</mtid>
          <link>/api/reference/69894966</link>
          <label>74. Ciechomska 2009: Bcl-2 complexed with Beclin-1 maintains full anti-apoptotic function., Oncogene, 28, p. 2128, DOI: 10.1038/onc.2009.60</label>
          <listPosition>74</listPosition>
          <doi>10.1038/onc.2009.60</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894967</mtid>
          <link>/api/reference/69894967</link>
          <label>75. Kroemer 2010: Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1., Oncogene, 29, p. 1717, DOI: 10.1038/onc.2009.519</label>
          <listPosition>75</listPosition>
          <doi>10.1038/onc.2009.519</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894968</mtid>
          <link>/api/reference/69894968</link>
          <label>76. G 2022: Dithiothreitol causes toxicity in C. elegans by modulating the methionine-homocysteine cycle., eLife, 11, p. e76021, DOI: 10.7554/eLife.76021</label>
          <listPosition>76</listPosition>
          <doi>10.7554/eLife.76021</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894969</mtid>
          <link>/api/reference/69894969</link>
          <label>77. Gross 2017: Non-apoptotic functions of BCL-2 family proteins., Cell Death Differ., 24, p. 1348, DOI: 10.1038/cdd.2017.22</label>
          <listPosition>77</listPosition>
          <doi>10.1038/cdd.2017.22</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894970</mtid>
          <link>/api/reference/69894970</link>
          <label>78. Guha 2017: Tunicamycin induced endoplasmic reticulum stress promotes apoptosis of prostate cancer cells by activating mTORC1., Oncotarget, 8, p. 68191, DOI: 10.18632/oncotarget.19277</label>
          <listPosition>78</listPosition>
          <doi>10.18632/oncotarget.19277</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894971</mtid>
          <link>/api/reference/69894971</link>
          <label>79. Hacki 2000: Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2., Oncogene, 19, p. 2286, DOI: 10.1038/sj.onc.1203592</label>
          <listPosition>79</listPosition>
          <doi>10.1038/sj.onc.1203592</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894972</mtid>
          <link>/api/reference/69894972</link>
          <label>80. Chang 2008: The endoplasmic reticulum in apoptosis and autophagy: Role of the BCL-2 protein family., Oncogene, 27, p. 6419, DOI: 10.1038/onc.2008.309</label>
          <listPosition>80</listPosition>
          <doi>10.1038/onc.2008.309</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894973</mtid>
          <link>/api/reference/69894973</link>
          <label>81. Held 1987: Toxicity of the sulfhydryl-containing radioprotector dithiothreitol., Radiat Res., 112, p. 544, DOI: 10.2307/3577106</label>
          <listPosition>81</listPosition>
          <doi>10.2307/3577106</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894974</mtid>
          <link>/api/reference/69894974</link>
          <label>82. Held 1996: Role of Fenton chemistry in thiol-induced toxicity and apoptosis., Radiat. Res., 145, p. 542, DOI: 10.2307/3579272</label>
          <listPosition>82</listPosition>
          <doi>10.2307/3579272</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894975</mtid>
          <link>/api/reference/69894975</link>
          <label>83. Hou 2010: Autophagic degradation of active caspase-8: A crosstalk mechanism between autophagy and apoptosis., Autophagy, 6, p. 891, DOI: 10.4161/auto.6.7.13038</label>
          <listPosition>83</listPosition>
          <doi>10.4161/auto.6.7.13038</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894976</mtid>
          <link>/api/reference/69894976</link>
          <label>84. Huang 2014: Beclin 1, an autophagy-related gene, augments apoptosis in U87 glioblastoma cells., Oncol. Rep., 31, p. 1761, DOI: 10.3892/or.2014.3015</label>
          <listPosition>84</listPosition>
          <doi>10.3892/or.2014.3015</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894977</mtid>
          <link>/api/reference/69894977</link>
          <label>85. Kang 2011: The Beclin 1 network regulates autophagy and apoptosis., Cell Death Differ., 18, p. 571, DOI: 10.1038/cdd.2010.191</label>
          <listPosition>85</listPosition>
          <doi>10.1038/cdd.2010.191</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894978</mtid>
