Lukas K. Tamm
- Phone: 434-982-3578; 434-982-3281
- Website: https://med.virginia.edu/tamm-lab/
Primary Appointment
Harrison Professor and Director Center for Membrane and Cell Physiology, Molecular Physiology and Biological Physics
Education
- Grad Res, Biochem and Biophysics, Cornell University
- Dipl Biol II, Biological Sciences, University of Basel
- PhD, Biophysics, University of Basel
- Postdoc-Res, Biophysics, Stanford University
Research Disciplines
Biochemistry, Biophysics, Biophysics & Structural Biology, Cell and Developmental Biology, Infectious Diseases/Biodefense, Microbiology, Molecular Biology, Physiology, Structural Biology, Translational Science
Research Interests
Biomembrane Structure and Function; Cell Entry of Enveloped Viruses; Neurosecretion by Exocytosis; Structure of Bacterial Pathogen Membrane Proteins; Lipid-Protein Interactions
Research Description
We investigate the entry of several enveloped viruses into cells, including influenza virus, human immunodeficiency virus, and Ebola virus. The mechanism of membrane fusion in this process and finding viral entry inhibitors are of particular interest.
We study the mechanism of neurotransmitter release at the synapse and its regulation by calcium. We are interested in elucidating the mechanism of exocytosis in neurons and insulin secreting cells by SNARE-mediated membrane fusion and the calcium control of this process by synaptotagmin. To this end, we use life-cell microscopy and ultrafast single particle tracking. The outcomes of these studies help to better understand neurological and neurodegenerative diseases, as well as diabetes.
Gram-negative bacteria like E.coli and Pseudomonas are enveloped by two membranes. We study channels of the outer membranes of these bacteria and their contribution to antibiotic resistance. Of particular interest is to understand and control the gating of the nanopores of OmpG from E. coli. Studies on the structure, lipid, and drug interactions OprG and OprH from Pseudomonas aeruginosa will help understanding the high antibiotic resistance of this serious human pathogen.
List of Publications in Pubmed
Personal Statement
Membrane Fusion in Viral Infection
We are studying the entry of several viruses into cells, including:
- Influenza virus
- Human immunodeficiency virus
- Ebola virus
Membrane Fusion in Neurotransmitter Release
We study the mechanism of neurotransmitter release at the synapse and its regulation by calcium.
- Synaptic exocytosis by SNARE-mediated membrane fusion
Calcium control by synaptotagmin
Ultrafast single particle tracking by live-cell microscopy
Relation to neurological and neurodegenerative diseases
Structure-Function-Dynamics-Antibiotic Interactions of Membrane Channels from Pathogenic Bacteria
Gram-negative bacteria like E. coli and Pseudomonas are enveloped by two membranes. We study channels of the outer membranes of these bacteria and their contribution to antibiotic resistance.
- Gating of OmpA and OmpG from E. coli
Structure, lipid, and drug interactions of Oprâs from Ps. aeruginosa
NMR spectroscopy and drug screening
Lab website: http://pages.shanti.virginia.edu/Tamm_Lab/
Selected recent publications:
Hong, H., Szabo, G., and Tamm, L.K. (2006) Electrostatic side-chain couplings in the gating of the OmpA ion channel suggest a mechanism for pore opening. Nature Chem. Biol. 11:627-635.
Liang, B. and Tamm, L.K. (2007) Structure of outer membrane protein G by solution NMR. Proc. Natl. Acad. Sci. USA 104:16140-16145.
Ellena, J., Liang, B., Wiktor, M. Cafiso, D.S., Jahn, R., and Tamm, L.K. (2009) Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. Proc. Natl. Acad. Sci. USA 106:20306-20311.
Kiessling, V., Domanska, M.K., and Tamm, L.K. (2010) Single SNARE-mediated vesicle fusion observed in vitro by polarized TIRFM. Biophys. J. 99:4047-4055.
Gregory, S.M., Harada,E., Liang, B., Delos, S.E., Judith M. White, J.M. and Tamm, L.K. (2011) Structure and function of the complete internal fusion loop from Ebolavirus GP2. Proc. Natl. Acad. Sci. USA 108, 11211-11216.
