(Q47868927)

6 February 2018

title

Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding. (English)

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6 February 2018

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Dickson R

1

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6 February 2018

Weiss C

2

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6 February 2018

Howard RJ

3

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6 February 2018

Alldrick SP

4

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6 February 2018

Ellis RJ

5

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6 February 2018

Lorimer G

6

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6 February 2018

Azem A

7

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6 February 2018

Viitanen PV

8

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6 February 2018

language of work or name

English

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publication date

1 April 2000

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6 February 2018

Journal of Biological Chemistry

number of pages

7

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based on heuristic

inferred from page(s)

published in

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6 February 2018

volume

275

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6 February 2018

page(s)

11829-11835

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6 February 2018

issue

16

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6 February 2018

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Reexamination of the folding of BPTI: predominance of native intermediates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Inhibition of ribulose bisphosphate carboxylase assembly by antibody to a binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Rubisco assembly: a model system for studying the mechanism of chaperonin action

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Molecular chaperones and protein folding in plants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Functional characterization of the higher plant chloroplast chaperonins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Conserved sequence motifs in bacterial and bacteriophage chaperonins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Purification, cDNA cloning and Northern-blot analysis of mitochondrial chaperonin 60 from pumpkin cotyledons

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Chloroplast molecular chaperone-assisted refolding and reconstitution of an active multisubunit coupling factor CF1 core

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

ATP-released large subunits participate in the assembly of RuBP carboxylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Purification of recombinant plant and animal GroES homologs: chloroplast and mitochondrial chaperonin 10

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Chloroplast chaperonins: evidence for heterogeneous assembly of alpha and beta Cpn60 polypeptides into a chaperonin oligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

Purification of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.16.11829

21 January 2018

Identifiers

DOI

10.1074/JBC.275.16.11829

1 reference

6 February 2018

PubMed ID

10766808

1 reference

6 February 2018