Comparative molecular dynamics simulations: Glutamate receptors and periplasmic binding proteins

Comparative molecular dynamics simulations: Glutamate receptors and periplasmic binding proteins

Manylion Llyfryddiaeth
Prif Awduron:	Sansom, M, Pang, A, Arinaminpathy, Y, Kaye, S, Tai, K, Wu, B, Biggin, P
Fformat:	Conference item
Cyhoeddwyd:	2004

Eitemau Tebyg

Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2.
gan: Arinaminpathy, Y, et al.
Cyhoeddwyd: (2002)

Binding site flexibility: Molecular simulation of partial and full agonists within a glutamate receptor
gan: Arinaminpathy, Y, et al.
Cyhoeddwyd: (2006)

Binding site flexibility: molecular simulation of partial and full agonists within a glutamate receptor.
gan: Arinaminpathy, Y, et al.
Cyhoeddwyd: (2006)

Interdomain dynamics and ligand binding: molecular dynamics simulations of glutamine binding protein.
gan: Pang, A, et al.
Cyhoeddwyd: (2003)

Conformational dynamics of glutamate receptors: MD simulations of the ligand-binding domains of GluR2 and GluR0
gan: Arinaminpathy, Y, et al.
Cyhoeddwyd: (2004)

A prokaryotic glutamate receptor: homology modelling and molecular dynamics simulations of GluR0.
gan: Arinaminpathy, Y, et al.
Cyhoeddwyd: (2003)

Molecular dynamics simulations of the ligand-binding domain of an N-methyl-D-aspartate receptor.
gan: Kaye, S, et al.
Cyhoeddwyd: (2006)

Homology modelling and molecular dynamics simulations of a prokaryotic glutamate receptor: GluR0
gan: Arinaminpathy, Y, et al.
Cyhoeddwyd: (2002)

Simulation studies of glutamate receptors.
gan: Biggin, P, et al.
Cyhoeddwyd: (2003)

Comparative molecular dynamics--similar folds and similar motions?
gan: Pang, A, et al.
Cyhoeddwyd: (2005)

Steered molecular dynamics simulations predict conformational stability of glutamate receptors.
gan: Musgaard, M, et al.
Cyhoeddwyd: (2016)

Ionontropic Glutamate Receptors: Insight into the Mechanism of Desensitization and Deactivation using Molecular Dynamics Simulations
gan: Amara, N, et al.
Cyhoeddwyd: (2012)

Computational investigation of the role of disulphide bonds in the ligand-binding domain of NMDA receptors.
gan: Kaye, S, et al.
Cyhoeddwyd: (2007)

A comparative analysis of the role of water in the binding pockets of ionotropic glutamate receptors.
gan: Vijayan, R, et al.
Cyhoeddwyd: (2010)

In silico mutation of cysteine residues in the ligand-binding domain of an N-methyl-D-aspartate receptor.
gan: Kaye, S, et al.
Cyhoeddwyd: (2007)

Glutamate receptors: desensitizing dimers.
gan: Biggin, P
Cyhoeddwyd: (2002)

Mapping periplasmic binding protein oligosaccharide recognition with neutron crystallography
gan: Shantanu Shukla, et al.
Cyhoeddwyd: (2022-10-01)

Solution NMR studies of periplasmic binding proteins and their interaction partners
gan: Pistolesi Sara, et al.
Cyhoeddwyd: (2011-04-01)

Molecular dynamics studies of AChBP with nicotine and carbamylcholine: the role of water in the binding pocket.
gan: Amiri, S, et al.
Cyhoeddwyd: (2007)

Membrane protein structure quality in molecular dynamics simulation.
gan: Law, R, et al.
Cyhoeddwyd: (2005)

Molecular dynamics simulations of membrane proteins.
gan: Biggin, P, et al.
Cyhoeddwyd: (2008)

Rigid body essential X-ray crystallography: distinguishing the bend and twist of glutamate receptor ligand binding domains.
gan: Bjerrum, E, et al.
Cyhoeddwyd: (2008)

Observing spontaneous, accelerated substrate binding in molecular dynamics simulations of glutamate transporters.
gan: Jiali Wang, et al.
Cyhoeddwyd: (2021-01-01)

Quantifying water-mediated protein-ligand interactions in a glutamate receptor: a DFT study
gan: Sahai, M, et al.
Cyhoeddwyd: (2011)

Quantifying water-mediated protein-ligand interactions in a glutamate receptor: a DFT study.
gan: Sahai, M, et al.
Cyhoeddwyd: (2011)

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation
gan: Takayuki Ohnuma, et al.
Cyhoeddwyd: (2023-11-01)

Crystallisation and Preliminary Crystallographic Analysis of Helicobacter pylori Periplasmic Binding Protein YckK
gan: Mohammad Mizanur Rahman, et al.
Cyhoeddwyd: (2017-10-01)

Role of cis-trans proline isomerization in the function of pathogenic enterobacterial Periplasmic Binding Proteins.
gan: Paulina Cortes-Hernandez, et al.
Cyhoeddwyd: (2017-01-01)

The alpha7 nicotinic acetylcholine receptor: molecular modelling, electrostatics, and energetics.
gan: Amiri, S, et al.
Cyhoeddwyd: (2005)

Membrane proteins: molecular dynamics simulations.
gan: Lindahl, E, et al.
Cyhoeddwyd: (2008)

Modulation of glutamate transport and receptor binding by glutamate receptor antagonists in EAE rat brain.
gan: Grzegorz Sulkowski, et al.
Cyhoeddwyd: (2014-01-01)

A refined open state of the glycine receptor obtained via molecular dynamics simulations
gan: Dämgen, M, et al.
Cyhoeddwyd: (2019)

A Refined Open State of the Glycine Receptor Obtained via Molecular Dynamics Simulations
gan: Dämgen, MA, et al.
Cyhoeddwyd: (2019)

Potassium and sodium ions in a potassium channel studied by molecular dynamics simulations.
gan: Biggin, P, et al.
Cyhoeddwyd: (2001)

Engineered fluorescent proteins illuminate the bacterial periplasm
gan: Thorben Dammeyer, et al.
Cyhoeddwyd: (2012-10-01)

Molecular simulations and biomembranes : from biophysics to function /
gan: Sansom, Mark S. P., et al.
Cyhoeddwyd: (2010)

Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story
gan: Sabato D'Auria, et al.
Cyhoeddwyd: (2013-02-01)

Molecular determinants of Neu5Ac binding to a tripartite ATP independent periplasmic (TRAP) transporter
gan: Parveen Goyal, et al.
Cyhoeddwyd: (2025-02-01)

Directional porin binding of intrinsically disordered protein sequences promotes colicin epitope display in the bacterial periplasm
gan: Housden, NG, et al.
Cyhoeddwyd: (2018)

Periplasmic-binding protein-based biosensors and bioanalytical assay platforms: Advances, considerations, and strategies for optimal utility
gan: Katie A. Edwards
Cyhoeddwyd: (2021-08-01)