          <link>/api/reference/69894978</link>
          <label>86. Kania, E., Pajak, B., and Orzechowski, A. (2015). Calcium homeostasis and ER stress in control of autophagy in cancer cells. BioMed Res. Int., 2015., DOI: 10.1155/2015/352794</label>
          <listPosition>86</listPosition>
          <doi>10.1155/2015/352794</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894979</mtid>
          <link>/api/reference/69894979</link>
          <label>87. Byndloss 2016: NOD1 and NOD2 signalling links ER stress with inflammation., Nature, 532, p. 394, DOI: 10.1038/nature17631</label>
          <listPosition>87</listPosition>
          <doi>10.1038/nature17631</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894980</mtid>
          <link>/api/reference/69894980</link>
          <label>88. Lam 2018: Confirming a critical role for death receptor 5 and caspase-8 in apoptosis induction by endoplasmic reticulum stress., Cell Death Differ., 25, p. 1530, DOI: 10.1038/s41418-018-0155-y</label>
          <listPosition>88</listPosition>
          <doi>10.1038/s41418-018-0155-y</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894981</mtid>
          <link>/api/reference/69894981</link>
          <label>89. Lee 2005: GABAA receptor-associated protein (GABARAP) induces apoptosis by interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47)., Biotechnol. Lett., 27, p. 623, DOI: 10.1007/s10529-005-3628-2</label>
          <listPosition>89</listPosition>
          <doi>10.1007/s10529-005-3628-2</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894982</mtid>
          <link>/api/reference/69894982</link>
          <label>90. Lei 2003: JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis., Proc. Natl. Acad. Sci. USA, 100, p. 2432, DOI: 10.1073/pnas.0438011100</label>
          <listPosition>90</listPosition>
          <doi>10.1073/pnas.0438011100</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894983</mtid>
          <link>/api/reference/69894983</link>
          <label>91. Li 2016: Caspase-mediated cleavage of Beclin1 inhibits autophagy and promotes apoptosis induced by S1 in human ovarian cancer SKOV3 cells., Apoptosis, 21, p. 225, DOI: 10.1007/s10495-015-1197-y</label>
          <listPosition>91</listPosition>
          <doi>10.1007/s10495-015-1197-y</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894984</mtid>
          <link>/api/reference/69894984</link>
          <label>92. Lu 2014: Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis., Science, 345, p. 98, DOI: 10.1126/science.1254312</label>
          <listPosition>92</listPosition>
          <doi>10.1126/science.1254312</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894985</mtid>
          <link>/api/reference/69894985</link>
          <label>93. Luhr 2019: The kinase PERK and the transcription factor ATF4 play distinct and essential roles in autophagy resulting from tunicamycin-induced ER stress., J. Biol. Chem., 294, p. 8197, DOI: 10.1074/jbc.RA118.002829</label>
          <listPosition>93</listPosition>
          <doi>10.1074/jbc.RA118.002829</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894986</mtid>
          <link>/api/reference/69894986</link>
          <label>94. Luo 2013: The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies., Oncogene, 32, p. 805, DOI: 10.1038/onc.2012.130</label>
          <listPosition>94</listPosition>
          <doi>10.1038/onc.2012.130</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894987</mtid>
          <link>/api/reference/69894987</link>
          <label>95. Luo 2010: Apoptosis blocks Beclin 1-dependent autophagosome synthesis: An effect rescued by Bcl-xL., Cell Death Differ., 17, p. 268, DOI: 10.1038/cdd.2009.121</label>
          <listPosition>95</listPosition>
          <doi>10.1038/cdd.2009.121</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894988</mtid>
          <link>/api/reference/69894988</link>
          <label>96. Ma, Z., Fan, C., Yang, Y., Di, S., Hu, W., Li, T., Zhu, Y., Han, J., Xin, Z., and Wu, G. (2016). Thapsigargin sensitizes human esophageal cancer to TRAIL-induced apoptosis via AMPK activation. Sci. Rep., 6., DOI: 10.1038/srep35196</label>
          <listPosition>96</listPosition>
          <doi>10.1038/srep35196</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894989</mtid>
          <link>/api/reference/69894989</link>
