Conformational folding and disulfide bonding drive distinct stages of protein structure formation.

about

In vitro generation and bioactivity evaluation of C-reactive protein intermediate.

P2860

Q55222117-F5AE1BB0-55A1-4789-926A-D34C5D4BB7DC

P2860

Conformational folding and disulfide bonding drive distinct stages of protein structure formation.

Item

http://www.wikidata.org/entity/Q48171807

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh

2018年學術文章

@zh-hant

name

Conformational folding and dis ...... f protein structure formation.

@en

Conformational folding and dis ...... f protein structure formation.

@nl

type

Item

label

Conformational folding and dis ...... f protein structure formation.

@en

Conformational folding and dis ...... f protein structure formation.

@nl

prefLabel

Conformational folding and dis ...... f protein structure formation.

@en

Conformational folding and dis ...... f protein structure formation.

@nl

P1476

Conformational folding and dis ...... f protein structure formation.

@en

P2093

Bo-Xuan Gao

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

Jian-Min Lv

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

Juan Zhang

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

Lawrence A Potempa

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

Mian Long

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

Shang-Rong Ji

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

Shou-Qin Lü

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

Yue-Xin Wu

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

Zhen-Yu Yao

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

Zu-Pei Liu

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

P2860

C-reactive protein: a critical update

The physiological structure of human C-reactive protein and its complex with phosphocholine

The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals

A staggered decameric assembly of human C-reactive protein stabilized by zinc ions revealed by X-ray crystallography

All-atom empirical potential for molecular modeling and dynamics studies of proteins

VMD: visual molecular dynamics

Scalable molecular dynamics with NAMD

Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.

Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.

Secretory production of recombinant human C-reactive protein in Escherichia coli, capable of binding with phosphorylcholine, and its characterization.

P2888

s41598-018-20014-y

P304

1494

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

P31

scholarly article

P356

10.1038/S41598-018-20014-Y

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

P407

English

P433

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

P478

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

P50

Yi Wu

P577

2018-01-24T00:00:00Z

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

P698

29367639

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

P921

protein structure

protein folding

P932

5784126

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

Conformational folding and disulfide bonding drive distinct stages of protein structure formation.

about

P2860

P2860

Conformational folding and disulfide bonding drive distinct stages of protein structure formation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932