Structure of the human voltage-dependent anion channel

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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

PENG, K., Vučetić, S., Predrag Radivojac, A., Brown, C. J., Dunker, A. K., & Zoran Obradovic, A. (2005) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720005000886 · Cited by 499

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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Chapter 11 Bacterial Membrane Proteins

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The Design and Structure of Outer Membrane Receptors from Peroxisomes, Mitochondria, and Chloroplasts

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Potential blockade of the human voltage-dependent anion channel by MoS 2 nanoflakes

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Voltage-Dependent Anion Channel (VDAC) in Health and Disease

Rajendran, M., Bezrukov, S. M., & Rostovtseva, T. K. (2023) · Oxford University Press eBooks · doi:10.1093/oxfordhb/9780190932183.013.6 · Cited by 1

Structure and Function-Associated Dynamics of Membrane Proteins Unveiled by Solution NMR

Takeuchi, K., Kofuku, Y., Imai, S., Tokunaga, Y., Ueda, T., & Shimada, I. (2025) · Springer eBooks · doi:10.1007/978-981-97-6834-9_11 · Cited by 1

VDAC1 inhibitor DIDS uncouples respiration in isolated tissue mitochondria and induces mitochondrial hyperfusion in mammalian cells

Das, S., Dutta, A., Bedi, M., Pal, A., Majumder, S., & Ghosh, A. (2025) · BBA Advances · doi:10.1016/j.bbadva.2025.100171 · Cited by 2

Novel Perspectives on Protein Structure Prediction

Berger, B., & Waldispühl, J. (2010) · Springer eBooks · doi:10.1007/978-0-387-09760-2_9 · Cited by 1

Channeling your inner energy

Faraldo‐Gómez, J. D. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2854 · Cited by 1

Targeting Mitochondrial Enzymes in Pancreatic Cancer

Srivani, G., Dariya, B., Alam, A., & Nagaraju, G. P. (2019) · Springer eBooks · doi:10.1007/978-981-32-9393-9_6 · Cited by 1

Mitochondrial disorders: Nuclear-encoded gene defects

Patel, K., Fassad, M. R., McFarland, R., & Taylor, R. W. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-99417-0.00032-x · Cited by 1

Differentiating Compromised Mitochondria of Lung Cancer Cells from Mitochondria in Healthy Cells

Sharma, B., Shafaee, Z., Twelker, K., Bhatia, N. D., Agriantonis, G., Dave, J., Mestre, J., Ghanta, H., Arora, S., & Whittington, J. (2024) · Journal of Biomedical Research & Environmental Sciences · doi:10.37871/jbres1900 · Cited by 1

Challenges of Protein-Protein Docking of the Membrane Proteins

Kiani, Y. S., & Jabeen, I. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3985-6_12 · Cited by 1

Mitochondria and cell metabolism

Ayturk, M. M., Sahin, H. Y., & Şımşek, G. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-18858-9.00002-0 · Cited by 1

Plant VDAC Permeability: Molecular Basis and Role in Oxidative Stress

Homblé, F., Kmita, H., Saidani, H., & Léonetti, M. (2017) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-55539-3_7 · Cited by 1

Molecular recognition and interaction between human plasminogen Kringle 5 and voltage-dependent anion channel-1 by biological specificity technologies and molecular dynamic simulation

Zhang, J., Wang, K., Xue, P., Chen, X., & Bian, L. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106710 · Cited by 1

In Silico Exploration of Alternative Conformational States of VDAC

Mannella, C. A. (2023) · Molecules · doi:10.3390/molecules28083309 · Cited by 1

Shedding Light on Transmembrane Topology

Tusnády, G., & Simon, I. (2010) · Wiley eBooks · doi:10.1002/9780470882207.ch6 · Cited by 1

Mitochondrial Channels in Neurodegeneration

Peixoto, P. M. V., Kinnally, K. W., & Pavlov, E. V. (2015) · Wiley eBooks · doi:10.1002/9781119017127.ch3 · Cited by 1

