Lukas K. Tamm

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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, 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

Our lab studies the structure and function of several membrane proteins of clinical importance in their natural membrane environment. We are also interested in the roles that membrane lipids play in the regulation of these proteins. Membrane proteins that play key roles in infectious and neurological diseases are of particular interest in our laboratory.
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

Our lab studies the structure and function of several membrane proteins of clinical importance in their natural membrane environment. We are also interested in the roles that membrane lipids play in the regulation of these proteins. Membrane proteins that play key roles in infectious and neurological diseases are of particular interest in our laboratory.

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

2023

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). 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

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

2013

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

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

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

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

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

2012

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

2011

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

2010

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

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

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

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

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

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