Year |
Citation |
Score |
2022 |
Roberts MF, Gershenson A, Reuter N. Phosphatidylcholine Cation-Tyrosine π Complexes: Motifs for Membrane Binding by a Bacterial Phospholipase C. Molecules (Basel, Switzerland). 27. PMID 36234717 DOI: 10.3390/molecules27196184 |
0.364 |
|
2020 |
Baboolall KD, Kaudeer YB, Gershenson A, O'Hara PB. pH Dependence of Oligomerization and Functional Activity of Alpha B Crystallin Biophysical Journal. 118: 510a. DOI: 10.1016/J.Bpj.2019.11.2809 |
0.335 |
|
2019 |
Johnson DT, Punshon-Smith B, Espino JA, Gershenson A, Jones LM. Implementing In-Cell Fast Photochemical Oxidation of Proteins in a Platform Incubator with Movable XY Stage. Analytical Chemistry. PMID 31860269 DOI: 10.1021/Acs.Analchem.9B04933 |
0.316 |
|
2019 |
Gershenson A, Gosavi S, Faccioli P, Wintrode PL. Successes and challenges in simulating the folding of large proteins. The Journal of Biological Chemistry. PMID 31712314 DOI: 10.1074/Jbc.Rev119.006794 |
0.351 |
|
2019 |
Adams BM, Ke H, Gierasch LM, Gershenson A, Hebert DN. Proper secretion of the serpin antithrombin relies strictly on thiol-dependent quality control. The Journal of Biological Chemistry. PMID 31662433 DOI: 10.1074/Jbc.Ra119.010450 |
0.33 |
|
2019 |
Waheed Q, Khan HM, He T, Roberts MF, Gershenson A, Reuter N. Interfacial Aromatics Mediating Cation-Π Interactions with Choline Containing Lipids Can Contribute As Much To Peripheral Protein Affinity for Membranes as Aromatics Inserted Below the Phosphates. The Journal of Physical Chemistry Letters. PMID 31246477 DOI: 10.1021/Acs.Jpclett.9B01639 |
0.375 |
|
2019 |
Stumper SK, Ravi H, Friedman LJ, Mooney RA, Corrêa IR, Gershenson A, Landick R, Gelles J. Delayed inhibition mechanism for secondary channel factor regulation of ribosomal RNA transcription. Elife. 8. PMID 30720429 DOI: 10.7554/Elife.40576 |
0.307 |
|
2018 |
Roberts MF, Khan HM, Goldstein R, Reuter N, Gershenson A. Search and Subvert: Minimalist Bacterial Phosphatidylinositol-Specific Phospholipase C Enzymes. Chemical Reviews. PMID 30148347 DOI: 10.1021/Acs.Chemrev.8B00208 |
0.418 |
|
2017 |
Navaratnarajah P, Gershenson A, Ross EM. The binding of activated Gαq to Phospholipase C-β exhibits anomalous affinity. The Journal of Biological Chemistry. PMID 28842497 DOI: 10.1074/Jbc.M117.809673 |
0.31 |
|
2017 |
Krishnan B, Hedstrom L, Hebert DN, Gierasch LM, Gershenson A. Expression and Purification of Active Recombinant Human Alpha-1 Antitrypsin (AAT) from Escherichia coli. Methods in Molecular Biology (Clifton, N.J.). 1639: 195-209. PMID 28752459 DOI: 10.1007/978-1-4939-7163-3_19 |
0.333 |
|
2017 |
Kuo W, Kaur U, Deredge D, Kilcoyne CJ, Clerico EM, Wintrode PL, Gierasch LM, Gershenson A. Folding in Pieces Biophysical Journal. 112: 167a. DOI: 10.1016/J.Bpj.2016.11.921 |
0.399 |
|
2016 |
Chandrasekhar K, Ke H, Wang N, Goodwin T, Gierasch LM, Gershenson A, Hebert DN. Cellular folding pathway of a metastable serpin. Proceedings of the National Academy of Sciences of the United States of America. PMID 27222580 DOI: 10.1073/Pnas.1603386113 |
0.415 |
|
2016 |
Khan HM, He T, Fuglebakk E, Grauffel C, Yang B, Roberts MF, Gershenson A, Reuter N. A Role for Weak Electrostatic Interactions in Peripheral Membrane Protein Binding. Biophysical Journal. 110: 1367-78. PMID 27028646 DOI: 10.1016/J.Bpj.2016.02.020 |
0.403 |
|
2016 |
Huang Q, Gershenson A, Roberts MF. Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH. Biochimica Et Biophysica Acta. PMID 26976751 DOI: 10.1016/J.Bbapap.2016.03.008 |
0.392 |
|
2016 |
Fatunmbi O, Abzalimov R, Savinov SN, Gershenson A, Kaltashov IA. Haptoglobin interactions with monomeric globin species: insights from molecular modeling and native electrospray ionization mass spectrometry. Biochemistry. PMID 26937685 DOI: 10.1021/Acs.Biochem.5B00807 |
0.372 |
|
2016 |
