Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2. - Test2 - elhamkhani - TriplyDB

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

http://www.wikidata.org/entity/Q36012132

about

CYP2D6-CYP2C9 protein-protein interactions and isoform-selective effects on substrate binding and catalysis Functional interactions between cytochromes P450 1A2 and 2B4 require both enzymes to reside in the same phospholipid vesicle: evidence for physical complex formation.Beta sheet 2-alpha helix C loop of cytochrome P450 reductase serves as a docking site for redox partners.CYP2C9-CYP3A4 protein-protein interactions: role of the hydrophobic N terminus.Human heme oxygenase-1 efficiently catabolizes heme in the absence of biliverdin reductase Altered CYP2C9 activity following modulation of CYP3A4 levels in human hepatocytes: an example of protein-protein interactions.Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3 Organization of NADPH-cytochrome P450 reductase and CYP1A2 in the endoplasmic reticulum--microdomain localization affects monooxygenase function Interactions among cytochromes P450 in microsomal membranes: oligomerization of cytochromes P450 3A4, 3A5, and 2E1 and its functional consequences Drug metabolism by CYP2C8.3 is determined by substrate dependent interactions with cytochrome P450 reductase and cytochrome b5.Simultaneous measurement of CYP1A2 activity, regioselectivity, and coupling: Implications for environmental sensitivity of enzyme-substrate binding.Inhibition of cytochrome P450 2B4 by environmentally persistent free radical-containing particulate matter.Heteromeric complex formation between CYP2E1 and CYP1A2: evidence for the involvement of electrostatic interactions.Inhibition of CYP2B4 by 2-ethynylnaphthalene: evidence for the co-binding of substrate and inhibitor within the active site.Environmentally persistent free radical-containing particulate matter competitively inhibits metabolism by cytochrome P450 1A2.Quantitation of heme oxygenase 1: heme titration increases yield of purified protein.Effect of homomeric P450-P450 complexes on P450 function.Global analysis of protein-protein interactions reveals multiple CYP2E1-reductase complexes.Interactions between cytochromes P450 2B4 (CYP2B4) and 1A2 (CYP1A2) lead to alterations in toluene disposition and P450 uncoupling Cooperative properties of cytochromes P450.Physical incorporation of NADPH-cytochrome P450 reductase and cytochrome P450 into phospholipid vesicles using glycocholate and Bio-Beads Physical Studies of P450-P450 Interactions: Predicting Quaternary Structures of P450 Complexes in Membranes from Their X-ray Crystal Structures.Overview of extracellular microvesicles in drug metabolism.Microsomal monooxygenase as a multienzyme system: the role of P450-P450 interactions.Formation of P450 · P450 complexes and their effect on P450 function The functional effects of physical interactions involving cytochromes P450: putative mechanisms of action and the extent of these effects in biological membranes.Evaluation of fluorescence- and mass spectrometry-based CYP inhibition assays for use in drug discovery.Co-expression of active human cytochrome P450 1A2 and cytochrome P450 reductase on the cell surface of Escherichia coli.Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein.An evaluation of methods for the reconstitution of cytochromes P450 and NADPH P450 reductase into lipid vesicles Characterization of interactions among CYP1A2, CYP2B4, and NADPH-cytochrome P450 reductase: Identification of specific protein complexes.Toward a systems approach to the human cytochrome P450 ensemble: interactions between CYP2D6 and CYP2E1 and their functional consequences.

