About: Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme

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About: Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 1958

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1958 (uk) im Oktober 1958 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 1958 (ast) scientific article published on 01 October 1958 (en) 1958 թվականի հոկտեմբերի 1-ին հրատարակված գիտական հոդված (hy)
publication date	wds:Q78368684-A224F9C4-6512-4AB0-B0E1-06C24C8A2A58
publication date	1958-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q78368684-4B966923-B570-439F-964D-61FF87902052
language of work or name	English
author name string	wds:Q78368684-04F2B517-3DD7-4DE2-A487-080C6CBCFDE4 wds:Q78368684-8ED25FFE-01F8-46B4-98E4-DB6A3FEA3CB9 wds:Q78368684-AABF5396-0BA5-4CCF-B986-C3540AA51D92
author name string	I B WILSON S GINSBURG C QUAN
rdfs:label	Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme (en) Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme (nl)
skos:prefLabel	Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme (en) Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme (nl)
name	Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme (en) Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme (nl)
title	wds:Q78368684-D979E440-AF42-419D-B861-990BAA8EAB30
title	Molecular complementariness as basis for reactivation of alkyl phosphate-inhibited enzyme (en)
page(s)	wds:Q78368684-7FF493ED-ED9C-4B63-BD60-563A43AA22CC
page(s)	286-296
instance of	wds:Q78368684-206C4821-591D-4DAD-BFF7-1EE94672985D
instance of	scholarly article
PubMed ID	wds:Q78368684-AE74EEB5-F486-4309-BE08-AE81EA485449
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13583993
PubMed ID	13583993
published in	wds:Q78368684-5B4C0BAC-0459-4CCE-A058-9142617DA397
published in	Archives of Biochemistry and Biophysics
issue	wds:Q78368684-6EF372A0-5405-4B95-B663-E7A54D022ACB
volume	wds:Q78368684-0D66B4E6-F9B0-46EE-97B3-7A219B44078B
issue	2
volume	77
DOI	wds:Q78368684-88AD066A-A3E4-4696-9354-24ED325D04E8
DOI	http://dx.doi.org/10.1016/0003-9861(58)90077-8
DOI	10.1016/0003-9861(58)90077-8
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q78368684
is cites work of	Stereochemistry of adrenergic receptors: newer concepts on the molecular mechanism of action of catecholamines and antiadrenergic drugs at the receptor level Electron microscope radioautography as a quantitative tool in enzyme cytochemistry. II. The distribution of DFP-reactive sties at motor endplates of a vertebrate twitch muscle The ultrastructural localization and quantitation of cholinergic receptors at the mouse motor endplate Quantitative studies on enzymes in structures in striated muscles by labeled inhibitor methods. I. The number of acetylcholinesterase molecules and of other DFP-reactive sites at motor endplates, measured by radioautography Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis Endplates after esterase inactivationin vivo: correlation between esterase concentration, functional response and fine structure Electron microscope radioautography as a quantitative tool in enzyme cytochemistry. I. The distribution of acetylcholinesterase at motor end plates of a vertebrate twitch muscle Quantitative studies on enzymes in structures in striated muscles by labeled inhibitor methods. II. Confirmation of radioautographic measurement by liquid-scintillation counting The molecular weight and subunit structure of acetylcholinesterase preparations from the electric organ of the electric EEL Chemical Factors Controlling Nerve Activity Reactivation and aging of diphenyl phosphoryl acetylcholinesterase Formation of an unstable covalent intermediate during the inhibition of electric-eel acetylcholinesterase with 1,3,2-dioxaphosphorinane 2-oxides The subunits of an acetylcholinesterase preparation purified from trypsin-treated electric eel tissue Novel selective and irreversible mosquito acetylcholinesterase inhibitors for controlling malaria and other mosquito-borne diseases Rational design of alkylene-linked bis-pyridiniumaldoximes as improved acetylcholinesterase reactivators Reactivation of phosphorylated acetocholinesterases by pyridinium aldoximes and related compounds Antidotes in Anticholinesterase Poisoning Acetylcholinesterase in the fast extraocular muscle of the mouse by light and electron microscope autoradiography Oxime Reactivation of Diethylphosphoryl Human Serum Cholinesterase Number and Location of Acetylcholinesterase Molecules at Motor Endplates of the Mouse Quantitative studies of the effect of antagonists on the acute toxicity of organophosphates in rats Synthesis of aldoxime analogs of arecoline as reactivators of organophosphorus inhibited cholinesterase Structure-activity relation in organophosphorus-inhibited acetylcholinesterase reactivators III: Methiodides of hydroxyimino derivatives of pyridylethanes Acetylcholinesterase: evidence that sodium ion binding at the anionic site causes inhibition of the second-order hydrolysis of acetylcholine and a decrease of its pKa as well as of deacetylation Biological responsiveness to cholinesterase inhibition: A test for exploring the developmental maturity of the cholinergic system Location and measurement of enzymes in single cells by isotopic methods. II. Application to electron microscopy.
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