Gershenson:Publications: Difference between revisions

From OpenWetWare
Jump to navigationJump to search
 
(No difference)

Latest revision as of 10:59, 30 August 2014

  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]
  6. Pu, M., Roberts, M.F. & Gershenson A. (2009) Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding. Biochemistry 48: 6835-6845. http://pubs.acs.org/doi/abs/10.1021/bi900633p

    [Paper6]
  7. Pu, M., Fang, X., Redfield, A.G., Gershenson, A. & Roberts, M.F. (2009) Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity: insights into phosphatidylcholine activation and surface dilution inhibition. J Biol Chem 284: 16099-16107. http://www.jbc.org/content/284/24/16099

    [Paper7]
  8. Farbman, M.E., Gershenson, A. & Licht, S. (2008) Role of a conserved pore residue in formation of a pre-hydrolytic high substrate affinity state in the AAA+ chaperone ClpA. Biochemistry 47: 13497–13505. http://pubs.acs.org/doi/abs/10.1021/bi801140y

    [Paper8]
  9. Farbman, M.E., Gershenson, A. & Licht, S. (2007) Single-Molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA. J Am Chem Soc 129: 12378-12379. http://pubs.acs.org/doi/abs/10.1021/ja074168x

    [Paper9]
  10. Liu, L., Mushero, N., Hedstrom, L. & Gershenson, A. (2007) Short-lived protease-serpin complexes: partial disruption of the rat trypsin active site. Protein Sci 16: 2403-2411. http://www.proteinscience.org/cgi/content/full/16/11/2403

    [Paper10]
  11. Liu, L., Mushero, N., Hedstrom, L. & Gershenson, A. (2006) Conformational distributions of protease-serpin complexes: a partially translocated complex. Biochemistry 45: 10865-10872. http://pubs.acs.org/doi/full/10.1021/bi0609568

    [Paper11]
  12. Tsutsui, Y., Liu, L., Gershenson, A. & Wintrode, P.L. (2006) The conformational dynamics of a metastable serpin studied by hydrogen exchange and mass spectrometry. Biochemistry 45: 6561-6569.

    http://pubs.acs.org/doi/full/10.1021/bi060431f

    [Paper12]

Reviews, Perspectives, Etc.

  1. 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]
  2. Gershenson, A. (2014) Deciphering protein stability in cells. J Mol Biol 426: 4-6. http://www.sciencedirect.com/science/article/pii/S002228361300630X

    [Commentary1]
  3. 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]
  4. 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]
  5. Gershenson, A. & Gierasch, L.M. (2009) Post-reductionist protein science, or putting Humpty Dumpty back together again. Nat Chem Biol 5: 774-777. http://www.nature.com/nchembio/journal/v5/n11/full/nchembio.241.html

    [Commentary2]
  6. Gershenson, A. (2009) Single molecule enzymology: watching the reaction. Curr Opin Chem Biol 13: 436-442. http://www.sciencedirect.com/science/article/pii/S1367593109000763

    [Review3]