Publication List

  • Nunez, M., K. Wisser, S.L. Veatch*, Synergistic factors organize kinase-phosphatase signaling in B cells engaged with supported bilayers. Mol Biol Cell in press (2020) https://dx.doi.org/10.1091/mbc.E19-09-0507
  • Cammarota E., C Soriani, J. Sakai, S.L. Veatch, C.E. Bryant, P. Cicuta. Criticality of plasma membrane lipids reflects activation state of macrophage cells. J R Soc Interface, 17 (163), 20190803 (2020). https://dx.doi.org/10.1098/rsif.2019.0803
  • Kimchi, O. S.L. Veatch, B. B. Machta*. Allosteric Regulation by a Critical Membrane. Journal of General Physiology 150(12): 1769.  https://doi.org/10.1085/jgp.201711900 Featured on the journal cover.
  • Rosselli-Murai LK, J.A. Yates, S. Yoshida, J. Bourg, K.K.Y. Ho, M. White, J. Prisby, X. Tan, M. Altemus, L. Bao, Z.F. Wu, S.L. Veatch, J.A. Swanson, S.D. Merajver, A.P. Liu. Loss of PTEN promotes formation of signaling-capable clathrin-coated pits. J Cell Sci. 131(8) jcs208926 (2018). https://dx.doi.org/10.1242/jcs.208926
  • Chang CC, E. Edwald, S.L. Veatch, D.G. Steel, A. Gafni Interactions of amyloid-β peptides on lipid bilayer studied by single molecule imaging and tracking. BBA biomembr. 1860(9)1616 (2018) http://dx.doi.org/10.1016/j.bbamem.2018.03.017
  • Gerstle, Z., R. Desai, S.L. Veatch*. Giant Plasma Membrane Vesicles: an Experimental Tool for Probing the Effects of Drugs and other Conditions on Membrane Domain Stability. Chapter in Chemical and Biochemical Approaches for the Study of Anesthetic Function.  Methods Enzymol 603:129-150 (2018). http://dx.doi.org/10.1016/bs.mie.2018.02.007.
  • Burns, M., K. Wisser, J. Wu, I, Levental, S.L. Veatch. Miscibility transition temperature scales with growth temperature in a zebrafish cell line. Biophys. J. 113(6):1212-1222 (2017) https://doi.org/10.1016/j.bpj.2017.04.052 . Featured on the journal cover and with a New and Notable.
  • CTMB Tom, JE Crellin, HF Motiwala, MB Stone, D Davda, W Walker, YH Kuo, JL Hernandez, KJ Labby, L Gomez-Rodriguez, PM Jenkins, SL Veatch, BR Martin. Chemoselective ratiometric imaging of protein S-sulfenylation. Chem Commun (Camb). 53(53):7385-7388 (2017). https://doi.org/10.1039/c7cc02285a.
  • Stone, M.B., S.A. Shelby, M. Nunez, K. Wisser, and S.L. Veatch, Protein sorting by phase-like domains supports emergent signaling function in B cell membranes. eLife 2017;6:e19891 (2017) http://dx.doi.org/10.7554/eLife.19891. Featured in an INSIGHT article.
  • Stone, M.B., S.A. Shelby, and S.L. Veatch, Super-resolution microscopy: shedding light on the cellular plasma membrane. Chemical Reviews 117(11):7457-7477 (2017). https://doi.org/10.1021/acs.chemrev.6b00716
  • Irajizad, N. Walani, S.L. Veatch, A.P. Liu, and A. Agrawal, Clathrin polymerization exhibits high mechano-geometric sensitivity. Soft Matter, 13(7):1455. (2017) http://dx.doi.og/10.1039/c6sm02623k.
  • A. Shelby, S. L. Veatch. D. A. Holowka, and B. A. Baird*, Functional nanoscale coupling of Lyn kinase with IgE-FcεRI is restricted by the actin cytoskeleton in early antigen-stimulated signaling. Mol. Biol. Cell 27(22):3645-3658 (2016). http://dx.doi.org/10.1091/mbc.E16-06-0425.
