Chaperonins (Q74664372)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

review article

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title

Chaperonins (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

author name string

K Braig

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

publication date

1 April 1998

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

Current Opinion in Structural Biology

12 November 2019

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

volume

8

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

issue

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

page(s)

159-165

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

Principles that govern the folding of protein chains

12 November 2019

cites work

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7 January 2021

Molecular chaperones in cellular protein folding

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7 January 2021

Proteins as molecular chaperones.

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7 January 2021

Chaperones get in touch: the Hip-Hop connection

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7 January 2021

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

1 reference

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7 January 2021

Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms

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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

Structure of a molecular chaperone from a thermophilic archaebacterium

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7 January 2021

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

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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

The molecular chaperonin TF55 from the Thermophilic archaeon Sulfolobus solfataricus. A biochemical and structural characterization

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7 January 2021

Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits

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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

A cytoplasmic chaperonin that catalyzes beta-actin folding

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7 January 2021

Chaperonin-mediated folding of actin and tubulin

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7 January 2021

TCP1 complex is a molecular chaperone in tubulin biogenesis

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

A polypeptide bound by the chaperonin groEL is localized within a central cavity

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

1 reference

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7 January 2021

Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

1 reference

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7 January 2021

Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

1 reference

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7 January 2021

Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding

1 reference

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7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

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7 January 2021

In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

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7 January 2021

A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

1 reference

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7 January 2021

A structural model for GroEL-polypeptide recognition

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.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Structural basis of allosteric changes in the GroEL mutant Arg197→Ala

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Detection of changes in pairwise interactions during allosteric transitions: coupling between local and global conformational changes in GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Molecular chaperones. Opening and closing the Anfinsen cage.

1 reference

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7 January 2021

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

1 reference

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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%2FS0959-440X%2898%2980033-X

7 January 2021

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

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7 January 2021

Release of both native and non-native proteins from a cis-only GroEL ternary complex

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

The effect of macromolecular crowding on chaperonin-mediated protein folding

1 reference

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7 January 2021

The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

1 reference

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7 January 2021

GroEL binds to and unfolds rhodanese posttranslationally

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

How GroES regulates binding of nonnative protein to GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980033-X

7 January 2021

10.1016/S0959-440X(98)80033-X

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9631288%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

1 reference