Structure of the human voltage-dependent anion channel

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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Translocation of Proteins into Mitochondria

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Automated Structure Solution With autoSHARP

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Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0

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Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins

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Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria

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OPTIMIZING LONG INTRINSIC DISORDER PREDICTORS WITH PROTEIN EVOLUTIONARY INFORMATION

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The structure of bacterial outer membrane proteins

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Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins

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Machinery for protein sorting and assembly in the mitochondrial outer membrane

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Porins as helpers in mitochondrial protein translocation

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Post-Translational Modification Analysis of VDAC1 in ALS-SOD1 Model Cells Reveals Specific Asparagine and Glutamine Deamidation

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VDAC—A Primal Perspective

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Voltage-Dependent Anion Selective Channel 3: Unraveling Structural and Functional Features of the Least Known Porin Isoform

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Origami in outer membrane mimetics: correlating the first detailed images of refolded VDAC with over 20 years of biochemical data

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A High Resolution Mass Spectrometry Study Reveals the Potential of Disulfide Formation in Human Mitochondrial Voltage-Dependent Anion Selective Channel Isoforms (hVDACs)

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The structure of the TOM core complex in the mitochondrial outer membrane

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Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets

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Improving the Resistance of a Eukaryotic β-Barrel Protein to Thermal and Chemical Perturbations

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Bayesian Modeling of Biomolecular Assemblies with Cryo-EM Maps

Habeck, M. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00015 · Cited by 22

Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions

Rosa, M. C. D., Guarino, F., Nibali, S. C., Magrì, A., & Pinto, V. D. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.675708 · Cited by 21

Probing Tubulin-Blocked State of VDAC by Varying Membrane Surface Charge

Gurnev, P. A., Queralt-Martín, M., Aguilella, V. M., Rostovtseva, T. K., & Bezrukov, S. M. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.03.058 · Cited by 22

The Use of Anti-VDAC2 Antibody for the Combined Assessment of Human Sperm Acrosome Integrity and Ionophore A23187-Induced Acrosome Reaction

Liu, B., Wang, P., Wang, Z., & Zhang, W. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016985 · Cited by 22

Dual Mechanism of Ion Permeation through VDAC Revealed with Inorganic Phosphate Ions and Phosphate Metabolites

Krammer, E., Vu, G. T., Homblé, F., & Prévost, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121746 · Cited by 21

NMR structures of polytopic integral membrane proteins

Patching, S. G. (2011) · Molecular Membrane Biology · doi:10.3109/09687688.2011.603100 · Cited by 21

The N-Terminal Peptides of the Three Human Isoforms of the Mitochondrial Voltage-Dependent Anion Channel Have Different Helical Propensities.

Guardiani, C., Scorciapino, M. A., Amodeo, G., Grdadolnik, J., Pappalardo, G., Pinto, V. D., Ceccarelli, M., & Casu, M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00469 · Cited by 20

Melatonin as a regulator of apoptosis in leukaemia: molecular mechanism and therapeutic perspectives

Mafi, A., Rismanchi, H., Gholinezhad, Y., Mohammadi, M. M., Mousavi, V., Hosseini, S. A., Milasi, Y. E., Reiter, R. J., Ghezelbash, B., Rezaee, M., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1224151 · Cited by 21

Non-Overlapping Distributions and Functions of the VDAC Family in Ciliogenesis

Majumder, S., Cash, A., & Fisk, H. A. (2015) · Cells · doi:10.3390/cells4030331 · Cited by 21

Stabilized finite element methods to simulate the conductances of ion channels

Tu, B., Xie, Y., Zhang, L., & Lu, B. (2014) · Computer Physics Communications · doi:10.1016/j.cpc.2014.11.018 · Cited by 21

Phosphorylation of voltage-dependent anion channel by c-Jun N-terminal Kinase-3 leads to closure of the channel

Gupta, R., & Ghosh, S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.077 · Cited by 21

Structural characterization of the human membrane protein VDAC2 in lipid bilayers by MAS NMR

Eddy, M. T., Yu, T., Wagner, G., & Griffin, R. G. (2019) · Journal of Biomolecular NMR · doi:10.1007/s10858-019-00242-8 · Cited by 22

Pore-Forming VDAC Proteins of the Outer Mitochondrial Membrane: Regulation and Pathophysiological Role