  • Machta, E. Gray, M. Nouri, N. McCarthy, E. Gray, A. Miller, N. Brooks, and S.L. Veatch. Conditions that Stabilize Membrane Domains Also Antagonize n-Alcohol Anesthesia. Biophys. J. 111(3) 537-45 (2016) http://dx.doi.org/10.1016/j.bpj.2016.06.039.
  • Levental* and S.L. Veatch. The continuing mystery of lipid rafts. J. Mol. Biol. 428(24 Pt A): 4749-4764 (2016). http://dx.doi.org/10.1016/j.jmb.2016.08.022
  • Burns, M. Nouri, S.L. Veatch. Spot size variation FCS in simulations of the 2D Ising model. J. Phys. D 49(21) 214001 (2016) http://iopscience.iop.org/article/10.1088/0022-3727/49/21/214001
  • Olety, S.L. Veatch, and A. Ono, Visualization of HIV-1 Gag binding to Giant Unilamellar Vesicle (GUV) membranes. JoVE, in press (2016)
  • Raghunathan. A. Ahsan, D. Ray, M.K. Nyati*, and S.L. Veatch. Membrane Transition Temperature Determines Cisplatin Response, PLoS ONE 10(10):e0140925 (2015) http://dx.doi.org/10.1371/journal.pone.0140925
  • M. Gray, G. Díaz-Vázquez, S.L. Veatch. Growth Conditions and Cell Cycle Phase Modulate Phase Transition Temperatures in RBL-2H3 Derived Plasma Membrane Vesicles. PLoS ONE 10(9): e0137741. (2015) http://dx.doi.org/10.1371/journal.pone.0137741
  • B. Stone and S.L. Veatch Steady-state cross-correlation analysis for live two-color super-resolution data-sets, Nature Communications 6:7347 (2015) http://dx.doi.org/ http://dx.doi.org/10.1038/ncomms8347
  • Olety, S.L. Veatch, and A. Ono* PI(4,5)P2 acyl chains differentiate membrane binding of HIV-1 Gag from that of the phospholipase Cδ1 PH domain Journal of Virology 89(15):7861-73 (2015) http://dx.doi.org/2010.1128/JVI.00794-15
  • R. Grover, S.L. Veatch*, A. Ono* Basic motifs target PSGL-1, CD43, and CD44 to plasma membrane sites where HIV-1 assembles. J Virol. 89(1):454-67 (2015) http://dx.doi.org/10.1128/JVI.02178-14
  • Edwald, M. B. Stone, E. M. Gray, J. Wu, and S.L. Veatch Oxygen depletion speeds and simplifies diffusion in HeLa cells. Biophys J 107(8):1873-84 (2014) http://dx.doi.org/10.1016/j.bpj.2014.08.023
  • B. Stone and S.L. Veatch Far-Red Organic Fluorophores Contain a Fluorescent Impurity. Chemphyschem 15(11):2240-6 (2014) http://dx.doi.org/10.1002/cphc.201402002
  • Soppina, S.R. Norris, A.S. Dizaji, M. Kortus, S.L. Veatch, M. Peckham, K.J.Verhey. Dimerization of mammalian kinesin-3 motors results in superprocessive motion. Proc Natl Acad Sci U S A. 111(15):5562-7 (2014) http://dx.doi.org/10.1073/pnas.1400759111
  • Gray, J. Karslake, B.B. Machta, B.B*, and S.L. Veatch*. Liquid general anesthetics lower critical temperatures in plasma membrane vesicles. Biophys. J. 105(12): 2751-9 (2013) http://dx.doi.org/10.1016/j.bpj.2013.11.005.
  • Shelby, D. Holowka, B. Baird, S.L. Veatch*, Distinct stages of stimulated FcεRI receptor clustering and immobilization are identified through superresolution imaging. Biophys. J. 105(10): 2343-54 (2013) http://dx.doi.org/10.1016/j.bpj.2013.09.049. Featured on the Journal cover, in a New and Notable, and in the ‘best of 2013’ special issue of BJ.