Wang F, Ke H, Beccara Sa, Gershenson A, Faccioli P, Wintrode P. Folding Mechanism of a Metastable Serpin at Atomic Resolution Biophysical Journal. 110: 369a. DOI: 10.1016/J.Bpj.2015.11.1988 |
0.372 |
|
2015 |
He T, Gershenson A, Eyles SJ, Lee YJ, Liu WR, Wang J, Gao J, Roberts MF. Fluorinated aromatic amino acids distinguish cation-π interactions from membrane insertion. The Journal of Biological Chemistry. PMID 26092728 DOI: 10.1074/Jbc.M115.668343 |
0.37 |
|
2015 |
Wintrode P, Faccioli P, Beccara Sa, Gershenson A, Cazzolli G, Wang F. Simulating the Serpin Latency Transition at Atomic Resolution Biophysical Journal. 108: 317a. DOI: 10.1016/J.Bpj.2014.11.1722 |
0.357 |
|
2015 |
He T, Khan HM, Grauffel C, Reuter N, Gershenson A, Roberts MF. Identifying the Choline-Cation Tyrosine-PI Interactions of an Amphitropic Protein Biophysical Journal. 108: 256a. DOI: 10.1016/J.Bpj.2014.11.1414 |
0.45 |
|
2015 |
Khan HM, Grauffel C, Roberts MF, Gershenson A, Reuter N. Interplay between Electrostatics and Cation-PI Interactions Governs the Specific Membrane Binding of Phosphatidylinositol-Specific Phospholipase-C Biophysical Journal. 108: 248a. DOI: 10.1016/J.Bpj.2014.11.1374 |
0.378 |
|
2014 |
Cazzolli G, Wang F, a Beccara S, Gershenson A, Faccioli P, Wintrode PL. Serpin latency transition at atomic resolution. Proceedings of the National Academy of Sciences of the United States of America. 111: 15414-9. PMID 25313058 DOI: 10.1073/Pnas.1407528111 |
0.321 |
|
2014 |
Theillet FX, Binolfi A, Frembgen-Kesner T, Hingorani K, Sarkar M, Kyne C, Li C, Crowley PB, Gierasch L, Pielak GJ, Elcock AH, Gershenson A, Selenko P. Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chemical Reviews. 114: 6661-714. PMID 24901537 DOI: 10.1021/Cr400695P |
0.303 |
|
2014 |
Liu L, Werner M, Gershenson A. Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding. Biochemistry. 53: 2903-14. PMID 24749911 DOI: 10.1021/Bi401622N |
0.37 |
|
2014 |
Gershenson A. Deciphering protein stability in cells. Journal of Molecular Biology. 426: 4-6. PMID 24112941 DOI: 10.1016/J.Jmb.2013.10.004 |
0.379 |
|
2014 |
Yang B, Roberts MF, Gershenson A. Revealing Transient Interactions Between Phosphatidylinositol-Specific Phospholipase C and Phosphatidylcholine-Rich Lipid Vesicles Biophysical Journal. 106: 716a. DOI: 10.1016/J.Bpj.2013.11.3957 |
0.408 |
|
2013 |
Cheng J, Goldstein R, Gershenson A, Stec B, Roberts MF. The cation-π box is a specific phosphatidylcholine membrane targeting motif. The Journal of Biological Chemistry. 288: 14863-73. PMID 23576432 DOI: 10.1074/Jbc.M113.466532 |
0.361 |
|
2013 |
Grauffel C, Yang B, He T, Roberts MF, Gershenson A, Reuter N. Cation-π interactions as lipid-specific anchors for phosphatidylinositol-specific phospholipase C. Journal of the American Chemical Society. 135: 5740-50. PMID 23506313 DOI: 10.1021/Ja312656V |
0.399 |
|
2013 |
Cheng J, Karri S, Grauffel C, Wang F, Reuter N, Roberts MF, Wintrode PL, Gershenson A. Does changing the predicted dynamics of a phospholipase C alter activity and membrane binding? Biophysical Journal. 104: 185-95. PMID 23332071 DOI: 10.1016/J.Bpj.2012.11.015 |
0.411 |
|
2013 |
Grauffel C, He T, Yang B, Wintrode PL, Gershenson A, Roberts MF, Reuter N. Cation-PI Interactions as Specific Anchors for B. Thurigiensis Phosphoinositol-Specific Phospholipase-C Binding to Phosphatidylcholine Bilayer Biophysical Journal. 104: 536a. DOI: 10.1016/J.Bpj.2012.11.2969 |
0.402 |
|
2013 |
He T, Yang B, Grauffel C, Reuter N, Gershenson A, Roberts MF. Probing for π-Cation Interactions in the Binding of B. Thuringiensis Phosphatidylinositol-Specific Phospholipase C Phosphatidylcholine-Rich Vesicles Biophysical Journal. 104: 363a-364a. DOI: 10.1016/J.Bpj.2012.11.2018 |
0.415 |
|
2012 |
Cheng J, Goldstein R, Stec B, Gershenson A, Roberts MF. Competition between anion binding and dimerization modulates Staphylococcus aureus phosphatidylinositol-specific phospholipase C enzymatic activity. The Journal of Biological Chemistry. 287: 40317-27. PMID 23038258 DOI: 10.1074/Jbc.M112.395277 |