Crystalline, membrane-embedded, and fibrillar proteins investigated by solid-state NMR spectroscopy

Schneider, R. (2009) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-2601 · Cited by 1

Integrating various Experimental Information to Assist Protein Complex Structure Prediction by GRASPPreprint

Xie, Y., Zhang, C., Li, S., Du, X., Wang, M., Hu, Y., Liu, S., & Gao, Y. Q. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.16.613256 · Cited by 1

Mitochondrial cardiolipin metabolism controlled by tafazzin enables ferroptosisPreprint

Wohlfarter, Y., Hagenbuchner, J., Horzum, U., Oemer, G., Winter, A., Seifert, M., Schwärzler, J., Kokot, J., Hernansanz‐Agustín, P., Jurić, V., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.25.620299 · Cited by 1

Unlocking the Distinct Roles of the Three Mammalian VDAC Isoforms in Mitochondrial Respiration and Cancer Cell MetabolismPreprint

Rajendran, M., Rosencrans, W. M., Fitzgerald, W., Huynh, D., Beyene, B. G., Quan, B., Hwang, J., Bautista, N. A., Chou, T., Bezrukov, S. M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.20.639106 · Cited by 1

Untersuchung sub-mitochondrialer Proteinverteilungen in unbehandelten und apoptotischen humanen Zellen mittels STED-Mikroskopie

Neumann, D. (2010) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-383

Análise interactômica da VDAC em mitocôndrias neuronais bovina e murina

Crepaldi, C. R. (2012) · doi:10.11606/d.74.2012.tde-04072012-112500

Solution NMR-based characterization of the structure of the outer mitochondrial membrane protein Tom40 and a novel method for NMR resonance assignment of large intrinsically disordered proteins

Yao, X. (2014) · doi:10.53846/goediss-4489

Electrophysiological Techniques for Mitochondrial Channels

Schindl, R., & Weghuber, J. (2012) · InTech eBooks · doi:10.5772/37088

Hexokinase II-vermittelte Hypoxietoleranz und endogene Neuroprotektion

Mergenthaler, P. (2011) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-17602

Targets and Strategies for the Mitochondrial Assault on Cancer

Biasutto, L., Szabó, I., & Zoratti, M. (2014) · Springer eBooks · doi:10.1007/978-94-017-8984-4_9

The impact of glucotoxicity on pancreatic β-cell function

Muhammed, S. J. (2012) · Lund University Publications (Lund University)

Isoforms of voltage-dependent anion channel of the outer mitochondrial membrane and experimental models to study their physiological role

Teplova, V. V., Odinokova, I. V., & Holmuhamedov, E. (2011) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747811020085

Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus

Wang, T., Langer, J. D., Peng, G., & Michel, H. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.07.004

Long QT syndrome : the identification and verification of putative KCNE2-interacting proteins

Neethling, A. (2013) · SUNScholar (Stellenbosch University)

Association between VDAC1 mRNA expression and intracellular ATP levels of cultured L-02 hepatocytes during hexavalent chromium toxicity

Yuan, Y. (2011) · AFRICAN JOURNAL OF BIOTECHNOLOGY · doi:10.5897/ajb11.3120

Trans-Plasma Membrane Electron Transport in Human Blood Platelets: An Update

Avigliano, L., Savini, I., Catani, M. V., & Principe, D. D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803961-8.50013-0

At the Crossroads Between Mitochondrial Metabolite Transport and Apoptosis: VDAC1 as an Emerging Cancer Drug Target

Shoshan‐Barmatz, V., Shteinfer‐Kuzmine, A., Ben-Hail, D., Arif, T., & Mizrachi, D. (2014) · Springer eBooks · doi:10.1007/978-94-017-9421-3_16

pH-Triggered Membrane Insertion of Proteins

Vargas‐Uribe, M. (2015) · KU ScholarWorks (The University of Kansas)

Hochohmige porenüberspannende Lipidmembranen: Elektrochemische Untersuchungen zur Aktivität von Gramicidin und Bacteriorhodpsin

