About: Catalytic Activity of Sub-units of Glutamic Dehydrogenase

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) Նեյչրում հրատարակված հոդված (hy) im Dezember 1962 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в грудні 1962 (uk)
publication date	wds:Q59023439-1AA56326-EF8C-427F-8D83-0AE568E34E91
publication date	1962-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59023439-A1D4CB92-2AE3-46EF-82FF-901F5DC9B6D0
language of work or name	English
exact match	wds:Q59023439-4AA71CDF-37F4-4AA4-AB77-FF20C3CDFA54
exact match	https://scigraph.springernature.com/pub.10.1038/196895b0
cites work	wds:Q59023439-085FDA58-EC7F-4227-9362-FE046745D6B9 wds:Q59023439-13131505-B0D4-4F90-B836-D9940F6BD869 wds:Q59023439-AA77D335-D6EC-4875-BA0B-23D7DBB124CE
cites work	The dissociation of glutamic dehydrogenase by reduced diphosphopyridine nucleotide (DPNH) STRUCTURAL ALTERATIONS IN CRYSTALLINE GLUTAMIC DEHYDROGENASE INDUCED BY STEROID HORMONES. The nature of the alkaline dissociation of the glutamic dehydrogenase molecule
author name string	wds:Q59023439-13AA2AC7-4B8A-43AB-B2DD-170C258E8D07 wds:Q59023439-622FE6A6-084A-4631-B307-8ED996369B1B wds:Q59023439-89D9D9AF-2307-4A4B-92A6-B54B807CB5B2
author name string	D G CROSS H F FISHER L L McGREGOR
rdfs:label	Catalytic Activity of Sub-units of Glutamic Dehydrogenase (en) Catalytic Activity of Sub-units of Glutamic Dehydrogenase (nl)
skos:prefLabel	Catalytic Activity of Sub-units of Glutamic Dehydrogenase (en) Catalytic Activity of Sub-units of Glutamic Dehydrogenase (nl)
name	Catalytic Activity of Sub-units of Glutamic Dehydrogenase (en) Catalytic Activity of Sub-units of Glutamic Dehydrogenase (nl)
title	wds:Q59023439-82A73B69-B935-439B-A40E-76469C695F67
title	Catalytic activity of sub-units of glutamic dehydrogenase (en)
page(s)	wds:Q59023439-ECC5BA62-3C6B-443E-9B57-69436FED44BE
page(s)	895-896
instance of	wds:Q59023439-F48FE65C-8383-4C03-99F4-58CD017DDBBB
instance of	scholarly article
PubMed ID	wds:Q59023439-C38601A8-035A-4D71-AC99-95681610ED8E
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13945284
PubMed ID	13945284
published in	wds:Q59023439-C57621CA-38B2-49DE-872D-03C12830390C
published in	Nature
issue	wds:Q59023439-CE4CC687-54B6-4343-BCFB-9BE3589EA972
volume	wds:Q59023439-C6E9C2A9-42E5-48EF-9A90-23C3C39E069C
issue	4857
volume	196
DOI	wds:Q59023439-D909F635-B64E-4A56-ACA2-A0B15801CD8B
DOI	http://dx.doi.org/10.1038/196895B0
DOI	10.1038/196895B0
Dimensions Publication ID	wds:Q59023439-626052C4-F082-42F0-8ED0-2FE0A7A7DDAF
Dimensions Publication ID	1005910493
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59023439
is cites work of	The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery Allosteric Regulation of Enzyme Activity Chemical modification of glutamate dehydrogenase by 2,4,6-trinitrobenzenesulphonic acid Ligand-induced oligomerization and regulatory mechanism THE DISSOCIATION AND ASSOCIATION OF PROTEIN STRUCTURES. Ox liver glutamate dehydrogenase. The use of chemical modification to study the relationship between catalytic sites for different amino acid substrates and the question of kinetic non-equivalence of the subunits REAGENT-INDUCED CHANGES IN THE STRUCTURE AND CATALYTIC ACTIVITY OF GLUTAMIC DEHYDROGENASE Bovine Liver Glutamate Dehydrogenase The functional relationship between polymerization and catalytic activity of beef liver glutamate dehydrogenase. I. Theory THE INDEPENDENCE OF THE SUBSTRATE SPECIFICITY OF GLUTAMATE DEHYDROGENASE ON ITS STATE OF AGGREGATION Properties of rat renal phosphate-dependent glutaminase coupled to Sepharose. Evidence that dimerization is essential for activation Reversible Inactivation and Dissociation of Yeast Hexokinase Subunit association and catalytic activity of uridine diphosphate galactose-4-epimerase from yeast Observations on ox-liver L-glutamate dehydrogenase with the electron microscope Effect of cofactors, oestrogens and magnesium ions on the activity and stability of human glutamate dehydrogenase A VISCOSITY AND SEDIMENTATION STUDY ON GLUTAMATE DEHYDROGENASE Determination of the stokes radius of native and succinylated glutamate dehydrogenase on sepharose 4B [Structure and function of proteins] Circular dichroism spectra of glutamate dehydrogenase plus reduced nicotinamide adenine dinucleotide
is cites work of	wds:Q39903288-3425C056-C401-4E27-B7EE-DDD0F56C4C2D wds:Q78483561-20A96A2F-16D6-4E83-819B-8409308E891A wds:Q33802949-B36D07A5-865F-4A18-A898-C926DD1B94DF wds:Q78520685-579F55D8-F4C8-43D2-A3E4-C5039C81A8DD wds:Q40041716-FFB8D967-0360-481E-BEDF-AB5F4DA9861D wds:Q68215075-069B22B3-1C8A-4F1F-8D7B-8D2D0022F2F4 wds:Q72604083-869064D5-6B64-413B-866B-1687C569E301 wds:Q30992659-D5B60A32-9D82-441D-A346-5AF7AF36EB63 wds:Q41839361-2FE765C4-C83C-4885-9966-52B6F8315966 wds:Q76894756-55FCC2EB-272A-49A3-95FF-FCF37DA3207D wds:Q39101320-21C0F945-1BD3-4404-ACE4-AAC2BDBCB7FD wds:Q39960679-5618B01A-B71E-49A6-8159-7E62113AC145 wds:Q27619175-18E1613D-DC2F-4341-BD94-4E8B03A0F89B wds:Q42934402-9AA175F0-FD05-46CC-AAE7-887D080640CF wds:Q42848072-B84DF284-0B0D-4AED-83B4-A079650291D6 wds:Q71461893-05CDD00D-88C1-42D8-9193-7C455D9D9876 wds:Q35442217-79A05471-BC3F-465F-AFC0-D4932741840E wds:Q42965244-7CBFAF30-C8B5-4576-91AF-37A4EF6612CB wds:Q69588486-D82463D4-5248-46B2-851F-99EE367BC838

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