sameAs
P688
Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymesAdaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2Radical intermediates in the catalytic oxidation of hydrocarbons by bacterial and human cytochrome P450 enzymesCharacterization of human cytochrome P450 enzymes catalyzing domperidone N-dealkylation and hydroxylation in vitroAcetaminophen bioactivation by human cytochrome P450 enzymes and animal microsomesThe relative contribution of human cytochrome P450 isoforms to the four caffeine oxidation pathways: an in vitro comparative study with cDNA-expressed P450s including CYP2C isoformsIdentification of the human cytochrome P450 enzymes involved in the in vitro biotransformation of lynestrenol and norethindroneComprehensive in vitro analysis of voriconazole inhibition of eight cytochrome P450 (CYP) enzymes: major effect on CYPs 2B6, 2C9, 2C19, and 3AHepatic cytochrome P450 enzyme alterations in humans with progressive stages of nonalcoholic fatty liver diseaseHuman cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylaminesCharacterization of the oxidative metabolites of 17beta-estradiol and estrone formed by 15 selectively expressed human cytochrome p450 isoforms.Role of human cytochrome P450 1A1, 1A2, 1B1, and 3A4 in the 2-, 4-, and 16alpha-hydroxylation of 17beta-estradiol.Biosynthesis of all-trans-retinoic acid from all-trans-retinol: catalysis of all-trans-retinol oxidation by human P-450 cytochromes
P921
Q50264736-C5C4C876-7999-42AA-B24C-C48951114F16Q50264737-898CC7E4-7357-4C9A-9112-2910272FA8D1Q50264740-13CD6EF7-C81D-4E2C-B157-EC615ADD9DC1Q50264741-EDBB3965-2821-4534-B3EE-B60F31E10C30Q50264744-622D2315-B601-4DEF-A12B-A8BBF9666CEBQ50267174-041CC5C1-2AF6-4EB5-A290-CE3F53674A02Q50267175-0511B924-B163-4365-8B0E-EAEABD95A8F3Q50295270-4A0C4F22-862F-4CDB-B2A1-8215AA2466BDQ50295271-84EA447E-9F8F-4ACB-863A-0BAB67C64AF1Q50295390-16191F7B-1535-4F1B-9A99-6CE0B5957A78Q50295423-B4ABFF4C-AE88-48EF-8C6E-8656949EEFFFQ55183175-53CC7B5B-89B3-46C2-ABE6-99C09D3EEC70Q55183181-F15CF53E-F352-4D48-A92E-2501170D6128
P527
Q24291576-D687662E-9F1A-46CB-9297-7957F48FFCE9Q24293148-7CF1FE16-F6F4-425D-B09B-CF848BC208BCQ24297785-4BCE6B35-BDEF-4976-8B9E-F3070B8AF925Q24300576-AF55A100-CEDD-4540-A3D3-AA5677F89363Q24301858-694A7080-961B-42D7-B5BF-9C4091B98977Q24311331-AEEA49CE-72F5-4A31-9727-34BDB0AC32E3Q24312232-9C2D2207-D4C8-4783-A3B1-1EB7D14C0C65Q24313179-19008935-903C-4384-A6FF-873D9A223B41Q24317436-97D806E8-6FF9-40ED-98C4-4949F3C48CFCQ24319917-A7F519C2-C9CD-4B99-975E-5807BA9A0EE1Q24339615-18981C5E-F2CF-4682-9B73-13446C6D675DQ34214631-504C664C-5961-4C38-B318-833C0437CE03Q43736582-3143AA9C-854D-40D0-BEE7-451FB6C9A7D3Q73462675-7B19A743-BD1D-457D-8E01-0454EB49AAC1
P921
description
Protein
@de
mammalian protein found in Homo sapiens
@en
menselijk eiwit
@nl
protein
@id
protein
@sv
proteinë
@sq
protèin
@ace
protéine humaine
@fr
بروتين في الإنسان العاقل
@ar
name
CYP1A2
@cy
CYP1A2
@en-ca
CYP1A2
@en-gb
CYP1A2
@es
CYP1A2
@ja
CYP1A2
@la
CYP1A2
@nl
CYP1A2
@uk
CYP1A2
@zh
Cytochrom P450 1A2
@de
type
label
CYP1A2
@cy
CYP1A2
@en-ca
CYP1A2
@en-gb
CYP1A2
@es
CYP1A2
@ja
CYP1A2
@la
CYP1A2
@nl
CYP1A2
@uk
CYP1A2
@zh
Cytochrom P450 1A2
@de
altLabel
CIP1A2
@es
CYP1A2
@de
CYP1A2
@en
CYPIA2
@en
P450 form 4
@en
aryl hydrocarbon hydroxylase
@en
cholesterol 25-hydroxylase
@en
cytochrome P(3)450
@en
cytochrome P450 1A2
@en
cytochrome P450 4
@en
prefLabel
CYP1A2
@cy
CYP1A2
@en-ca
CYP1A2
@en-gb
CYP1A2
@es
CYP1A2
@ja
CYP1A2
@la
CYP1A2
@nl
CYP1A2
@uk
CYP1A2
@zh
Cytochrom P450 1A2
@de
P680
P681
P682
P352
P486
P6366
P637
P638
P31
P352
P486
P6366
P637
P680
P681
P682
P702
P703
P705
ENSP00000342007