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Erwin London, Ph.D.


Distinguished Professor
Department of Biochemistry and Cell Biology

420 Life Sciences Building
Stony Brook University
Stony Brook, NY 11794-5215

Office telephone: 631-632-8564


  • Research Description

    The Structure and Function of Cholesterol-Rich Membrane Domains

          Together with Dr. Deborah Brown in the Dept. Of Biochemistry and Cell Biology we have been studying the structure and function of lipid domains enriched in cholesterol and sphingolipid. These domains have been proposed to have a functional role in processes such as viral and toxin entry into cells, protein sorting among organelles, signal transduction, prion formation and amyloid formation. Our studies involve determining in artificial lipid vesicles the basic principles that drive the formation of these domains and regulate their lipid and protein composition.   We are also carrying out studies on these domains in mammalian cells (see below).

    Membrane Asymmetry:  Effect Upon Membrane Domains, Membrane Protein Function, and Drug Delivery

           A limitation of using artificial membranes has been that they lack lipid asymmetry, the difference in lipid composition in their inner and outer layers found in many natural membranes.  We invented a method to prepare asymmetric artificial vesicles that more closely mimic natural membranes using cyclodextrins, and are applying this methodology: to analyze the rules for domain formation in natural membranes, to examine how asymmetry affects amyloid formation (in collaboration with the lab of Dr. Daniel Raleigh), and to determine how asymmetric lipid vesicles (asymmetric liposomes) may have improved properties for delivery of drugs into cells. 

    Controlling Lipid Composition in Membranes of Living Cells

           The lab also has developed a method to efficiently replace the natural lipid composition of the outer leaflet of cell plasma membranes with other lipids using cyclodextrins.  Using this novel method we are studying domain formation in the plasma membrane of cells, and how its lipid composition influences the function of membrane proteins such as the insulin receptor (in collaboration with the lab of Dr. Todd Miller, Physiology and Biophysics).

  • Publications
    1. Publications 2000-2021

      1.         Xu, X., and London, E. (2000) “The Effect of Sterol Structure on Membrane Lipid Domains Reveals How Cholesterol Can Induce Lipid Domain Formation” Biochemistry 39, 844-849.

      2.         Brown, D.A., and London, E. (2000) “Structure and Function of Sphingolipid- and Cholesterol-rich Rafts” J. Biol. Chem. 275, 17221-17224.

      3.         Lew, S., and London, E. (2000) “The Effects of Polar and/or Ionizable Residues in the Core and Flanking Regions of Hydrophobic Helices on Transmembrane Conformation and Oligomerization” Biochemistry 39, 9632-9640.

      4.         London, E., Brown, D.A., and Xu, X. (2000) "Fluorescence Quenching Assay of Sphingolipid/Phospholipid Phase Separation" Meth. Enzymol. 312, 272-290.

      5.         London, E., and Brown, D.A. (2000) “Insolubility of Lipids in Triton X-100: Physical Origin and Relationship to Sphingolipid/Cholesterol Membrane Domains (rafts)” Biochim. Biophys. Acta 1508, 182-195.

      6.         Xu, X., Bittman, R., Duportail, G., Heissler, D., Vilcheze, C., and London, E. (2001) “Effect of the Structure of Natural Sterols and Sphingolipids on the Formation of Ordered Sphingolipid/Sterol Domains (Rafts): Comparison of Cholesterol to Plant, Fungal and Disease-Associated Sterols, and Comparison of Sphingomyelin, Cerebrosides and Ceramide” J. Biol. Chem. 276, 33540-33546.

      7.         Dhanvantari, S., Arnaoutova, I., Snell, C.R., Steinbach, P.J., Hammond, K., Caputo, G.A., London, E., and Loh, Y.P. (2002) “Carboxypeptidase E, a Prohormone Sorting Receptor, is Anchored to Secretory Granules Via a C-Terminal Transmembrane Insertion” Biochemistry 41, 52-60.

      8.         London, E., and Ladokhin, A.S. (2002) “Measuring the Depth of Amino Acid Residues in Membrane-Inserted Peptides by Fluorescence Quenching” in Current Topics in Membranes: Peptide-Lipid Interactions (Simon, S.A., and McIntosh, T.J. Eds.) Vol. 52 Academic Press, 89-115.

