About: Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase

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scientific article (publication date: 28 March 2003)

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rdf:type	Item
description	article scientifique (publié 2003/03/28) (fr) articolo scientifico (pubblicato il 2003/03/28) (it) artigo científico (publicado na 2003/03/28) (pt) artículu científicu espublizáu en 2003 (ast) vedecký článok (publikovaný 2003/03/28) (sk) vetenskaplig artikel (publicerad på 2003/03/28) (sv) videnskabelig artikel (udgivet 2003/03/28) (da) vědecký článek publikovaný v roce 2003 (cs) 2003 թվականի մարտին հրատարակված գիտական հոդված (hy) научни чланак (објављен 2003/03/28) (sr) مقالة علمية (نشرت في 28-3-2003) (ar) наукова стаття, опублікована в березні 2003 (uk) 2003 թուականի Մարտին հրատարակուած գիտական յօդուած (hyw) wetenschappelijk artikel (gepubliceerd op 28.03.2003) (nl) scientific article (publication date: 28 March 2003) (en) im März 2003 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q27640850-284C82FF-1A1F-41EC-811E-6FF9800AD7B1
publication date	2003-03-28 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q27640850-B8BFBF14-CB76-4409-AA91-9B531F47112E
language of work or name	English
author name string	wds:Q27640850-3A79284E-5F31-4083-B59D-2BABB07284DA wds:Q27640850-8984981F-30A6-4E7D-BAD1-6176EC9CE76A wds:Q27640850-C9E540FE-6195-4A85-A315-AA9E8CB61964 wds:Q27640850-E492D43B-B92C-480A-BF6C-0878EC14934E
OpenCitations bibliographic resource ID	wds:Q27640850-CB97E1E0-6D35-448E-84EA-B37B38762130
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2345874
author name string	Yang Shen Hailong Zhang Liang Tong Zhiru Yang
OpenCitations bibliographic resource ID	2345874
rdfs:label	Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (en) Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (nl) Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (ast)
skos:prefLabel	Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (en) Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (nl) Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (ast)
name	Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (en) Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (nl) Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (ast)
title	wds:Q27640850-70DDB875-8B72-454A-8A6F-FDF918C5B355
title	Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (en)
page(s)	wds:Q27640850-5CB0C71A-B6D1-47BF-B5DD-194F24698044
page(s)	2064-7
instance of	wds:Q27640850-CBA2ED07-8512-4EFF-9D95-7CE1CCA7783C
instance of	scholarly article
main subject	wds:Q27640850-75C614A5-CB00-4E07-B4DB-7F4D64F5D1C8
main subject	crystal structure
PubMed ID	wds:Q27640850-D6D6DC60-369F-4B08-8CFB-AF40DB379B95
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12663926
PubMed ID	12663926
published in	wds:Q27640850-895A5596-23A7-4AA4-BCC4-4D8AEFE92AC4
published in	Science
issue	wds:Q27640850-DD0D9C97-04C6-4E9A-A37D-4762AC9CEC1C
volume	wds:Q27640850-3AC3B381-D2BE-4977-88A1-C3D8B6672BF5
issue	5615
volume	299
DOI	wds:Q27640850-8E7E5A12-7626-48FA-A655-6D13D5955913
DOI	http://dx.doi.org/10.1126/SCIENCE.1081366
DOI	10.1126/SCIENCE.1081366
Fatcat ID	wds:Q27640850-975C4501-2CBF-4FB4-8ABB-63C3C4F6A0CC
Fatcat ID	release_i7h42oteivaktlzob5xfpugtmy
ResearchGate publication ID	wds:Q27640850-1A43C31C-2AEE-421C-9EDA-409A471192DB
ResearchGate publication ID	10832087
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q27640850
is cites work of	Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats. Treating the metabolic syndrome: acetyl-CoA carboxylase inhibition Acetyl-coenzyme A carboxylases: versatile targets for drug discovery Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation Inhibiting bacterial fatty acid synthesis Plant acetyl-CoA carboxylase: structure, biosynthesis, regulation, and gene manipulation for plant breeding Lipid metabolic enzymes: emerging drug targets for the treatment of obesity Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer Crystal structure of Spot 14, a modulator of fatty acid synthesis Enzymatic characterization of a prokaryotic urea carboxylase Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism Crystal structure of the α6β6 holoenzyme of propionyl-coenzyme A carboxylase Fungal metabolic model for 3-methylcrotonyl-CoA carboxylase deficiency. A different mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by tepraloxydim Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden Structure-guided Inhibitor Design for Human Acetyl-coenzyme A Carboxylase by Interspecies Active Site Conversion Structure, Activity, and Inhibition of the Carboxyltransferase -Subunit of Acetyl Coenzyme A Carboxylase (AccD6) from Mycobacterium tuberculosis Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop. Linking genotype and phenotype of Saccharomyces cerevisiae strains reveals metabolic engineering targets and leads to triterpene hyper-producers. Structure and function of biotin-dependent carboxylases The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms Chemical genetics of acetyl-CoA carboxylases. Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasites Andrimid producers encode an acetyl-CoA carboxyltransferase subunit resistant to the action of the antibiotic Molecular bases for sensitivity to acetyl-coenzyme A carboxylase inhibitors in black-grass Potential functional replacement of the plastidic acetyl-CoA carboxylase subunit (accD) gene by recent transfers to the nucleus in some angiosperm lineages. Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected] Structure, function and selective inhibition of bacterial acetyl-coa carboxylase Characterization of the mycobacterial acyl-CoA carboxylase holo complexes reveals their functional expansion into amino acid catabolism Resistance to acetyl-CoA carboxylase-inhibiting herbicides Overproduction of fatty acids in engineered Saccharomyces cerevisiae.

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