about
Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamilyP450 subfamily CYP2J and their role in the bioactivation of arachidonic acid in extrahepatic tissuesHuman NADPH-P450 oxidoreductase modulates the level of cytochrome P450 CYP2D6 holoprotein via haem oxygenase-dependent and -independent pathwaysA single cytochrome P-450 system is involved in degradation of the herbicides EPTC (S-ethyl dipropylthiocarbamate) and atrazine by Rhodococcus sp. strain NI86/21Toluene and ethylbenzene oxidation by purified naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4Persistent induction of hepatic and pulmonary phase II enzymes by 3-methylcholanthrene in ratsMalignant transformation potentials of human umbilical cord mesenchymal stem cells both spontaneously and via 3-methycholanthrene inductionMembrane topology and cell surface targeting of microsomal epoxide hydrolase. Evidence for multiple topological orientationsScaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genesCreating context for the use of DNA adduct data in cancer risk assessment: I. Data organization.On the general mechanism of selective induction of cytochrome P450 enzymes by chemicals: some theoretical considerations.An insight into the origin and functional evolution of bacterial aromatic ring-hydroxylating oxygenases.Mice deficient in the gene for cytochrome P450 (CYP)1A1 are more susceptible than wild-type to hyperoxic lung injury: evidence for protective role of CYP1A1 against oxidative stress.Sex-specific differences in hyperoxic lung injury in mice: implications for acute and chronic lung disease in humans.Cytochrome P450 polymorphisms and response to antipsychotic therapy.N-oxidative transformation of free and N-substituted amine functions by cytochrome P450 as means of bioactivation and detoxication.Transformation of Mouse Liver Cells by Methylcholanthrene Leads to Phenotypic Changes Associated with Epithelial-mesenchymal Transition.Engineered yeasts simulating P450-dependent metabolisms: tricks, myths and reality.Oxidation of 6,7-dihydro-5H-benzocycloheptene by bacterial strains expressing naphthalene dioxygenase, biphenyl dioxygenase, and toluene dioxygenase yields homochiral monol or cis-diol enantiomers as major products.Omeprazole attenuates hyperoxic lung injury in mice via aryl hydrocarbon receptor activation and is associated with increased expression of cytochrome P4501A enzymes.Prenatal administration of the cytochrome P4501A inducer, Β-naphthoflavone (BNF), attenuates hyperoxic lung injury in newborn mice: implications for bronchopulmonary dysplasia (BPD) in premature infants.Disruption of cytochrome P4501A2 in mice leads to increased susceptibility to hyperoxic lung injury.Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase.Desaturation, dioxygenation, and monooxygenation reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp. strain 9816-4Aldehyde dehydrogenases and their role in carcinogenesis.The human hepatic cytochromes P450 involved in drug metabolism.Leflunomide Induces Pulmonary and Hepatic CYP1A Enzymes via Aryl Hydrocarbon Receptor.Partial characterization of the human CYP1A1 negatively acting transcription factor and mutational analysis of its cognate DNA recognition sequence.A novel cis-acting element controlling the rat CYP2D5 gene and requiring cooperativity between C/EBP beta and an Sp1 factor.Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer.Roles of UDP-glucuronosyltransferases in chemical carcinogenesis.Toxicological actions of plant-derived and anthropogenic methylenedioxyphenyl-substituted chemicals in mammals and insects.Degradation of morpholine by an environmental Mycobacterium strain involves a cytochrome P-450.Stabilization of microbial cytochrome P-450 activity by creation of station-phase conditions in a continuously operated immobilized-cell reactor.Characterization of the expression of the thcB gene, coding for a pesticide-degrading cytochrome P-450 in Rhodococcus strainsMetabolism of the herbicide atrazine by Rhodococcus strains.Transformations of Aromatic Compounds by Nitrosomonas europaea.Radical cation intermediates in N-dealkylation reactions.On the mechanism of amine oxidations by P450.Sigmoidal kinetic model for two co-operative substrate-binding sites in a cytochrome P450 3A4 active site: an example of the metabolism of diazepam and its derivatives.
