Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2. - Wikidata - wikimedia - TriplyDB

Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2.

Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2.

http://www.wikidata.org/entity/Q33229690

about

Toxicology in the fast lane: application of high-throughput bioassays to detect modulation of key enzymes and receptors Development of highly sensitive fluorescent assays for fatty acid amide hydrolase Characterization of α-cypermethrin exposure in Egyptian agricultural workers Parabens inhibit fatty acid amide hydrolase: A potential role in paraben-enhanced 3T3-L1 adipocyte differentiation Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism Heterologous expression and characterization of a malathion-hydrolyzing carboxylesterase from a thermophilic bacterium, Alicyclobacillus tengchongensis.A novel toxicokinetic modeling of cypermethrin and permethrin and their metabolites in humans for dose reconstruction from biomarker data Inactivation of lipid glyceryl ester metabolism in human THP1 monocytes/macrophages by activated organophosphorus insecticides: role of carboxylesterases 1 and 2 Carboxylesterases: Dual roles in lipid and pesticide metabolism.Reactivity versus steric effects in fluorinated ketones as esterase inhibitors: a quantum mechanical and molecular dynamics study Molecular and functional characterization of cDNAs putatively encoding carboxylesterases from the migratory locust, Locusta migratoria.Time profiles and toxicokinetic parameters of key biomarkers of exposure to cypermethrin in orally exposed volunteers compared with previously available kinetic data following permethrin exposure.Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1 A cultured approach to canine urothelial carcinoma: molecular characterization of five cell lines Examination of the carboxylesterase phenotype in human liver Diet and nondiet predictors of urinary 3-phenoxybenzoic acid in NHANES 1999-2002 Human carboxylesterases HCE1 and HCE2: ontogenic expression, inter-individual variability and differential hydrolysis of oseltamivir, aspirin, deltamethrin and permethrin.Hydrolysis of pyrethroids by human and rat tissues: examination of intestinal, liver and serum carboxylesterases.Influence of sulfur oxidation state and steric bulk upon trifluoromethyl ketone (TFK) binding kinetics to carboxylesterases and fatty acid amide hydrolase (FAAH).Pyrethroid insecticides: isoform-dependent hydrolysis, induction of cytochrome P450 3A4 and evidence on the involvement of the pregnane X receptor.Nuclear receptor-mediated regulation of carboxylesterase expression and activity.Regulations of Xenobiotics and Endobiotics on Carboxylesterases: A Comprehensive Review.Efficient in vitro refolding and functional characterization of recombinant human liver carboxylesterase (CES1) expressed in E. coli.Tissue time course and bioavailability of the pyrethroid insecticide bifenthrin in the Long-Evans rat.Design of bioavailable derivatives of 12-(3-adamantan-1-yl-ureido)dodecanoic acid, a potent inhibitor of the soluble epoxide hydrolase.Contribution of carboxylesterase and cytochrome P450 to the bioactivation and detoxification of isocarbophos and its enantiomers in human liver microsomes.Development of amide-based fluorescent probes for selective measurement of carboxylesterase 1 activity in tissue extracts.Investigation of cis-trans isomer dependent dermatotoxicokinetics of UV filter ethylhexyl methoxycinnamate through stratum corneum in vivo.Dose reconstruction in workers exposed to two major pyrethroid pesticides and determination of biological reference values using a toxicokinetic model.Carboxylesterases in the Metabolism and Toxicity of Pesticides

P2860

Q23911122-4547EFAB-8775-4381-A8DB-56DF34C02102 Q23913685-8064955A-4A5D-403F-8506-736600AA7058 Q28383165-35205029-F731-4392-89A1-F74DBAFD6460 Q28393331-33F4ED3D-E660-43AE-8E56-BCFDDF894DED Q28541009-72473FFB-C88D-421D-8163-526555ABAA5A Q30393491-5718D99B-9915-421E-A8C6-0F360097179B Q30768582-E496C2BE-BF8A-4A0A-9B58-B4189B6A0EF4 Q30981876-70A7880E-D759-4BDD-B675-68F4675BCD68 Q33865109-0ADDA001-3081-49FE-BEA6-FC1DD1AB559D Q34461642-D5B31692-E7FC-4C86-85FB-5A6BBE1923D2 Q35145607-2821A46C-89D5-4414-A0E1-ED1CAC358686 Q35577538-7405BB3E-4D39-4477-8548-0B7810E79428 Q35866329-98B50FF6-074B-440A-8F1D-EBBF36E592F5 Q36084359-CB97A80D-12F3-49F5-BE32-039DBD40741D Q36602751-F1FCDF35-A162-4CF5-9F9C-F3265B9248EF Q36838226-DFF6F227-A7ED-4CF7-95F3-048903D4B291 Q37163881-5CDB5AF8-94BE-402B-88B4-DC613BE3EA0F Q37216353-FCBA8E20-FBDE-4BE7-A626-68CDA02AF3C6 Q37287291-5148FC88-6735-411F-AFAD-A7389BF815A1 Q37308959-438EB7B6-F718-41FB-A8C7-EF2F9A2C8E71 Q37693954-AB358A04-C567-4464-B934-4249729AE9A9 Q38749602-680130A3-296F-4CB5-991C-70498DC91247 Q38914678-7B7E7FEC-8C0A-4D0F-93C0-4A1CBA85CB18 Q40542400-0D96DD80-D990-4283-BCCC-C9ABE59819D8 Q41833401-F1C34194-4E79-4D8A-BEAF-6BE258B873B3 Q42705914-3151ED3C-F2A2-4948-929C-229187ED3D9F Q46242909-ABCF12EF-86DF-42C4-9F0A-14BDDF059E31 Q47787991-6372B6E7-B8C6-4BD6-9D9C-97FAA9007BD3 Q50128126-4CDE0002-1E12-4D87-B593-4C9AC3A34CCF Q58416068-B0E6ECA9-060F-4F8C-A134-C02D5BDCD7F3

