(Q46577646)

English

Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin

scientific article published in September 1997

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin (English)

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

1 reference

based on heuristic

inferred from title

author name string

Radić Z

1

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

Kirchhoff PD

2

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

Quinn DM

3

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

McCammon JA

4

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

Taylor P

5

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

language of work or name

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publication date

1 September 1997

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

272

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

37

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

23265-23277

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands.

1 reference

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21 January 2018

Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

The determinants of pKas in proteins

1 reference

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21 January 2018

Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding Protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Acetylcholinesterase: electrostatic steering increases the rate of ligand binding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Simulation of charge-mutant acetylcholinesterases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Interaction of fluorescence probes with acetylcholinesterase. Site and specificity of propidium binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Ligand-induced conformational changes in acetylcholinesterase investigated with fluorescent phosphonates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

A new and rapid colorimetric determination of acetylcholinesterase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Allosteric control of acetylcholinesterase catalysis by fasciculin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Open "back door" in a molecular dynamics simulation of acetylcholinesterase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Acetylcholinesterase: diffusional encounter rate constants for dumbbell models of ligand

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp

1 reference

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21 January 2018

Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Ligand exclusion on acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Acetylcholinesterase as polyelectrolyte in reaction with cationic substrates.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

A model of the nicotinic receptor extracellular domain based on sequence identity and residue location

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian Dynamics program

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.37.23265

21 January 2018

Identifiers

10.1074/JBC.272.37.23265

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/9287336

ResearchGate publication ID

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