Schmitt, E. K. (2009) · doi:10.53846/goediss-2075

The use of nuclear magnetic resonance in study of structurally dynamic membrane proteins

Phillips, M. (2016) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/68476

Proteome study of nasopharyngeal carcinoma

Feng, X. (2012) · doi:10.32657/10356/50504

Computational Studies of Biological Ion Channels

Kowallis, W. (2016) · D-Scholarship@Pitt (University of Pittsburgh)

Roles of periplasmic chaperones and BamA in outer membrane protein folding

Schiffrin, R. (2016) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

Efficient and Qualified Mesh Generation for Gaussian Molecular Surface Using Piecewise Trilinear Polynomial ApproximationPreprint

Liu, T., Chen, M., & Lu, B. (2016) · arXiv (Cornell University) · doi:10.48550/arxiv.1611.03474

Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins

Surya, W. (2017) · doi:10.32657/10356/69964

Structural and Functional Studies of AlgK: A Protein Required for the Secretion of High-molecular Weight Alginate in Pseudomonas aeruginosa

Keiski, C.-L. (2010) · TSpace (University of Toronto)

Structural plasticity of BCL-2 family proteins and its functional implication in apoptosis

Choi, M. (2018) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/73522

Elucidation of protein interactions in complex samples by protein-protein cross-linking of synaptosomes

Parfentev, I. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7615

Smart hybrid nanomaterials for biomimetic membranes

Lopes‐Rodrigues, M. (2019) · doi:10.5821/dissertation-2117-173360

Elucidation of protein-protein interactions in mitochondria by cross-linking mass spectrometry

Linden, A. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8148

The Role of Mdivi-1 in Colorectal Cancer

Wang, S. (2018) · TSpace (University of Toronto)

Molecular mechanism of thiamine pyrophosphate import into mitochondria: a molecular simulation study

Liefferinge, F. V., Krammer, E., Waeytens, J., & Prévost, M. (2021) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-021-00414-5

In and through the membrane by solid-state NMR: investigations of the human voltage-dependent anion channel 1 and Nup98-derived FG-domains

Najbauer, E. É. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-52

Faculty Opinions recommendation of Facile backbone structure determination of human membrane proteins by NMR spectroscopy.

Doren, S. R. V. (2012) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.716747901.793003008

Faculty Opinions recommendation of Facile backbone structure determination of human membrane proteins by NMR spectroscopy.

Columbus, L. M., & Dewald, A. H. (2012) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.716747901.792102901

Effect of CLN3-loss-of-function on cellular metabolism and signalling

Więciorek-Płuciennik, K. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9277

Mitochondrial Dysfunction and Their Management by Antioxidants

Koteeswaran, K., & Keerthana, N. (2022) · Asian Plant Research Journal · doi:10.9734/aprj/2022/v9i430215

NMR of Membrane Proteins

Bostock, M. J., & Nietlispach, D. (2012) · Royal Society of Chemistry eBooks · doi:10.1039/9781849731201-00271

Modular Assembly of Mitochondrial β-Barrel Proteins

Bhowmik, R., den Brave, F., & Becker, T. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3734-0_13

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

Belosludtseva, N. V., Dubinin, M. V., & Belosludtsev, K. N. (2024) · Biochemistry (Moscow) · doi:10.31857/s0320972524060075

Structure and Dynamic Properties of Membrane Proteins using NMR

Rösner, H. I., & Kragelund, B. B. (2012) · Comprehensive physiology · doi:10.1002/j.2040-4603.2012.tb00430.x

Structural characterization of intra- and intermolecular disulfide bonds in voltage-dependent anion channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry

Pittalà, M. G. G., Cucina, A., Nibali, S. C., Cunsolo, V., Francesco, A. D., Battiato, G., Reina, S., Foti, S., Pinto, V. D., & Saletti, R. (2025) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-025-06074-w

Structure Prediction of Transmembrane Proteins

Tusnády, G., & Kozma, D. (2014) · Springer eBooks · doi:10.1007/978-3-319-09976-7_9