Belosludtseva, N. V., Dubinin, M. V., & Belosludtsev, K. N. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924060075 · Cited by 20

Function and Regulation of Mitochondrial Voltage-Dependent Anion Channel

Rostovtseva, T. K., & Bezrukov, S. M. (2015) · Springer series in biophysics · doi:10.1007/978-3-319-20149-8_1 · Cited by 20

Exploring lipid-dependent conformations of membrane-bound α-synuclein with the VDAC nanopore

Hoogerheide, D. P., Rostovtseva, T. K., & Bezrukov, S. M. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183643 · Cited by 20

Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids

Campo, M. L., Peixoto, P. M. V., & Martinez‐Caballero, S. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9662-z · Cited by 22

Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins

Rosencrans, W. M., Khuntia, H., Larimi, M. G., Mahalakshmi, R., Yu, T., Bezrukov, S. M., & Rostovtseva, T. K. (2025) · Science Advances · doi:10.1126/sciadv.adv4410 · Cited by 19

Deuterated detergents for structural and functional studies of membrane proteins: Properties, chemical synthesis and applications

Hiruma‐Shimizu, K., Shimizu, H., Thompson, G. S., Kalverda, A. P., & Patching, S. G. (2015) · Molecular Membrane Biology · doi:10.3109/09687688.2015.1125536 · Cited by 19

Functional Refolding and Characterization of Two Tom40 Isoforms from Human Mitochondria

Mager, F., Gessmann, D., Nußberger, S., & Zeth, K. (2011) · The Journal of Membrane Biology · doi:10.1007/s00232-011-9372-8 · Cited by 19

Influence of Protein – Micelle Ratios and Cysteine Residues on the Kinetic Stability and Unfolding Rates of Human Mitochondrial VDAC-2

Maurya, S. R., & Mahalakshmi, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087701 · Cited by 19

VDACs Post-Translational Modifications Discovery by Mass Spectrometry: Impact on Their Hub Function

Pittalà, M. G. G., Nibali, S. C., Reina, S., Cunsolo, V., Francesco, A. D., Pinto, V. D., Messina, A. A., Foti, S., & Saletti, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312833 · Cited by 19

Voltage-dependent anion channel in mammalian spermatozoa

Liu, B., Zhang, W., & Wang, Z. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.06.025 · Cited by 19

Characterization of Oyster Voltage-Dependent Anion Channel 2 (VDAC2) Suggests Its Involvement in Apoptosis and Host Defense

Li, Y., Zhang, L., Qu, T., Li, L., & Zhang, G. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146049 · Cited by 19

Decoding Cancer through Silencing the Mitochondrial Gatekeeper VDAC1

Arif, T., Shteinfer‐Kuzmine, A., & Shoshan‐Barmatz, V. (2024) · Biomolecules · doi:10.3390/biom14101304 · Cited by 23

OMPdb: A Global Hub of Beta-Barrel Outer Membrane Proteins

Roumia, A. F., Tsirigos, K. D., Theodoropoulou, M. C., Tamposis, I., Hamodrakas, S. J., & Bagos, P. G. (2021) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2021.646581 · Cited by 18

The Single Residue K12 Governs the Exceptional Voltage Sensitivity of Mitochondrial Voltage-Dependent Anion Channel Gating

Ngo, V. A., Queralt-Martín, M., Khan, F., Bergdoll, L. A., Abramson, J., Bezrukov, S. M., Rostovtseva, T. K., Hoogerheide, D. P., & Noskov, S. Y. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c03316 · Cited by 18

Origin of ion selectivity in Phaseolus coccineus mitochondrial VDAC

Krammer, E., Saidani, H., Prévost, M., & Homblé, F. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.04.003 · Cited by 18

Molecular origin of VDAC selectivity towards inorganic ions: A combined molecular and Brownian dynamics study

Krammer, E., Homblé, F., & Prévost, M. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.12.018 · Cited by 18

Solid-state NMR structures of integral membrane proteins

Patching, S. G. (2015) · Molecular Membrane Biology · doi:10.3109/09687688.2016.1139754 · Cited by 18

Evidence Supporting the 19 β-Strand Model for Tom40 from Cysteine Scanning and Protease Site Accessibility Studies

Lackey, S. W. K., Taylor, R. D., Go, N. E., Wong, A., Sherman, E. L., & Nargang, F. E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.578765 · Cited by 17

