Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

about

Structural basis of a thiol-disulfide oxidoreductase in the hedgehog-forming actinobacterium Corynebacterium matruchotii.

P2860

Q50027206-C8D9BE00-8CB6-4F3A-B14E-40BFB111651B

P2860

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

Item

http://www.wikidata.org/entity/Q47967800

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

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

@en

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

@nl

type

Item

label

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

@en

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

@nl

prefLabel

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

@en

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

@nl

P1476

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

@en

P2093

L Davey

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

S F Lee

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

P2860

Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria

Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis

Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding

An Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression Analysis

Structural, dynamic, and chemical characterization of a novel S-glycosylated bacteriocin

Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence

Trimeric structure of major outer membrane proteins homologous to OmpA in Porphyromonas gingivalis.

Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168.

Virulence properties of cariogenic bacteria.

Outer membrane proteome and antigens of Tannerella forsythia.

P304

1465-1473

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

P31

scholarly article

P356

10.1177/0022034517725059

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

P577

2017-08-01T00:00:00Z

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

P698

28797211

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

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

about

P2860

P2860

Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698