Structural comparison of prokaryotic and eukaryotic chaperonins. (Q33971880)

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8 November 2019

review article

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title

Structural comparison of prokaryotic and eukaryotic chaperonins (English)

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8 November 2019

2

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8 November 2019

José María Valpuesta

series ordinal

3

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8 November 2019

author name string

J L Carrascosa

series ordinal

1

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8 November 2019

publication date

1 January 2001

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8 November 2019

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8 November 2019

volume

32

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8 November 2019

issue

1

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8 November 2019

page(s)

43-50

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The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

8 November 2019

cites work

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7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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A structural model for GroEL-polypeptide recognition

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The Hsp70 and Hsp60 chaperone machines

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Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii

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

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7 January 2021

Proteins as molecular chaperones.

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Residues in chaperonin GroEL required for polypeptide binding and release

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7 January 2021

A cytoplasmic chaperonin that catalyzes beta-actin folding

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7 January 2021

Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin

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7 January 2021

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

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7 January 2021

Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells

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7 January 2021

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

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7 January 2021

Molecular chaperones in cellular protein folding

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7 January 2021

Chaperone rings in protein folding and degradation.

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7 January 2021

Identification of in vivo substrates of the chaperonin GroEL

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7 January 2021

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

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7 January 2021

The thermosome: archetype of group II chaperonins

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7 January 2021

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

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7 January 2021

Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin

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7 January 2021

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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7 January 2021

T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

Biochemical Characterization of Symmetric GroEL-GroES Complexes

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7 January 2021

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

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7 January 2021

Conformational changes in the GroEL oligomer during the functional cycle.

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7 January 2021

Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings

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7 January 2021

ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 Complex

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7 January 2021

3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin

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7 January 2021

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

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7 January 2021

Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin

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7 January 2021

Group II chaperonin in an open conformation examined by electron tomography

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7 January 2021

The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins.

1 reference

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7 January 2021

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

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7 January 2021

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

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7 January 2021

Binding of chaperonins.

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7 January 2021

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

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7 January 2021

Symmetric complexes of GroE chaperonins as part of the functional cycle

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7 January 2021

Chaperonin function: folding by forced unfolding

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7 January 2021

Structure and function in GroEL-mediated protein folding

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7 January 2021

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

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7 January 2021

In vivo newly translated polypeptides are sequestered in a protected folding environment

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7 January 2021

A yeast TCP-1-like protein is required for actin function in vivo

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7 January 2021

GroEL/GroES: structure and function of a two-stroke folding machine

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7 January 2021

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

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7 January 2021

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

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7 January 2021

10.1016/S0968-4328(00)00027-5

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10900379%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

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