Evidence map›Paper›PMID 20138030›Full record

ArticleChemico-biological interactions2010

Acetylcholinesterase: from 3D structure to function.

Hay Dvir, Israel Silman, Michal Harel, Terrone L Rosenberry, Joel L Sussman

Abstract read
In one paragraph

Article in Chemico-biological interactions, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 207 papers.

0numbers the graph read from it
0cells of the map it votes in
207citing papers in PubMed
19.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

207 citing papers in PubMed, 757 citations in OpenAlex.

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147 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Hay DvirDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
Israel Silman
Michal Harel
Terrone L Rosenberry
Joel L Sussman
Weizmann Institute of Science · ILJacksonville College · US

Funding

Training and Education CoreU54NS058183 · NINDS · U.S. ARMY MEDICAL RESEARCH INST CHEM DEF · PI CERASOLI, DOUGLAS MARK, MAGLIERY, THOMAS J · 2006 to 2013
$20.6M
STRUCTURAL DISTINCTIONS AMONG ACETYLCHOLINESTERASESR01NS016577 · NINDS · MAYO CLINIC JACKSONVILLE · PI ROSENBERRY, TERRONE L · 1985 to 2005
$1.3M
NINDS NIH HHS 1U54NS058183NINDS NIH HHS NS-16577NINDS NIH HHS R01 NS016577NINDS NIH HHS U54 NS058183
6 · The paper itself

Abstract

By rapid hydrolysis of the neurotransmitter, acetylcholine, acetylcholinesterase terminates neurotransmission at cholinergic synapses. Acetylcholinesterase is a very fast enzyme, functioning at a rate approaching that of a diffusion-controlled reaction. The powerful toxicity of organophosphate poisons is attributed primarily to their potent inhibition of acetylcholinesterase. Acetylcholinesterase inhibitors are utilized in the treatment of various neurological disorders, and are the principal drugs approved thus far by the FDA for management of Alzheimer's disease. Many organophosphates and carbamates serve as potent insecticides, by selectively inhibiting insect acetylcholinesterase. The determination of the crystal structure of Torpedo californica acetylcholinesterase permitted visualization, for the first time, at atomic resolution, of a binding pocket for acetylcholine. It also allowed identification of the active site of acetylcholinesterase, which, unexpectedly, is located at the bottom of a deep gorge lined largely by aromatic residues. The crystal structure of recombinant human acetylcholinesterase in its apo-state is similar in its overall features to that of the Torpedo enzyme; however, the unique crystal packing reveals a novel peptide sequence which blocks access to the active-site gorge.

Indexed as

AcetylcholinesteraseAnimalsApoenzymesCatalytic DomainCrystallography, X-RayHumansModels, MolecularProtein Structure, QuaternaryStatic ElectricityStructure-Activity RelationshipAcetylcholinesteraseApoenzymes

Identifiers

PMID20138030
PMCPMC2894301
OpenAlexW2149098307

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.