Edrington, T.C., Kintz, E., Goldberg, J.B., and Tamm, L.K. (2011) Structural basis for the interaction of lipopolysaccharide with the outer membrane protein OprH from Pseudomonas aeruginosa. J. Biol. Chem. 286, 39211-39223.
Lai, A.L. Moorthy, A,E., Li, Y, and Tamm, L.K. (2012) Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion. J. Mol. Biol. 418, 3-15 (on cover).
Training
- Biodefense & Infectious Diseases Short-Term Training to Increase Diversity in Biomedical Sciences
- Biotechnology Training Grant
- Training in Cell and Molecular Biology
- Training in Molecular Biophysics
Selected Publications
2025
Preobraschenski J, Kreutzberger AJB, Ganzella M, MuÌnster-Wandowski A, Kreutzberger MAB, Oolsthorn LHM, Seibert S, Kiessling V, Riedel D, Witkowska A, Ahnert-Hilger G, Tamm LK, Jahn R (2025). Synaptophysin accelerates synaptic vesicle fusion by expanding the membrane upon neurotransmitter loading. Science Advances, in press.
Kraichely K, Sandall CA, Liang B, Kiessling V, Tamm LK (2025). Functionally distinct SNARE motifs of SNAP25 cooperate in SNARE assembly and membrane fusion. Biophys J 124:637-650. doi: 10.1016/j.bpj.2024.12.034.
2024
Doyle CA, Busey GW, Iobst WH, Kiessling V, Renken C, Doppalapudi H, Stremska ME, Manjegowda MC, Arish M, Wang W, Naphade S, Kennedy J, Bloyet LM, Thompson CE, Rothlauf PW, Stipes EJ, Whelan SPJ, Tamm LK, Kreutzberger AJB, Sun J, Desai BN (2024). Endosomal fusion of pH-dependent enveloped viruses requires ion channel TRPM7. Nature Communications 15:8479. https://doi.org/10.1038/s41467-024-52773-w. PMID: 39353909
Berhanu, S., Majumder, S., Müntener, T., Whitehouse, J., Berner, C., Bera, A. K., . . . Vorobieva, A. A. (2024). Sculpting conducting nanopore size and shape through de novo protein design.. SCIENCE, 385(6706), 282-288. doi:10.1126/science.adn3796
Amos, C., Kiessling, V., Kreutzberger, A. J. B., Schenk, N. A., Mohan, R., Nyenhuis, S., . . . Tamm, L. K. (2024). Membrane lipids couple synaptotagmin to SNARE-mediated granule fusion in insulin-secreting cells. MOLECULAR BIOLOGY OF THE CELL, 35(3). doi:10.1091/mbc.E23-06-0225
Jahn, R., Cafiso, D. C., & Tamm, L. K. (2024). Mechanisms of SNARE proteins in membrane fusion. NATURE REVIEWS MOLECULAR CELL BIOLOGY, 25(2), 101-118. doi:10.1038/s41580-023-00668-x
2023
White, J. M., Ward, A. E., Odongo, L., & Tamm, L. K. (2023). Viral Membrane Fusion: A Dance Between Proteins and Lipids. ANNUAL REVIEW OF VIROLOGY, 10, 139-161. doi:10.1146/annurev-virology-111821-093413
Odongo, L., Habtegebrael, B. H., Kiessling, V., White, J. M., & Tamm, L. K. (2023). A novel in vitro system of supported planar endosomal membranes (SPEMs) reveals an enhancing role for cathepsin B in the final stage of Ebola virus fusion and entry. MICROBIOLOGY SPECTRUM, 11(5). doi:10.1128/spectrum.01908-23
Ward, A. E., Sokovikova, D., Waxham, M. N., Heberle, F. A., Levental, I., Levental, K. R., . . . Tamm, L. K. (2023). Serinc5 Restricts HIV Membrane Fusion by Altering Lipid Order and Heterogeneity in the Viral Membrane. ACS INFECTIOUS DISEASES, 9(4), 773-784. doi:10.1021/acsinfecdis.2c00478
