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The crystal structure of the bacterial chaperonin GroEL at 2.8 A
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title
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
(English)
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main subject
crystal structure
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author
Zbyszek Otwinowski
series ordinal
2
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Arthur L. Horwich
series ordinal
6
object named as
A L Horwich
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Andrzej Joachimiak
series ordinal
5
object named as
A Joachimiak
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author name string
K Braig
series ordinal
1
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R Hegde
series ordinal
3
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D C Boisvert
series ordinal
4
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P B Sigler
series ordinal
7
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language of work or name
English
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publication date
13 October 1994
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published in
Nature
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volume
371
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page(s)
578-86
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issue
6498
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cites work
Molecular Chaperones
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
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inferred from DOI database lookup
Protein folding in the cell
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Molecular chaperone functions of heat-shock proteins
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
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Purification and properties of groE, a host protein involved in bacteriophage assembly
1 reference
stated in
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reference URL
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retrieved
7 January 2021
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inferred from DOI database lookup
A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophila
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
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A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
A cytoplasmic chaperonin that catalyzes beta-actin folding
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
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inferred from DOI database lookup
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
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inferred from DOI database lookup
The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes
1 reference
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reference URL
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retrieved
7 January 2021
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inferred from DOI database lookup
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
1 reference
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Crossref
reference URL
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retrieved
7 January 2021
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inferred from DOI database lookup
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
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inferred from DOI database lookup
Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
A polypeptide bound by the chaperonin groEL is localized within a central cavity
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
ATP induces large quaternary rearrangements in a cage-like chaperonin structure.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
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inferred from DOI database lookup
Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
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inferred from DOI database lookup
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
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inferred from DOI database lookup
Symmetric complexes of GroE chaperonins as part of the functional cycle
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
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inferred from DOI database lookup
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding
1 reference
stated in
Crossref
reference URL
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7 January 2021
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Improved methods for building protein models in electron density maps and the location of errors in these models
1 reference
stated in
Crossref
reference URL
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7 January 2021
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Residues in chaperonin GroEL required for polypeptide binding and release
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
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inferred from DOI database lookup
Improved Fourier coefficients for maps using phases from partial structures with errors
1 reference
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Crossref
reference URL
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7 January 2021
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Assessment of protein models with three-dimensional profiles
1 reference
stated in
Crossref
reference URL
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7 January 2021
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The interpretation of protein structures: Estimation of static accessibility
1 reference
stated in
Crossref
reference URL
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7 January 2021
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inferred from DOI database lookup
Surface, subunit interfaces and interior of oligomeric proteins
1 reference
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Crossref
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7 January 2021
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The structure of interfaces between subunits of dimeric and tetrameric proteins
1 reference
stated in
Crossref
reference URL
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7 January 2021
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Chaperonin duet
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F371578A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1038/371578A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2366060
Dimensions Publication ID
1022157325
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OpenCitations bibliographic resource ID
2366060
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2366060
PubMed ID
7935790
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2366060
ResearchGate publication ID
15263027
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Springer Nature article ID
10.1038/371578a0
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