P2860

Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2.

http://www.wikidata.org/entity/Q33229690

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Characterization of pyrethroid ...... oxylesterases hCE-1 and hCE-2.

@ast

Characterization of pyrethroid ...... oxylesterases hCE-1 and hCE-2.

@en

type

label

Characterization of pyrethroid ...... oxylesterases hCE-1 and hCE-2.

@ast

Characterization of pyrethroid ...... oxylesterases hCE-1 and hCE-2.

@en

prefLabel

Characterization of pyrethroid ...... oxylesterases hCE-1 and hCE-2.

@ast

Characterization of pyrethroid ...... oxylesterases hCE-1 and hCE-2.

@en

P1433

Q33229690-5FB0B429-4BFE-4C23-B696-B1D14E067BF0

P1476

Q33229690-EE6AB593-9F52-42D3-8994-97BC90D83D7A

P2093

Q33229690-204E64B6-44DB-4D7F-9D2A-FEFA35481ECD

Q33229690-479AF7F8-B216-496A-ACDC-690C7B8360B1

Q33229690-6E96BA55-7361-4152-AFC3-A741F6F52488

Q33229690-D1FEFF83-3D5D-4C47-8C5C-A0FEB153E365

Q33229690-E2361BCE-AB34-40D4-96C3-3FE29F78B169

P2860

Q33229690-18C63F07-FE49-4CED-8CCC-E739A364069E

Q33229690-1914A05E-FF71-45B9-A8D9-8DBFECA04AFC

Q33229690-1AE59401-7237-4788-8E0A-C1B5B3E14A0E

Q33229690-22E34324-02E5-4BBB-A6AA-631075EC68AB

Q33229690-24555ADB-5FFD-435A-A48A-510336B00AA6

Q33229690-2A2F9546-D750-4145-AAE8-ECEF14AA2B8B

Q33229690-2F27ABE1-9EB8-448F-BD4A-4D42554768A6

Q33229690-329DF04C-87E9-441D-B4E3-27B1F1D26B89

Q33229690-3A4F1086-29F0-4B19-B662-AD7FD627926E

Q33229690-3C476C50-DDE4-4C1F-A187-0BD4774FDC4A

P304

Q33229690-4C5B8721-0BDB-4DF0-9AF9-058CA2C83ED3

P31

Q33229690-8E47EEA1-0986-45E5-8192-B7D967EBF0F2

P356

Q33229690-684D2F8C-0E41-49DB-B01D-6EB1D453D8A6

P407

Q33229690-145916C0-E461-4040-AB49-9446936F0CAB

P433

Q33229690-62D609E3-4A9B-47B5-BF7B-10C3D9289FF6

P478

Q33229690-13B76EF6-D1E3-45F0-BDAB-5DCCEFD41B4B

P50

Q33229690-B35261FC-0F80-4388-8443-013AF91A90B0

P577

Q33229690-F2082517-870D-48B5-9CD5-4BB37DF23684

P5875

Q33229690-BFF1DE97-92C2-4DDB-B6FA-3F46298D0ECB

P698

Q33229690-321FAA27-1152-4375-930D-1EAFFE7A3664

P932

Q33229690-DF945E4D-B62B-4948-8D09-AEB931ADCAE2

P356

J.ABB.2005.11.005

P1433

Archives of Biochemistry and Biophysics

P1476

Characterization of pyrethroid ...... oxylesterases hCE-1 and hCE-2.

@en

P2093

Bruce D Hammock

http://www.w3.org/2001/XMLSchema#string

Christophe Morisseau

http://www.w3.org/2001/XMLSchema#string

Huazhang Huang

http://www.w3.org/2001/XMLSchema#string

In-Hae Kim

http://www.w3.org/2001/XMLSchema#string

Shizuo G Kamita

http://www.w3.org/2001/XMLSchema#string

P2860

Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme

Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition

Pharmacogenomic assessment of carboxylesterases 1 and 2

Determination and analysis of single nucleotide polymorphisms and haplotype structure of the human carboxylesterase 2 gene

Metabolism of cocaine and heroin is catalyzed by the same human liver carboxylesterases

Pharmacogenetics of human carboxylesterase 2, an enzyme involved in the activation of irinotecan into SN-38

Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2

Binding and hydrolysis of meperidine by human liver carboxylesterase hCE-1

P304

115-123

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.ABB.2005.11.005

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

445

http://www.w3.org/2001/XMLSchema#string

P50

P577

2006-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

7409945

http://www.w3.org/2001/XMLSchema#string

P698

16359636

http://www.w3.org/2001/XMLSchema#string

P932

1444892

http://www.w3.org/2001/XMLSchema#string