Odongo, L., Zadrozny, K. K., Diehl, W. E., Luban, J., White, J. M., Ganser-Pornillos, B. K., . . . Pornillos, O. (2023). Purification and structure of luminal domain C of human Niemann-Pick C1 protein. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 79, 45-50. doi:10.1107/S2053230X23000705
2022
Crawford, M. A., Ward, A. E., Gray, V., Bailer, P., Fisher, D. J., Kubicka, E., . . . Hughes, M. A. (2022). Disparate Regions of the Human Chemokine CXCL10 Exhibit Broad-Spectrum Antimicrobial Activity against Biodefense and Antibiotic-Resistant Bacterial Pathogens. ACS INFECTIOUS DISEASES. doi:10.1021/acsinfecdis.2c00456
Liang, Q., Ofosuhene, A. P., Kiessling, V., Liang, B., Kreutzberger, A. J. B., Tamm, L. K., & Cafiso, D. S. (2022). Complexin-1 and synaptotagmin-1 compete for binding sites on membranes containing PtdInsP2. BIOPHYSICAL JOURNAL, 121(18), 3370-3380. doi:10.1016/j.bpj.2022.08.023
Cabot, M., Kiessling, V., White, J. M., & Tamm, L. K. (2022). Endosomes supporting fusion mediated by vesicular stomatitis virus glycoprotein have distinctive motion and acidification. TRAFFIC, 23(4), 221-234. doi:10.1111/tra.12836
2021
Vorobieva, A. A., White, P., Liang, B., Horne, J. E., Bera, A. K., Chow, C. M., . . . Baker, D. (2021). De novo design of transmembrane β barrels. SCIENCE, 371(6531), 801-+. doi:10.1126/science.abc8182
Nyenhuis, S. B., Karandikar, N., Kiessling, V., Kreutzberger, A. J. B., Thapa, A., Liang, B., . . . Cafiso, D. S. (2021). Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact. NATURE COMMUNICATIONS, 12(1). doi:10.1038/s41467-021-21090-x
Lee, J., Kreutzberger, A. J. B., Odongo, L., Nelson, E. A., Nyenhuis, D. A., Kiessling, V., . . . Tamm, L. K. (2021). Ebola virus glycoprotein interacts with cholesterol to enhance membrane fusion and cell entry. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 28(2), 181-+. doi:10.1038/s41594-020-00548-4
Narahari, A. K., Kreutzberger, A. J. B., Gaete, P. S., Chiu, Y. -H., Leonhardt, S. A., Medina, C. B., . . . Bayliss, D. A. (2021). ATP and large signaling metabolites flux through caspase-activated Pannexin 1 channels. ELIFE, 10. doi:10.7554/eLife.64787
2020
Kreutzberger, A. J. B., Kiessling, V., Doyle, C. A., Schenk, N., Upchurch, C. M., Elmer-Dixon, M., . . . Tamm, L. K. (2020). Distinct insulin granule subpopulations implicated in the secretory pathology of diabetes types 1 and 2. ELIFE, 9. doi:10.7554/eLife.62506
Ward, A. E., Kiessling, V., Pornillos, O., White, J. M., Ganser-Pornillos, B. K., & Tamm, L. K. (2020). HIV-cell membrane fusion intermediates are restricted by Serincs as revealed by cryo-electron and TIRF microscopy. JOURNAL OF BIOLOGICAL CHEMISTRY, 295(45), 15183-15195. doi:10.1074/jbc.RA120.014466
Bendahmane, M., Morales, A., Kreutzberger, A. J. B., Schenk, N. A., Mohan, R., Bakshi, S., . . . Anantharam, A. (2020). Synaptotagmin-7 enhances calcium-sensing of chromaffin cell granules and slows discharge of granule cargos. JOURNAL OF NEUROCHEMISTRY, 154(6), 598-617. doi:10.1111/jnc.14986
2019
Kreutzberger, A. J. B., Kiessling, V., Stroupe, C., Liang, B., Preobraschenski, J., Ganzella, M., . . . Tamm, L. K. (2019). In vitro fusion of single synaptic and dense core vesicles reproduces key physiological properties. NATURE COMMUNICATIONS, 10. doi:10.1038/s41467-019-11873-8
