TY - JOUR AU - Kodirov, Sodikdjon A. TI - Adam, amigo, brain, and K channel JF - BIOPHYSICAL REVIEWS J2 - BIOPHYSICAL REVIEWS PY - 2023 PG - 32 SN - 1867-2450 DO - 10.1007/s12551-023-01163-5 UR - https://m2.mtmt.hu/api/publication/34360373 ID - 34360373 AB - Voltage-dependent K+ (Kv) channels are diverse, comprising the classical Shab - Kv2, Shaker - Kv1, Shal - Kv4, and Shaw - Kv3 families. The Shaker family alone consists of Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6, and Kv1.7. Moreover, the Shab family comprises two functional (Kv2.1 and Kv2.2) and several "silent" alpha subunits (Kv2.3, Kv5, Kv6, Kv8, and Kv9), which do not generate K current. However, e.g., Kv8.1, via heteromerization, inhibits outward currents of the same family or even that of Shaw. This property of Kv8.1 is similar to those of designated beta subunits or non-selective auxiliary elements, including ADAM or AMIGO proteins. Kv channels and, in turn, ADAM may modulate the synaptic long-term potentiation (LTP). Prevailingly, Kv1.1 and Kv1.5 are attributed to respective brain and heart pathologies, some of which may occur simultaneously. The aforementioned channel proteins are apparently involved in several brain pathologies, including schizophrenia and seizures. LA - English DB - MTMT ER - TY - JOUR AU - Zhou, Lin AU - Wang, Kang AU - Xu, Yuxiang AU - Dong, Bin-Bin AU - Wu, Deng-Chang AU - Wang, Zhao-Xiang AU - Wang, Xin-Tai AU - Cai, Xin-Yu AU - Yang, Jin-Tao AU - Zheng, Rui AU - Chen, Wei AU - Shen, Ying AU - Wei, Jian-She TI - A patient-derived mutation of epilepsy-linked LGI1 increases seizure susceptibility through regulating K(v)1.1 JF - CELL AND BIOSCIENCE J2 - CELL BIOSCI VL - 13 PY - 2023 IS - 1 PG - 18 SN - 2045-3701 DO - 10.1186/s13578-023-00983-y UR - https://m2.mtmt.hu/api/publication/33932520 ID - 33932520 AB - BackgroundAutosomal dominant lateral temporal epilepsy (ADLTE) is an inherited syndrome caused by mutations in the leucine-rich glioma inactivated 1 (LGI1) gene. It is known that functional LGI1 is secreted by excitatory neurons, GABAergic interneurons, and astrocytes, and regulates AMPA-type glutamate receptor-mediated synaptic transmission by binding ADAM22 and ADAM23. However, > 40 LGI1 mutations have been reported in familial ADLTE patients, more than half of which are secretion-defective. How these secretion-defective LGI1 mutations lead to epilepsy is unknown.ResultsWe identified a novel secretion-defective LGI1 mutation from a Chinese ADLTE family, LGI1-W183R. We specifically expressed mutant LGI1(W183R) in excitatory neurons lacking natural LGI1, and found that this mutation downregulated K(v)1.1 activity, led to neuronal hyperexcitability and irregular spiking, and increased epilepsy susceptibility in mice. Further analysis revealed that restoring K(v)1.1 in excitatory neurons rescued the defect of spiking capacity, improved epilepsy susceptibility, and prolonged the life-span of mice.ConclusionsThese results describe a role of secretion-defective LGI1 in maintaining neuronal excitability and reveal a new mechanism in the pathology of LGI1 mutation-related epilepsy. LA - English DB - MTMT ER - TY - JOUR AU - Zhou, Lin AU - Wang, Kang AU - Xu, Yuxiang AU - Dong, Bin-Bin AU - Wu, Deng-Chang AU - Wang, Zhao-Xiang AU - Wang, Xin-Tai AU - Cai, Xin-Yu AU - Yang, Jin-Tao AU - Zheng, Rui TI - A patient-derived mutation of epilepsy-linked LGI1 increases seizure susceptibility through regulating Kv1. 