PAK: an essential motif for forming beta-turn structures and exhibiting the thrombolytic effect of P6A and its analogs.

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PAK: an essential motif for forming beta-turn structures and exhibiting the thrombolytic effect of P6A and its analogs.

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http://www.wikidata.org/entity/Q46865977

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2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

@zh-hant

name

PAK: an essential motif for fo ...... effect of P6A and its analogs.

@en

PAK: an essential motif for fo ...... effect of P6A and its analogs.

@nl

type

Item

label

PAK: an essential motif for fo ...... effect of P6A and its analogs.

@en

PAK: an essential motif for fo ...... effect of P6A and its analogs.

@nl

prefLabel

PAK: an essential motif for fo ...... effect of P6A and its analogs.

@en

PAK: an essential motif for fo ...... effect of P6A and its analogs.

@nl

P1476

PAK: an essential motif for fo ...... effect of P6A and its analogs.

@en

P2093

Chao Wang

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

Hu Liu

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

Kexiang Zhou

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

Lili Wang

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

Ming Zhao

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

Qin Li

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

Shiqi Peng

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

Xin Jia

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

P2860

A revised set of potentials for beta-turn formation in proteins

Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase

Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges

Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer

Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli

The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis

NMR solution structure of the periplasmic chaperone FimC

Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition

P304

730-740

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

P31

scholarly article

P356

10.1139/O07-143

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P433

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

P478

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

P577

2007-12-01T00:00:00Z

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

P698

18059531

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

P921

thrombolysis