Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

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Crystal structure of the precursor of galactose oxidase: An unusual self-processing enzyme The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability Glutamyl Endopeptidases: The Puzzle of Substrate Specificity

P2860

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P2860

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

Item

http://www.wikidata.org/entity/Q39569367

description

1998 nî lūn-bûn

@nan

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

1998年论文

@zh

1998年论文

@zh-cn

name

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

@en

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

@nl

type

Item

label

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

@en

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

@nl

prefLabel

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

@en

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

@nl

P1476

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

@en

P2093

Baardsnes J

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

Borgford T

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

Elliott J

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

MacLeod A

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

Morden D

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

Sidhu S

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

Watson J

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

P2860

Prediction of the secondary structure of proteins from their amino acid sequence

Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli

Families and clans of serine peptidases.

Characterization and structure of genes for proteases A and B from Streptomyces griseus.

Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neutral proteases.

Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.

The 2.8 A resolution structure of Streptomyces griseus protease B and its homology with alpha-chymotrypsin and Streptomyces griseus protease A.

Pro-sequence-assisted protein folding.

Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis.

Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site.

P304

3241-3244

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P31

scholarly article

P407

English

P433

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

P478

180

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P577

1998-06-01T00:00:00Z

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

P698

9620979

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

P932

107830

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

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

about

P2860

P2860

Streptomyces griseus protease B: secretion correlates with the length of the propeptide.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P407

P433

P478

P577

P698

P932

P1433

P1476

P2093

P2860

P304

P31

P407

P433

P478

P577

P698

P932