          <label>97. Maiuri 2007: Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1., EMBO J., 26, p. 2527, DOI: 10.1038/sj.emboj.7601689</label>
          <listPosition>97</listPosition>
          <doi>10.1038/sj.emboj.7601689</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894990</mtid>
          <link>/api/reference/69894990</link>
          <label>98. Marquez 2012: Bcl-2:Beclin 1 complex: Multiple, mechanisms regulating autophagy/apoptosis toggle switch., Am. J. Cancer Res., 2, p. 214</label>
          <listPosition>98</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894991</mtid>
          <link>/api/reference/69894991</link>
          <label>99. McCullough 2001: Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state., Mol. Cell Biol., 21, p. 1249, DOI: 10.1128/MCB.21.4.1249-1259.2001</label>
          <listPosition>99</listPosition>
          <doi>10.1128/MCB.21.4.1249-1259.2001</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894992</mtid>
          <link>/api/reference/69894992</link>
          <label>100. 2018: A role for caspase-8 and TRAIL-R2/DR5 in ER-stress-induced apoptosis., Cell Death Differ., 25, p. 226, DOI: 10.1038/cdd.2017.155</label>
          <listPosition>100</listPosition>
          <doi>10.1038/cdd.2017.155</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894993</mtid>
          <link>/api/reference/69894993</link>
          <label>101. Oakes 2006: The control of endoplasmic reticulum-initiated apoptosis by the BCL-2 family of proteins., Curr. Mol. Med., 6, p. 99, DOI: 10.2174/156652406775574587</label>
          <listPosition>101</listPosition>
          <doi>10.2174/156652406775574587</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894994</mtid>
          <link>/api/reference/69894994</link>
          <label>102. Pihan 2017: BCL-2 family: Integrating stress responses at the ER to control cell demise., Cell Death Differ., 24, p. 1478, DOI: 10.1038/cdd.2017.82</label>
          <listPosition>102</listPosition>
          <doi>10.1038/cdd.2017.82</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894995</mtid>
          <link>/api/reference/69894995</link>
          <label>103. Puthalakath 2007: ER stress triggers apoptosis by activating BH3-only protein Bim., Cell, 129, p. 1337, DOI: 10.1016/j.cell.2007.04.027</label>
          <listPosition>103</listPosition>
          <doi>10.1016/j.cell.2007.04.027</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894996</mtid>
          <link>/api/reference/69894996</link>
          <label>104. Rashid 2015: ER stress: Autophagy induction, inhibition and selection., Autophagy, 11, p. 1956, DOI: 10.1080/15548627.2015.1091141</label>
          <listPosition>104</listPosition>
          <doi>10.1080/15548627.2015.1091141</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894997</mtid>
          <link>/api/reference/69894997</link>
          <label>105. Ravi 2023: Thiol reductive stress activates the hypoxia response pathway., EMBO J., 42, p. e114093, DOI: 10.15252/embj.2023114093</label>
          <listPosition>105</listPosition>
          <doi>10.15252/embj.2023114093</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894998</mtid>
          <link>/api/reference/69894998</link>
          <label>106. Rodriguez 2011: Integrating stress signals at the endoplasmic reticulum: The BCL-2 protein family rheostat., Biochim. Biophys. Acta Mol. Cell Res., 1813, p. 564, DOI: 10.1016/j.bbamcr.2010.11.012</label>
          <listPosition>106</listPosition>
          <doi>10.1016/j.bbamcr.2010.11.012</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69894999</mtid>
          <link>/api/reference/69894999</link>
          <label>107. Rong 2009: The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor., Proc. Natl. Acad. Sci. USA, 106, p. 14397, DOI: 10.1073/pnas.0907555106</label>
          <listPosition>107</listPosition>
          <doi>10.1073/pnas.0907555106</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895000</mtid>
          <link>/api/reference/69895000</link>
          <label>108. Sakaki 2008: Protein kinase Ctheta is required for autophagy in response to stress in the endoplasmic reticulum., J. Biol. Chem., 283, p. 15370, DOI: 10.1074/jbc.M710209200</label>
          <listPosition>108</listPosition>
