Molecular recognition and binding of beta-lactamase II from Bacillus cereus with penicillin V and sulbactam by spectroscopic analysis in combination with docking simulation.

about

Molecular recognition and binding of beta-lactamase II from Bacillus cereus with penicillin V and sulbactam by spectroscopic analysis in combination with docking simulation.

Item

http://www.wikidata.org/entity/Q51142703

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Molecular recognition and bind ...... ation with docking simulation.

@en

Molecular recognition and bind ...... ation with docking simulation.

@nl

type

Item

label

Molecular recognition and bind ...... ation with docking simulation.

@en

Molecular recognition and bind ...... ation with docking simulation.

@nl

prefLabel

Molecular recognition and bind ...... ation with docking simulation.

@en

Molecular recognition and bind ...... ation with docking simulation.

@nl

P1476

Molecular recognition and bind ...... ation with docking simulation.

@en

P2093

Liujiao Bian

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

Pan Qiao

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

Shuaihua Li

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

Xuan Feng

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

Yeli Zhang

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

P2860

The Zn2 position in metallo-beta-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold

Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme

The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity.

Metallo-beta-lactamase: structure and mechanism.

Metallo-beta-lactamases: the quiet before the storm?

Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity.

Metallo-beta-lactamases: two binding sites for one catalytic metal ion?

Beta-lactam antibiotic resistance: a current structural perspective.

The amino acid sequence of the zinc-requiring beta-lactamase II from the bacterium Bacillus cereus 569.

X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus.

P304

932-941

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

P31

scholarly article

P356

10.1002/BIO.3274

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

P433

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

P478

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

P577

2017-02-10T00:00:00Z

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

P698

28185399

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