P2860
Q24533519-87719C61-7861-4B40-A63E-2B5E85140B04Q28138121-1366AA4E-6788-422C-8CCA-B4E29B6E5CD6Q28365626-44BC6183-9012-4504-BD83-7DCF7EF79554Q28367968-EE6BDCAF-0F96-400F-B20C-23E17F040CADQ28379109-7CD75DB5-F666-47C2-A28A-4C67441F2543Q28387997-FA258437-6234-4C71-89C5-927F3CFED420Q28536701-9C64D7AA-132C-4F8D-AF55-CA7FA80ED706Q28582020-03EE67F1-01A6-4639-B488-E7256B4A31F1Q28593237-01D3D804-1C11-4BA2-B1E3-DA2873D0C8BEQ33501831-CA20C83E-3A4A-4F60-8B82-4A4E51B1497FQ33742250-095BBA5F-2A5C-4FE2-A5B5-8EC46420459DQ34302711-CCAFF066-B46A-473F-94AE-C08F96FA0FD9Q34354194-6E7DCFE2-D3C7-4231-99B8-BD6D1DA97BB6Q34362352-4978F297-DC3D-4A3E-82DA-1E93E8D5D676Q34612118-6022008D-D9A8-4B67-915A-BEE226827120Q34818942-C09B7621-4405-4781-B050-1B5AA1D85851Q34906502-ACD2BE09-E2D9-4DA5-B082-2580D7353653Q34951334-463DE001-AF9E-4258-9A1B-DBF86B8C50F3Q35189845-E5780087-0548-4A67-9822-563BAFF734CAQ35265520-23A7D672-2A85-4247-88E3-C42B068502ECQ35381595-CC658B4F-A43D-48FF-BB77-190EC61B486AQ35566747-C31F85EF-3638-4DD4-81A3-D22BB03E4181Q35578764-F3616DCA-7E7D-453F-AED3-C4A28EAA0B56Q35585218-0145E8B4-E999-4BD3-879B-79D1B3330700Q35815650-8A5AFCA8-6E24-402A-B596-A589B66BB3A9Q36258518-75FE296D-6B4A-4D59-BBA4-D785ABB5A530Q36316481-5CF302C9-78A5-4D1C-BFCB-729759EB1200Q36554803-60D48DA8-931D-4CD4-943A-7EF4F2D58E67Q36646897-AFF0822C-8DFD-4265-9815-D17CF11BDE68Q36672374-78814444-4CC1-43F9-A6FC-BC8B8AC8CBA6Q37368782-A89429FF-9E9E-4E5C-96C8-EF20F7AC62D3Q38039138-314493E7-B3A3-4195-B46B-D2B95987DDB5Q39642645-CA5F9541-5765-477D-9F60-10B46C31354BQ39797157-0A009DEF-D8DA-44F0-9CE0-7092AE8230D1Q39799211-0A414A3B-8955-4CD4-9C00-4C80B27C939DQ39857866-4F7A4551-9B8D-45EA-B172-2F4BA88AAF1BQ39915133-5770F9A0-46CE-4620-8300-5C94DCFF0F51Q40372739-706EF72C-AC6D-4AB5-9334-BCF206786025Q40372746-81F8F356-8A04-4336-AAB1-DC2710D7F16EQ40949921-B47D91D8-AA34-4F87-ABC3-D5C85A83A03C
P2860
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Enzymatic oxidation of xenobiotic chemicals.
@ast
Enzymatic oxidation of xenobiotic chemicals.
@en
type
label
Enzymatic oxidation of xenobiotic chemicals.
@ast
Enzymatic oxidation of xenobiotic chemicals.
@en
prefLabel
Enzymatic oxidation of xenobiotic chemicals.
@ast
Enzymatic oxidation of xenobiotic chemicals.
@en
P2860
P1476
Enzymatic oxidation of xenobiotic chemicals.
@en
P2093
Guengerich FP
P2860
P304
P356
10.3109/10409239009090607
P577
1990-01-01T00:00:00Z