          <doi>10.1074/jbc.M710209200</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895001</mtid>
          <link>/api/reference/69895001</link>
          <label>109. Sano 2013: ER stress-induced cell death mechanisms., Biochim. Biophys. Acta Mol. Cell Res., 1833, p. 3460, DOI: 10.1016/j.bbamcr.2013.06.028</label>
          <listPosition>109</listPosition>
          <doi>10.1016/j.bbamcr.2013.06.028</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895002</mtid>
          <link>/api/reference/69895002</link>
          <label>110. Sramek, J., Nemcova-Furstova, V., and Kovar, J. (2021). Molecular Mechanisms of Apoptosis Induction and Its Regulation by Fatty Acids in Pancreatic beta-Cells. Int. J. Mol. Sci., 22., DOI: 10.3390/ijms22084285</label>
          <listPosition>110</listPosition>
          <doi>10.3390/ijms22084285</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895003</mtid>
          <link>/api/reference/69895003</link>
          <label>111. Szegezdi 2009: Bcl-2 family on guard at the ER., Am. J. Physiol. Cell Physiol., 296, p. C941, DOI: 10.1152/ajpcell.00612.2008</label>
          <listPosition>111</listPosition>
          <doi>10.1152/ajpcell.00612.2008</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895004</mtid>
          <link>/api/reference/69895004</link>
          <label>112. Tartier 2000: Apoptosis induced by dithiothreitol in HL-60 cells shows early activation of caspase 3 and is independent of mitochondria., Cell Death Differ., 7, p. 1002, DOI: 10.1038/sj.cdd.4400726</label>
          <listPosition>112</listPosition>
          <doi>10.1038/sj.cdd.4400726</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895005</mtid>
          <link>/api/reference/69895005</link>
          <label>113. Vicencio 2009: The inositol 1,4,5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1., Cell Death Differ., 16, p. 1006, DOI: 10.1038/cdd.2009.34</label>
          <listPosition>113</listPosition>
          <doi>10.1038/cdd.2009.34</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895006</mtid>
          <link>/api/reference/69895006</link>
          <label>114. Wang 2020: Tunicamycin induces ER stress and inhibits tumorigenesis of head and neck cancer cells by inhibiting N-glycosylation., Am. J. Transl. Res., 12, p. 541</label>
          <listPosition>114</listPosition>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895007</mtid>
          <link>/api/reference/69895007</link>
          <label>115. Wei 2008: JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy., Mol. Cell, 30, p. 678, DOI: 10.1016/j.molcel.2008.06.001</label>
          <listPosition>115</listPosition>
          <doi>10.1016/j.molcel.2008.06.001</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895008</mtid>
          <link>/api/reference/69895008</link>
          <label>116. Wirawan 2010: Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria., Cell Death Dis., 1, p. e18, DOI: 10.1038/cddis.2009.16</label>
          <listPosition>116</listPosition>
          <doi>10.1038/cddis.2009.16</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895009</mtid>
          <link>/api/reference/69895009</link>
          <label>117. Yamaguchi 2004: CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells., J. Biol. Chem., 279, p. 45495, DOI: 10.1074/jbc.M406933200</label>
          <listPosition>117</listPosition>
          <doi>10.1074/jbc.M406933200</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895010</mtid>
          <link>/api/reference/69895010</link>
          <label>118. Yang 2016: Activation of autophagy by unfolded proteins during endoplasmic reticulum stress., Plant J., 85, p. 83, DOI: 10.1111/tpj.13091</label>
          <listPosition>118</listPosition>
          <doi>10.1111/tpj.13091</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895011</mtid>
          <link>/api/reference/69895011</link>
          <label>119. Yorimitsu 2006: Endoplasmic reticulum stress triggers autophagy., J. Biol. Chem., 281, p. 30299, DOI: 10.1074/jbc.M607007200</label>
          <listPosition>119</listPosition>
          <doi>10.1074/jbc.M607007200</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
        <reference>
          <otype>Reference</otype>
          <mtid>69895012</mtid>
          <link>/api/reference/69895012</link>
