Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer. - Wikidata - awgldk - TriplyDB

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

http://www.wikidata.org/entity/Q37281897

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Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members The role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthase Paths of long-range communication in the E2 enzymes of family 3: a molecular dynamics investigation.Diffusion and association processes in biological systems: theory, computation and experiment.Gated Diffusion-controlled Reactions Theory and simulation on the kinetics of protein-ligand binding coupled to conformational change.Distribution of intravenously administered acetylcholinesterase inhibitor and acetylcholinesterase activity in the adrenal gland: 11C-donepezil PET study in the normal rat Computational Studies on Acetylcholinesterases.

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P2860

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

http://www.wikidata.org/entity/Q37281897

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on August 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

@en

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

@nl

type

label

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

@en

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

@nl

prefLabel

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

@en

Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

@nl

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J.BPJ.2009.05.033

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Biophysical Journal

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Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.

@en

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Alemayehu A Gorfe

http://www.w3.org/2001/XMLSchema#string

Benzhuo Lu

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Zeyun Yu

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The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix

The association of tetrameric acetylcholinesterase with ColQ tail: a block normal mode analysis.

Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography

Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly

PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations

Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein

PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations

Finite element solution of the steady-state Smoluchowski equation for rate constant calculations

Tetrameric mouse acetylcholinesterase: continuum diffusion rate calculations by solving the steady-state Smoluchowski equation using finite element methods.

The peripheral anionic site of acetylcholinesterase: structure, functions and potential role in rational drug design.

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897-905

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scholarly article

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10.1016/J.BPJ.2009.05.033

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J. Andrew McCammon

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