The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

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http://www.wikidata.org/entity/Q42314400

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

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2016年论文

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name

The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

@en

The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

@nl

type

Item

label

The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

@en

The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

@nl

prefLabel

The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

@en

The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

@nl

P1476

The GTPase hGBP1 converts GTP to GMP in two steps via proton shuttle mechanisms.

@en

P2093

Dominik Marx

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

Rachel Glaves

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

Ravi Tripathi

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P2860

Biological phosphoryl-transfer reactions: understanding mechanism and catalysis

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The guanylate binding protein-1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP-1 expression

Guanylate-binding protein-1 expression is selectively induced by inflammatory cytokines and is an activation marker of endothelial cells during inflammatory diseases

Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins

Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

The mechanism of pentabromopseudilin inhibition of myosin motor activity

The Initiation of GTP Hydrolysis by the G-Domain of FeoB: Insights from a Transition-State Complex Structure

Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis

P304

371-380

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P31

scholarly article

P356

10.1039/C6SC02045C

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P433

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

P478

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

P577

2016-08-22T00:00:00Z

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P698

28451182

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P932

5365056

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