About: Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative

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scientific article published on 01 April 1988

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 1988 (uk) im April 1988 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'abril de 1988 (ast) scientific article published on 01 April 1988 (en)
publication date	wds:Q68325529-EEBDED5B-5C6C-4482-8BBA-2C68C3084D7E
publication date	1988-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68325529-AD221308-6A90-4345-B6CE-9663C49F2B81
language of work or name	English
cites work	wds:Q68325529-41190634-F645-40D1-B410-259483E1B8DC wds:Q68325529-6BC58CF8-F81D-4D74-913D-D3B62A220FDD wds:Q68325529-8BE0DB0C-8243-4680-9014-61341A32FEFA wds:Q68325529-91B85B2D-A33F-4B17-9642-DF1BB977F4C3
cites work	Crystallization and a preliminary X-ray diffraction study of isozyme 3-3 of glutathione S-transferase from rat liver Multiple Forms of Human Glutathione S-Transferase and Their Affinity for Bilirubin Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing. Gamma-glutamylcysteine: a substrate for glutathione S-transferases
author name string	wds:Q68325529-A43C8C37-A5D0-4D52-92F4-439037F8EE24 wds:Q68325529-BA7B66A5-4197-4AFA-A3EB-1D2CD5435385
author name string	Mannervik B Danielson UH
rdfs:label	Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative (en) Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative (nl)
skos:prefLabel	Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative (en) Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative (nl)
name	Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative (en) Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative (nl)
author	wds:Q68325529-DE8D2D27-4910-4261-9607-92791606012B
author	Giovanni Principato
title	wds:Q68325529-FE34AA01-8CF7-4C44-A2C2-72264E209163
title	Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative (en)
page(s)	wds:Q68325529-ED7385AE-420C-468B-BE15-F71C4389F0B4
page(s)	155-158
instance of	wds:Q68325529-EAF3E016-0FE3-49BA-B4D4-BB44614F282F
instance of	scholarly article
main subject	wds:Q68325529-ECA02A65-B1FA-4E4A-B863-35D7BFD9C766
main subject	glutathione
PubMed ID	wds:Q68325529-2B09C0CF-9CF8-40B7-B5F1-640545E44FEF
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3360119
PubMed ID	3360119
published in	wds:Q68325529-16561950-681A-41EF-8C57-8A6CE1E09D90
published in	FEBS Letters
issue	wds:Q68325529-EFF40B58-63CF-43D7-9A20-54C908B3AD3A
volume	wds:Q68325529-DA6C4D98-F461-4D73-A11C-7E06BD63FC38
issue	1
volume	231
DOI	wds:Q68325529-AC6448DF-6362-42ED-9BAA-932A504A089B
DOI	http://dx.doi.org/10.1016/0014-5793(88)80722-1
DOI	10.1016/0014-5793(88)80722-1
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68325529
is cites work of	Site-directed mutagenesis and chemical modification of cysteine residues of rat glutathione S-transferase 3-3 The role of tyrosine-9 and the C-terminal helix in the catalytic mechanism of Alpha-class glutathione S-transferases The initial-rate kinetics of mouse glutathione S-transferase YfYf. Evidence for an allosteric site for ethacrynic acid Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme The inhibition of glutathione S-transferases: Mechanisms, toxic consequences and therapeutic benefits Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues Substrate specificity of rat liver glutathione S-transferase isoenzymes for a series of glutathione analogues, modified at the gamma-glutamyl moiety Effects of directed mutagenesis on conserved arginine residues in a human Class Alpha glutathione transferase Reversible modification of rat liver glutathione S-transferase 3-3 with 1-chloro-2,4-dinitrobenzene: specific labelling of Tyr-115. A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis Inhibition of glutathione S-transferase 3-3 by glutathione derivatives that bind covalently to the active site Effect of DOPA-loading on glutathione metabolising enzymes and tyrosinase in relation to 5-S-cysteinyl-DOPA genesis in cultured B-16 melanoma cells
is cites work of	wds:Q28318679-8D89C077-5A2A-43C1-96D9-857652EDA267 wds:Q41807951-172E8C42-BE7C-47EC-8650-16467C39624B wds:Q41784544-AB209309-73AE-4F2C-B87F-0172C181D7BF wds:Q43723324-9B3FB6A0-AC32-4438-BAB5-D391FC9BDB16 wds:Q73561096-7CCC0168-A3E4-455E-B978-6BC38C25B4AD wds:Q42414920-A0D333F5-D9C5-476F-A9E7-B8EBDC7C1B79 wds:Q41887637-30D93BAB-40EB-41DA-AA3B-16D054EF87FB wds:Q41986526-0FC18EBD-D35D-4A6C-B917-A463114CD44F wds:Q28360090-860FE503-12CC-4D1F-8955-3412C2F78FB1 wds:Q28332939-6BC3E0A7-7C74-4C7C-BBE4-3D289DB717C5 wds:Q36915586-9B26F5A3-C3A2-4D1A-A2FE-8500FF7EADE5 wds:Q42209400-6350CF0F-1329-498B-A23A-486DF06666D9

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