Alexander V. Grishaev, Ph.D.
Affiliations: | 2001 | Carnegie Mellon University, Pittsburgh, PA |
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"Alexander Grishaev"Mean distance: 8237.17
Parents
Sign in to add mentorMiguel Llinás | grad student | 2001 | Carnegie Mellon | |
(CLOUDS: A computational protocol for protein structure elucidation via NMR proton densities.) |
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Publications
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Lawrence C, Grishaev AV. (2020) Chemical shifts-based similarity restraints improve accuracy of RNA structures determined via NMR. Rna (New York, N.Y.) |
Xu X, Godoy-Ruiz R, Adipietro KA, et al. (2020) Structure of the cell-binding component of the binary toxin reveals a di-heptamer macromolecular assembly. Proceedings of the National Academy of Sciences of the United States of America |
Bergonzo C, Grishaev A. (2019) Accuracy of MD solvent models in RNA structure refinement assessed via liquid-crystal NMR and spin relaxation data. Journal of Structural Biology |
Bergonzo C, Grishaev A. (2019) Maximizing accuracy of RNA structure in refinement against residual dipolar couplings. Journal of Biomolecular Nmr |
Best RB, Zheng W, Borgia A, et al. (2018) Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water". Science (New York, N.Y.). 361 |
Lin X, Roy S, Jolly MK, et al. (2018) PAGE4 and Conformational Switching: Insights from Molecular Dynamics Simulations and Implications for Prostate Cancer. Journal of Molecular Biology |
Debnath S, Kosek D, Tagad HD, et al. (2018) A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity. The Journal of Biological Chemistry |
Grishaev AV. (2017) Hybrid Applications of Solution Scattering to Aid Structural Biology. Advances in Experimental Medicine and Biology. 1009: 215-227 |
Shen Y, Roche J, Grishaev A, et al. (2017) Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins. Protein Science : a Publication of the Protein Society |
Kulkarni P, Jolly MK, Jia D, et al. (2017) Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity. Proceedings of the National Academy of Sciences of the United States of America |