0.448 |
|
2012 |
Cheng J, Roberts MF, Gershenson A. Identifying Motifs for Phosphatidylcholine Activation of Bacterial Phosphatidylinositol-Specific Phospholipase C Enzymes Biophysical Journal. 102: 79a-80a. DOI: 10.1016/J.Bpj.2011.11.460 |
0.421 |
|
2012 |
Grauffel C, He T, Yang B, Guo S, Wintrode PL, Gershenson A, Roberts MF, Reuter N. Anchoring of PI-PLC to DMPC Bilayers Involves Specific Cation-PI Interactions Biophysical Journal. 102: 78a-79a. DOI: 10.1016/J.Bpj.2011.11.455 |
0.409 |
|
2011 |
Mushero N, Gershenson A. Determining serpin conformational distributions with single molecule fluorescence. Methods in Enzymology. 501: 351-77. PMID 22078542 DOI: 10.1016/B978-0-12-385950-1.00016-X |
0.685 |
|
2011 |
Gershenson A, Gierasch LM. Protein folding in the cell: challenges and progress. Current Opinion in Structural Biology. 21: 32-41. PMID 21112769 DOI: 10.1016/J.Sbi.2010.11.001 |
0.31 |
|
2009 |
Gierasch LM, Gershenson A. Post-reductionist protein science, or putting Humpty Dumpty back together again. Nature Chemical Biology. 5: 774-7. PMID 19841622 DOI: 10.1038/Nchembio.241 |
0.314 |
|
2009 |
Gershenson A. Single molecule enzymology: watching the reaction. Current Opinion in Chemical Biology. 13: 436-42. PMID 19632886 DOI: 10.1016/J.Cbpa.2009.06.011 |
0.398 |
|
2009 |
Pu M, Roberts MF, Gershenson A. Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding. Biochemistry. 48: 6835-45. PMID 19548649 DOI: 10.1021/Bi900633P |
0.425 |
|
2009 |
Pu M, Fang X, Redfield AG, Gershenson A, Roberts MF. Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity: insights into phosphatidylcholine activation and surface dilution inhibition. The Journal of Biological Chemistry. 284: 16099-107. PMID 19336401 DOI: 10.1074/Jbc.M809600200 |
0.608 |
|
2009 |
Pu M, Roberts MF, Gershenson A. FCS of Mutated Phosphatidylinositol-specific Phospholipase C Enzymes Monitors the Interplay of Substrate and Activator Lipid Binding Biophysical Journal. 96: 612a. DOI: 10.1016/J.Bpj.2008.12.3237 |
0.442 |
|
2008 |
Farbman ME, Gershenson A, Licht S. Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA. Biochemistry. 47: 13497-505. PMID 19053261 DOI: 10.1021/Bi801140Y |
0.433 |
|
2007 |
Liu L, Mushero N, Hedstrom L, Gershenson A. Short-lived protease serpin complexes: partial disruption of the rat trypsin active site. Protein Science : a Publication of the Protein Society. 16: 2403-11. PMID 17962402 DOI: 10.1110/Ps.073111207 |
0.689 |
|
2006 |
Liu L, Mushero N, Hedstrom L, Gershenson A. Conformational distributions of protease-serpin complexes: a partially translocated complex. Biochemistry. 45: 10865-72. PMID 16953572 DOI: 10.1021/Bi0609568 |
0.697 |
|
2001 |
Arnold FH, Wintrode PL, Miyazaki K, Gershenson A. How enzymes adapt: lessons from directed evolution. Trends in Biochemical Sciences. 26: 100-6. PMID 11166567 DOI: 10.1016/S0968-0004(00)01755-2 |
0.323 |
|
2000 |
Gershenson A, Arnold FH. Enzyme stabilization by directed evolution. Genetic Engineering. 22: 55-76. PMID 11501381 DOI: 10.1007/978-1-4615-4199-8_5 |
0.352 |
|
2000 |
Gershenson A, Schauerte JA, Giver L, Arnold FH. Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases Biochemistry. 39: 4658-4665. PMID 10769121 DOI: 10.1021/Bi992473S |
0.37 |
|
1999 |
Spiller B, Gershenson A, Arnold FH, Stevens RC. A structural view of evolutionary divergence. Proceedings of the National Academy of Sciences of the United States of America. 96: 12305-10. PMID 10535917 DOI: 10.1073/Pnas.96.22.12305 |
0.384 |
|
1998 |
Giver L, Gershenson A, Freskgard PO, Arnold FH. Directed evolution of a thermostable esterase. Proceedings of the National Academy of Sciences of the United States of America. 95: 12809-13. PMID 9788996 DOI: 10.1073/Pnas.95.22.12809 |
0.33 |
|
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