Gari, R. R. S., Seelheim, P., Liang, B., & Tamm, L. K. (2019). Quiet Outer Membrane Protein G (OmpG) Nanopore for Biosensing. ACS SENSORS, 4(5), 1230-1235. doi:10.1021/acssensors.8b01645
2018
Kiessling, V., Kreutzberger, A. B., Liang, B., Nyenhuis, S. B., Seelheim, P., Castle, J. D., . . . Tamm, L. K. (2018). A molecular mechanism for calcium-mediated synaptotagmin-triggered exocytosis. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 25(10), 911-+. doi:10.1038/s41594-018-0130-9
Gari, R. R. S., Seelheim, P., Marsh, B., Kiessling, V., Creutz, C. E., & Tamm, L. K. (2018). Quaternary structure of the small amino acid transporter OprG from Pseudomonas aeruginosa. JOURNAL OF BIOLOGICAL CHEMISTRY, 293(44), 17267-17277. doi:10.1074/jbc.RA118.004461
Liang, B., & Tamm, L. K. (2018). Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics. PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 105, 41-53. doi:10.1016/j.pnmrs.2018.02.001
Gari, R. R. S., Seelheim, P., Marsh, B., Kiessling, V., Creutz, C., & Tamm, L. (2018). Quaternary Structure of Small Amino Acids Transporter OprG of Pseudomonas aeruginosa. BIOPHYSICAL JOURNAL, 114(3), 236A-237A. Retrieved from https://www.webofscience.com/
2017
Blackburn, M. R., Hubbard, C., Kiessling, V., Bi, Y., Kloss, B., Tamm, L. K., & Zimmer, J. (2018). Distinct reaction mechanisms for hyaluronan biosynthesis in different kingdoms of life. GLYCOBIOLOGY, 28(2), 108-121. doi:10.1093/glycob/cwx096
Kreutzberger, A. J. B., Kiessling, V., Liang, B., Yang, S. -T., Castle, J. D., & Tamm, L. K. (2017). Asymmetric Phosphatidylethanolamine Distribution Controls Fusion Pore Lifetime and Probability. BIOPHYSICAL JOURNAL, 113(9), 1912-1915. doi:10.1016/j.bpj.2017.09.014
Tamm, L. K. (2017). Special Issue on Liposomes, Exosomes, and Virosomes. BIOPHYSICAL JOURNAL, 113(6), E1. doi:10.1016/j.bpj.2017.08.002
Kreutzberger, A. J. B., Kiessling, V., Liang, B., Seelheim, P., Jakhanwal, S., Jahn, R., . . . Tamm, L. K. (2017). Reconstitution of calcium-mediated exocytosis of dense-core vesicles. SCIENCE ADVANCES, 3(7). doi:10.1126/sciadv.1603208
Yang, S. -T., Kreutzberger, A. J. B., Kiessling, V., Ganser-Pornillos, B. K., White, J. M., & Tamm, L. K. (2017). HIV virions sense plasma membrane heterogeneity for cell entry. SCIENCE ADVANCES, 3(6). doi:10.1126/sciadv.1700338
Kucharska, I., & Tamm, L. K. (2017). Solution NMR Provides New Insight into Lipid-Protein Interaction. BIOCHEMISTRY, 56(33), 4291-4292. doi:10.1021/acs.biochem.7b00336
Zdanowicz, R., Kreutzberger, A., Liang, B., Kiessling, V., Tamm, L. K., & Cafiso, D. S. (2017). Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion. BIOPHYSICAL JOURNAL, 113(6), 1235-1250. doi:10.1016/j.bpj.2017.04.002
Sanganna Gari, R. R., Seelheim, P., Liang, B., & Tamm, L. (2017). Structural Investigations of Quiet Outer Membrane Protein G Nanopores. Biophysical Journal, 112(3), 459a. doi:10.1016/j.bpj.2016.11.2458