Regulation of BAX/BAK-Dependent Cell Death Program

Kim, H. (2009) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7rb72m2

Counting strands in outer membrane β-barrels

Lim, S., Nimmagadda, T., Khamis, A., Montezano, D., Feehan, R., Copeland, M. M., & Slusky, J. S. G. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2026.03.016

Molecular basis of BCL2L10/Nrh oncogenic activity in breast cancer

Nougarède, A. (2016) · theses.fr (ABES) · doi:10.70675/67283ec1z7040z4d6eza688z407667ae770d

Influence de la génétique mitochondriale en pathologie : apport des techniques de séquençage haut débit

Bris, C. (2017) · theses.fr (ABES) · doi:10.70675/6c36a70az1fa2z4a9fzae9cz5f3344cffaeb

Translocator protein (TSPO) functions on erythropoiesis and red blood cell infection by plasmodium falciparum

Marginedas-Freixa, I. (2017) · theses.fr (ABES) · doi:10.70675/c493d7f5zc4b3z4debzb54fza7d98f55233f

Role of VDAC1 hypoxic form, VDAC1-∆C, in the expression of primary cilia and tumor progression

Fabbri, L. (2019) · theses.fr (ABES) · doi:10.70675/7a53239dzc652z4ea4z8b95z4a71961c83b4

Rôle du complexe VDAC1/TSPO1 au cours de l'érythropoïèse humaine, focus sur la mitophagie

Moras, M. (2020) · theses.fr (ABES) · doi:10.70675/a4c63cc2z949az4474zb1acz38e7f433fd35

Rôle de la signalisation calcique dans les troubles métaboliques associés à la dysfonction myocardique

Lacôte, M. (2018) · theses.fr (ABES) · doi:10.70675/bc9b8426z5718z40e1zadc2zaa52fb20a6fd

Involvements of Bcl-2 family of proteins during early zebrafish development

Popgeorgiev, N. (2011) · theses.fr (ABES) · doi:10.70675/d1fa4100z5c50z4a30z9f26z0ee43285ce5f

Rôles des régulateurs de l’apoptose Bcl-wav et Nrz, au cours du développement embryonnaire du poisson zèbre

Prudent, J. (2011) · theses.fr (ABES) · doi:10.70675/1f03460cze5d6z42c6za18ez352e34a4dee4

Bcl2L10 : polymorphisme, résistance oncogénique et conséquences thérapeutique dans le cancer du sein

Quang, D. M. (2021) · theses.fr (ABES) · doi:10.70675/86dd7fafzcb40z4cedz8eb7zbb41268cd809

Etude du rôle de la mitophagie et de la tafazzin dans la résistance des cellules cancéreuses du sein à la doxorubicine

Pour, S. T. A. (2021) · theses.fr (ABES) · doi:10.70675/5882b58ez88ecz44d2zaa23z5ad03d04e88c

Étude d’une mitofusine atypique impliquée dans la dynamique mitochondriale chez Trypanosoma brucei

Morel, C. (2023) · theses.fr (ABES) · doi:10.70675/4d52b50cz10fdz40a4zb0ebze752bb950b89

Développement de peptides ciblant VDAC pour l’étude et le traitement de maladies démyélinisantes

Jacquard, M. F. (2023) · theses.fr (ABES) · doi:10.70675/33c8bd67z22cfz47b0zb14bz58b975b2f7d4

Membrane protein structure and dynamics probed by MicroED

Paz, O., & Gonen, T. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250098

Functional exploration of mitochondrial carrier family proteins in faba bean for drought tolerance improvement

Zhang, Z.-H., Liu, C.-Y., Chen, H., Li, L., Zhao, Y.-G., Xiang, X., Wei, W.-H., & Sha, A.-H. (2026) · Plant Science · doi:10.1016/j.plantsci.2026.113211

Small molecule inhibition of voltage dependent anion channel 1 reroutes mitochondrial metabolite flux

Modaresi, S. M., Zhang, L., Saei, A. A., Degen, M., Khavani, M., Gharibi, H., Végvári, Á., Ye, Z., Zhang, J., Pavlov, E. V., et al. (2026) · Molecules and Cells · doi:10.1016/j.mocell.2026.100369

