User:Anne Gershenson

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Contact Info

Anne Gershenson (an artistic interpretation)
  • Anne Gershenson
  • University of Massachusetts Amherst
  • Department of Biochemistry & Molecular Biology
  • Life Sciences Laboratory 240 Thatcher Road
  • Amherst, MA, US 01003
  • Email me through OpenWetWare

Education

  • PhD, University of Michigan
  • AB, Bryn Mawr College

Research interests

  1. Protein Folding in vitro and in cells
  2. Protein-Membrane Interactions
  3. Single Molecule Fluorescence Spectroscopy
  4. Serpins
  5. Phospholipase C enzymes

Recent Publications

  1. Lu, L., Werner, M. & Gershenson, A. (2014) Collapse of a long axis: single molecule FRET and serpin equilibrium unfolding Biochemistry 53: 2903-2914. http://pubs.acs.org/doi/abs/10.1021/bi401622n

    [Paper1]
  2. Cheng, J., Goldstein, R., Gershenson, A., Stec, B. & Roberts, M.F. (2013) The cation-π box is a specific phosphatidylcholine membrane targeting motif. J Biol Chem 288: 14863-14873. http://www.jbc.org/content/288/21/14863.long

    [Paper2]
  3. Grauffel, C., Yang, B., He, T., Roberts, M.F., Gershenson, A. & Reuter, N. (2013) Cation-π interactions as lipid specific anchors for phosphatidylinositol-specific phospholipase-C. J Am Chem Soc 135: 5740-5745. http://pubs.acs.org/doi/abs/10.1021/ja312656v

    [Paper3]
  4. Cheng, J., Karri, S., Grauffel, C., Wang, F., Reuter, N., Roberts, M.F., Wintrode, P.L. & Gershenson, A. (2013) Does changing the predicted dynamics of a phospholipase C alter activity and membrane binding? Biophys J 104: 185-195. http://www.cell.com/biophysj/fulltext/S0006-3495%2812%2901236-2

    [Paper4]
  5. Cheng, J., Goldstein, R., Stec, B., Gershenson, A. & Roberts, M.F. (2012) Competition between anion binding and dimerization modulates S. aureus phosphatidylinositol-specific phospholipase C enzymatic activity. J Biol Chem 287: 40317-40327. http://www.jbc.org/content/287/48/40317.long

    [Paper5]

Recent Reviews, Perspectives, Etc.

  1. Gershenson, A., Gierasch, L.M., Pastore, A. & Radford, S.E. (2014) Energy landscapes of functional proteins are inherently risky. Nat Chem Biol 10: 884-891. http://www.nature.com/nchembio/journal/v10/n11/full/nchembio.1670.html

    [Perspective1]
  2. Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P., Gierasch, L., Pielak, G., Elcock, A., Gershenson, A. & Selenko, P. (2014) Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev 114: 6661-6714. http://pubs.acs.org/doi/abs/10.1021/cr400695p

    [Review1]
  3. Gershenson, A. (2014) Deciphering protein stability in cells. J Mol Biol 426: 4-6. http://www.sciencedirect.com/science/article/pii/S002228361300630X

    [Commentary1]
  4. Mushero, N. & Gershenson, A. (2011) Determining serpin conformational distributions with single molecule fluorescence. Methods Enzymol 501: 351-377. http://www.sciencedirect.com/science/article/pii/B978012385950100016X

    [Methods1]
  5. Gershenson, A. & Gierasch, L.M. (2011) Protein folding in the cell: Challenges and progress. Curr Opin Struct Biol 21: 32-41. http://www.sciencedirect.com/science/article/pii/S0959440X10001739

    [Review2]

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