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Identification of in vivo substrates of the chaperonin GroEL
scientific article published in Nature
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10647006%20AND%20SRC:MED&resulttype=core&format=json
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3 November 2019
title
Identification of in vivo substrates of the chaperonin GroEL
(English)
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10647006%20AND%20SRC:MED&resulttype=core&format=json
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3 November 2019
author
Franz-Ulrich Hartl
series ordinal
5
object named as
F. Ulrich Hartl
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Franz-Ulrich Hartl
series ordinal
5
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Hartl FU
1 reference
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10647006%20AND%20SRC:MED&resulttype=core&format=json
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3 November 2019
author name string
Houry WA
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1
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Europe PubMed Central
PubMed publication ID
10647006
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3 November 2019
Frishman D
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2
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Europe PubMed Central
PubMed publication ID
10647006
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3 November 2019
Eckerskorn C
series ordinal
3
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
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3 November 2019
Lottspeich F
series ordinal
4
1 reference
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
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3 November 2019
language of work or name
English
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publication date
1 November 1999
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
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retrieved
3 November 2019
published in
Nature
1 reference
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
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retrieved
3 November 2019
volume
402
1 reference
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
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3 November 2019
issue
6758
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10647006%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
page(s)
147-154
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Europe PubMed Central
PubMed publication ID
10647006
reference URL
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retrieved
3 November 2019
cites work
Role of the major heat shock proteins as molecular chaperones
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Crossref
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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
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Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.
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7 January 2021
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Residues in chaperonin GroEL required for polypeptide binding and release
1 reference
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Crossref
reference URL
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7 January 2021
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Structural and mechanistic consequences of polypeptide binding by GroEL.
1 reference
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Crossref
reference URL
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7 January 2021
based on heuristic
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Structure and function in GroEL-mediated protein folding
1 reference
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Crossref
reference URL
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7 January 2021
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Chaperonins
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Crossref
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7 January 2021
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In vivo observation of polypeptide flux through the bacterial chaperonin system.
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Crossref
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Escherichia coli ribosomes translate in vivo with variable rate
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7 January 2021
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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
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Crossref
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7 January 2021
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Protein folding in the cell: competing models of chaperonin function.
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Crossref
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7 January 2021
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GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
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Molecular chaperones: avoiding the crowd
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The cloning and sequence of the gene encoding the omega subunit of Escherichia coli RNA polymerase
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Genetic suppression of a temperature-sensitive groES mutation by an altered subunit of RNA polymerase of Escherichia coli K-12
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The gene‐protein database of Escherichia coli: Edition 5
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The CATH Database provides insights into protein structure/function relationships.
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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
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7 January 2021
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Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent
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Contact order, transition state placement and the refolding rates of single domain proteins.
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7 January 2021
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Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.
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7 January 2021
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Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
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7 January 2021
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Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein.
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7 January 2021
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Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.
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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
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Identifiers
DOI
10.1038/45977
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10647006
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10647006%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
Dimensions Publication ID
1002860173
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PubMed publication ID
10647006
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10647006
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10647006%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 November 2019
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