Chiu, Y. -H., Jin, X., Medina, C. B., Leonhardt, S. A., Kiessling, V., Bennett, B. C., . . . Bayliss, D. A. (2017). A quantized mechanism for activation of pannexin channels. Nature Communications, 8. doi:10.1038/ncomms14324
Lee, J., Patel, D. S., Kucharska, I., Tamm, L. K., & Im, W. (2017). Refinement of OprH-LPS Interactions by Molecular Simulations. BIOPHYSICAL JOURNAL, 112(2), 346-355. doi:10.1016/j.bpj.2016.12.006
Lee, J., Nyenhuis, D. A., Nelson, E. A., Cafiso, D. S., White, J. M., & Tamm, L. K. (2017). Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 114(38), E7987-E7996. doi:10.1073/pnas.1708052114
Kiessling, V., Liang, B., Kreutzberger, A. J. B., & Tamm, L. K. (2017). Planar Supported Membranes with Mobile SNARE Proteins and Quantitative Fluorescence Microscopy Assays to Study Synaptic Vesicle Fusion. FRONTIERS IN MOLECULAR NEUROSCIENCE, 10. doi:10.3389/fnmol.2017.00072
2016
Yang, S. -T., Lim, S. I., Kiessling, V., Kwon, I., & Tamm, L. K. (2016). Site-specific fluorescent labeling to visualize membrane translocation of a myristoyl switch protein. SCIENTIFIC REPORTS, 6. doi:10.1038/srep32866
Kucharska, I., Liang, B., Ursini, N., & Tamm, L. K. (2016). Molecular Interactions of Lipopolysaccharide with an Outer Membrane Protein from Pseudomonas aeruginosa Probed by Solution NMR. BIOCHEMISTRY, 55(36), 5061-5072. doi:10.1021/acs.biochem.6b00630
Liang, B., & Tamm, L. K. (2016). NMR as a tool to investigate the structure, dynamics and function of membrane proteins. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 23(6), 468-474. doi:10.1038/nsmb.3226
Yang, S. -T., Kreutzberger, A. J. B., Lee, J., Kiessling, V., & Tamm, L. K. (2016). The role of cholesterol in membrane fusion. CHEMISTRY AND PHYSICS OF LIPIDS, 199, 136-143. doi:10.1016/j.chemphyslip.2016.05.003
Kreutzberger, A. J. B., Liang, B., Kiessling, V., & Tamm, L. K. (2016). Assembly and Comparison of Plasma Membrane SNARE Acceptor Complexes. BIOPHYSICAL JOURNAL, 110(10), 2147-2150. doi:10.1016/j.bpj.2016.04.011
Yang, S. -T., Kiessling, V., & Tamm, L. K. (2016). Line tension at lipid phase boundaries as driving force for HIV fusion peptide-mediated fusion. NATURE COMMUNICATIONS, 7. doi:10.1038/ncomms11401
Seelheim, P., Kucharska, I., & Tamm, L. K. (2016). OprG Facilitates the Transport of Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa. BIOPHYSICAL JOURNAL, 110(3), 226A. doi:10.1016/j.bpj.2015.11.1248
Lee, J., Gregory, S. M., Nelson, E. A., White, J. M., & Tamm, L. K. (2016). The Roles of Histidines and Charged Residues as Potential Triggers of a Conformational Change in the Fusion Loop of Ebola Virus Glycoprotein. PLOS ONE, 11(3). doi:10.1371/journal.pone.0152527
2015
Kucharska, I., Seelheim, P., Edrington, T., Liang, B., & Tamm, L. K. (2015). OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa. STRUCTURE, 23(12), 2234-2245. doi:10.1016/j.str.2015.10.009
Kreutzberger, A. J. B., Kiessling, V., & Tamm, L. K. (2015). High Cholesterol Obviates a Prolonged Hemifusion Intermediate in Fast SNARE-Mediated Membrane Fusion. BIOPHYSICAL JOURNAL, 109(2), 319-329. doi:10.1016/j.bpj.2015.06.022