1 JF - CELL AND BIOSCIENCE J2 - CELL BIOSCI VL - 13 PY - 2023 IS - 1 SP - 34 SN - 2045-3701 UR - https://m2.mtmt.hu/api/publication/33688719 ID - 33688719 LA - English DB - MTMT ER - TY - JOUR AU - Kovács, Tamás AU - Nagy, Péter AU - Panyi, György AU - Szente, Lajos AU - Varga, Zoltán AU - Zákány, Florina TI - Cyclodextrins: Only Pharmaceutical Excipients or Full-Fledged Drug Candidates? JF - PHARMACEUTICS J2 - PHARMACEUTICS VL - 14 PY - 2022 PG - 36 SN - 1999-4923 DO - 10.3390/pharmaceutics14122559 UR - https://m2.mtmt.hu/api/publication/33274154 ID - 33274154 N1 - Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary CycloLab Cyclodextrin R & D Laboratory Ltd, Budapest, H-1097, Hungary Export Date: 2 March 2023 Correspondence Address: Zakany, F.; Department of Biophysics and Cell Biology, Hungary; email: florina.zakany@med.unideb.hu AB - Cyclodextrins, representing a versatile family of cyclic oligosaccharides, have extensive pharmaceutical applications due to their unique truncated cone-shaped structure with a hydrophilic outer surface and a hydrophobic cavity, which enables them to form non-covalent host–guest inclusion complexes in pharmaceutical formulations to enhance the solubility, stability and bioavailability of numerous drug molecules. As a result, cyclodextrins are mostly considered as inert carriers during their medical application, while their ability to interact not only with small molecules but also with lipids and proteins is largely neglected. By forming inclusion complexes with cholesterol, cyclodextrins deplete cholesterol from cellular membranes and thereby influence protein function indirectly through alterations in biophysical properties and lateral heterogeneity of bilayers. In this review, we summarize the general chemical principles of direct cyclodextrin–protein interactions and highlight, through relevant examples, how these interactions can modify protein functions in vivo, which, despite their huge potential, have been completely unexploited in therapy so far. Finally, we give a brief overview of disorders such as Niemann–Pick type C disease, atherosclerosis, Alzheimer’s and Parkinson’s disease, in which cyclodextrins already have or could have the potential to be active therapeutic agents due to their cholesterol-complexing or direct protein-targeting properties. LA - English DB - MTMT ER - TY - GEN AU - Ma, Shuqin AU - Lin, Hao AU - Peng, Xudong AU - Li, Cui AU - Wang, Qian AU - Xu, Qiang AU - He, Mengting AU - Shao, Dan AU - Liu, Xing AU - Zhao, Guiqiu TI - Hinokitiol alters Gene Expression in Aspergillus fumigatus, protects against fungal keratitis by Reducing Fungal Load, LOX-1, Proinflammatory cytokines and Neutrophil Infiltration PY - 2022 SP - 2022 UR - https://m2.mtmt.hu/api/publication/33688725 ID - 33688725 AB - peer review LA - English DB - MTMT ER - TY - CHAP AU - Potier-Cartereau, Marie AU - Raoul, William AU - Weber, Gunther AU - Maheo, Karine AU - Rapetti-Mauss, Raphael AU - Gueguinou, Maxime AU - Buscaglia, Paul AU - Goupille, Caroline AU - Le, Goux Nelig AU - Abdoul-Azize, Souleymane AU - Lecomte, Thierry AU - Fromont, Gaelle AU - Chantome, Aurelie AU - Mignen, Olivier AU - Soriani, Olivier AU - Vandier, Christophe ED - Stock, Christian ED - Pardo, Luis A. TI - Potassium and Calcium Channel Complexes as Novel Targets for Cancer Research T2 - Targets of Cancer Diagnosis and Treatment PB - Springer Netherlands CY - Cham SN - 9783031039942 T3 - Reviews of Physiology, Biochemistry and Pharmacology, ISSN 0303-4240 ; 183. PY - 2022 SP - 157 EP - 176 PG - 20 DO - 10.1007/112_2020_24 UR - https://m2.mtmt.hu/api/publication/34567593 ID - 34567593 AB - The intracellular Ca2+ concentration is mainly controlled by Ca2+ channels. These channels form complexes with K+ channels, which function to amplify Ca2+ flux. In cancer cells, voltage-gated/voltage-dependent Ca2+ channels and non-voltage-gated/ voltage-independent Ca2+ channels have been reported to interact