About: Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme

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scientific article published on 01 July 1974

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1974 (uk) im Juli 1974 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 July 1974 (en) artículu científicu espublizáu en xunetu de 1974 (ast)
publication date	wds:Q70048506-4F4ADC6F-87B5-463B-8FF1-97E2897BCB82
publication date	1974-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q70048506-19C3271D-0C64-413C-8D86-762B22AC6D1A
language of work or name	English
cites work	wds:Q70048506-052DD8F8-73CE-424E-BAD0-4687CB5BC355 wds:Q70048506-2FD153C4-957D-4B42-8371-16FADC7EC213 wds:Q70048506-699B41AD-AA24-4C06-B0A6-B6E3DA53DC11 wds:Q70048506-787D869D-61D4-46F7-984D-96703D0B3AA8 wds:Q70048506-802A546B-23CB-4F14-A5F1-FE19C357BC10 wds:Q70048506-842F6A44-C7BC-4921-87AA-3B26C3F3F684 wds:Q70048506-885C3528-6FD7-4E43-9E1A-91A5561F6F02 wds:Q70048506-89A269E7-6846-4D92-A803-74B62D407530 wds:Q70048506-9EAB1312-E42D-44DC-BA0D-84ABF7E0BAE9 wds:Q70048506-BBDB8AD8-F9EA-4F23-9597-F3626AA529DC
cites work	EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. Discrete conformational states stabilized by NADP + and NADPH Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH. Human erythrocyte glucose 6-phosphate dehydrogenase: electron microscope studies on structure and interconversion of tetramers, dimers and monomers Human glucose 6-phosphate dehydrogenase: purification and characterization of Negro type variant (A+) and comparison with normal enzyme (B+) Subunit interactions of glucose-6-phosphate dehydrogenase from human erythrocytes Human erythrocyte glucose 6-phosphate dehydrogenase. Physical properties Active molecular unit and NADP content of human glucose 6-phosphate dehydrogenase. A new hepatic protein inactivating glucose 6-phosphate dehydrogenase Metabolism of human erythrocyte glucose-6-phosphate dehydrogenase. VI. Interconversion of multiple molecular forms.
author name string	wds:Q70048506-A0CF4160-0D2F-485B-B927-19775A1A063E wds:Q70048506-AEB7EE60-C137-479B-9170-62000E306921 wds:Q70048506-C87123A4-D8A9-4B75-AB9A-B965C1A1872B
author name string	A Morelli F Giuliano A De Flora
rdfs:label	Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme (en) Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme (nl)
skos:prefLabel	Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme (en) Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme (nl)
name	Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme (en) Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme (nl)
title	wds:Q70048506-135E10DA-BF00-437A-BE95-D63C6B54270F
title	Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme (en)
page(s)	wds:Q70048506-83FD138C-FBF4-40A9-A67D-60BF011A95C1
page(s)	406-413
instance of	wds:Q70048506-D829C0AA-A919-4B1C-862C-3A46F2818C50
instance of	scholarly article
main subject	wds:Q70048506-66542767-2A46-44C3-8C83-F67D19C03226
main subject	human erythrocyte
PubMed ID	wds:Q70048506-6AF36859-957A-490A-B80D-A8B5A2302A92
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4152246
PubMed ID	4152246
published in	wds:Q70048506-9DCC62F1-0D56-4358-B2FC-7B32D2EA8B88
published in	Biochemical and Biophysical Research Communications
issue	wds:Q70048506-1823E608-7D36-422C-80E0-C1863C7C5E16
volume	wds:Q70048506-C8F60D30-388B-4D7B-8B1B-465432088BCD
issue	1
volume	59
DOI	wds:Q70048506-D9AD0996-0165-47B6-8F94-76299BA477C7
DOI	http://dx.doi.org/10.1016/S0006-291X(74)80221-4
DOI	10.1016/S0006-291X(74)80221-4
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70048506
is cites work of	Glucose-6-Phosphate Dehydrogenases Expression, purification and characterization of GDP-D-mannose 4,6-dehydratase from Escherichia coli. Human erythrocyte glucose 6-phosphate dehydrogenase. Evidence for competitive binding of NADP and NADPH Hyperanodic forms of human glucose-6-phosphate dehydrogenase Identification of the binding domain for NADP+ of human glucose-6-phosphate dehydrogenase by sequence analysis of mutants Mutants of Chinese hamster ovary cells with altered glucose-6-phosphate dehydrogenase activity Half-site reactivity in 6-phosphogluconate dehydrogenase from human erythrocytes What is the role of the second "structural" NADP+-binding site in human glucose 6-phosphate dehydrogenase? A circadian study of liver antioxidant enzyme systems of female Fischer-344 rats subjected to dietary restriction for six weeks
is cites work of	wds:Q67062310-2F34A9DB-837E-418A-BE9E-7509070D9A99 wds:Q39784408-3880174C-1AAD-4A55-8975-9C713B069B1D wds:Q39102059-1793D2DF-933E-47B0-8636-CB7EBB85D339 wds:Q86630361-DAA264E2-442B-4C54-A00A-0F446A731742 wds:Q39221280-C9538C21-5D1D-4F9E-B50F-BEBB9D3568B5 wds:Q48047134-22D6B55E-C201-4579-B457-B76503AA406B wds:Q28637025-13589902-63A2-4225-9F9C-9CEBA23C835F wds:Q34326338-D8BE504E-0F05-4F68-8A8E-142FBA7C8A1A wds:Q28280773-AC0BBBF9-1C98-4C40-8627-AD3C78ADCA9E

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