      9.         Hammond, K., Caputo, G.A., and London, E. (2002) “Interaction of the Membrane‑Inserted Diphtheria Toxin T Domain with Peptides and Its Possible Implications for Chaperone‑like T Domain Behavior” Biochemistry 41, 3243‑3253.

      10.       Rosconi, M.P., and London, E. (2002) “Topography of Helices 5-7 in Membrane-Inserted Diphtheria Toxin T Domain: Identification and Insertion Boundaries of Two Hydrophobic Sequences That Do Not Form a Stable Transmembrane Hairpin” J. Biol. Chem., 277, 16517-16527.

      11.       London, E. (2002) “Insights into Lipid Domain/Raft Structure and Formation from Experiments in Model Membranes” Curr. Opin. Struct. Bio., 12, 480-486.

      12.       Caputo, G.A., and London, E. (2003) “Using a Novel Dual Fluorescence Quenching Assay for Measurement of Trp Depth Within Lipid Bilayers to Determine Hydrophobic Alpha-Helix Locations Within Membranes” Biochemistry 42, 3265-3274.

      13.       Caputo, G.A., and London, E. (2003) “Cumulative Effects of Amino Acid Substitutions and Hydrophobic Mismatch Upon the Transmembrane Stability and Conformation of Hydrophobic Alpha-Helices” Biochemistry 42, 3275-3285.

      14.       Lew, S., Caputo, G.A., and London, E. (2003) “The Effect of Interactions Involving Ionizable Residues Flanking Membrane-Inserted Hydrophobic Helices Upon Helix-Helix Interaction” Biochemistry 42, 10833-10842.

      15.       Fastenberg, M.E., Shogomori, H., Xu, X., Brown, D.A., and London, E. (2003) “Exclusion of a Transmembrane-Type Peptide from Ordered Lipid Domains (Rafts) Detected by Fluorescence Quenching: Extension of Quenching Analysis to Account for the Effects of Domain Size and Domain Boundaries” Biochemistry 42, 12376-12390.

      16.       Wang, J., Megha, and London, E. (2004) “Relationship Between Sterol/Steroid Structure and Participation in Ordered Lipid Domains (Lipid Rafts): Implications for Lipid Raft Structure and Function” Biochemistry 43, 1010-1018.

      17.       Megha, and London, E. (2004) “Ceramide Displaces Cholesterol From Ordered Lipid Domains (Rafts): Implications for Raft Structure and Function” J. Biol. Chem. 279, 9997-10004. Selected as a Faculty of 1000 article.

      18.       Caputo, G.A., and London, E. (2004) “The Position and Ionization State of Asp Residues in the Hydrophobic Core of Membrane Inserted alpha-Helices Can Control Both the Equilibrium Between Transmembrane Topography and Non-Transmembrane Topography and Transmembrane Helix Positioning in the Bilayer” Biochemistry 43, 8794-8806.

      19.       Rosconi, M.P., Zhao, G., and London, E. (2004) “Analyzing Topographical Equilibria for Membrane-Inserted Diphtheria Toxin T Domain Using BODIPY-Streptavidin:  At Low pH Helices 8 and 9 form a Stable Transmembrane Hairpin But Helices 5-7 Form Stable Non-Classical Inserted Segments that Remain on the Cis Side of the Bilayer” Biochemistry 43, 9127-9139.  

      20.       London, E. (2004) “Lipid Bilayer Structure” in Encyclopedia of Biological Chemistry (W.J. Lennarz and M.D. Lane Eds.) Elsevier Science USA, San Diego, CA. pp 576-579.

      21.       Ryndak, M. B., London, E., and Bliska, J.B. (2005) “Role of Predicted Transmembrane Domains for Type III Translocation, Pore Formation and Signaling by the Yersinia pseudotuberculosis YopB protein” Infection and Immunity 73, 2433-2443.

      22.       Hayashibara, M., and London, E. (2005) “Topography of Diphtheria Toxin A Chain Inserted into Lipid Vesicles” Biochemistry 44, 2183-2196.

