about
Hydroxysteroid 11-beta dehydrogenase 1Dihydrofolate reductaseCatalase3-hydroxy-3-methylglutaryl-Coenzyme A reductaseMethylenetetrahydrofolate reductaseGlucose-6-phosphate dehydrogenase X-linkedGlutathione reductaseGlyceraldehyde-3-phosphate dehydrogenase7-dehydrocholesterol reductaseP450 (cytochrome) oxidoreductaseFlavin containing monooxygenase 3Nitric oxide synthase 3, endothelial cellPutative dimethylaniline monooxygenase [N-oxide-forming] 6Flavin containing dimethylaniline monoxygenase 4Flavin containing dimethylaniline monoxygenase 5Flavin containing dimethylaniline monoxygenase 1Flavin containing dimethylaniline monoxygenase 2Dihydrofolate reductase 2Hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenaseTransmembrane 7 superfamily member 2Glyoxylate reductase 1 homologAspartate dehydrogenase domain containingCrystallin muGlyceraldehyde-3-phosphate dehydrogenase, spermatogenicNitric oxide synthase 2Phosphogluconate dehydrogenaseNADPH dependent diflavin oxidoreductase 1Isocitrate dehydrogenase (NADP(+)) 1Nicotinamide nucleotide transhydrogenaseGlucose-6-phosphate 1-dehydrogenaseDihydropyrimidine dehydrogenaseMalic enzyme 1Nitric oxide synthase 1Crystallin zeta like 15-methyltetrahydrofolate-homocysteine methyltransferase reductaseNADPH oxidase 53-hydroxy-3-methylglutaryl coenzyme A reductaseNADPH oxidase 16-phosphogluconate dehydrogenase CT_063Glyceraldehyde-3-phosphate dehydrogenase CT_505
P680
Cell transformation by the superoxide-generating oxidase Mox1Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanismCrystal structure of human micro-crystallin complexed with NADPHCloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyteStructural characterization and pharmacodynamic effects of an orally active 11beta-hydroxysteroid dehydrogenase type 1 inhibitorPyridine amides as potent and selective inhibitors of 11beta-hydroxysteroid dehydrogenase type 1Discovery of novel, potent benzamide inhibitors of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) exhibiting oral activity in an enzyme inhibition ex vivo modelDiscovery and optimization of piperidyl benzamide derivatives as a novel class of 11beta-HSD1 inhibitorsThe structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitorsConformational flexibility in crystal structures of human 11beta-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation.
P921
Q14329327-985667EC-2684-41E4-B292-A84186E4D0B8Q14819390-1E7DB8ED-5BA2-480E-BE7A-ECC6F8C8CC82Q14819390-796D42DF-D6E5-4B37-AF2A-BA8328484DE7Q14849204-202D845B-3513-4F14-B5D5-E64762A791E9Q14864142-B0E0A109-E396-4A0B-9892-D57F4F8CBBE1Q14864925-396541D3-BC54-4491-9737-1338E117C63CQ14877643-AD8C8503-205F-4746-9DFD-4131A94AC5C9Q14878284-A9A729F8-D136-4B54-9B06-6FEF974AFB22Q14878284-C968E204-C313-4830-93BD-ACAEAF8EB642Q14890093-B4945D5B-FB78-4E85-AF2B-6866D6E5A10AQ14905457-18322F75-7C56-4CEB-B39D-8927CC4A8854Q14909447-A5BE9F2B-6C65-458E-B098-684A7A3788E0Q14914446-2FEB1122-3BFA-4827-9F4E-A32709358645Q15328616-4FD21822-4BDF-4983-A590-7BFB686C4F77Q21101448-6F803C5C-1023-4568-83D6-B90F99031981Q21101453-C37ED31E-2377-4EB0-9696-03F5D78C8782Q21101457-97DEC7CE-0871-42A6-9CD8-CB23A2644AEAQ21101459-614C7988-7E78-4E40-A6F5-857E1E814671Q21101467-A52154F5-AEAF-4157-9E65-E0D2DD6A02B1Q21102712-A4DF247A-E020-4083-A729-9B28D98FF66BQ21103110-58952224-DDE9-416E-B77D-5F7AC6B7710DQ21105914-4793BDA9-ADDB-4A04-8C72-ACDFF708A03BQ21109671-6B2BADCF-0B9C-450F-858A-1EE49A9C9E4AQ21110456-AC36008E-B3E6-4261-866C-53A3400AD932Q21112053-4A57FFE4-C830-46D9-A8AF-5B7DCFA4E0FCQ21112479-7F772D0E-0A11-4C1A-8C25-31BB9CA77BA1Q21114547-8769B359-1002-4B44-A9D2-1F961704C106Q21115127-A07CC617-EDDE-4CB9-A392-02EBF68F509CQ21115127-A9898B71-C9BB-441B-8572-BF0AF0217D96Q21115715-0F6B094B-FF1F-473F-A177-692A1F322CCBQ21115715-629EC19C-CC67-4B13-8A30-356F4186C0C7Q21116029-6FF798F6-9A7E-464C-92A3-5366AEB63A4BQ21117744-2265E592-770C-4D47-87BF-6759677ED00BQ21117744-85917A11-D6A6-46F2-9163-26E474C49CE2Q21117873-2FBFFC44-886D-49AF-BDE6-EBE00FD7B8F8Q21118006-D374B2C4-72F6-43EA-8048-348B66C7EBC1Q21118006-F93968C4-D42D-44B0-994F-7AB67194B5D3Q21119972-657FECC2-AF43-44ED-980D-EB70D0B140A5Q21121716-07E7B401-FB82-4656-9CAD-E9E9DEF525EEQ21122619-47C063C7-B1B9-4EA8-BD30-34CD2C755A46
P680
Q22010372-B706EF89-2C07-47F0-AB60-F0D221BFC55DQ22011191-79D79192-661D-4CC4-9167-8D1F1E01DF0BQ24294217-F100E372-6319-4A45-B0FC-19139566A442Q24304897-D1714A62-6A18-4E96-BA89-E5E22FE5BFAEQ27649250-211E9D16-E7C1-410E-ABAE-D20660FEB71CQ27650633-525F6028-733F-479A-B1CA-26F72FBE223CQ27650834-7B44BD7D-6C5B-497D-B3F6-2872403F8205Q27653807-82BB9346-D49B-4A23-8CB1-E11844A7923DQ27733398-480F776C-AD83-4DFB-B903-52FD8695E15CQ45129829-7AD2A612-A982-476A-B024-3B3A385020A1
P921
description
Interacting selectively and no ...... +, or the reduced form, NADPH.
@en
moleculaire functie
@nl
name
NADP binding
@en
legare a NADP
@ro
type
label
NADP binding
@en
legare a NADP
@ro
altLabel
GO:0050661
@en
nicotinamide adenine dinucleotide phosphate binding
@en
prefLabel
NADP binding
@en
legare a NADP
@ro
P2888
P686
GO:0050661