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Revisiting the Anfinsen cage
scientific article published on January 1996
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instance of
scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
review article
1 reference
stated in
Europe PubMed Central
title
Revisiting the Anfinsen cage
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
author name string
Ellis RJ
series ordinal
1
1 reference
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Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
publication date
1 January 1996
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stated in
Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
published in
Folding & design
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stated in
Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
volume
1
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Europe PubMed Central
PubMed ID
9079356
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30 September 2017
page(s)
R9-15
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Europe PubMed Central
PubMed ID
9079356
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30 September 2017
issue
1
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stated in
Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
cites work
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol.
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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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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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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The role of molecular chaperones in protein folding
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Principles that govern the folding of protein chains
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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inferred from DOI database lookup
Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Molecular Chaperones
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Molecular chaperone functions of heat-shock proteins
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
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7 January 2021
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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
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7 January 2021
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Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Molecular chaperones. Opening and closing the Anfinsen cage.
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Quasi-native chaperonin-bound intermediates in facilitated protein folding
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Purification and properties of groE, a host protein involved in bacteriophage assembly
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7 January 2021
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Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly
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Binding of chaperonins.
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7 January 2021
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Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts
1 reference
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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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
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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GroE facilitates refolding of citrate synthase by suppressing aggregation
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Cooperativity in ATP hydrolysis by GroEL is increased by GroES
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Unfolding protein folding
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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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%2FS1359-0278%2896%2900004-1
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7 January 2021
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Refolding of barnase in the presence of GroE
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Nature and consequences of GroEL-protein interactions.
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7 January 2021
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ATP induces large quaternary rearrangements in a cage-like chaperonin structure.
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7 January 2021
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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Residues in chaperonin GroEL required for polypeptide binding and release
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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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The crystal structure of the bacterial chaperonin GroEL at 2.8 A
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
based on heuristic
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Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
based on heuristic
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The folding of hen lysozyme involves partially structured intermediates and multiple pathways
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1
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7 January 2021
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Identifiers
DOI
10.1016/S1359-0278(96)00004-1
1 reference
stated in
Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
PubMed ID
9079356
1 reference
stated in
Europe PubMed Central
PubMed ID
9079356
retrieved
30 September 2017
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