Lab website: http://pages.shanti.virginia.edu/Tamm_Lab/

Selected recent publications:

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).

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

Berhanu, S., Majumder, S., Müntener, T., Whitehouse, J., Berner, C., Bera, A. K., . . . Vorobieva, A. A. (2023). Sculpting conducting nanopore size and shape through de novo protein design.. bioRxiv. doi:10.1101/2023.12.20.572500

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), ar12. doi:10.1091/mbc.e23-06-0225

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

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., 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

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

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

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

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

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

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

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

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

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., & Tamm, L. (2018). Quaternary Structure of Small Amino Acids Transporter OprG of Pseudomonas aeruginosa. BIOPHYSICAL JOURNAL, 114(3), 236A-237A.

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

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

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

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

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

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

Tamm, L. K. (2017). Special Issue on Liposomes, Exosomes, and Virosomes. BIOPHYSICAL JOURNAL, 113(6), E1. doi:10.1016/j.bpj.2017.08.002

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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., Kiessling, V., & Tamm, L. K. (2013). Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 110(48), 19384-19389. doi:10.1073/pnas.1314699110

Zhuang, T., Chisholm, C., Chen, M., & Tamm, L. K. (2013). NMR-Based Conformational Ensembles Explain pH-Gated Opening and Closing of OmpG Channel. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 135(40), 15101-15113. doi:10.1021/ja408206e

Hong, H., Rinehart, D., & Tamm, L. K. (2013). Membrane Depth-Dependent Energetic Contribution of the Tryptophan Side Chain to the Stability of Integral Membrane Proteins. BIOCHEMISTRY, 52(25), 4413-4421. doi:10.1021/bi400344b

Gregory, S. M., White, J. M., & Tamm, L. K. (2013). Inhibition of Ebola Virus Entry through Biophysical Identification of Functionally Important Residues in the GP2 Fusion Loop. BIOPHYSICAL JOURNAL, 104(2), 384A. doi:10.1016/j.bpj.2012.11.2139

Wang, D. -N., Stieglitz, H., Marden, J., & Tamm, L. K. (2013). Benjamin Franklin, Philadelphia's Favorite Son, was a Membrane Biophysicist. BIOPHYSICAL JOURNAL, 104(2), 287-291. doi:10.1016/j.bpj.2012.12.028

Tamm, L. K. (2013). Lateral Membrane Diffusion Corralled. BIOPHYSICAL JOURNAL, 104(7), 1399-1400. doi:10.1016/j.bpj.2013.02.046

Kiessling, V., Ahmed, S., Domanska, M. K., Holt, M. G., Jahn, R., & Tamm, L. K. (2013). Rapid Fusion of Synaptic Vesicles with Reconstituted Target SNARE Membranes. BIOPHYSICAL JOURNAL, 104(9), 1950-1958. doi:10.1016/j.bpj.2013.03.038

Smith, E. C., Gregory, S. M., Tamm, L. K., Creamer, T. P., & Dutch, R. E. (2012). Role of Sequence and Structure of the Hendra Fusion Protein Fusion Peptide in Membrane Fusion. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(35), 30035-30048. doi:10.1074/jbc.M112.367862

Lai, A. L., Moorthy, A. E., Li, Y., & 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. JOURNAL OF MOLECULAR BIOLOGY, 418(1-2), 3-15. doi:10.1016/j.jmb.2012.02.010

Murray, D. H., & Tamm, L. K. (2011). Molecular Mechanism of Cholesterol- and Polyphosphoinositide-Mediated Syntaxin Clustering. BIOCHEMISTRY, 50(42), 9014-9022. doi:10.1021/bi201307u

Edrington, T. C., Kintz, E., Goldberg, J. B., & Tamm, L. K. (2011). Structural Basis for the Interaction of Lipopolysaccharide with Outer Membrane Protein H (OprH) from Pseudomonas aeruginosa. JOURNAL OF BIOLOGICAL CHEMISTRY, 286(45), 39211-39223. doi:10.1074/jbc.M111.280933

Gregory, S. M., Harada, E., Liang, B., Delos, S. E., White, J. M., & Tamm, L. K. (2011). Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 108(27), 11211-11216. doi:10.1073/pnas.1104760108

Lai, A. L., Tamm, L. K., Ellena, J. F., & Cafiso, D. S. (2011). Synaptotagmin 1 Modulates Lipid Acyl Chain Order in Lipid Bilayers by Demixing Phosphatidylserine. JOURNAL OF BIOLOGICAL CHEMISTRY, 286(28), 25291-25300. doi:10.1074/jbc.M111.258848

Wan, C., Kiessling, V., Cafiso, D. S., & Tamm, L. K. (2011). Partitioning of Synaptotagmin I C2 Domains between Liquid-Ordered and Liquid-Disordered Inner Leaflet Lipid Phases. BIOCHEMISTRY, 50(13), 2478-2485. doi:10.1021/bi101864k

Arouri, A., Kiessling, V., Tamm, L., Dathe, M., & Blume, A. (2011). Morphological Changes Induced by the Action of Antimicrobial Peptides on Supported Lipid Bilayers. JOURNAL OF PHYSICAL CHEMISTRY B, 115(1), 158-167. doi:10.1021/jp107577k

Murray, D. H., & Tamm, L. K. (2010). Syntaxin Clustering in Membranes. BIOPHYSICAL JOURNAL, 98(3), 616A. doi:10.1016/j.bpj.2009.12.3361

Lai, A. L., Li, Y., Cieslinska, A., & Tamm, L. K. (2010). Fusion Activity of HIV Gp41 Fusion Domain Is Related to its Secondary Structure. BIOPHYSICAL JOURNAL, 98(3), 671A. doi:10.1016/j.bpj.2009.12.3684

Lai, A. L., & Tamm, L. K. (2010). Shallow Boomerang-shaped Influenza Hemagglutinin G13A Mutant Structure Promotes Leaky Membrane Fusion. JOURNAL OF BIOLOGICAL CHEMISTRY, 285(48), 37467-37475. doi:10.1074/jbc.M110.153700

Domanska, M. K., Kiessling, V., Stein, A., Fasshauer, D., & Tamm, L. K. (2010). Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion. (vol 284, pg 32158, 2009). JOURNAL OF BIOLOGICAL CHEMISTRY, 285(15), 11753. doi:10.1074/jbc.A109.047381

Domanska, M. K., Kiessling, V., & Tamm, L. K. (2010). Fast Single Vesicle SNARE-Mediated Membrane Fusion Assay in Planar Supported Bilayers Reveals Details About Fusion Mechanism. BIOPHYSICAL JOURNAL, 98(3), 669A. doi:10.1016/j.bpj.2009.12.3678

Kiessling, V., Domanska, M. K., & Tamm, L. K. (2010). Single SNARE-Mediated Vesicle Fusion Observed In Vitro by Polarized TIRFM. BIOPHYSICAL JOURNAL, 99(12), 4047-4055. doi:10.1016/j.bpj.2010.10.022

Domanska, M. K., Kiessling, V., & Tamm, L. K. (2010). Docking and Fast Fusion of Synaptobrevin Vesicles Depends on the Lipid Compositions of the Vesicle and the Acceptor SNARE Complex-Containing Target Membrane. BIOPHYSICAL JOURNAL, 99(9), 2936-2946. doi:10.1016/j.bpj.2010.09.011

Wan, C., Kiessling, V., & Tamm, L. K. (2010). Lipid Targeting of Synaptotagmin I C2 Domains on Asymmetric Two-Phase Planar Bilayers. BIOPHYSICAL JOURNAL, 98(3), 483A. doi:10.1016/j.bpj.2009.12.2628