with K+ channels such as Ca2+-activated K+ channels and voltage-gated K+ channels. These channels are activated by an increase in cytosolic Ca2+ concentration or by membrane depolarization, which induces membrane hyperpolarization, increasing the driving force for Ca2+ flux. These complexes, composed of K+ and Ca2+ channels, are regulated by several molecules including lipids (ether lipids and cholesterol), proteins (e.g. STIM), receptors (e.g. S1R/SIGMAR1), and peptides (e.g. LL-37) and can be targeted by monoclonal antibodies, making them novel targets for cancer research. LA - English DB - MTMT ER - TY - JOUR AU - Batta, Gyula Gábor (Ifj.) AU - Kárpáti, Levente AU - Henrique, Gabriela Fulaneto AU - Tóth, Gabriella AU - Tarapcsák, Szabolcs AU - Kovács, Tamás AU - Zákány, Florina AU - Mándity, István AU - Nagy, Péter TI - Statin‐boosted cellular uptake and endosomal escape of penetratin due to reduced membrane dipole potential JF - BRITISH JOURNAL OF PHARMACOLOGY J2 - BR J PHARMACOL VL - 178 PY - 2021 IS - 18 SP - 3667 EP - 3681 PG - 15 SN - 0007-1188 DO - 10.1111/bph.15509 UR - https://m2.mtmt.hu/api/publication/31996377 ID - 31996377 N1 - Batta Gyula és Kárpáti Levente megosztott első szerzők Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary Department of Genetics and Applied Microbiology, Faculty of Science and Technology, University of Debrecen, Debrecen, Hungary Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University, Budapest, Hungary TTK Lendület Artificial Transporter Research Group, Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Budapest, Hungary Utah Center for Genetic Discovery, Eccles Institute of Human Genetics, University of Utah, Salt Lake City, UT, United States Export Date: 3 July 2021 CODEN: BJPCB Correspondence Address: Nagy, P.; Department of Biophysics and Cell Biology, Hungary; email: nagyp@med.unideb.hu Correspondence Address: Mándity, I.M.; Department of Organic Chemistry, Hungary; email: mandity.istvan@ttk.hu LA - English DB - MTMT ER - TY - JOUR AU - Capera, Jesusa AU - Perez-Verdaguer, Mireia AU - Peruzzo, Roberta AU - Navarro-Perez, Maria AU - Martinez-Pinna, Juan AU - Alberola-Die, Armando AU - Morales, Andres AU - Leanza, Luigi AU - Szabo, Ildiko AU - Felipe, Antonio TI - A novel mitochondrial Kv1.3-caveolin axis controls cell survival and apoptosis JF - ELIFE J2 - ELIFE VL - 10 PY - 2021 PG - 24 SN - 2050-084X DO - 10.7554/eLife.69099 UR - https://m2.mtmt.hu/api/publication/32276748 ID - 32276748 AB - The voltage-gated potassium channel Kv1.3 plays an apparent dual physiological role by participating in activation and proliferation of leukocytes as well as promoting apoptosis in several types of tumor cells. Therefore, Kv1.3 is considered a potential pharmacological target for immunodeficiency and cancer. Different cellular locations of Kv1.3, at the plasma membrane or the mitochondria, could be responsible for such duality. While plasma membrane Kv1.3 facilitates proliferation, the mitochondrial channel modulates apoptotic signaling. Several molecular determinants of Kv1.3 drive the channel to the cell surface, but no information is available about its mitochondrial targeting. Caveolins, which are able to modulate cell survival, participate in the plasma membrane targeting of Kv1.3. The channel, via a caveolin-binding domain (CDB), associates with caveolin 1 (Cav1), which localizes Kv1.3 to lipid raft membrane microdomains. The aim of our study was to understand the role of such interactions not only for channel targeting but also for cell survival in mammalian cells. By using a caveolin association-deficient channel (Kv1.3 CDBless), we demonstrate here that while the Kv1.3-Cav1 interaction is