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Steric chaperones.
scientific article published on February 1998
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instance of
scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
retrieved
8 October 2017
review article
1 reference
stated in
Europe PubMed Central
title
Steric chaperones.
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
retrieved
8 October 2017
main subject
molecular chaperones
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author name string
Ellis RJ
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
retrieved
8 October 2017
publication date
1 February 1998
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
retrieved
8 October 2017
published in
Trends in Biochemical Sciences
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
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8 October 2017
volume
23
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stated in
Europe PubMed Central
PubMed ID
9538685
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8 October 2017
page(s)
43-45
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stated in
Europe PubMed Central
PubMed ID
9538685
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8 October 2017
issue
2
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
retrieved
8 October 2017
cites work
Protein memory through altered folding mediated by intramolecular chaperones.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
retrieved
7 January 2021
based on heuristic
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Do molecular chaperones have to be proteins?
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA.
1 reference
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https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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Homologous plant and bacterial proteins chaperone oligomeric protein assembly
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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Molecular chaperones in cellular protein folding
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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How the molten globule became.
1 reference
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https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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Principles that govern the folding of protein chains
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7 January 2021
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Macromolecular crowding: biochemical, biophysical, and physiological consequences.
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https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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Molecular chaperones: avoiding the crowd.
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7 January 2021
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Revisiting the Anfinsen cage.
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7 January 2021
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Intramolecular chaperones and protein folding.
1 reference
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Crossref
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7 January 2021
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Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.
1 reference
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Crossref
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https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
based on heuristic
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The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo.
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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A protein-folding reaction under kinetic control.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
based on heuristic
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Structure of a protein in a kinetic trap
1 reference
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7 January 2021
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Prion protein and the transmissible spongiform encephalopathies.
1 reference
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7 January 2021
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Mammalian subtilisins: the long-sought dibasic processing endoproteases.
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https://api.crossref.org/works/10.1016%2FS0968-0004%2898%2901175-X
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7 January 2021
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Identifiers
DOI
10.1016/S0968-0004(98)01175-X
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
retrieved
8 October 2017
PubMed ID
9538685
1 reference
stated in
Europe PubMed Central
PubMed ID
9538685
retrieved
8 October 2017
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