      23.       Zhao, G., and London, E. (2005) “Behavior of Diphtheria Toxin T Domain Containing Substitutions That Block Normal Membrane Insertion at Pro345 and Leu307:  Control of Deep Membrane Insertion and Coupling Between Deep Insertion of Hydrophobic Sub-Domains” Biochemistry 44, 4448-4498.

      24.       Shogomori, H., Hammond, A.T., Ostermeyer-Fay, A.G., Barr, D.J., Feigenson, G.W., London, E., and Brown, D.A. (2005) “Palmitoylation and Intracellular Domain Interactions Both Contribute to Raft Targeting of Linker for Activation of T Cells (LAT)” J. Biol. Chem. 280, 18931-18942.

      25.       London, E. (2005) “How Principles of Domain Formation in Model Membranes May Explain Ambiguities Concerning Lipid Raft Formation in Cells” Biochim. Biophys. Acta 1746, 203-220.

      26.       Musse, A.A., Wang, J., deLeon, G.P., Prentice, G.A., London, E., and Merrill, A.R. (2006) "Scanning the Membrane-Bound Conformation of Helix 1 in the Colicin E1 Channel Domain by Site-Directed Fluorescence Labeling" J. Biol. Chem. 281, 885-895.

      27.       Wang, J., Rosconi, M.P., and London, E. (2006) "The Topography of the Hydrophilic Helices of Membrane-Inserted Diphtheria Toxin T Domain:  TH 1-3 As a Hydrophilic Tether" Biochemistry 45, 8124-8134.

      28.       Zhao, G., and London, E. (2006) “An Amino Acid Transmembrane Tendency Scale that Approaches the Theoretical Limit to Accuracy for Prediction of Transmembrane Helices:  Relationship to Biological Hydrophobicity Scale” Protein Science 15, 1987-2001.

      29.       Megha, Bakht, O., and London, E. (2006) "Cholesterol Precursors Stabilize Ordinary and

      Ceramide-Rich Ordered Lipid Domains (Lipid Rafts) to Different Degrees:  Implications for the Bloch Hypothesis and Sterol Biosynthesis Disorders" J. Biol. Chem. 281, 21903-21913.

      30.      Wu, Z., Jakes, K.S., Samuelson-Jones, B., Lai, B., Zhao, G., London, E., and Finkelstein,             A. (2006) “Protein Translocation by Bacterial Toxin Channels: A Comparison of

                  Diphtheria Toxin and Colicin Ia” Biophys. J. 91, 3249-3256.


      31.       White, D., Musse, A.A., Wang, J., London, E., and Merrill A.R. (2006) “Toward Elucidating the Membrane Topography of Helix 2 of the Colicin E1 Channel Domain” J. Biol. Chem. 281, 32375-32384.

      32.      Fujita, K., Krishnakumar, S.S., Franco, D., Paul, A.V., London, E., and Wimmer, E. (2007) “Membrane Topography of the Hydrophobic Anchor Sequence of Poliovirus 3A and 3AB Proteins and the Functional Effect of 3A/3AB Membrane Association Upon RNA Replication” Biochemistry 46, 5185-5199.  

      33.       Bakht, O., and London, E. (2007) “Detecting Ordered Domain Formation (Lipid Rafts) in Model Membranes Using Tempo” in Methods in Molecular Biology Volume 398: Lipid Rafts (McIntosh, T.J. Ed.) Humana Press, Totowa, NJ. p 29-40.

      34  .     London. E. (2007) “Using Model Membrane-Inserted Hydrophobic

      Helices to Study the Equilibrium Between Transmembrane and Non-Transmembrane States” J. Gen. Physiol. 130, 229-232.

      35.      Megha, Sawatzki, P., Kolter, T., Bittman, R., and London, E. (2007) “Effect of

      Ceramide N-acyl Chain and Polar Headgroup Structure on the Properties of Ordered Lipid Domains (Lipid Rafts)” Biochim. Biophys. Acta 1768, 2205-2212.

      36.     Bakht, O., Delgado, J., Amat-Guerri, F., Acuña, A.U., and London, E. (2007) “The 

      Phenyltetraene Lysophospholipid Analog PTE-ET-18-OMe as a Fluorescent Anisotropy Probe of Liquid Ordered Membrane Domains (Lipid Rafts) and Ceramide-Rich Membrane Domains” Biochim. Biophys. Acta 1768, 2213-2221.

