Revisiting the Anfinsen cage (Q41394293)

30 September 2017

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title

Revisiting the Anfinsen cage (English)

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30 September 2017

Ellis RJ

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30 September 2017

1 January 1996

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30 September 2017

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30 September 2017

1

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30 September 2017

R9-15

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30 September 2017

1

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

30 September 2017

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

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

7 January 2021

The role of molecular chaperones in protein folding

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Principles that govern the folding of protein chains

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

1 reference

7 January 2021

Molecular chaperone functions of heat-shock proteins

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Molecular chaperones. Opening and closing the Anfinsen cage.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Quasi-native chaperonin-bound intermediates in facilitated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Purification and properties of groE, a host protein involved in bacteriophage assembly

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Binding of chaperonins.

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

GroE facilitates refolding of citrate synthase by suppressing aggregation

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Unfolding protein folding

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Macromolecular crowding: biochemical, biophysical, and physiological consequences

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Refolding of barnase in the presence of GroE

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Nature and consequences of GroEL-protein interactions.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

The folding of hen lysozyme involves partially structured intermediates and multiple pathways

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900004-1

7 January 2021

10.1016/S1359-0278(96)00004-1

Identifiers

DOI

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30 September 2017

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PubMed ID

9079356