About: Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation

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About: Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation Goto Sponge NotDistinct Permalink

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scientific article published on May 1971

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 1971 (ast) 1971年學術文章 (zh) наукова стаття, опублікована в травні 1971 (uk) مقالة علمية نشرت في مايو 1971 (ar) scientific article published on May 1971 (en)
publication date	wds:Q37474810-40F0EBBD-C4DB-4916-AC5B-D6E89C0C1337
publication date	1971-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37474810-B73201C9-CCF1-4848-B953-467C1A950CE6
language of work or name	English
cites work	wds:Q37474810-57A3B3C0-A496-4E0F-80B1-F693218EDEA9 wds:Q37474810-9769D46C-5148-438A-922D-2D75BDDA4757 wds:Q37474810-9B3B9EEB-C407-4422-AA74-AFA6E549C033 wds:Q37474810-B26DAA78-C0FB-4C88-B183-9D9D9999B31B wds:Q37474810-C8AB080E-5E6C-4D96-8814-CA28AFE8B5F6 wds:Q37474810-CBA1BCB9-06AF-480B-A8EE-AAD98289454A wds:Q37474810-E47DCC5E-3E27-477A-B1A9-69411981E200 wds:Q37474810-F04B1976-56AF-47CD-ADDC-D64B56DE001F
cites work	ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL The Catalytic and Regulatory Properties of Enzymes Conformational changes in glutamine synthetase from Escherichia coli. II. Some characteristics of the equilibrium binding of feedback inhibitors to the enzyme Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits* STRUCTURAL ALTERATIONS IN CRYSTALLINE GLUTAMIC DEHYDROGENASE INDUCED BY STEROID HORMONES. On the role of amino groups in the structure and function of glutamate dehydrogenase. II. Effect of acetylation on molecular properties GLUTAMATE DEHYDROGENASE. V. THE RELATION OF ENZYME STRUCTURE TO THE CATALYTIC FUNCTION THE REVERSAL BY ORGANIC MERCURIALS OF "ALLOSTERIC" CHANGES IN GLUTAMATE DEHYDROGENASE
author name string	wds:Q37474810-8BC9079C-97E8-4F02-B525-444E42B40E89 wds:Q37474810-8C25531A-F834-4CF5-9A9D-40B9723CF10A
author name string	Kallos J Shaw KP
rdfs:label	Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (en) Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (nl) Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (ast)
skos:prefLabel	Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (en) Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (nl) Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (ast)
name	Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (en) Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (nl) Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (ast)
title	wds:Q37474810-68568E2B-1F23-4E67-BCA3-1EC53270E099
title	Covalent attachment of diethylstilbestrol to glutamate dehydrogenase: implications for allosteric regulation (en)
page(s)	wds:Q37474810-A1361E5D-0A15-4CFD-9F91-CE5307237048
page(s)	916-919
instance of	wds:Q37474810-A91AD143-9FF9-49BE-86AF-D2536943C4FD
instance of	scholarly article
PubMed ID	wds:Q37474810-F35D529B-23A5-4AB7-BF1E-570C3C2C00A3
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4325003
PubMed ID	4325003
published in	wds:Q37474810-DE52136F-060D-48B6-AEA4-A9F0B26C8598
published in	Proceedings of the National Academy of Sciences of the United States of America
issue	wds:Q37474810-20B94EC9-4F69-4F4E-967A-B430A3481D96
volume	wds:Q37474810-1F34B7E7-E8D4-4E8A-8764-F1D32B0BE30C
issue	5
volume	68
number of pages	wds:Q37474810-3D8DF194-73AB-498C-B94A-3D3061C4EA05
number of pages	4 (xsd:decimal)
DOI	wds:Q37474810-99A7247A-8E09-41E1-9F40-0CC26BE50432
DOI	http://dx.doi.org/10.1073/PNAS.68.5.916
DOI	10.1073/PNAS.68.5.916
ResearchGate publication ID	wds:Q37474810-F8ACF65D-3DD6-41C0-9062-AEBF439AB359
ResearchGate publication ID	18840926
ADS bibcode	wds:Q37474810-4B1133FA-3A1C-4EB3-B69B-9DE829985CE1
ADS bibcode	1971PNAS...68..916K
PMCID	wds:Q37474810-C8AE73BF-FF94-4B87-9D88-8E44E18791BE
PMCID	389080
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37474810
is cites work of	The reaction of a histidine residue in glutamate dehydrogenase with diethyl pyrocarbonate Estrogen modification of human glutamate dehydrogenases is linked to enzyme activation state. Bovine Liver Glutamate Dehydrogenase Affinity Labelling of the Estrogen Binding Site of Glutamate Dehydrogenase with Iodoacetyldiethylstilbestrol. Selective Alkylation of Cysteine-89
is cites work of	wds:Q28363117-41443A58-2E20-445F-A939-DEAA036F1E21 wds:Q28316970-FBA39952-27BC-4F3B-A8B7-341EFAEA8F3D wds:Q39101320-DBF64237-8D10-4C7E-BF9D-096671B4F6FA wds:Q34181345-03963FB1-D09D-4542-AC05-71A173DED3BC

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