Adrenodoxin: structure, stability, and electron transfer properties
about
The human steroid hydroxylases CYP1B1 and CYP11B2Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesisCrystal Structure of CYP24A1, a Mitochondrial Cytochrome P450 Involved in Vitamin D MetabolismCrystal Structure of the Putidaredoxin Reductase·Putidaredoxin Electron Transfer ComplexMolecular Characterization of a Class I P450 Electron Transfer System from Novosphingobium aromaticivorans DSM12444Allostery in the ferredoxin protein motif does not involve a conformational switchThe crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilisAntioxidant protective mechanisms against reactive oxygen species (ROS) generated by mitochondrial P450 systems in steroidogenic cellsVariations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamilyKinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprATemporal and spatial patterns of ovarian gene transcription following an ovulatory dose of gonadotropin in the ratGene expression profiles in testis of pigs with extreme high and low levels of androstenoneThe autodisplay story, from discovery to biotechnical and biomedical applications.Identification of differentially expressed markers in human follicular cells associated with competent oocytes.Oxidative stress and adrenocortical insufficiency.Functional consequences of seven novel mutations in the CYP11B1 gene: four mutations associated with nonclassic and three mutations causing classic 11{beta}-hydroxylase deficiency.Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis.Ferredoxins of the third kind.Cytochrome P450 alkane hydroxylases of the CYP153 family are common in alkane-degrading eubacteria lacking integral membrane alkane hydroxylases.A recombinant CYP11B1 dependent Escherichia coli biocatalyst for selective cortisol production and optimization towards a preparative scale.Transient complexes of redox proteins: structural and dynamic details from NMR studies.Functionalized PHB granules provide the basis for the efficient side-chain cleavage of cholesterol and analogs in recombinant Bacillus megateriumImpact of a novel homozygous mutation in nicotinamide nucleotide transhydrogenase on mitochondrial DNA integrity in a case of familial glucocorticoid deficiency.Ferredoxin 1b (Fdx1b) Is the Essential Mitochondrial Redox Partner for Cortisol Biosynthesis in Zebrafish.Human ferredoxin-2 displays a unique conformational changeHuman Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis.Adrenodoxin--a versatile ferredoxin.Using SILAC proteomics to investigate the effect of the mycotoxin, alternariol, in the human H295R steroidogenesis model.Interactions of natural polyamines with mammalian proteins.Highly Efficient CYP167A1 (EpoK) dependent Epothilone B Formation and Production of 7-Ketone Epothilone D as a New Epothilone Derivative.Genome mining in Sorangium cellulosum So ce56: identification and characterization of the homologous electron transfer proteins of a myxobacterial cytochrome P450.Genome-wide association study of chronic hepatitis B virus infection reveals a novel candidate risk allele on 11q22.3.Protein phosphorylation and intermolecular electron transfer: a joint experimental and computational study of a hormone biosynthesis pathway.Ferredoxin, in conjunction with NADPH and ferredoxin-NADP reductase, transfers electrons to the IscS/IscU complex to promote iron-sulfur cluster assembly.Construction of 3D models of the CYP11B family as a tool to predict ligand binding characteristicsThe reduced [2Fe-2S] clusters in adrenodoxin and Arthrospira platensis ferredoxin share spin density with protein nitrogens, probed using 2D ESEEM.Selective oxidative demethylation of veratric acid to vanillic acid by CYP199A4 from Rhodopseudomonas palustris HaA2.The loop region covering the iron-sulfur cluster in bovine adrenodoxin comprises a new interaction site for redox partners.Apicomplexan parasites possess distinct nuclear-encoded, but apicoplast-localized, plant-type ferredoxin-NADP+ reductase and ferredoxin.CYP11A1 stimulates the hydroxylase activity of CYP11B1 in mitochondria of recombinant yeast in vivo and in vitro.
