About: Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes

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About: Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes Goto Sponge NotDistinct Permalink

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scientific article published on 01 September 1987

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у вересні 1987 (uk) im September 1987 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en setiembre de 1987 (ast) scientific article published on 01 September 1987 (en)
publication date	wds:Q69212308-0744B33C-134C-4374-BA79-678EBC7EE9FB
publication date	1987-09-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q69212308-BBF71C96-33A9-4EB6-A058-EEEE662DDF46 wds:Q69212308-D8E62A02-D4E7-489E-A791-A86F6415FA89 wds:Q69212308-EB6713E0-342A-4974-AD66-14DD31A1AFA7 wds:Q69212308-F67CBA3D-9CF2-4802-9602-0AD098E7A094
author name string	B L Vallee H Jörnvall H Eklund E Horjales
rdfs:label	Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes (en) Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes (nl)
skos:prefLabel	Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes (en) Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes (nl)
name	Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes (en) Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes (nl)
title	wds:Q69212308-676B483A-97F7-46AE-A195-0B556FF3857E
title	Computer-graphics interpretations of residue exchanges between the alpha, beta and gamma subunits of human-liver alcohol dehydrogenase class I isozymes (en)
page(s)	wds:Q69212308-44A876EE-B907-45CE-A947-55D1ED328EE9
page(s)	185-193
instance of	wds:Q69212308-B0D89D46-36BC-44E9-BB55-5E55F38098E7
instance of	scholarly article
PubMed ID	wds:Q69212308-0C89AF10-9108-4C95-B4DE-7154A5631153
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3622513
PubMed ID	3622513
published in	wds:Q69212308-091ACF22-BA80-4AAD-9DF5-3E3E436B344B
published in	FEBS Journal
issue	wds:Q69212308-CF3B5A90-7290-4CC6-816B-B9E7CBD1089A
volume	wds:Q69212308-DF61C7AB-44B2-4CEA-B88C-A91196313F14
issue	2
volume	167
DOI	wds:Q69212308-F2B81584-5A4D-4B25-8110-814687C3B10E
DOI	http://dx.doi.org/10.1111/J.1432-1033.1987.TB13322.X
DOI	10.1111/J.1432-1033.1987.TB13322.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q69212308
is cites work of	Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93. Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions "Enzymogenesis": classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites Genetic polymorphism and activities of human lung alcohol and aldehyde dehydrogenases: implications for ethanol metabolism and cytotoxicity Mutations of gamma-aminobutyric acid and glycine receptors change alcohol cutoff: evidence for an alcohol receptor? A review of alcohol clearance in humans Interaction between the functional polymorphisms of the alcohol-metabolism genes in protection against alcoholism Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family Site specificity of protein glycation. Closely related isozymes of alcohol dehydrogenase. Carboxymethylation: gamma 1 gamma 1 differs widely from both beta 1 beta 1 and its equine equivalence EE Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by Castellaniella defragrans H8Zn(c)2 and Zn(c)2Co(n)2 human liver alcohol dehydrogenase Active-site-specific zinc-depleted and reconstituted cobalt(II) human-liver alcohol dehydrogenase. Preparation, characterization and complexation with NADH and trans-4-(N,N-dimethylamino)-cinnamaldehyde Human class III alcohol dehydrogenase/glutathione-dependent formaldehyde dehydrogenase Cloning of the Arabidopsis and rice formaldehyde dehydrogenase genes: implications for the origin of plant ADH enzymes Three-dimensional structures of the three human class I alcohol dehydrogenases Targeting Metalloenzymes for Therapeutic Intervention Cloning and sequencing of cDNA encoding baboon liver alcohol dehydrogenase: evidence for a common ancestral lineage with the human alcohol dehydrogenase beta subunit and for class I ADH gene duplications predating primate radiation Crystallisation and crystallographic investigations of cod alcohol dehydrogenase class I and class III enzymes Alcohol dehydrogenase of class III: consistent patterns of structural and functional conservation in relation to class I and other proteins. Use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase The role of serotonin and possible interaction of serotonin-related genes with alcohol dehydrogenase and aldehyde dehydrogenase genes in alcohol dependence-a review The effect of metal ions on the binding of ethanol to human alcohol dehydrogenase β2β2 cDNA sequence of the beta 2-subunit of human liver alcohol dehydrogenase Genotyping of human class I alcohol dehydrogenase. Analysis of enzymatically amplified DNA with allele-specific oligonucleotides Determination of the absolute configuration of (+)-neopentyl-1-d alcohol by neutron and x-ray diffraction analysis
is cites work of	wds:Q24562113-2BCA5A35-892D-4FEA-A461-38A7C2814D76 wds:Q24563768-A1B8870D-D5AE-40FC-9A41-FE8E1AF6424D wds:Q45106965-A9B75EB6-F16B-43E5-B114-AEC55142B2C2 wds:Q59830619-4E67EAC5-D56E-47CC-8C21-7C5BE2A8DCFE wds:Q41708910-22B68BF0-94C0-43E5-8CAD-5F4DB75AD20F wds:Q45236704-46A145A0-51B8-4803-805D-F34E7B031159 wds:Q68198151-786C6758-B1DE-4575-9788-1853674EA3B5 wds:Q74453046-90258E48-58C6-4EE4-9595-438F8BDC80EE wds:Q24304464-8EBEC288-85FD-4C11-A60E-7DAB83BCEC98 wds:Q41848699-BD23ED87-3A47-4EB5-BF9E-92C68B27FAC4 wds:Q44414794-CD5B2391-A3BC-4ADB-BCA2-992EFB559437 wds:Q24617205-25013D57-FAE7-490E-88EC-2A12B2CC4A78 wds:Q34390264-9F266AC9-AF2C-4E9D-AA9E-A28785001453 wds:Q33264686-583CED58-616F-4C44-A5ED-EF40803A3E94 wds:Q48069848-29F27F58-2FBC-4912-9B91-08B1A0875F81 wds:Q47728588-8A58C883-ACB9-48AA-A846-90D9767B8733 wds:Q28776600-4679B06A-3F27-4897-9BDC-20B6177C15B3 wds:Q33793503-E76699BC-C429-4817-BD90-22A8A44B846D wds:Q37438358-370B981A-4589-4B72-9EDE-34B0A8985C1D wds:Q36421487-C1F629C0-F12F-46DC-98E3-167F88DD4DD9 wds:Q72134248-D4A37D06-3B57-4951-AB45-4CE2F6ECFD45 wds:Q68325046-9841E852-DFE4-4D40-9D6A-00AAD6D3C333 wds:Q68267609-EEEA3551-AA73-4EDF-87F8-B9830E8BBFE2 wds:Q24644663-AB50B268-5517-4FA5-82DA-586547BED28D wds:Q36009645-CB4B6258-674D-49CA-B9E9-8AB023B250F3 wds:Q44272467-C000E483-37DE-4C2A-9E24-D34256338CA8 wds:Q51234587-6C585D7C-3E7C-4D1E-BF49-F88BC13A0702

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