Yang, S. -T., Kiessling, V., Simmons, J. A., White, J. M., & Tamm, L. K. (2015). HIV gp41-mediated membrane fusion occurs at edges of cholesterol-rich lipid domains. NATURE CHEMICAL BIOLOGY, 11(6), 424-+. doi:10.1038/NCHEMBIO.1800
Kucharska, I., Edrington, T. C., Liang, B., & Tamm, L. K. (2015). Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins. JOURNAL OF BIOMOLECULAR NMR, 61(3-4), 261-274. doi:10.1007/s10858-015-9905-z
Kucharska, I., & Tamm, L. (2015). Prolines Around Hypothetical Active Site are Important for the Structure and Dynamics of the Outer Membrane Protein G from Pseudomonas Aeruginosa. Biophysical Journal, 108(2), 89a. doi:10.1016/j.bpj.2014.11.521
Kiessling, V., Yang, S. -T., & Tamm, L. K. (2015). Supported Lipid Bilayers as Models for Studying Membrane Domains. LIPID DOMAINS, 75, 1-23. doi:10.1016/bs.ctm.2015.03.001
Kiessling, V., Liang, B., & Tamm, L. K. (2015). Reconstituting SNARE-mediated membrane fusion at the single liposome level. BUILDING A CELL FROM ITS COMPONENT PARTS, 128, 339-363. doi:10.1016/bs.mcb.2015.02.005
2014
Tamm, L. K., Lee, J., & Liang, B. (2014). Capturing Glimpses of an Elusive HIV Gp41 Prehairpin Fusion Intermediate. STRUCTURE, 22(9), 1225-1226. doi:10.1016/j.str.2014.08.010
Hernandez, J. M., Kreutzberger, A. J. B., Kiessling, V., Tamm, L. K., & Jahn, R. (2014). Variable cooperativity in SNARE-mediated membrane fusion. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 111(33), 12037-12042. doi:10.1073/pnas.1407435111
Lu, B., Kiessling, V., Tamm, L. K., & Cafiso, D. S. (2014). The Juxtamembrane Linker of Full-length Synaptotagmin 1 Controls Oligomerization and Calcium-dependent Membrane Binding. JOURNAL OF BIOLOGICAL CHEMISTRY, 289(32), 22161-22171. doi:10.1074/jbc.M114.569327
Zhuang, T., & Tamm, L. K. (2014). Control of the Conductance of Engineered Protein Nanopores through Concerted Loop Motions. Angewandte Chemie, 126(23), 6007-6012. doi:10.1002/ange.201400400
Zhuang, T., & Tamm, L. K. (2014). Control of the Conductance of Engineered Protein Nanopores through Concerted Loop Motions. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 53(23), 5897-5902. doi:10.1002/anie.201400400
Marcoux, J., Politis, A., Rinehart, D., Marshall, D. P., Wallace, M. I., Tamm, L. K., & Robinson, C. V. (2014). Mass Spectrometry Defines the C-Terminal Dimerization Domain and Enables Modeling of the Structure of Full-Length OmpA. STRUCTURE, 22(5), 781-790. doi:10.1016/j.str.2014.03.004
Moissoglu, K., Kiessling, V., Wan, C., Hoffman, B. D., Norambuena, A., Tamm, L. K., & Schwartz, M. A. (2014). Regulation of Rac1 translocation and activation by membrane domains and their boundaries. JOURNAL OF CELL SCIENCE, 127(11), 2565-2576. doi:10.1242/jcs.149088
Gregory, S. M., Larsson, P., Nelson, E. A., Kasson, P. M., White, J. M., & Tamm, L. K. (2014). Ebolavirus Entry Requires a Compact Hydrophobic Fist at the Tip of the Fusion Loop. JOURNAL OF VIROLOGY, 88(12), 6636-6649. doi:10.1128/JVI.00396-14
Liang, B., Dawidowski, D., Ellena, J. F., Tamm, L. K., & Cafiso, D. S. (2014). The SNARE Motif of Synaptobrevin Exhibits an Aqueous-Interfacial Partitioning That Is Modulated by Membrane Curvature. BIOCHEMISTRY, 53(9), 1485-1494. doi:10.1021/bi401638u