Kinetic alteration of a human dihydrodiol/3alpha-hydroxysteroid dehydrogenase isoenzyme, AKR1C4, by replacement of histidine-216 with tyrosine or phenylalanine.

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Kinetic alteration of a human dihydrodiol/3alpha-hydroxysteroid dehydrogenase isoenzyme, AKR1C4, by replacement of histidine-216 with tyrosine or phenylalanine.

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2000 nî lūn-bûn

@nan

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

2000年论文

@zh

2000年论文

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name

Kinetic alteration of a human ...... ith tyrosine or phenylalanine.

@en

Kinetic alteration of a human ...... ith tyrosine or phenylalanine.

@nl

type

Item

label

Kinetic alteration of a human ...... ith tyrosine or phenylalanine.

@en

Kinetic alteration of a human ...... ith tyrosine or phenylalanine.

@nl

prefLabel

Kinetic alteration of a human ...... ith tyrosine or phenylalanine.

@en

Kinetic alteration of a human ...... ith tyrosine or phenylalanine.

@nl

P1476

Kinetic alteration of a human ...... ith tyrosine or phenylalanine.

@en

P2093

Hara A

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Ishikura S

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Ohta T

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Shintani S

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Usami N

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P2860

Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity

Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder

Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase

Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases

cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family

Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor

An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate

P304

685-691

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P31

scholarly article

P356

10.1042/0264-6021:3520685

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P407

English

P478

352 Pt 3

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P577

2000-12-01T00:00:00Z

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P5875

247447699

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P698

11104674

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P932

1221505

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