Analysis of the Kinetics of Folding and Insertion of β-Barrel Membrane Proteins by Gel-Electrophoresis

Hoppe, J., Marszal, A., Herwig, S., Schüßler, A., & Kleinschmidt, J. H. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5054-7_7

Elliptical β ‐barrel deformation underlies gating in VDAC1

Bergdoll, L. A., Elgeti, M., Belyaeva, J., Zlobin, A. S., Duneau, J., Hubbell, W. L., & Abramson, J. (2026) · Protein Science · doi:10.1002/pro.70677

The TOM Complex in the Outer Membrane of Mitochondria: A Supramolecular Assembly for Protein Import

Nußberger, S., Ghosh, R., & Wang, S. (2026) · Advances in experimental medicine and biology · doi:10.1007/978-3-032-26629-3_5

Inhibiting VDAC1 oligomerization attenuated cerebral ischemia-reperfusion injury by promoting mitophagy via reduced LONP1 interaction

Guo, X., Jiang, H., Lu, Y., Lin, Y., Liu, J., Qin, Z., & Tao, T. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.07.010

Field-driven peptide transport across the inner mitochondrial membrane via a transient membrane pore

Nguyen, S. V., & Vashisth, H. (2026) · The Journal of Chemical Physics · doi:10.1063/5.0349142

Cucumber Mosaic Virus Promotes Sphingolipid Biosynthesis to Alleviate Host Unfolded Protein Response ( UPR )‐Mediated Immunity

Yao, J., Wu, S., Gao, S., Xiang, Z., Wang, Q., Ye, F., Liao, Q., Gu, Z., & Du, Z. (2026) · Molecular Plant Pathology · doi:10.1111/mpp.70353

So similar, yet so different: α-synuclein recognition of the isoform-specific VDAC protein–lipid interfacePreprint

Rostovtseva, T. K., Rajendran, M., Rosencrans, W. M., Queralt-Martín, M., Wolfe, M. S., Bautista, N. A., Beyene, B. G., Larimi, M. G., Sodt, A. J., & Bezrukov, S. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.13.758914

Small-molecule modulation of VDAC enhances glucose-stimulated insulin secretion by promoting ATP flux

Matsunaga, K., Honda, K., Ali, M., Hameed, A., Inoue, R., Tsuno, T., Kin, T., Shapiro, A. M. J., Obinata, H., Kondoh, Y., et al. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.09.019

Mechanisms and Therapeutic Target Potential of Mitochondrial Voltage-Dependent Anion Channel 1 in Breast Cancer

李, 云. (2026) · Journal of Clinical Personalized Medicine · doi:10.12677/jcpm.2026.55378

Entwicklung von Lanthanoid-Tags für die biomolekulare NMR-Spektroskopie

Peters, F. (2011) · doi:10.53846/goediss-2066

Structure of the voltage dependent anion channel: state of the art

Pinto, V. D., Reina, S., Guarino, F., & Messina, A. A. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9140-3 · Cited by 75

The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating

Ujwal, R., Cascio, D., Colletier, J., Faham, S., Zhang, J., Toro, L., Ping, P., & Abramson, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809634105 · Cited by 566

Crystal structure of the murine Voltage Dependent Anion Channel 1 (mVDAC1) at 2.3 Å resolution

Ujwal, R., Cascio, D., Colletier, J., Faham, S., Zhang, J., Toro, L., Ping, P., & Abramson, J. (2009) · The FASEB Journal · doi:10.1096/fasebj.23.1_supplement.698.5

Magic Angle Spinning NMR Investigations of the Human Voltage Dependent Anion Channel

Eddy, M. T., Garces, R. G., van der Wel, P. C. A., Wagner, G., & Griffin, R. G. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.12.2090

Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer

Najbauer, E. E., Movellan, K. T., Giller, K., Benz, R., Becker, S., Griesinger, C., & Andreas, L. B. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c09848 · Cited by 36