Chaperonins--keeping a lid on folding proteins (Q34384151)

1 August 2017

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title

Chaperonins--keeping a lid on folding proteins (English)

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1 August 2017

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Kusmierczyk AR

1

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1 August 2017

Martin J

series ordinal

2

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1 August 2017

language of work or name

English

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publication date

1 September 2001

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1 August 2017

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1 August 2017

volume

505

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1 August 2017

issue

3

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1 August 2017

page(s)

343-347

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Folding of newly translated proteins in vivo: the role of molecular chaperones

1 August 2017

cites work

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A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.

21 January 2018

1 reference

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Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Recurrent paralogy in the evolution of archaeal chaperonins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

21 January 2018

1 reference

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Characterization of a functionally important mobile domain of GroES.

21 January 2018

1 reference

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

21 January 2018

1 reference

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

21 January 2018

1 reference

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In vivo observation of polypeptide flux through the bacterial chaperonin system.

21 January 2018

1 reference

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

21 January 2018

1 reference

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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

21 January 2018

1 reference

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In vivo and in vitro function of GroEL mutants with impaired allosteric properties

21 January 2018

1 reference

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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

21 January 2018

1 reference

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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

21 January 2018

1 reference

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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

21 January 2018

1 reference

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Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings

21 January 2018

1 reference

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Coupling between protein folding and allostery in the GroE chaperonin system

21 January 2018

1 reference

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Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Recombination of protein domains facilitated by co-translational folding in eukaryotes.

21 January 2018

1 reference

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The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking

21 January 2018

1 reference

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Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins

21 January 2018

1 reference

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Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1

21 January 2018

1 reference

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Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization

21 January 2018

1 reference

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Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

21 January 2018

1 reference

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Successive action of Escherichia coli chaperones in vivo.

21 January 2018

1 reference

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Conformational rearrangements of an archaeal chaperonin upon ATPase cycling.

21 January 2018

1 reference

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MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains

21 January 2018

1 reference

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Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Partial Occlusion of Both Cavities of the Eukaryotic Chaperonin with Antibody Has No Effect upon the Rates of β-Actin or α-Tubulin Folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

21 January 2018

2 references

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21 January 2018

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

inferred from DOI database lookup

7 January 2021

based on heuristic

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

Group II chaperonin in an open conformation examined by electron tomography

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

ATPase cycle of an archaeal chaperonin

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902838-1

10.1016/S0014-5793(01)02838-1

21 January 2018

Identifiers

DOI

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1 August 2017

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