About: Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex

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About: Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 1977

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1977 (uk) im Oktober 1977 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 October 1977 (en) artículu científicu espublizáu n'ochobre de 1977 (ast)
publication date	wds:Q67694986-2644795C-0F83-4951-9B7C-846916099E97
publication date	1977-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q67694986-EB030EB1-1D9A-4387-896B-9E24DD460014
language of work or name	English
cites work	wds:Q67694986-0E6E0B15-F3E1-496C-80ED-89525D516022 wds:Q67694986-1637663D-502D-4701-B339-FF8BB871B102 wds:Q67694986-16E6B22F-2B0A-4EF9-98DA-B382CC879E06 wds:Q67694986-1A950FCB-1CC7-4157-92F9-C4379AF5D1DC wds:Q67694986-6DC1D43B-D06E-4382-9CFB-79C4935B4144 wds:Q67694986-8645DE0D-F32B-4793-959A-12DD439A3A3B wds:Q67694986-872F52D3-EDCC-466A-A2F4-9DEA566E27D2 wds:Q67694986-A4C0FBAC-885A-4F93-B054-478E2B6F2514 wds:Q67694986-A983150E-194C-45FB-963F-6F176E19BF1E wds:Q67694986-BC3A5347-CD81-42CF-BCAC-791BDC287106 wds:Q67694986-BFCFF68F-0C1E-4062-AE62-A9E5BF528E9C wds:Q67694986-C276A155-552A-4696-8C7E-35A38DDDF435 wds:Q67694986-CBA98F32-3AC8-4A12-8EAA-D617C955F98E wds:Q67694986-E12BCEF2-5D50-4C2A-8A4F-0BD234AC9186
cites work	Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Esherichia coli pyruvate dehydrogenase complex: Improved purification and the flavin content Structure of Yeast Phosphoglycerate Kinase -Keto acid dehydrogenase complexes. 18. Subunit composition of the Escherichia coli pyruvate dehydrogenase complex Rapid purification of lactate dehydrogenase from rat liver and hepatoma: a new approach. Blue dextran-sepharose: an affinity column for the dinucleotide fold in proteins Studies on the reaction mechanism of lipoyl dehydrogenase D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance Binding of human interferons to immobolized Cibacron Blue F3GA: The nature of molecular interaction The Pyruvate-Dehydrogenase Complex from Azotobacter vinelandii. 2. Regulation of the Activity Regulation of the activity of the pyruvate dehydrogenase complex of Escherichia coli. The Pyruvate‐Dehydrogenase Complex from Azotobacter vinelandii Studies on the formation of acetoin from acetaldehyde by the pyruvate dehydrogenase complex and its regulation The subunit structure of the pyruvate-dehydrogenase complex from Escherichia coli K-12. The core complex.
author name string	wds:Q67694986-6B572AFF-CFE4-419F-A54C-758FF0157B34 wds:Q67694986-9FDD2F04-0EAB-40FE-9EDE-DB3687CDC8BC wds:Q67694986-D0154EEF-8CFE-42E2-8A7A-FB692B3EB104
author name string	De Abreu RA Veeger C De Kok A
rdfs:label	Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex (en) Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex (nl)
skos:prefLabel	Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex (en) Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex (nl)
name	Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex (en) Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex (nl)
title	wds:Q67694986-C410331A-ABC6-41A0-82FE-D0DB1A92C7D5
title	Transformation of the 4-component pyruvate dehydrogenase complex from Azotobacter vinelandii into a 3-component complex (en)
page(s)	wds:Q67694986-8CFC0530-4530-4A56-B2B4-B035E7894B3E
page(s)	89-92
instance of	wds:Q67694986-D8FE8C72-CA02-475F-9016-AFD8478FBD6F
instance of	scholarly article
PubMed ID	wds:Q67694986-6FAA1BC1-8312-44D9-990A-EC078EDD1E17
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/913582
PubMed ID	913582
published in	wds:Q67694986-FCA9524F-5FD7-45E0-B889-B3896B262B90
published in	FEBS Letters
issue	wds:Q67694986-14E35A66-97D0-4B90-A398-2F15622614D5
volume	wds:Q67694986-6E26653B-472B-4E24-BDD2-59FE85489134
issue	1
volume	82
DOI	wds:Q67694986-5415EBE6-2C82-4A61-9CA6-9596E130F1F8
DOI	http://dx.doi.org/10.1016/0014-5793(77)80892-2
DOI	10.1016/0014-5793(77)80892-2
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q67694986
is cites work of	Structure and symmetry of B. stearothermophilus pyruvate dehydrogenase multienzyme complex and implications for eucaryote evolution Self-association of the pyruvate dehydrogenase complex from Azotobacter vinelandii in the presence of polyethylene glycol Protein purification using immobilised triazine dyes 4 Affinity chromatography on immobilized dyes Determination of the Chain Stoichiometries from the Number of Reactive Sulfhydryl Groups in the Pyruvate Dehydrogenase Complexes of Azotobacter vinelandii and Escherichia coli Crosslinking Studies with the Pyruvate Dehydrogenase Complexes from Azotobacter vinelandii and Escherichia coli Binding and dissociation of the pyruvate dehydrogenase complex of Azotobacter vinelandii on thiol--Sepharose
is cites work of	wds:Q41078791-D5C6A037-602C-4CC9-A688-D742FCB1B428 wds:Q66898514-3751BFDD-666F-46E5-81AB-16138D442261 wds:Q41674483-E81CC591-F62F-43EF-82BA-F5C310C67578 wds:Q70450894-E56D6D15-DB89-4A2C-AAF0-18FAF85901D7 wds:Q71397638-1E64A04C-36CE-4B89-B655-0D7E82FC3502 wds:Q72578350-9E2DFBC4-7046-4516-AC59-362630CC7B1B wds:Q40846787-4FB8030F-6015-44C3-B079-B56728CAC237

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