Heme-containing enzymes and inhibitors for tryptophan metabolism.

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Targeting the IDO1 pathway in cancer: from bench to bedside

P2860

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P2860

Heme-containing enzymes and inhibitors for tryptophan metabolism.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

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2017年論文

@zh-tw

2017年论文

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2017年论文

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2017年论文

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name

Heme-containing enzymes and inhibitors for tryptophan metabolism.

@en

Heme-containing enzymes and inhibitors for tryptophan metabolism.

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type

Item

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Heme-containing enzymes and inhibitors for tryptophan metabolism.

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Heme-containing enzymes and inhibitors for tryptophan metabolism.

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prefLabel

Heme-containing enzymes and inhibitors for tryptophan metabolism.

@en

Heme-containing enzymes and inhibitors for tryptophan metabolism.

@nl

P1476

Heme-containing enzymes and inhibitors for tryptophan metabolism.

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P2093

Daojing Yan

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

Xiangshi Tan

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

P2860

Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice

Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan

Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase

Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis

Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding

Crystal structure of Drosophila melanogaster tryptophan 2,3-dioxygenase reveals insights into substrate recognition and catalytic mechanism

Important Hydrogen Bond Networks in Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitor Design Revealed by Crystal Structures of Imidazoleisoindole Derivatives with IDO1

Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase

Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism

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1230-1240

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scholarly article

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10.1039/C7MT00105C

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P433

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P478

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Ying-Wu Lin

P577

2017-06-26T00:00:00Z

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P698

28650043

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Heme-containing enzymes and inhibitors for tryptophan metabolism.

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P2860

P2860

Heme-containing enzymes and inhibitors for tryptophan metabolism.

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698