(Q72330339)

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Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor

scientific article published on 01 April 1994

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scholarly article

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8143876%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8143876%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

author name string

M Matsubara

1

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26 October 2019

E Kurimoto

2

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26 October 2019

S Kojima

3

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26 October 2019

K Miura

4

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26 October 2019

T Sakai

5

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26 October 2019

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publication date

1 April 1994

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26 October 2019

1 reference

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26 October 2019

342

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26 October 2019

193-196

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26 October 2019

2

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26 October 2019

Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Folding of subtilisin BPN': role of the pro-sequence.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Folding of subtilisin BPN': characterization of a folding intermediate.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide [corrected]

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Functional analysis of the intramolecular chaperone. Mutational hot spots in the subtilisin pro-peptide and a second-site suppressor mutation within the subtilisin molecule

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Folding pathway mediated by an intramolecular chaperone

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Intramolecular chaperones and protein folding

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Inhibition of subtilisin BPN' by reaction site P1 mutants of Streptomyces subtilisin inhibitor

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Requirement for a disulfide bridge near the reactive site of protease inhibitor SSI (Streptomyces subtilisin inhibitor) for its inhibitory action

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Dissecting the catalytic triad of a serine protease

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Energetics of folding subtilisin BPN'

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

An engineered disulfide cross-link accelerates the refolding rate of calcium-free subtilisin by 850-fold

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Protease pro region required for folding is a potent inhibitor of the mature enzyme.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

The pro region required for folding of carboxypeptidase Y is a partially folded domain with little regular structural core

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Protein folding in the cell

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Intermediates in the folding reactions of small proteins

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2980499-0

21 January 2018

Identifiers

10.1016/0014-5793(94)80499-0

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8143876%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8143876%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

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