P2860
Q24321759-0D21D128-B066-476A-9394-0FC3B7EEF946Q27627708-A5F7E6DA-DDCB-4488-8FE9-9982374F28CFQ27658435-1DA256A8-A4A6-4C34-A9C7-87CEB784823BQ27660026-4A86C030-3C45-45F2-BCD2-5BF6B8F40506Q27662700-4CA2E139-6BD1-4A97-ABFD-57A6CAC4085FQ27666732-DDF2E8B7-D55B-4AD7-A420-E23F79A14033Q27697474-7B9064D8-90A5-4183-AE28-16A73112F743Q28239151-4E8EE429-CD80-41B0-A123-66A152D99CC3Q28304165-C9B39DDB-5B7F-4187-8638-A97D986526E3Q28487239-94A6A87A-265D-4508-BFAB-B7B4188AB011Q28582867-78854DC5-F91F-4372-8B74-477EFA8324BEQ33305281-5532DF79-8F2E-4AF5-B648-C33BE14A8B26Q33308956-5A6459F5-6255-48E0-AB1D-0727902E2C3BQ33321811-12EED2E1-9867-4BD7-8A4B-9C7DD914BEF8Q33709973-90FBAEC7-792C-4B3D-8969-FDEBD184C277Q33759066-1CD3CF12-4203-4B8B-9369-9C1028BC5CFAQ33977876-6086D86F-A391-43BF-A317-7D931EBDA5E5Q34104146-74E02502-743E-4532-AB9E-497FFA75B0FFQ34315977-75EF408E-FE58-4F39-84D7-325E2FFA271BQ35603547-DA46F87A-26C6-4A99-BB0E-ABE858400C2DQ35896267-4DD9196E-807F-4414-9EBA-155D52030386Q35896740-6A10358A-8C1F-4A9D-8528-5FB867968993Q35984686-2F24BFDD-8F7C-42A7-93AD-773FF8ABCC47Q36625120-C37DDAED-FC4C-48C8-85CB-022F5FE97CEEQ36754487-7794B3D4-3075-4D5B-B9FF-E32B43CD8776Q37607678-22766414-FAAB-4872-872C-32765C11C555Q38007406-5A9CA896-517E-4B16-BCE7-10B0986AE773Q38470215-7BE81039-6F4B-49BF-8493-8AD5944470DAQ38472529-CA952574-7624-4BCB-90C7-0E875418B145Q41141496-52ED4BFC-6598-4C51-8AA9-03B915124B8CQ41897962-A623FABC-132B-4FA4-9F0A-7EA654F02E9BQ42267178-A36F02FC-2573-4EEF-8584-D2B743A2C815Q42426534-5D968EF0-9C96-470E-9A25-532497E02B02Q42588454-6FF422AD-0CF8-450A-B3AA-ADB1EAF93572Q42609883-DAC66044-CD2D-4566-9D82-014A904B96C3Q42615551-9867A0C7-DB94-4CCC-9128-88949D564334Q43213969-35300BD9-70DE-4994-9412-7DDD24548B81Q43507740-0B964BDD-6811-4443-86E0-789C2A2A2312Q43509070-7314EC1A-5BA8-42AF-8922-55118ED0D6D2Q43674590-BA1DAD62-D161-471E-96E6-98C0262DA8FE
P2860
Adrenodoxin: structure, stability, and electron transfer properties
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Adrenodoxin: structure, stability, and electron transfer properties
@ast
Adrenodoxin: structure, stability, and electron transfer properties
@en
Adrenodoxin: structure, stability, and electron transfer properties
@nl
type
label
Adrenodoxin: structure, stability, and electron transfer properties
@ast
Adrenodoxin: structure, stability, and electron transfer properties
@en
Adrenodoxin: structure, stability, and electron transfer properties
@nl
prefLabel
Adrenodoxin: structure, stability, and electron transfer properties
@ast
Adrenodoxin: structure, stability, and electron transfer properties
@en
Adrenodoxin: structure, stability, and electron transfer properties
@nl
P2093
P2860
P1433
P1476
Adrenodoxin: structure, stability, and electron transfer properties
@en
P2093
A V Grinberg
B Schiffler
F Hannemann
R Bernhardt
U Heinemann
P2860
P304
P356
10.1002/1097-0134(20000901)40:4<590::AID-PROT50>3.0.CO;2-P
P407
P577
2000-09-01T00:00:00Z