Source: http://sagardkharelab.org/papers/
Timestamp: 2019-04-22 16:38:20+00:00

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17. F. Richter, R. Blomberg, S. D. Khare, G. Kiss, A. P. Kuzin, A. J. Smith, J. L. Gallaher, Z. Pianowski, R. C. Helgeson, A. Grjasnow, R. Xiao, J. Seetharaman, M. Su, S. Vorobiev, S. Lew, F. Forouhar, G. J. Kornhaber, J. F. Hunt, G. T. Montelione, L. Tong, K. N. Houk, D. Hilvert, and D. Baker, “ Computational design of catalytic dyads and oxyanion holes for ester hydrolysis” J. Am. Chem. Soc. 134: 16197-207 (2012).
16. S. J. Fleishman, S. D. Khare, N. Koga, and D. Baker, “Restricted sidechain plasticity in the structures of native proteins and complexes” Protein Science, 20: 753-7 (2011).
15. F. Richter, A. Leaver-Fay, S. D. Khare, S. Bjelic, and D. Baker, “De novo enzyme design using Rosetta3” PLoS One, 6: e19230 (2011).
14. S. J. Fleishman, A. Leaver-Fay, J. E. Corn, E.-M. Strauch, S. D. Khare, N. Koga, J. Ashworth, P. Murphy, F. Richter, G. Lemmon, J. Meiler, and D. Baker, “RosettaScripts: a scripting language interface to the Rosetta macromolecular modeling suite” PLoS One, 6: e20161 (2011).
13. E. Weerapana, C. Wang, G. M. Simon, F. Richter, S. Khare, M. B. D. Dillon, D. A. Bachovchin, K. Mowen, D. Baker, and B. F. Cravatt, “Quantitative reactivity profiling predicts functional cysteines in proteomes” Nature, 468: 790-5 (2010).
12. R. Das, B. Qian, S. Raman, R. Vernon, J. Thompson, P. Bradley, S. Khare, M. D. Tyka, D. Bhat, D. Chivian, D. E. Kim, W. H. Sheffler, L. Malmström, A. M. Wollacott, C. Wang, I. Andre, and D. Baker, “Structure prediction for CASP7 targets using extensive all-atom refinement with Rosetta@home.” Proteins 69: Suppl 8, 118-28 (2007).
11. S. Barton, R. Jacak, S. D. Khare, F. Ding, and N. V. Dokholyan, “The length dependence of the polyQ- mediated protein aggregation” J. Biol. Chem., 282: 25487-25492 (2007).
10. S. D. Khare, and N. V. Dokholyan, “Molecular mechanisms of polypeptide aggregation in human diseases” Curr. Protein Pept. Sci., 8: 573-579 (2007).
9. S. D. Khare, and N. V. Dokholyan, “Common dynamical signatures of FALS-associated structurally- diverse Cu, Zn superoxide dismutase mutants” Proc. Natl. Acad. Sci. USA, 103: 3147-3152 (2006).
8. S. D. Khare, M. Caplow, and N. V. Dokholyan, “FALS mutations in Cu, Zn superoxide dismutase destabilize the dimer and increase dimer dissociation propensity: a large-scale thermodynamic analysis” Amyloid, 13: 226-235 (2006).
7. S. D. Khare, K. C. Wilcox, P. Gong, and N. V. Dokholyan, “Sequence and structural determinants of Cu, Zn superoxide dismutase aggregation” Proteins: Struct. Funct. Bioinfo., 61: 617-632 (2005).
6. S. D. Khare, F. Ding, K. N. Gwanmesia, and N. V. Dokholyan, “Molecular origin of polyglutamine- mediated aggregation in neurodegenerative diseases” PLoS Comp. Biol., 1: e30 (2005).
5. S. D. Khare, M. Caplow, and N. V. Dokholyan, “The rate and equilibrium constants for a multi-step reaction sequence for the aggregation of superoxide dismutase in ALS” Proc. Natl. Acad. Sci. USA, 101: 15094-15099 (2004).
3. R. D. S. Dixon, Y. Chen, F. Ding, S. D. Khare, K. C. Prutzman, M. D. Schaller, S. L. Campbell, and N. V. Dokholyan, “New insights into FAK signaling and localization based on detection of a FAT domain folding intermediate” Structure, 12: 2161-2171 (2004).
2. B. Urbanc, L. Cruz, F. Ding, D. Sammond, S. Khare, S. V. Buldyrev, H. E. Stanley, and N. V. Dokholyan, “Molecular dynamics simulation of Amyloid-beta dimer formation” Biophys. J., 87: 2310-2321 (2004).
1. S. D. Khare, F. Ding, and N. V. Dokholyan, “Folding of Cu, Zn superoxide dismutase and Familial Amyotrophic Lateral Sclerosis” J. Mol. Biol., 334: 515-525 (2003).
Sagar Khare. Copyright © 2015.

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