Evolutionary selection of a 19-stranded mitochondrial β-barrel scaffold bears structural and functional significance

Srivastava, S. R., & Mahalakshmi, R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014366 · Cited by 17

The movement of mitochondria in breast cancer: internal motility and intercellular transfer of mitochondria

Libring, S., Berestesky, E. D., & Reinhart‐King, C. A. (2024) · Clinical & Experimental Metastasis · doi:10.1007/s10585-024-10269-3 · Cited by 17

Cysteine Residues Impact the Stability and Micelle Interaction Dynamics of the Human Mitochondrial β-Barrel Anion Channel hVDAC-2

Maurya, S. R., & Mahalakshmi, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092183 · Cited by 18

VDAC blockage by phosphorothioate oligonucleotides and its implication in apoptosis

Tan, W. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.12.032 · Cited by 17

Phylogenetic Analysis of Mitochondrial Outer Membrane β-Barrel Channels

Wojtkowska, M., Jąkalski, M., Pieńkowska, J. R., Stobienia, O., Karachitos, A., Przytycka, T. M., Weiner, J. M., Kmita, H., & Makałowski, W. (2011) · Genome Biology and Evolution · doi:10.1093/gbe/evr130 · Cited by 17

A computational study of ion current modulation in hVDAC3 induced by disulfide bonds

Guardiani, C., Leggio, L., Scorciapino, M. A., Pinto, V. D., & Ceccarelli, M. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.01.013 · Cited by 17

Hypoxic-induced truncation of voltage-dependent anion channel 1 is mediated by both asparagine endopeptidase and calpain 1 activities

Pahima, H. T., Reina, S., Tadmor, N., Dadon-Klein, D., Shteinfer‐Kuzmine, A., Mazure, N. M., Pinto, V. D., & Shoshan‐Barmatz, V. (2018) · Oncotarget · doi:10.18632/oncotarget.24377 · Cited by 17

Structure-based modeling of turnover of Bcl-2 family proteins bound to voltage-dependent anion channel 2 (VDAC2): Implications for the mechanisms of proapoptotic activation of Bak and Bax in vivo

Dudko, H. V., Urban, V. A., Davidovskii, A. I., & Veresov, V. G. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107203 · Cited by 18

An Escherichia coli-Based Cell-Free System for Large-Scale Production of Functional Mammalian Membrane Proteins Suitable for X-Ray Crystallography

Nguyen, T. A., Lieu, S. S., & Chang, G. A. (2010) · Microbial Physiology · doi:10.1159/000283512 · Cited by 17

Mitochondrial tyrosine phosphoproteome: New insights from an up‐to‐date analysis

Cesaro, L., & Salvi, M. (2010) · BioFactors · doi:10.1002/biof.123 · Cited by 17

A Tag at the Carboxy Terminus Prevents Membrane Integration of VDAC1 in Mammalian Mitochondria

Kozjak‐Pavlovic, V., Roß, K., Götz, M., Goosmann, C., & Rudel, T. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.01.047 · Cited by 17

Mechanism of translation control of the alternative Drosophila melanogaster Voltage Dependent Anion-selective Channel 1 mRNAs

Leggio, L., Guarino, F., Magrì, A., Accardi, R., Reina, S., Specchia, V., Damiano, F., Tomasello, M. F., Tommasino, M., & Messina, A. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-23730-7 · Cited by 17

Bacterial Expression, Purification and Characterization of a Rice Voltage-Dependent, Anion-Selective Channel Isoform, OsVDAC4

Godbole, A., Mitra, R., Dubey, A. K., Reddy, P. S., & Mathew, M. K. (2011) · The Journal of Membrane Biology · doi:10.1007/s00232-011-9399-x · Cited by 16

Calcium channels as pharmacological targets for cancer therapy

Liu, X., Feng, C., Li, Y., Cao, J., Zhu, X., Li, M., & Guizhi, Z. (2025) · Clinical and Experimental Medicine · doi:10.1007/s10238-025-01632-z · Cited by 15

Protein import into bacterial endosymbionts and evolving organelles

Sørensen, M. E. S., Stiller, M., Kröninger, L., & Nowack, E. (2024) · The FEBS Journal · doi:10.1111/febs.17356 · Cited by 13