P2860

Q24311614-0F353466-AA3D-4723-8944-37CCF120EA4B Q33726532-10899C3A-EEFC-49D6-9FBB-8720E552446E Q33759278-77DF5550-E566-41E9-A97D-21C75973C2BE Q33891038-0F3AF8AB-9D69-482C-A6D7-E7040E80CB3E Q34257481-63DCA507-8745-48D3-BFC9-EA657D8E8C21 Q34360051-26EF8E0D-A33D-4BC5-9AAD-9FE711EF7521 Q34480258-10BF570E-7E01-432A-913B-E34A5AD3E64C Q34701004-299E32EC-17D1-4219-943D-8602569CE716 Q35055663-5BB3DAC0-0D71-4CCA-A8A1-E1F72FFC79C0 Q35175018-12AF6C9C-6A3F-4F39-9819-814295AE993D Q35231748-B142072A-14C7-45D0-A7DD-00B2960C1604 Q35528666-29C6C670-A049-4843-B8CA-A3C9882DF081 Q36013302-01AD9CEA-615C-4350-808D-F9C4C4F706E6 Q36238767-B77B0603-F642-4725-9A9E-E0D032842121 Q36296841-E283F1E1-7663-4048-9432-1BF240EEBA81 Q36345069-7840F32F-4F17-44A6-887E-D292727735AB Q36456390-1210B3BC-06C2-4526-834B-9D2654EB6BFC Q36992700-13EEC11D-F7B9-4B12-A07A-05C6250A06C6 Q37112456-0A3C398E-655D-49DF-9BC2-01C353A3E9B8 Q37366156-D1181566-0B7A-4B60-BE31-A90E840CC81B Q37460469-6528EA96-2683-40D9-80C4-D404EF5FE70F Q37611698-100B0DFD-CC4C-43B9-A0B8-66B46BC71331 Q37700753-F1A69496-565F-4DE3-960F-A3B504DAA31E Q37852000-522CB1DE-4AC7-4656-95B8-565F48DC7DE7 Q37966569-8950A297-2507-4E10-8EF4-98E8ED418308 Q38833525-56CED715-AE4E-49E8-9740-308401E01A54 Q39846278-C0285C77-89E7-406F-AA49-11E98FF4B1B8 Q40030314-91CC4391-D849-4C22-8795-526A80FCD6B4 Q41904468-948DDD18-7AA8-417E-A0D1-B2DCEC2FD21F Q42620240-E0863279-E691-4047-9168-3B3508C1AA06 Q47301320-546C0E02-FBED-4F37-973D-0F2C234019BF Q47806908-FD548486-EDCB-4781-9FDF-32092BC2DE7F

P2860

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

http://www.wikidata.org/entity/Q36012132

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

2005年论文

@zh

2005年论文

@zh-cn

name

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

@ast

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

@en

type

label

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

@ast

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

@en

prefLabel

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

@ast

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

@en

P1433

Q36012132-3164C6B9-161A-4075-A8AC-759C2985CF6D

P1476

Q36012132-E7E918CA-ED24-47D1-A4B0-082C08D86180

P2093

Q36012132-014787C7-6436-405C-B6F3-53225987B295

Q36012132-57E6AA7D-FDF3-44A2-997F-D50D82EFA106

Q36012132-C08249C8-28D6-447B-92E1-53CB1553191D

P2860

Q36012132-217E0698-5C98-481F-9B8C-5B66046AF1E4

Q36012132-220F901A-A339-4D1F-A840-3379BD74AD72

Q36012132-24A673F7-11D4-4F88-ADA4-0EAB36F83059

Q36012132-36759984-30E1-4D41-828C-488F5649E029

Q36012132-3ABCB453-2729-4519-AB66-081F43D704C3

Q36012132-3D66146F-E6DC-4387-A630-4570D9C9D368

Q36012132-47A8D442-EC82-4364-9E7B-79C42D543597

Q36012132-48BF7C22-3DEA-4824-9935-760376F3F558

Q36012132-48BFDA58-7E43-4731-989A-5D7217F2FEF0

Q36012132-494A54FA-F116-4A31-ACEB-BA2C37A89173

P304

Q36012132-F5FA2B48-670F-49DB-BA24-FC563484A9B4

P31

Q36012132-13DE7FCF-73ED-465F-8DEE-B0C7D095B661

P356

Q36012132-F18C8AF7-8B32-4F93-BC05-6486A6A963EE

P407

Q36012132-91354D8B-D012-44D7-A783-5029DD3FD4BA

P433

Q36012132-DEC3369D-E6D2-4C4B-8A91-9EB978C44F8A

P478

Q36012132-B2754C1B-3F65-49A5-B35E-C02CC3472529

P577

Q36012132-FE0710CE-2C18-4407-9D48-DD2921D9E76B

P5875

Q36012132-29312C18-6345-4DC2-A0F4-CB10BCEE6E21

P698

Q36012132-2D739D15-9FF6-4389-8236-D72852952A40

P932

Q36012132-CB2A71C0-3C19-4D37-8156-5BB2BB526062

P356

P1433

P1476

Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2.

@en

P2093

James R Reed

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

Rusty W Kelley

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

Wayne L Backes

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

P2860

Protein measurement with the Folin phenol reagent

Genomic sequencing

The many roles of cytochrome b5

Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components

Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450

THE CARBON MONOXIDE-BINDING PIGMENT OF LIVER MICROSOMES. II. SOLUBILIZATION, PURIFICATION, AND PROPERTIES

Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

Association of cytochromes P450 with their reductases: opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system.

Comparison of P450s from human and fugu: 420 million years of vertebrate P450 evolution.

Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes.

P304

2632-2641

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

P31

scholarly article

P356

10.1021/BI0477900

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

P407

P433

7

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

P478

44

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

P577

2005-02-01T00:00:00Z

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

P5875

8022924

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

P698

15709776

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

P932

1993544

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