responsible for the channel localization in the plasma membrane, a lack of such interaction accumulates Kv1.3 in the mitochondria. Kv1.3 CDBless severely affects mitochondrial physiology and cell survival, indicating that a functional link of Kv1.3 with Cav1 within the mitochondria modulates the pro-apoptotic effects of the channel. Therefore, the balance exerted by these two complementary mechanisms fine-tune the physiological role of Kv1.3 during cell survival or apoptosis. Our data highlight an unexpected role for the mitochondrial caveolin-Kv1.3 axis during cell survival and apoptosis. LA - English DB - MTMT ER - TY - JOUR AU - Kovács, Tamás AU - Sohajda, Tamás AU - Szente, Lajos AU - Nagy, Péter AU - Panyi, György AU - Varga, Zoltán AU - Zákány, Florina TI - Cyclodextrins Exert a Ligand-like Current Inhibitory Effect on the KV1.3 Ion Channel Independent of Membrane Cholesterol Extraction JF - FRONTIERS IN MOLECULAR BIOSCIENCES J2 - FRONT MOL BIOSCI VL - 8 PY - 2021 SN - 2296-889X DO - 10.3389/fmolb.2021.735357 UR - https://m2.mtmt.hu/api/publication/32510829 ID - 32510829 N1 - Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary CycloLab Cyclodextrin R and D Laboratory Ltd, Budapest, Hungary Cited By :1 Export Date: 20 February 2022 Correspondence Address: Varga, Z.; Division of Biophysics, Hungary; email: veze@med.unideb.hu Correspondence Address: Zakany, F.; Division of Biophysics, Hungary; email: florina.zakany@med.unideb.hu LA - English DB - MTMT ER - TY - JOUR AU - Zákány, Florina AU - Szabó, Máté AU - Batta, Gyula Gábor (Ifj.) AU - Kárpáti, Levente AU - Mándity, István AU - Fülöp, Péter AU - Varga, Zoltán AU - Panyi, György AU - Nagy, Péter AU - Kovács, Tamás TI - An omega-3, but Not an omega-6 Polyunsaturated Fatty Acid Decreases Membrane Dipole Potential and Stimulates Endo-Lysosomal Escape of Penetratin JF - FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY J2 - FRONT CELL DEV BIOL VL - 9 PY - 2021 PG - 17 SN - 2296-634X DO - 10.3389/fcell.2021.647300 UR - https://m2.mtmt.hu/api/publication/32219377 ID - 32219377 N1 - Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary Department of Genetics and Applied Microbiology, Faculty of Science and Technology, University of Debrecen, Debrecen, Hungary Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University, Budapest, Hungary Lendület-Artificial Chloride Ion Transporter Group, Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Budapest, Hungary Division of Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Debrecen, Debrecen, Hungary Cited By :7 Export Date: 2 March 2023 Correspondence Address: Kovacs, T.; Division of Biophysics, Hungary; email: kovacs.tamas@med.unideb.hu AB - Although the largely positive intramembrane dipole potential (DP) may substantially influence the function of transmembrane proteins, its investigation is deeply hampered by the lack of measurement techniques suitable for high-throughput examination of living cells. Here, we describe a novel emission ratiometric flow cytometry method based on F66, a 3-hydroxiflavon derivative, and demonstrate that 6-ketocholestanol, cholesterol and 7-dehydrocholesterol, saturated stearic acid (SA) and omega-6 gamma-linolenic acid (GLA) increase, while omega-3 alpha-linolenic acid (ALA) decreases the DP. These changes do not correlate with alterations in cell viability or membrane fluidity. Pretreatment with ALA counteracts, while SA or GLA enhances cholesterol-induced DP elevations. Furthermore, ALA (but not SA or GLA) increases endo-lysosomal escape of penetratin, a cell-penetrating peptide. In summary, we have developed a novel method to measure DP in large quantities of individual living cells and propose ALA as a