Antisense Oligonucleotide Modified with Disulfide Units Induces Efficient Exon Skipping in mdx Myotubes through Enhanced Membrane Permeability and Nucleus Internalization

Hiraoka, H., Shu, Z., Le, B. T., Masuda, K., Nakamoto, K., Lyu, F., Abe, N., Hashiya, F., Kimura, Y., Shimizu, Y., et al. (2021) · ChemBioChem · doi:10.1002/cbic.202100413 · Cited by 15

Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century

Benz, R. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.734226 · Cited by 15

Outer Membrane Proteins

Mirus, O., Hahn, A. S., & Schleiff, E. (2010) · Springer eBooks · doi:10.1007/978-3-642-05062-6_6 · Cited by 15

After all, plasmalemmal expression of type-1 VDAC can be understood. Phosphorylation, nitrosylation, and channel modulators work together in vertebrate cell volume regulation and either apoptotic pathway

THINNES, F. P. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00126 · Cited by 15

Phosphorylation of purified mitochondrial Voltage-Dependent Anion Channel by c-Jun N-terminal Kinase-3 modifies channel voltage-dependence

Gupta, R., & Ghosh, S. (2017) · Biochimie Open · doi:10.1016/j.biopen.2017.03.002 · Cited by 15

An immunoproteomic approach to identifying immunoreactive proteins inLeishmania infantumamastigotes using sera of dogs infected with canine visceral leishmaniasis

Rashidi, S., Mojtahedi, Z., Sarkari, B., Kalantar, K., Ghalamfarsa, G., Mohebali, M., & Hatam, G. (2019) · Pathogens and Global Health · doi:10.1080/20477724.2019.1616952 · Cited by 15

Porin 1 Modulates Autophagy in Yeast

Broeskamp, F., Edrich, E. S. M., Knittelfelder, O. L., Neuhaus, L., Meyer, T., Heyden, J., Habernig, L., Kreppel, F., Gourlay, C. W., & Rockenfeller, P. (2021) · Cells · doi:10.3390/cells10092416 · Cited by 12

The dual role of VDAC in cancer: Molecular mechanisms and advances in targeted therapy

Huang, H., Chen, M., Feng, S., Lin, Z., & Liu, Y. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118530 · Cited by 18

HSP90 C-terminal domain inhibition promotes VDAC1 oligomerization via decreasing K274 mono-ubiquitination in Hepatocellular Carcinoma

Zhang, J., Liu, L., Li, Y., Huang, Y., Xiao, S., Deng, Z., Zheng, Z., Li, J., Liang, M., Xie, G., et al. (2023) · Neoplasia · doi:10.1016/j.neo.2023.100935 · Cited by 15

New findings concerning vertebrate porin II — On the relevance of glycine motifs of type-1 VDAC

THINNES, F. P. (2013) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2013.01.008 · Cited by 14

Quinidine partially blocks mitochondrial voltage-dependent anion channel (VDAC)

Malik, C., & Ghosh, S. (2020) · European Biophysics Journal · doi:10.1007/s00249-020-01426-z · Cited by 14

Computational modeling on mitochondrial channel nanotoxicity

González‐Durruthy, M., Giri, A. K., Moreira, I. S., Concu, R., Melo, A., Ruso, J. M., & Cordeiro, M. N. D. S. (2020) · Nano Today · doi:10.1016/j.nantod.2020.100913 · Cited by 14

Voltage‐dependent anion channels (VDACs, porin) expressed in the plasma membrane regulate the differentiation and function of human osteoclasts

Kotake, S., Yago, T., Kawamoto, M., & Nanke, Y. (2012) · Cell Biology International · doi:10.1002/cbin.10013 · Cited by 14

Cytosolic Ca2+–Induced Apoptosis in Rat Cardiomyocytes via Mitochondrial NO-cGMP-Protein Kinase G Pathway

Seya, K., Ono, K., Fujisawa, S., Okumura, K., Motomura, S., & Furukawa, K. (2012) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.198176 · Cited by 14

A size‐modified poisson–boltzmann ion channel model in a solvent of multiple ionic species: Application to voltage‐dependent anion channel

Xie, D., Audi, S. H., & Dash, R. K. (2019) · Journal of Computational Chemistry · doi:10.1002/jcc.26091 · Cited by 14

Combining nano-differential scanning fluorimetry and microscale thermophoresis to investigate VDAC1 interaction with small molecules