      37.       Krishnakumar, S.S., and London, E. (2007) “Effect of Sequence Hydrophobicity and Bilayer Width Upon the Minimum Length Required for Formation of Transmembrane Helices in Membranes” J. Mol. Biol. 374, 671-687.

      38.       Krishnakumar, S.S., and London, E. (2007) “The Control of Transmembrane Helix

      Transverse Position Within Membranes by Hydrophilic Residues” J. Mol. Biol. 374, 1251–1269.

      39.       Bakht, O., Pathak, P., and London, E. (2007) “Effect of the Structure of Lipids Favoring

      Disordered Domain Formation on the Stability of Cholesterol-Containing Ordered Domains (Lipid Rafts): Identification of Multiple Raft-Stabilization Mechanisms” Biophys. J. 93, 4302-4318.

      40.       Nelson, L.D., Johnson, A.E., and London, E. (2008) “Interaction of Perfringolysin O with Membranes is Controlled by Sterol Structure, Lipid Structure and Physiological Low pH: Insights into the Origin of Perfringolysin O-Lipid Raft Interaction” J. Biol. Chem. 283, 4632-4642. 

      41.       Lai, B., Zhao, G., and London, E.  (2008) “Mutations Inhibiting Deep Membrane Insertion of Diphtheria Toxin T Domain Show That Deeply Inserted Helices 5 and 8-9 Interact Strongly and Promote in Pore Formation While Deep Insertion of TH 6/7 Limits Pore Formation” Biochemistry 47, 4565-4574.

      42.      Drover, V.A., Nguyen, D.V., Bastie, C.C., Darlington, Y.F., Abumrad, N.A, Pessin, J.E.,  

      London, E., Sahoo, D., and Phillips, M.C. (2008) “CD36 Mediates Both Cellular Uptake of Very Long Chain Fatty Acids and Their Intestinal Absorption in Mice” J. Biol. Chem. 283, 13108-13115.

      43.       Shahidullah, K., and London, E. (2008) “Effect of Lipid Composition on the Topography of Membrane-Associated Hydrophobic Helices: Stabilization of Transmembrane Topography by Anionic Lipids” J. Mol. Biol. 379, 704-718.

      44.       Cheng, H.-T., Megha, and London, E. (2009) “Preparation and Properties of Asymmetric Vesicles That Mimic Cell Membranes:  Implications for Lipid Raft Formation and Transmembrane Helix Orientation” J. Biol. Chem.  284, 6079-6092.

      45.      Zhao, G., and London, E. (2009) “Strong Correlation Between Statistical Transmembrane

      Tendency and Experimental Hydrophobicity Scales for Identification of Transmembrane Helices” J. Memb. Bio. 229, 165-168.

      46.       Shahidullah, K., and London, E. (2009) “Transmembrane vs. Non-Transmembrane Hydrophobic Helix Topography in Model and Natural Membranes” Curr. Opin. Struct. Bio. 19, 464-472.

      47.      Wang, J., and London, E. (2009) “The Membrane Topography of Diphtheria Toxin

      T Domain Linked to the A Chain Reveals a Transient Transmembrane Hairpin and Potential Translocation Mechanisms” Biochemistry 48, 10446–10456.

      48.      Shahidullah, K., Krishnakumar, S.S., and London, E. (2010) “The Effect of Hydrophilic

      Substitutions and Anionic Lipids Upon the Transverse Positioning of the Transmembrane Helix of the Erb b2 (neu) Protein Incorporated into Model Membrane Vesicles” J. Mol. Biol., 396, 209-220.  

      49.       Lai, B., Agarwal, R., Nelson, L.D., Swaminathan, S., and London, E. (2010) “Low pH        Induced Pore Formation by the T Domain of Botulinum Toxin Type A is Dependent Upon NaCl Concentration” J. Memb. Bio. 236, 191-201.

      50.      LaRocca, T.J., Crowley, J.T., Cusack, B.J., Pathak, P., Benach, J., London, E., Garcia-

      Monco, J.C., and Benach, J.L. (2010) “Cholesterol lipids of Borrelia burgdorferi participate in lipid raft formation and are required for the bactericidal activity of a complement-independent antibody” Cell, Host and Microbe 8, 331-342.

