Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.
about
The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twistStructure and function of biotin-dependent carboxylasesA different mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by tepraloxydimCrystal Structures and Mutational Analyses of Acyl-CoA Carboxylase β Subunit of Streptomyces coelicolor ,Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxadenStructure-guided Inhibitor Design for Human Acetyl-coenzyme A Carboxylase by Interspecies Active Site ConversionStructure, Activity, and Inhibition of the Carboxyltransferase -Subunit of Acetyl Coenzyme A Carboxylase (AccD6) from Mycobacterium tuberculosisIdentification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37RvBroad resistance to ACCase inhibiting herbicides in a ryegrass population is due only to a cysteine to arginine mutation in the target enzymeNanomolecular HLA-DR10 antibody mimics: A potent system for molecular targeted therapy and imaging.Role of a novel I1781T mutation and other mechanisms in conferring resistance to acetyl-CoA carboxylase inhibiting herbicides in a black-grass populationSingle-site mutations in the carboxyltransferase domain of plastid acetyl-CoA carboxylase confer resistance to grass-specific herbicides.Trypanosoma brucei: inhibition of acetyl-CoA carboxylase by haloxyfopTreating the metabolic syndrome: acetyl-CoA carboxylase inhibition.Inhibiting bacterial fatty acid synthesis.Acetyl-coenzyme A carboxylases: versatile targets for drug discovery.Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats.Mechanism of metamifop inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in Echinochloa crus-galliStructure, function and selective inhibition of bacterial acetyl-coa carboxylase.The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.Resistance to acetyl-CoA carboxylase-inhibiting herbicides.Propesticides and their use as agrochemicals.Analysis of Arabidopsis Accessions Hypersensitive to a Loss of Chloroplast Translation.Malonyl coenzyme A affects insulin-stimulated glucose transport in myotubes.Effect of herbicide resistance endowing Ile-1781-Leu and Asp-2078-Gly ACCase gene mutations on ACCase kinetics and growth traits in Lolium rigidum.Study on the enantioselectivity inhibition mechanism of acetyl-coenzyme A carboxylase toward haloxyfop by homology modeling and MM-PBSA analysis.Clarification of pathway-specific inhibition by Fourier transform ion cyclotron resonance/mass spectrometry-based metabolic phenotyping studies.Designing an enzyme-based nanobiosensor using molecular modeling techniques.Resistance to spiromesifen in Trialeurodes vaporariorum is associated with a single amino acid replacement in its target enzyme acetyl-coenzyme A carboxylase.
P2860
Q24652953-44344E17-5AB1-4C36-A145-A295A24F1D06Q26851762-D6D4E04F-9342-42BD-9274-DAE1AD56D3B5Q27658275-4D991A26-EBAD-42C3-808C-70B4BBC216D3Q27663890-382D575A-9232-446C-8173-41386A324E11Q27666211-21FD6585-6262-4959-8D03-E5A3654B71E9Q27674547-383ACDC6-B248-41D7-9747-145DDB42D202Q27684939-F0D3C43C-2277-4373-88CA-D71D58CDB455Q28486833-9FCC181D-C7A3-4C0E-A1D8-CF8254B31E91Q28727677-C8AE68F5-94E4-465D-92E4-2D28D719DC26Q34117105-D1D3F030-C9F4-474F-8A99-4DDE163F4ECCQ34920459-DFCBE621-9696-4A21-BA07-66D3C0DD3CEEQ35645591-9F0BBA44-8E61-4A42-9366-2795A426A3BEQ35690720-718228ED-4AA6-4D1F-91F6-996C58F959CCQ36150834-B3A75501-8E9A-49F9-8FAA-2B79775D1466Q36464020-F54F800F-2A25-452C-A9D4-8F69339184B5Q36597445-7586C2FC-AE30-4B8F-B158-DA926A2CE446Q36770743-E46B9BBA-67A1-429F-91C8-CE32F4F7CE19Q37282360-8BCC6454-56BF-48CB-B33B-F781A88FA9F6Q37969915-EFCE9B2C-8C39-4A6F-8A57-1D67835DE866Q38042585-E50DA03A-2C5E-4D65-88C9-26680D3DE8C6Q38202075-0FFB0E27-2160-4389-A0FC-BC74CB6C34BDQ38602659-3289DC38-06D6-41BB-B798-07B194CCA65CQ38809395-36468621-1373-4851-962D-7E6645D7E845Q40128426-9DAA0D69-0541-4A25-BBD7-9CCFBE51F53CQ41923101-FEBADB30-ACF8-46FA-8CB6-434046A77496Q46778878-E82FADE7-DC4E-469D-B968-D4009EE88CC0Q51146896-3E484A7C-0F76-44F0-B739-E830FA32F7A3Q51583147-95C9551C-D464-49B3-AFFA-4AB1EF873230Q52735859-8D59A1EA-5975-4413-8B04-47B7D98B231B
P2860
Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 12 April 2004
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Molecular basis for the inhibi ...... ase by haloxyfop and diclofop.
@en
Molecular basis for the inhibi ...... ase by haloxyfop and diclofop.
@nl
type
label
Molecular basis for the inhibi ...... ase by haloxyfop and diclofop.
@en
Molecular basis for the inhibi ...... ase by haloxyfop and diclofop.
@nl
prefLabel
Molecular basis for the inhibi ...... ase by haloxyfop and diclofop.
@en
Molecular basis for the inhibi ...... ase by haloxyfop and diclofop.
@nl
P2860
P356
P1476
Molecular basis for the inhibi ...... lase by haloxyfop and diclofop
@en
P2093
Benjamin Tweel
Hailong Zhang
P2860
P304
P356
10.1073/PNAS.0400891101
P407
P50
P577
2004-04-12T00:00:00Z