Acetylcholinesterase complexes with the natural product inhibitors dihydrotanshinone I and territrem B: binding site assignment from inhibitor competition and validation through crystal structure determination.

Acetylcholinesterase complexes with the natural product inhibitors dihydrotanshinone I and territrem B: binding site assignment from inhibitor competition and validation through crystal structure determination.

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Acetylcholinesterase complexes with the natural product inhibitors dihydrotanshinone I and territrem B: binding site assignment from inhibitor competition and validation through crystal structure determination.

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http://www.wikidata.org/entity/Q38191460

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article científic

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article scientifique

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articol științific

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articolo scientifico

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artigo científico

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artigo científico

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Acetylcholinesterase complexes ...... ystal structure determination.

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Acetylcholinesterase complexes ...... ystal structure determination.

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Acetylcholinesterase complexes ...... ystal structure determination.

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P1476

Acetylcholinesterase complexes ...... ystal structure determination.

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P2093

Jonah Cheung

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Kazuro Shiomi

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Terrone L Rosenberry

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Veena Beri

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P2860

Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.

Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo californica Acetylcholinesterase Reveals How Thioflavin T Acts as a Sensitive Fluorescent Reporter of Ligand Binding to the Acylation Site

Structures of human acetylcholinesterase in complex with pharmacologically important ligands

Structures of Human Acetylcholinesterase Bound to Dihydrotanshinone I and Territrem B Show Peripheral Site Flexibility

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

Interaction of fluorescence probes with acetylcholinesterase. The site and specificity of propidium binding

Molecular basis of inhibition of substrate hydrolysis by a ligand bound to the peripheral site of acetylcholinesterase.

Acetylcholinesterase inhibitors from plants and fungi.

Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites.

Interaction study of two diterpenes, cryptotanshinone and dihydrotanshinone, to human acetylcholinesterase and butyrylcholinesterase by molecular docking and kinetic analysis.

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s12031-014-0261-3

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506-510

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scholarly article

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10.1007/S12031-014-0261-3

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2014-02-27T00:00:00Z

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1006659939

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Acetylcholinesterase complexes with the natural product inhibitors dihydrotanshinone I and territrem B: binding site assignment from inhibitor competition and validation through crystal structure determination.

about

Acetylcholinesterase complexes with the natural product inhibitors dihydrotanshinone I and territrem B: binding site assignment from inhibitor competition and validation through crystal structure determination.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P6179

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P6179

P698