      51.      Nelson, L.D., Chiantia, S., and London, E. (2010) “Perfringolysin O Association with          Ordered Lipid Domains:  Implications for Transmembrane Protein Raft Affinity”        Biophys. J. 99, 3255-3263.

      52.      Chiantia, S., Schwille, P., Klymchenko, A.S., and London, E. (2011) “Asymmetric GUVs   Prepared by MßCD-Mediated Lipid exchange: an FCS Study” Biophys. J. 100, L1-L3.

      53.     Cheng, H.T., and London, E. (2011) “Preparation and Properties of Asymmetric Large       Unilamellar Vesicles: Interleaflet Coupling in Asymmetric Vesicles is Dependent Upon  

                  Temperature but Not Curvature” Biophys. J. 100, 2671-2678.

      54.       Pathak, P., and London, E. (2011) “Measurement of Lipid Nanodomain (Raft) Formation and Size in Sphingomyelin/POPC/Cholesterol Vesicles Shows TX-100 and           Transmembrane Helices Increase Domain Size by Coalescing Pre-Existing

      Nanodomains, But DO NOT Induce Domain Formation” Biophys. J. 101, 2417-2425.

      55.      Kaczocha, M., Lin, Q, Nelson, L.D., McKinney, M.K., Cravatt, B.F., London, E., and

                  Deutsch, D.G. (2012) “Anandamide Externally-added to Lipid Vesicles Containing

      trapped Fatty Acid Amide Hydrolase (FAAH) is Readily Hydrolyzed in a Sterol-modulated Fashion” ACS Chemical Neuroscience 3, 364-368.     

      56.       Chiantia, S., Klymchenko, A.S., and London, E. (2012) “A Novel Leaflet-Selective Fluorescence Labeling Technique Reveals Differences between Inner and Outer Leaflets at High Bilayer Curvature” Biochim. Biophys. Acta 1818, 1284-1290.

      57.       Chiantia, S., and London, E. (2012) “Acyl Chain Length and Saturation Modulate

      Interleaflet Coupling in Asymmetric Bilayers: Effects on Dynamics and Structural Order” Biophys. J. 103, 2311-2319. 

      58.      Son, M., and London, E. (2013) “The Dependence of Lipid Asymmetry Upon

      Phosphatidylcholine Acyl Chain Structure” J. Lipid Res. 54, 223-231.

      59.       Lin, Q., and London E. (2013) “Altering Hydrophobic Sequence Lengths Shows That

      Hydrophobic Mismatch Controls Affinity for Ordered Lipid Domains (rafts) in the Multi-Transmembrane Strand Protein Perfringolysin O”, J. Biol. Chem. 288, 1340–1352.

      60.       Chiantia, S., and London, E. (2013) “Lipid Bilayer Asymmetry” in Encyclopedia of Biophysics 2nd ed (Roberts. G.C.K. Ed.)  Springer-Verlag. Heidelberg: Berlin, pp. 1250-1253.

      61.      Caputo, G.A., and London, E. (2013) “Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching” in Methods in Molecular Biology series Volume 974, Lipid-Protein Interactions: Methods and Protocols (Kleinschmidt, J.H. Ed.) Humana Press/Springer, New York, pp. 279-295.

      62.       Crowley, J.T. Toledo, A.M., LaRocca, T.J., Coleman, J.L., London, E., and Benach, J.L. (2013) “Lipid Exchange between Borrelia burgdorferi and host cells” PLoS Pathogens 9, e1003109.

      63.       Chiantia, S., and London, E. (2013) “Sphingolipids and Membrane Domains: Recent

      Advances” in Handbook of Experimental Pharmacology:Sphingolipids

      in Health and Disease (Gulbins, E., and Petrache, I. Eds.)  Volume 215, pp 33-55 Springer, New York.

      64.       LaRocca, T.J., Pathak, P., Chiantia, S., Toledo, A., Silvius, J.R., Benach, J.L., and           London, E. (2013) “Proving Lipid Rafts Exist: Membrane Domains in the Prokaryote

      Borrelia burgdorferi Have the Same Properties as Eukaryotic Lipid Rafts” PLoS Pathogens, 9, e1003353.