          <label>120. Zong 2003: Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis., J. Cell Biol., 162, p. 59, DOI: 10.1083/jcb.200302084</label>
          <listPosition>120</listPosition>
          <doi>10.1083/jcb.200302084</doi>
          <published>false</published>
          <snippet>true</snippet>
        </reference>
      </references>
      <link>/api/publication/36435938</link>
      <label>Holczer Marianna et al. Fine-Tuning of the Endoplasmic Reticulum Stress Response Mechanism Plays a Key Role in Cellular Survival—A Mathematical Study. (2025) INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 1661-6596 1422-0067 26 22</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;10057448&quot;&gt; &lt;a href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10057448&quot; target=&quot;_blank&quot;&gt;Holczer, Marianna&lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;author-type&quot;&gt; &lt;/span&gt; ; &lt;span class=&quot;author-name&quot; mtid=&quot;10057447&quot;&gt; &lt;a href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10057447&quot; target=&quot;_blank&quot;&gt;Márton, Margita&lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;author-type&quot;&gt; &lt;/span&gt; ; &lt;span class=&quot;author-name&quot; mtid=&quot;10026775&quot;&gt; &lt;a href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10026775&quot; target=&quot;_blank&quot;&gt;Stiller, Ibolya&lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;author-type&quot;&gt; &lt;/span&gt; ; &lt;span class=&quot;author-name&quot; mtid=&quot;10026029&quot;&gt; &lt;a href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10026029&quot; target=&quot;_blank&quot;&gt;Lizák, Beáta&lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;author-type&quot;&gt; &lt;/span&gt; ; &lt;span class=&quot;author-name&quot; mtid=&quot;10011674&quot;&gt; &lt;a href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10011674&quot; target=&quot;_blank&quot;&gt;Bánhegyi, Gábor&lt;/a&gt; &lt;/span&gt; &lt;span class=&quot;author-type&quot;&gt; &lt;/span&gt; ; &lt;span class=&quot;author-name&quot; mtid=&quot;10026330&quot;&gt; &lt;a href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10026330&quot; target=&quot;_blank&quot;&gt;Kapuy, Orsolya ✉&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;36435938&quot; mtid=&quot;36435938&quot; target=&quot;_blank&quot;&gt;Fine-Tuning of the Endoplasmic Reticulum Stress Response Mechanism Plays a Key Role in Cellular Survival—A Mathematical Study&lt;/a&gt;&lt;/div&gt; &lt;div class=&quot;pub-info&quot;&gt; &lt;span class=&quot;journal-title&quot;&gt;INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES&lt;/span&gt; &lt;span class=&quot;journal-volume&quot;&gt;26&lt;/span&gt; : &lt;span class=&quot;journal-issue&quot;&gt;22&lt;/span&gt; &lt;span class=&quot;page&quot;&gt; Paper: 10961 , 19 p. &lt;/span&gt; &lt;span class=&quot;year&quot;&gt;(2025)&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_none&quot; title=&quot;none&quot;&gt; &lt;a style=&quot;color:blue&quot; title=&quot;10.3390/ijms262210961&quot; target=&quot;_blank&quot; href=&quot;https://doi.org/10.3390/ijms262210961&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;001623852500001&quot; target=&quot;_blank&quot; href=&quot;https://www.webofscience.com/wos/woscc/full-record/001623852500001&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;105023176395&quot; target=&quot;_blank&quot; href=&quot;http://www.scopus.com/record/display.url?origin=inward&amp;eid=2-s2.0-105023176395&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;41303444&quot; target=&quot;_blank&quot; href=&quot;http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;list_uids=41303444&amp;dopt=Abstract&quot;&gt; PubMed &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:36435938 &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 (Szakcikk ) &lt;/span&gt; &lt;!-- &amp;&amp; !record.category.scientific --&gt; &lt;span class=&quot;pub-category&quot;&gt;Tudományos&lt;/span&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;10057448&quot;&gt;&lt;a 
																				   href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10057448&quot; target=&quot;_blank&quot;&gt;Holczer Marianna
            (&lt;span class=&quot;authorship-author-name&quot;&gt;Holczer Marianna&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;/Molekuláris Biológiai Tanszék&lt;/span&gt;