  • Pore , N. Parameswaran, K. Matsui,4, M.B. Stone, I, Saotome, A. I. McClatchey, S.L. Veatch, and N. Gupta* Ezrin tunes the magnitude of humoral immunity. J Immunol. 191(8):4048-58. (2013) http://dx.doi.org/10.4049/jimmunol.1301315
  • Grover, G. Llewellyn, F. Soheilian, K. Nagashima, S.L. Veatch*, and A. Ono*. Roles played by capsid-dependent induction of membrane curvature and Gag-ESCRT interactions in tetherin recruitment to HIV-1 assembly sites. J. Virology. 87(8): 4650-64 (2013) http://dx.doi.org/10.1128/JVI.03526-12
  • Zhao, J. Wu., and S. L. Veatch*, Adhesion Stabilizes Robust Lipid Heterogeneity in Supercritical Membranes at Physiological Temperature. Biophys. J. 104(4):825-34 (2013) http://dx.doi.org/10.1016/j.bpj.2012.12.047. Featured in a New and Notable.
  • Lee, J. L. Veatch, D. A. Holowka, and B. A. Baird*, Molecular Mechanisms of Spontaneous and Directed Mast Cell Motility. Journal of Leukocyte Biology 92(5):1029-41 (2012) http://dx.doi.org/10.1189/jlb.0212091
  • M. Machta, S.L. Veatch, J. P. Sethna, Critical Casimir forces in cellular membranes, Phys. Rev. Lett. 109(13):138101 (2012). http://dx.doi.org/10.1103/PhysRevLett.109.138101
  • L. Veatch, E. N. Chaing, P. Sengupta, D. Holowka, B. Baird*, Quantitative Nano-scale Analysis of IgE-FcεRI Clustering and Coupling to Early Signaling Proteins. J Phys Chem B. 116(23): 6923-6935. (2012) http://dx.doi.org/10.1021/jp300197p
  • L. Veatch*, B, Machta, S. Shelby, E. N. Chiang, D. Holowka, B.Baird. Correlation functions estimate apparent clustering from over-counting and quantify super-resolution images. PLoS ONE 7(2):e31457 (2012) http://dx.doi.org/10.1371/journal.pone.0031457
  • Sengupta, T. Jovanovic-Talisman, D. Skoko, M. Renz, S. L. Veatch, J. Lippincott-Schwartz*, Probing protein heterogeneity in the plasma membrane using PALM and pair correlation analysis. Nature Methods 8(11):969-75 (2011) http://dx.doi.org/10.1038/nmeth.1704
  • Machta, S. Papanikolaou, J.P. Sethna, S.L. Veatch*. A minimal model of plasma membrane heterogeneity requires coupling cortical actin to Ising criticality. Biophys. J. 100(7)1668-77 (2011). http://dx.doi.org/10.1016/j.bpj.2011.02.029.

2010 & EARLIER

  • S. Hammond, A. Wagenknecht-Wiesne, S. L. Veatch, D. Holowka, B. Baird*. Roles for SH2 and SH3 domains in Lyn kinase association with activated FcεRI in RBL mast cells revealed by patterned surface analysis. J. Struct. Biol. 168(1):161-7 (2009).
  • S. L. Veatch*, P. Sengupta, A. Honerkamp-Smith, D. Holowka, B. Baird.  Critical Fluctuations in Plasma Membrane Vesicles. ACS Chem. Bio. 3(5):287-93 (2008).
  • A. R. Honerkamp-Smith, P. Cicuta, M. Collins, S. L. Veatch, M. Schick, M. den Nijs, and S. L. Keller*, Line tensions, correlation lengths, and critical exponents in lipid membranes near critical points.  Biophys. J. Biophys. J. 95(1) 236-46 (2008).
  • S. L. Veatch, O. Soubias, S. L. Keller, and K. Gawrisch*. Critical fluctuations in domain forming lipid mixtures.  Proc Natl Acad Sci 104(45) 17650–17655 (2007).