      65.       Su, C.-Y., London, E., and Sampson, N.S. (2013) “Mapping peptide thiol accessibility in

      membranes using a quarternary ammonium isotope-coded mass tag (ICMT)” Bioconjugate Chemistry 24, 1235-1247.

      66.      Son, M., and London, E. (2013) “The Dependence of Lipid Asymmetry Upon Polar

      Headgroup Structure” J. Lipid Res. 54, 3385-3393.  

      67.      Huang, Z., and London, E. (2013) “Effect of Cyclodextrin and Membrane Lipid Structure 

      upon Cyclodextrin-Lipid Interaction” Langmuir 29, 14631-14638.

      68.      Lin, Q., and London, E. (2013) “Transmembrane Protein (Perfringolysin O) Association

      with Ordered Membrane Domains (Rafts) Depends Upon the Raft-Associating Properties of the Protein-Bound Sterol” Biophys. J. 105, 2733-2742.

      69.       Lin, Q., and London, E. (2014) “Preparation of Artificial Plasma Membrane Mimicking

      Vesicles With Lipid Asymmetry” PLoS ONE 9, e87903.

      70.       Lin, Q., and London, E. (2014) “The Influence of Lipid Asymmetry Upon the

      Conformation of a Membrane-Inserted Protein (Perfringolysin O)” J. Biol. Chem. 289, 5467–5478.

      71.      Toledo, A., Crowley, J.T., Coleman, J.L., LaRocca, T.J., Chiantia, S., London, E., and

      Benach, J.L. (2014) “Selective Association of the Outer Surface Lipoproteins With the Lipid Rafts of Borrelia burgdorferimBio 5, e00899-14.

      72.       Lin, Q., and London, E. (2015) “Ordered Raft Domains Induced by Outer Leaflet

      Sphingomyelin in Cholesterol-Rich Asymmetric Vesicles” Biophys. J. 108, 2212-2022.

      Discussed as a “New and Notable” article in Biophys. J. (May 5, 2015)

      73.       London, E. (2015) “Membrane Fusion: A New Role For Membrane Domains?” Nature

      Chemical Biology, 11, 383-384.

      74.       Farnoud, A, Toledo, A.M., Konopka J.B., Del Poeta, M., and London, E. (2015) “Raft-

      Like Membrane Domains in Pathogenic Microorganisms”, Current Topics in Membranes, Volume 75 “Membrane Domains” (A. Kenworthy, Editor), Academic Press/Elsevier, Amsterdam, pages 233-268.

      75.       Lin, Q., Wang, T., Li. H, and London, E. (2015) “Decreasing Transmembrane Segment

      Length Greatly Decreases Perfringolysin O Pore Size” J. Memb. Biol. 248, 517-527.

      76.       Kim, J., and London, E. (2015) “Using Sterol Substitution to Probe the Role of

      Membrane Domains in Membrane Functions” Lipids 50, 721-734.

      77.       Pathak, P., and London, E. (2015) “Effect of Membrane Lipid Composition Upon the

      Formation of Ultra-Nanodomains” Biophys. J. 109, 1630-1638.

      78.       Yu, H., Takeuchi, M., LeBarron, J., Kantharia, J., London, E., Bakker, H., Haltiwanger,

      R.S., Li, H., and Takeuchi, H. (2015) “Structures of a Notch-modifying xylosyltransferase support an SNi-like retaining mechanism” Nature Chemical Biology 11, 847-854.

      79.       London, E. (2016) “Lipid Rafts/Membrane Rafts”, Encyclopedia of

      Cell Biology (Bradshaw, R.A. and Stahl, P., Eds.)  Vol 1, Academic Press, Waltham, MA

      pp. 208-217.

      80.      LeBarron, J., and London, E. (2016) “Effect of Lipid Composition and Amino Acid

      Sequence Upon Transmembrane Peptide-Accelerated Lipid Transleaflet Diffusion (Flip- Flop)” Biochim. Biophys. Acta 1858, 1812–1820.

      81.      Heberle, F.A., Marquardt, D., Doktorova, M., Geier, B., Standaert, R., Heftberger,

      P., Kollmitzer, B., Nickels, J.D., Feigenson, G.W., Katsaras, J., London, E., and Pabst, G. (2016) “Sub-nanometer Structure of an Asymmetric Model Membrane: Interleaflet Coupling Influences Domain Properties” Langmuir 32, 5195-5200.

