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Search results 401 to 421 out of 421 for Cyp1b1

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0.019s

Type

Details

Score

Publication

26493931 | J:227919

First Author:	Zhang F
Year:	2015
Journal:	Toxicol Appl Pharmacol
Title:	Effects of sexually dimorphic growth hormone secretory patterns on arachidonic acid metabolizing enzymes in rodent heart.
Volume:	289
Issue:	3
Pages:	495-506

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Publication

37156770 | J:335556

First Author:	Sinha S
Year:	2023
Journal:	Nat Commun
Title:	Hepatic stellate cell stearoyl co-A desaturase activates leukotriene B4 receptor 2 - β-catenin cascade to promote liver tumorigenesis.
Volume:	14
Issue:	1
Pages:	2651

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Publication

22761658 | J:187925

First Author:	Yueh MF
Year:	2012
Journal:	PLoS One
Title:	Triclocarban mediates induction of xenobiotic metabolism through activation of the constitutive androstane receptor and the estrogen receptor alpha.
Volume:	7
Issue:	6
Pages:	e37705

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Publication

11376689 | J:69988

First Author:	Gonzalez FJ
Year:	2001
Journal:	Mutat Res
Title:	Understanding the role of xenobiotic-metabolism in chemical carcinogenesis using gene knockout mice.
Volume:	477
Issue:	1-2
Pages:	79-87

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Publication

10828274 | J:62981

First Author:	Gressani KM
Year:	2000
Journal:	Toxicol Sci
Title:	Prenatal toxicity and lack of carcinogenicity of 2-amino-3-methylimidazo[4,5-f]quinoline (IQ) following transplacental exposure.
Volume:	55
Issue:	2
Pages:	407-14

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Publication

15183014 | J:102095

First Author:	Filbrandt CR
Year:	2004
Journal:	Neurotoxicology
Title:	Presence and functional activity of the aryl hydrocarbon receptor in isolated murine cerebral vascular endothelial cells and astrocytes.
Volume:	25
Issue:	4
Pages:	605-16

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Publication

16929009 | J:113290

First Author:	Choi SS
Year:	2006
Journal:	Toxicol Sci
Title:	In utero exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin induces amphiregulin gene expression in the developing mouse ureter.
Volume:	94
Issue:	1
Pages:	163-74

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Publication

32376276 | J:296876

First Author:	Hu J
Year:	2020
Journal:	Mol Cell Endocrinol
Title:	ERO1α inhibits cell apoptosis and regulates steroidogenesis in mouse granulosa cells.
Volume:	511

Pages:	110842

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Publication

16112414 | -

First Author:	Tsuchiya Y
Year:	2005
Journal:	Cancer Lett
Title:	Cytochrome P450-mediated metabolism of estrogens and its regulation in human.
Volume:	227
Issue:	2
Pages:	115-24

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Publication

16922636 | -

First Author:	Roos PH
Year:	2005
Journal:	Expert Opin Drug Metab Toxicol
Title:	Cytochrome P450 interactions in human cancers: new aspects considering CYP1B1.
Volume:	1
Issue:	2
Pages:	187-202

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Publication

16485905 | -

First Author:	Shimada T
Year:	2006
Journal:	Chem Res Toxicol
Title:	Inhibition of human cytochrome P450 1A1-, 1A2-, and 1B1-mediated activation of procarcinogens to genotoxic metabolites by polycyclic aromatic hydrocarbons.
Volume:	19
Issue:	2
Pages:	288-94

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Protein Domain

IPR008066 | Cyt_P450_E_grp-I_CYP1

Type:

Family

Description:

Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of life, and which show extraordinary diversity in their reaction chemistry. In mammals, these proteins are found primarily in microsomes of hepatocytes and other cell types, where they oxidise steroids, fatty acids and xenobiotics, and are important for the detoxification and clearance of various compounds, as well as for hormone synthesis and breakdown, cholesterol synthesis and vitamin D metabolism. In plants, these proteins are important for the biosynthesis of several compounds such as hormones, defensive compounds and fatty acids. In bacteria, they are important for several metabolic processes, such as the biosynthesis of antibiotic erythromycin in Saccharopolyspora erythraea (Streptomyces erythraeus).Cytochrome P450 enzymes use haem to oxidise their substrates, using protons derived from NADH or NADPH to split the oxygen so a single atom can be added to a substrate. They also require electrons, which they receive from a variety of redox partners. In certain cases, cytochrome P450 can be fused to its redox partner to produce a bi-functional protein, such as with P450BM-3 from Bacillus megaterium [], which has haem and flavin domains.Organisms produce many different cytochrome P450 enzymes (at least 58 in humans), which together with alternative splicing can provide a wide array of enzymes with different substrate and tissue specificities. Individual cytochrome P450 proteins follow the nomenclature: CYP, followed by a number (family), then a letter (subfamily), and another number (protein); e.g. CYP3A4 is the fourth protein in family 3, subfamily A. In general, family members should share >40% identity, while subfamily members should share >55% identity.Cytochrome P450 proteins can also be grouped by two different schemes. One scheme was based on a taxonomic split: class I (prokaryotic/mitochondrial) and class II (eukaryotic microsomes). The other scheme was based on the number of components in the system: class B (3-components) and class E (2-components). These classes merge to a certain degree. Most prokaryotes and mitochondria (and fungal CYP55) have 3-component systems (class I/class B) - a FAD-containing flavoprotein (NAD(P)H-dependent reductase), an iron-sulphur protein and P450. Most eukaryotic microsomes have 2-component systems (class II/class E) - NADPH:P450 reductase (FAD and FMN-containing flavoprotein) and P450. There are exceptions to this scheme, such as 1-component systems that resemble class E enzymes [, , ]. The class E enzymes can be further subdivided into five sequence clusters, groups I-V, each of which may contain more than one cytochrome P450 family (eg, CYP1 and CYP2 are both found in group I). The divergence of the cytochrome P450 superfamily into B- and E-classes, and further divergence into stable clusters within the E-class, appears to be very ancient, occurring before the appearance of eukaryotes.This entry represents the CYP1 family from group I, class E, cytochrome P450 proteins. CYP1 enzymes mainly metabolise exogenous substrates and are found in mammalia (1A, 1B), bony fishes (1A), sharks, skates, rays (1A) and birds (1A). CYP1A contains five proteins, namely, CYP1A1, 1A2, 1A3, 1A4 and 1A5. CYP1 family members are closely associated with the metabolic activation of pro-carcinogens and mutagens []. For example, CYP1B1 may play an important role in susceptibility to mammary and ovarian cancer through its involvement in oestrogen metabolism [], as well as with various cancers associated with the activation of polycyclic aromatic hydrocarbons in cigarette smoke [].

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Publication

18353537 | J:136076

First Author:	Courter LA
Year:	2008
Journal:	Cancer Lett
Title:	The influence of diesel exhaust on polycyclic aromatic hydrocarbon-induced DNA damage, gene expression, and tumor initiation in Sencar mice in vivo.
Volume:	265
Issue:	1
Pages:	135-47

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Protein

P00184

Organism:	Mus musculus/domesticus
Length:	524
Fragment?:	false

•

Protein

P00186

Organism:	Mus musculus/domesticus
Length:	513
Fragment?:	false

•

Protein

Q05A20

Organism:	Mus musculus/domesticus
Length:	524
Fragment?:	false

•

Protein

B6VGH4

Organism:	Mus musculus/domesticus
Length:	513
Fragment?:	false

•

Publication

16042601 | -

First Author:	McLean KJ
Year:	2005
Journal:	Biochem Soc Trans
Title:	Biodiversity of cytochrome P450 redox systems.
Volume:	33
Issue:	Pt 4
Pages:	796-801

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Publication

17023115 | -

First Author:	Munro AW
Year:	2007
Journal:	Biochim Biophys Acta
Title:	Cytochrome P450--redox partner fusion enzymes.
Volume:	1770
Issue:	3
Pages:	345-59

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Publication

15128046 | J:87417

First Author:	Nelson DR
Year:	2004
Journal:	Pharmacogenetics
Title:	Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.
Volume:	14
Issue:	1
Pages:	1-18

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Publication

8637843 | -

First Author:	Degtyarenko KN
Year:	1995
Journal:	Protein Eng
Title:	Structural domains of P450-containing monooxygenase systems.
Volume:	8
Issue:	8
Pages:	737-47

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