;&amp;nbsp;&amp;nbsp;&amp;nbsp;
							&lt;span class=&quot;author-name&quot; mtid=&quot;10057447&quot;&gt;&lt;a 
																				   href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10057447&quot; target=&quot;_blank&quot;&gt;Márton Margita
            (&lt;span class=&quot;authorship-author-name&quot;&gt;Márton Margita&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;/Molekuláris Biológiai Tanszék&lt;/span&gt;
;&amp;nbsp;&amp;nbsp;&amp;nbsp;
							&lt;span class=&quot;author-name&quot; mtid=&quot;10026775&quot;&gt;&lt;a 
																				   href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10026775&quot; target=&quot;_blank&quot;&gt;Stiller Ibolya
            (&lt;span class=&quot;authorship-author-name&quot;&gt;Stiller Ibolya&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;/Molekuláris Biológiai Tanszék&lt;/span&gt;
;&amp;nbsp;&amp;nbsp;&amp;nbsp;
							&lt;span class=&quot;author-name&quot; mtid=&quot;10026029&quot;&gt;&lt;a 
																				   href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10026029&quot; target=&quot;_blank&quot;&gt;Lizák Beáta
            (&lt;span class=&quot;authorship-author-name&quot;&gt;Lizák Beáta&lt;/span&gt;
            &lt;span class=&quot;authorAux-mtmt&quot;&gt; biokémia, molekuláris biológia&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;/Molekuláris Biológiai Tanszék&lt;/span&gt;
;&amp;nbsp;&amp;nbsp;&amp;nbsp;
							&lt;span class=&quot;author-name&quot; mtid=&quot;10011674&quot;&gt;&lt;a 
																				   href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10011674&quot; target=&quot;_blank&quot;&gt;Bánhegyi Gábor
            (&lt;span class=&quot;authorship-author-name&quot;&gt;Bánhegyi Gábor&lt;/span&gt;
            &lt;span class=&quot;authorAux-mtmt&quot;&gt; Biokémia, molekuláris biológia&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;/Molekuláris Biológiai Tanszék&lt;/span&gt;
;&amp;nbsp;&amp;nbsp;&amp;nbsp;
							&lt;span class=&quot;author-name&quot; mtid=&quot;10026330&quot;&gt;&lt;a 
																				   href=&quot;/gui2/?type=authors&amp;mode=browse&amp;sel=10026330&quot; target=&quot;_blank&quot;&gt;Kapuy Orsolya ✉
            (&lt;span class=&quot;authorship-author-name&quot;&gt;Kapuy Orsolya&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;/Molekuláris Biológiai Tanszék&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;36435938&quot; target=&quot;_blank&quot;&gt;Fine-Tuning of the Endoplasmic Reticulum Stress Response Mechanism Plays a Key Role in Cellular Survival—A Mathematical Study&lt;/a&gt;&lt;/div&gt;    &lt;div&gt;		&lt;span class=&quot;journal-title&quot;&gt;INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES&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/1661-6596&quot;&gt;1661-6596&lt;/a&gt; &lt;a target=&quot;_blank&quot; href=&quot;https://portal.issn.org/resource/ISSN/1422-0067&quot;&gt;1422-0067&lt;/a&gt;)&lt;/span&gt;:
		&lt;span class=&quot;journal-volume&quot;&gt;26&lt;/span&gt; &lt;span class=&quot;journal-issue&quot;&gt;22&lt;/span&gt;
&lt;span class=&quot;page&quot;&gt;
		Paper 10961.
	 19 p. 
&lt;/span&gt;		 &lt;span class=&quot;year&quot;&gt;(2025)&lt;/span&gt;  
    &lt;/div&gt;
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									DOI
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			Idézett közlemények száma: 8
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    &lt;div class=&quot;mtid&quot;&gt;&lt;span class=&quot;long-pub-mtid&quot;&gt;Közlemény: 36435938&lt;/span&gt;
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      		| &lt;span class=&quot;pub-category&quot;&gt;Tudományos&lt;/span&gt;
	| &lt;span class=&quot;publication-sourceOfData&quot;&gt;DOI XML&lt;/span&gt;
&lt;/div&gt;

&lt;div class=&quot;funder&quot;&gt; (FK-134267),    (FK-143205)   &lt;/div&gt;
&lt;div class=&quot;lastModified&quot;&gt;Utolsó módosítás: 2026.04.20. 09:20 Sonnevend Kinga (SE_AOK_OrvVegytan_Admin5_SK, 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;: Funding Agency and Grant Number: National Research, Development and Innovation Office, Hungary [NKFIH FK-134267, FK-143205]
            Funding text: This work was supported by NKFIH FK-134267 and FK-143205 (National Research, Development and Innovation Office, Hungary).&lt;/pre&gt;
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