(Q38295580)

English

Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60.

scientific article published on May 1995

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60. (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

author name string

Baneyx F

1

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Bertsch U

2

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Kalbach CE

3

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

van der Vies SM

4

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Soll J

5

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

Gatenby AA

6

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

language of work or name

0 references

publication date

1 May 1995

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Europe PubMed Central

PubMed publication ID

1 September 2017

number of pages

8

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

1 September 2017

270

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

18

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

10695-10702

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

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/10.1074%2FJBC.270.18.10695

21 January 2018

Studies on the assembly of large subunits of ribulose bisphosphate carboxylase in isolated pea chloroplasts

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Light-dependent assembly of ribulose-1,5-bisphosphate carboxylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

The Rubisco subunit binding protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Demonstration by genetic suppression of interaction of GroE products with many proteins.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Identification of a groES-like chaperonin in mitochondria that facilitates protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Host participation in bacteriophage lambda head assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Cleavage of head and tail proteins during bacteriophage T5 assembly: Selective host involvement in the cleavage of a tail protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Characterization of a functionally important mobile domain of GroES.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Molecular chaperone functions of heat-shock proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

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/10.1074%2FJBC.270.18.10695

21 January 2018

Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Structural evidence for gene duplication in the evolution of the acid proteases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Protein folding: local structures, domains, subunits, and assemblies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Expression in E. coli of maize and wheat chloroplast genes for large subunit of ribulose bisphosphate carboxylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.18.10695

21 January 2018

Identifiers

10.1074/JBC.270.18.10695

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 September 2017

ResearchGate publication ID

0 references

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