  • P. Cicuta, S. L. Keller, and S. L. Veatch*, Diffusion of liquid domains in lipid bilayer membranes. J. Phys. Chem. B. 111(13) 3328-3331 (2007)
  • S. L. Veatch, S. Leung, R. E. W Hancock, and J. Thewalt*, Fluorescent probes alter miscibility phase boundaries in ternary vesicles. J. Phys. Chem. B 111(3) 502-504 (2007)
  • N. Mookherjee, H. L. Wilson, S. Doria, Y. Popowych, R. Falsafi, J. J. Yu, Y. Li, S. Veatch, F. M. Roche, K. L. Brown, F. S. Brinkman, K. Hokamp, A. Potter, L. A. Babiuk, P. J. Griebel, and R. E. Hancock*.  Bovine and human cathelicidin cationic host defense peptides similarly suppress transcriptional responses to bacterial lipopolysaccharide. J Leukoc Biol. 80(6):1563-74. (2006).
  • S. L. Veatch, K. Gawrisch, and S. L. Keller*. Closed-loop miscibility gap and quantitative tie-lines in ternary membranes containing diphytanoyl PC. Biophys J. 90(12) 4428-36 (2006)
  • M. E. Beattie, S. L. Veatch, B. S. Stottrup, and S. L. Keller*, Sterol Structure Determines Miscibility vs. Melting Transitions in Lipid Vesicles, Biophys. J. 89(3) 1760-8 (2005)
  • S. L. Veatch and S. L. Keller*, Miscibility Phase Diagrams of Giant Vesicles Containing Sphingomyelin. Phys. Rev. Lett. (2005) 94(14), 148101.
  • B. L. Stottrup, S. L. Veatch, and S. L. Keller*, Nonequilibrium Behavior in Supported Lipid Membranes Containing Cholesterol. Biophys. J. (2004) 86(5) 2942-50.
  • S. L. Veatch, I. V. Polozov, K. Gawrisch, and S. L. Keller*, Liquid domains in vesicles investigated by NMR and fluorescence microscopy. Biophys. J. (2004) 86(5) 2910-22.
  • S. L. Veatch and S.L. Keller*, Separation of Liquid Phases in Giant Vesicles of Ternary Mixtures of Phospholipids and Cholesterol Biophys. J. (2003) 85(5) 3074-83.
  • S. L. Veatch and S.L. Keller*. A closer look at the canonical ‘raft mixture’ in model membrane studies. Biophys. J. (2003) 84(1) 725-6.
  • S. L. Veatch and S.L. Keller*. Organization in Lipid Membranes Containing Cholesterol Phys. Rev. Lett. (2002) 89(26), 268101.
  • S. Bezzine, J. G. Bollinger, A. G. Singer, S. L. Veatch, S. L. Keller, M. H. Gelb*. On the binding preference of human groups IIA and X phospholipases A2 for membranes with anionic phospholipids. J. Biol. Chem. (2002) 277(50) 48523-34.

BOOK CHAPTERS AND REVIEWS

  • A. R. Honerkamp-Smith, S. L. Veatch, and S. L. Keller*. An Introduction to Critical Points for Biophysicists: Observations of Compositional Heterogeneity in Lipid Membranes. Biochim. Biophys. Acta. 1788(1) 53-63. (2009). Review.
  • S. L. Veatch* Lipids out of order, Nat. Chem. Biol. 4(4) 225-6 (2008). News and Views
  • S. L. Veatch*, From small fluctuations to large-scale phase separation: Lateral organization in model membranes containing cholesterol, Semin. Cell Dev. Biol. 18(5) 573–582 (2007) Review
  • S. L. Veatch*, Electroformation and Fluorescence Microscopy of Giant Vesicles with coexisting liquid phases Lipid Rafts in Methods in Molecular Biology 398. Ed T. McIntosh, Humana Press, Totowa, NJ   59-72 (2007) Book Chapter
  • S. L. Veatch and S. L. Keller*, Seeing Spots: Complex Phase Behavior in Simple Membranes Biochim. Biophys. Acta. 1746(3) 172-85. (2005) Review.

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