(Q57844653)

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General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease

scientific article published on 01 February 2003

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scholarly article

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Europe PubMed Central

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31 October 2019

General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12589825%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

protein folding

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Motomitsu Kitaoka

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12589825%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

Cynthia Marie-Claire

4

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31 October 2019

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Bing Tang

1

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31 October 2019

Satoru Nirasawa

2

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31 October 2019

Kiyoshi Hayashi

5

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31 October 2019

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1 February 2003

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31 October 2019

Biochemical and Biophysical Research Communications

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31 October 2019

301

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31 October 2019

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31 October 2019

1093-1098

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31 October 2019

Molecular cloning and expression in Escherichia coli of the extracellular endoprotease of Aeromonas caviae T-64, a pro-aminopeptidase processing enzyme(1).

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https://api.crossref.org/works/10.1016%2FS0006-291X%2803%2900084-6

7 January 2021

In vitro stepwise autoprocessing of the proform of pro-aminopeptidase processing protease from Aeromonas caviae T-64.

1 reference

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7 January 2021

The role of the N-terminal propeptide of the pro-aminopeptidase processing protease: refolding, processing, and enzyme inhibition

1 reference

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7 January 2021

Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked

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7 January 2021

A protein-folding reaction under kinetic control

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7 January 2021

Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases

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7 January 2021

The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro

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7 January 2021

A major secreted elastase is essential for pathogenicity of Aeromonas hydrophila

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Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus

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7 January 2021

Cloning and nucleotide sequencing of the protease gene of Vibrio vulnificus

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7 January 2021

Cloning and nucleotide sequence of the Vibrio cholerae hemagglutinin/protease (HA/protease) gene and construction of an HA/protease-negative strain

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7 January 2021

Cloning of a metalloprotease gene involved in the virulence mechanism of Vibrio anguillarum

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7 January 2021

The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus

1 reference

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7 January 2021

Two allelic forms of the aureolysin gene (aur) within Staphylococcus aureus

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7 January 2021

Structure of thermolysin

1 reference

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7 January 2021

Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin

1 reference

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7 January 2021

Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution

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7 January 2021

Polypeptides of the tail fibres of bacteriophage T4

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Folding pathway mediated by an intramolecular chaperone: the structural and functional characterization of the aqualysin I propeptide

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7 January 2021

Identifiers

10.1016/S0006-291X(03)00084-6

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12589825%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12589825%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

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