Current Search:  Research Repository (x) » Citation (x) » Shukla, P. (x) » Department of Physics (x) » Institute of Molecular Biophysics (x)

Search results

  • CSV Spreadsheet
(1 - 20 of 20)
Advancing NMDA Receptor Physiology by Integrating Multiple Approaches.
Allosteric activation of SENP1 by SUMO1 β-grasp domain involves a dock-and-coalesce mechanism.
Challenges in structural approaches to cell modeling.
Conserved Glycine Harboring Disease-associated Mutations Permits Nmda Receptor Slow Deactivation And High Ca2+ Permeability
Divergent roles of a peripheral transmembrane segment in AMPA and NMDA receptors.
dock-and-coalesce mechanism for the association of a WASP disordered region with the Cdc42 GTPase.
Electrostatic effects on the folding stability of FKBP12.
Fast Method for Computing Chemical Potentials and Liquid-Liquid Phase Equilibria of Macromolecular Solutions.
Gating Motions and Stationary Gating Properties of Ionotropic Glutamate Receptors
Liquid-liquid Phase Separation Of Patchy Particles Illuminates Diverse Effects Of Regulatory Components On Protein Droplet Formation
Mechanism and rate constants of the Cdc42 GTPase binding with intrinsically disordered effectors.
Prediction of homoprotein and heteroprotein complexes by protein docking and template-based modeling
Protein Allostery and Conformational Dynamics.
Protein folding, binding, and droplet formation in cell-like conditions.
Rate Constants and Mechanisms of Protein-Ligand Binding.
Semiclosed Conformations of the Ligand-Binding Domains of NMDA Receptors during Stationary Gating.
Structural modeling for the open state of an NMDA receptor.
The Transmembrane Domain Mediates Tetramerization of -Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors
Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors.
Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.