physiological DP lowering agent facilitating cytoplasmic entry of penetratin. LA - English DB - MTMT ER - TY - JOUR AU - Lee, Anthony G. TI - Interfacial Binding Sites for Cholesterol on Kir, Kv, K-2P, and Related Potassium Channels JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 119 PY - 2020 IS - 1 SP - 35 EP - 47 PG - 13 SN - 0006-3495 DO - 10.1016/j.bpj.2020.05.028 UR - https://m2.mtmt.hu/api/publication/31507319 ID - 31507319 AB - Inwardly rectifying, voltage-gated, two-pore domain, and related K+ channels are located in eukaryotic membranes rich in cholesterol. Here, molecular docking is used to detect specific binding sites ("hot spots") for cholesterol on K+ channels with characteristics that match those of known cholesterol binding sites. The transmembrane surfaces of all available high-resolution structures for K+ channels were swept for potential binding sites. Cholesterol poses were found to be located largely in hollows between protein ridges. A comparison between cholesterol poses and resolved phospholipids suggests that not all cholesterol molecules binding to the transmembrane surface of a K+ channel will result in displacement of a phospholipid molecule from the surface. Competition between cholesterol binding and binding of anionic phospholipids essential for activity could explain some of the effects of cholesterol on channel function. LA - English DB - MTMT ER - TY - JOUR AU - Zákány, Florina AU - Kovács, Tamás AU - Panyi, György AU - Varga, Zoltán TI - Direct and indirect cholesterol effects on membrane proteins with special focus on potassium channels JF - BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS J2 - BBA-MOL CELL BIOL L VL - 1865 PY - 2020 IS - 8 SN - 1388-1981 DO - 10.1016/j.bbalip.2020.158706 UR - https://m2.mtmt.hu/api/publication/31312818 ID - 31312818 N1 - Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary Doctoral School of Molecular Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary Export Date: 14 May 2020 CODEN: BBMLF Correspondence Address: Varga, Z.; Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Hungary; email: veze@med.unideb.hu Chemicals/CAS: adenosine triphosphatase (potassium sodium); calcium, 7440-70-2, 14092-94-5; cholesterol, 57-88-5; epidermal growth factor receptor, 79079-06-4; potassium, 7440-09-7; protein tyrosine kinase, 80449-02-1; sodium, 7440-23-5 Funding details: Emberi Eroforrások Minisztériuma, EMMI, ÚNKP-19-3-III-DE-92 Funding details: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal, NKFI, K120302, GINOP-2.3.2-15-2016-00015, EFOP-3.6.2-16-2017-00006, K119417, GINOP-2.3.2-15-2016-00020 Funding details: Magyar Tudományos Akadémia, MTA, KTIA_NAP_13-2-2015-0009, KTIA_NAP_13-2-2017-0013 Funding details: Hungarian Scientific Research Fund, OTKA, K132906, ÚNKP-18-3-IV-DE-54 Funding text 1: This work was supported by the Hungarian Academy of Sciences projects KTIA_NAP_13-2-2015-0009 and KTIA_NAP_13-2-2017-0013 (Z.V.); OTKA K132906 (Z.V.), the ÚNKP-18-3-IV-DE-54 New National Excellence Program of the Ministry of Human Capacities (F.Z.); ÚNKP-19-3-III-DE-92 New National Excellence Program of the Ministry for Innovation and Technology (F.Z.), the National Research Development and Innovation Office ( GINOP-2.3.2-15-2016-00020 ) (T.K.), EFOP-3.6.2-16-2017-00006 (G.P.), GINOP-2.3.2-15-2016-00015 (G.P.) and OTKA K119417 (G.P., F.Z.) and K120302 (T.K.). Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary Doctoral School of Molecular Medicine, University of Debrecen, Egyetem ter 1, Debrecen, H-4032, Hungary Export Date: 15 May 2020 CODEN: BBMLF Correspondence Address: Varga, Z.; Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Hungary; email: veze@med.unideb.hu Chemicals/CAS: adenosine triphosphatase (potassium sodium); calcium, 7440-70-2, 14092-94-5; cholesterol, 57-88-5; epidermal growth factor receptor, 79079-06-4; potassium, 7440-09-7; protein tyrosine kinase, 80449-02-1; sodium, 7440-23-5 Funding details: Emberi Eroforrások Minisztériuma, EMMI, ÚNKP-19-3-III-DE-92 Funding details: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal, NKFI, K120302, GINOP-2.3.2-15-2016-00015, EFOP-3.6.2-16-2017-00006, K119417, GINOP-2.3.2-15-2016-00020 Funding details: Magyar Tudományos Akadémia, MTA, KTIA_NAP_13-2-2015-0009, KTIA_NAP_13-2-2017-0013 Funding details: Hungarian Scientific Research Fund, OTKA, K132906, ÚNKP-18-3-IV-DE-54 Funding text 1: This work was supported by the Hungarian Academy of Sciences projects KTIA_NAP_13-2-2015-0009 and KTIA_NAP_13-2-2017-0013 (Z.V.); OTKA K132906 (Z.V.), the ÚNKP-18-3-IV-DE-54 New National Excellence Program of the Ministry of Human Capacities (F.Z.); ÚNKP-19-3-III-DE-92 New National Excellence Program of the Ministry for Innovation and Technology (F.Z.), the National Research Development and Innovation Office ( GINOP-2.3.2-15-2016-00020 ) (T.K.), EFOP-3.6.2-16-2017-00006 (G.P.), GINOP-2.3.2-15-2016-00015 (G.P.) and OTKA K119417 (G.P., F.Z.) and K120302 (T.K.). AB - As described in the literature the interaction between cholesterol and membrane proteins can occur via direct, ligand-like and indirect mechanisms, in which cholesterol effects are mediated by alterations in the biophysical properties or in the protein-organizing functions of the lipid membrane. Early studies emphasized the importance of indirect and raft-mediated effects, but improvements in computational and structural imaging techniques allowed the definition of a wide range of functionally active cholesterol binding domains and sites suggesting the relevance of direct cholesterol effects in various proteins. However, the intramolecular rearrangements induced by cholesterol leading to modulation of ion channel gating, membrane transport and receptor functions still have not been revealed. In this review we summarize the novel findings of the topic by focusing on recent studies about direct and indirect effects of cholesterol on potassium ion channels, and we extend the review to transporters and receptors with different domain structures to introduce the general mechanisms of cholesterol action among membrane proteins. We propose that rather than pure direct or indirect effects, cholesterol action on membrane proteins can be better described as a mixture of indirect and direct interactions with system-specific variability in their contributions, which can be explored by using a multi-level approach employing multiple experimental techniques. © 2020 The Authors LA - English DB - MTMT ER - TY - JOUR AU - Corradi, Valentina AU - Sejdiu, Besian I AU - Mesa-Galloso, Haydee AU - Abdizadeh, Haleh AU - Noskov, Sergei Yu AU - Marrink, Siewert J AU - Tieleman, D Peter TI - Emerging Diversity in Lipid–Protein Interactions JF - CHEMICAL REVIEWS J2 - CHEM REV VL - 119 PY - 2018 IS - 9 SP - 5775 EP - 5848 PG - 74 SN - 0009-2665 DO - 10.1021/acs.chemrev.8b00451 UR - https://m2.mtmt.hu/api/publication/30669164 ID - 30669164 N1 - Centre for Molecular Simulation and Department of Biological Sciences, University of Calgary, 2500 University Drive, Calgary, AB T2N 1N4, Canada Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 7, Groningen, 9747 AG, Netherlands Cited By :10 Export Date: 27 September 2019 CODEN: CHREA Correspondence Address: Tieleman, D.P.; Centre for Molecular Simulation and Department of Biological Sciences, University of Calgary, 2500 University Drive, Canada; email: tieleman@ucalgary.ca LA - English DB - MTMT ER -