      82.       Huang, Z., and London, E. (2016) “Cholesterol lipids and cholesterol-containing  

                  lipid rafts in bacteria” Chem. Phys. Lipids 199, 11-16.

      83.       London, E. (2016) “New Insights into How Cholesterol and Unsaturation Control Lipid

      Domain Formation” Biophys. J. 111, 465-466.

      84.       LeBarron, J., and London, E. (2016) “Highly Hydrophilic Segments Attached       

                  Hydrophobic Peptides Translocate Rapidly Across Membranes” Langmuir 32, 10752-


      85.       Li, G., Kim, J., Huang, Z., St. Clair, J.R., Brown, D.A., and London, E. (2016) “Efficient

      Replacement of Plasma Membrane Outer Leaflet Phospholipids and Sphingolipids in      Cells with Exogenous Lipids” Proc. Natl. Acad. Sci. USA, 113, 14025-14030. 

      86.       Huang, Z., Toledo, A.M., Benach, J.L., and London, E. (2016) “Ordered Membrane 

      Domain Forming Properties of the Lipids of Borrelia burgdorferiBiophys. J., 111, 2666–2675.

      87.       Zhang, X., St Clair, J.R., London, E.*, and Raleigh, D.P.* (2017) “Islet Amyloid   

       Polypeptide Membrane Interactions: Effects of Membrane Composition” Biochemistry,   

       56, 376-390. *co-corresponding authors

      88.      Marquardt, D., Heberle, F.A., Miti, T., Eicher. B., London, E., Katsaras, J., and Pabst, G.

      (2017) “1H NMR Shows Phospholipid Flip-Flop in Vesicles is Extremely Slow in Both Gel and Fluid States” Langmuir 33, 3731–3741.

      89.       Kim, J., Singh, A., DelPoeta, M., Brown, D.A.*, and London, E.* (2017) “The effect of sterol structure upon clathrin-mediated and clathrin-independent endocytosis” J. Cell Sci. 130, 2682-2695.  Featured article in the “in this issue” section. *co-corresponding authors.

      90.      St. Clair, J.R., Wang, Q., Li, G., and London, E. (2017) “Preparation and Physical

      Properties of Asymmetric Model Membrane Vesicles” in “Springer Series in Biophysics: The Role of the Physical Properties of Membranes in Influencing Biological Phenomena”   (Eds. R.M. Epand and J.M. Ruysschaert), Springer Nature Singapore, 1-27.

      91.       Farnoud, A.M., Raj, S., Kim J., Joffe, L., Zhang, X., Singh, A., Mor, V., Desmarini, D., 

      Djordjevic, J., Raleigh, D.P., Rodrigues, M.L., London, E., and Del Poeta, M. (2017) “Changes in Glucosylceramide Structure Affect Virulence and Membrane Biophysical Properties of Cryptococcus neoformansBiochim Biophys. Acta 1859, 2224-2233.

      92.      Toledo, A.M., Huang, Z., Benach J.L., and London, E. (2018) “Analysis of Lipids and

      Lipid Rafts in BorreliaMethods Mol Biol. 1690, 69-82.

      93.       Kim, J., Fukuto, H.S., Bliska, J.B., Brown, D.A., and London, E. (2018) “Effects of host

      cell sterol composition upon internalization of Yersinia pseudotuberculosis and clustered beta-1 integrin” J. Biol. Chem. 293, 1466-1479. 

      94.       Toledo, A., Huang, Z., Coleman, J.L., London, E., and Benach, J.L. (2018) “Lipid rafts can form in both the inner and outer membranes of Borrelia burgdorferi and have different properties and associated proteins” Mol. Microbiol. 108, 63-76.

      95.       Zhang, X., London, E., and Raleigh, D.P. (2018) “Sterol Structure Strongly Modulates

      Membrane-IAPP Interactions” Biochemistry 57, 1868-1879.

      96.       Wang, Q., and London, E. (2018), “Lipid Structure and Composition Control Consequences of Interleaflet Coupling in Asymmetric Vesicles” Biophys. J. 115, 664-678.

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