(Q34450306)

2 August 2017

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title

Assembly of chaperonin complexes (English)

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2 August 2017

Kusmierczyk AR

1

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PubMed ID

11725484

2 August 2017

Martin J

series ordinal

2

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2 August 2017

1 October 2001

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2 August 2017

Molecular Biotechnology

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2 August 2017

19

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2 August 2017

2

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2 August 2017

141-152

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https://scigraph.springernature.com/pub.10.1385/mb:19:2:141

2 August 2017

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cites work

The N terminus of the molecular chaperonin GroEL is a crucial structural element for its assembly.

1 reference

12 December 2020

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

1 reference

12 December 2020

Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability

1 reference

12 December 2020

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

1 reference

12 December 2020

Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain

1 reference

12 December 2020

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

1 reference

12 December 2020

Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES.

1 reference

12 December 2020

The recombinant thermosome from the hyperthermophilic archaeon Methanopyrus kandleri: in vitro analysis of its chaperone activity

1 reference

12 December 2020

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

12 December 2020

Sequence and structural homology between a mouse T-complex protein TCP-1 and the 'chaperonin' family of bacterial (GroEL, 60-65 kDa heat shock antigen) and eukaryotic proteins

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12 December 2020

In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP

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12 December 2020

Role of the amino terminal domain in GroES oligomerization

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12 December 2020

Refolding and reassembly of active chaperonin GroEL after denaturation

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12 December 2020

The tail of a chaperonin: the C-terminal region of Escherichia coli GroEL protein

1 reference

12 December 2020

A cytoplasmic chaperonin that catalyzes beta-actin folding

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12 December 2020

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

1 reference

12 December 2020

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

1 reference

12 December 2020

The structural stability of the co-chaperonin GroES

1 reference

12 December 2020

Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1.

1 reference

12 December 2020

Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides

1 reference

12 December 2020

The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.

1 reference

12 December 2020

The Single-Ring Thermoanaerobacter brockii Chaperonin 60 (Tbr-EL7) Dimerizes to Tbr-EL14.cntdot.Tbr-ES7 under Protein Folding Conditions

1 reference

12 December 2020

Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers

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12 December 2020

Disassembly of the cytosolic chaperonin in mammalian cell extracts at intracellular levels of K+ and ATP

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12 December 2020

The C-terminal sequence of the chaperonin GroES is required for oligomerization

1 reference

12 December 2020

Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro

1 reference

12 December 2020

Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

1 reference

12 December 2020

Purification and properties of the groES morphogenetic protein of Escherichia coli

1 reference

12 December 2020

In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1.

1 reference

12 December 2020

Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent

1 reference

12 December 2020

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

1 reference

12 December 2020

Coupling between protein folding and allostery in the GroE chaperonin system

1 reference

12 December 2020

Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

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12 December 2020

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

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12 December 2020

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

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12 December 2020

The essential yeast Tcp1 protein affects actin and microtubules

1 reference

12 December 2020

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

1 reference

12 December 2020

Chaperonin filaments: the archaeal cytoskeleton?

1 reference

12 December 2020

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

1 reference

12 December 2020

Residual Structure in Urea-Denatured Chaperonin GroEL

1 reference

12 December 2020

Role of the GroEL chaperonin intermediate domain in coupling ATP hydrolysis to polypeptide release

1 reference

12 December 2020

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

1 reference

12 December 2020

(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.

1 reference

12 December 2020

The mitochondrial chaperonin hsp60 is required for its own assembly

1 reference

12 December 2020

Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein

1 reference

12 December 2020

Principles that govern the folding of protein chains

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12 December 2020

Purification of GroEL with low fluorescence background

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12 December 2020

Characterization of a functionally important mobile domain of GroES.

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12 December 2020

Chaperonin filaments: their formation and an evaluation of methods for studying them

1 reference

12 December 2020

A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.

1 reference

12 December 2020

Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides.

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12 December 2020

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

1 reference

12 December 2020

Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.

1 reference

12 December 2020

Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding

1 reference

12 December 2020

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

1 reference

12 December 2020

Protein stability and molecular adaptation to extreme conditions

1 reference

12 December 2020

Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates

1 reference

12 December 2020

Chemical synthesis of 10 kDa chaperonin Biological activity suggests chaperonins do not require other molecular chaperones

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12 December 2020

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

1 reference

12 December 2020

1 reference

12 December 2020

Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring

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12 December 2020

Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta

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12 December 2020

Allosteric control by ATP of non-folded protein binding to GroEL

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12 December 2020

Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model

1 reference

12 December 2020

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

1 reference

12 December 2020

Characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the acidothermophilic archaeon, Sulfolobus sp. strain 7

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12 December 2020

Preformed GroES oligomers are not required as functional cochaperonins

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12 December 2020

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

1 reference

12 December 2020

Expression of an archaeal chaperonin in E. coli: formation of homo- (alpha, beta) and hetero-oligomeric (alpha+beta) thermosome complexes.

1 reference

12 December 2020

The chaperonin containing TCP-1 (CCT) displays a single-ring mediated disassembly and reassembly cycle

1 reference

12 December 2020

The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60)

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12 December 2020

Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent.

1 reference

12 December 2020

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

12 December 2020

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

1 reference

12 December 2020

Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

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12 December 2020

Reversible oligomerization and denaturation of the chaperonin GroES

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12 December 2020

Chaperone-assisted protein folding.

1 reference

12 December 2020

Identifiers

DOI

10.1385/MB:19:2:141

1 reference

PubMed ID

11725484

Dimensions Publication ID

2 August 2017

0 references

1 reference

PubMed ID

11725484