Gorny, H., Mularoni, A., Delcros, J., Freton, C., Preto, J., & Krimm, I. (2023) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2121821 · Cited by 15

Protocol for the production and reconstitution of VDAC1 for functional assays

Dearden, G. I., Ravishankar, V., Sakata, K., Menon, A. K., & Bergdoll, L. A. (2024) · STAR Protocols · doi:10.1016/j.xpro.2024.103240 · Cited by 13

Channel characteristics of VDAC-3 from Arabidopsis thaliana

Berrier, C., Peyronnet, R., Betton, J., Ephritikhine, G., Barbier‐Brygoo, H., Frachisse, J., & Ghazi, A. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.034 · Cited by 13

Yeast Mitochondrial Interactosome Model: Metabolon Membrane Proteins Complex Involved in the Channeling of ADP/ATP

Clémençon, B. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13021858 · Cited by 14

Studying membrane proteins with MicroED

Gallenito, M. J., & Gonen, T. (2022) · Biochemical Society Transactions · doi:10.1042/bst20210911 · Cited by 13

Dominant-negative VDAC1 mutants reveal oligomeric VDAC1 to be the active unit in mitochondria-mediated apoptosis

Mader, A., Abu‐Hamad, S., Arbel, N., Gutierr-Asuilar, M., & Shoshan‐Barmatz, V. (2010) · Biochemical Journal · doi:10.1042/bj20091338 · Cited by 13

Synthetic Ubiquinones Specifically Bind to Mitochondrial Voltage-Dependent Anion Channel 1 (VDAC1) in Saccharomyces cerevisiae Mitochondria

Murai, M., Okuda, A., Yamamoto, T., Shinohara, Y., & Miyoshi, H. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b01011 · Cited by 15

The intrinsically disordered N-terminus of the voltage-dependent anion channel

Preto, J., & Krimm, I. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008750 · Cited by 13

Membrane Transport

Yèagle, P. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-800047-2.00013-9 · Cited by 16

Integrating diverse experimental information to assist protein complex structure prediction by GRASP

Xie, Y., Zhang, C., Li, S., Du, X., Lu, Y., Wang, M., Hu, Y., Chen, Z., Liu, S., & Gao, Y. Q. (2025) · Nature Methods · doi:10.1038/s41592-025-02820-1 · Cited by 14

Amyloid Aß , cut from APP by ß-secretase BACE1 and γ-secretase, induces apoptosis via opening type-1 porin/VDAC in cell membranes of hypometabolic cells—A basic model for the induction of apoptosis!?

THINNES, F. P. (2010) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2010.07.007 · Cited by 12

Identification of 4‐hydroxynonenal protein targets in rat, mouse and human liver microsomes by two‐dimensional liquid chromatography/tandem mass spectrometry

Golizeh, M., Geib, T., & Sleno, L. (2016) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.7577 · Cited by 12

Detergent Titration as an Efficient Method for NMR Resonance Assignments of Membrane Proteins in Lipid–Bilayer Nanodiscs

Bibow, S., Böhm, R., Modaresi, S. M., & Hiller, S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c00917 · Cited by 12

Folded Structure and Membrane Affinity of the N-Terminal Domain of the Three Human Isoforms of the Mitochondrial Voltage-Dependent Anion-Selective Channel

Manzo, G., Serra, I., Magrì, A., Casu, M., Pinto, V. D., Ceccarelli, M., & Scorciapino, M. A. (2018) · ACS Omega · doi:10.1021/acsomega.8b01536 · Cited by 12

Hypothermia-Induced Ubiquitination of Voltage-Dependent Anion Channel 3 Protects BV2 Microglia Cells From Cytotoxicity Following Oxygen-Glucose Deprivation/Recovery

Zhao, S., Peng, X., Cui, H. Z., Gong, P., Lin, C., Chen, F., & Tang, Z. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00100 · Cited by 12

Model reduction-based initialization methods for solving the Poisson-Nernst-Plank equations in three-dimensional ion channel simulations

Zhang, Q., Gui, S., Li, H., & Lu, B. (2020) · Journal of Computational Physics · doi:10.1016/j.jcp.2020.109627 · Cited by 12

5.8 Structure and Folding of Outer Membrane Proteins

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NMR studies of membrane proteins

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