(Q54608039)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7629128%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

title

Functional characterization of the higher plant chloroplast chaperonins (English)

1 reference

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22 October 2019

5

1 reference

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22 October 2019

author name string

P V Viitanen

1

1 reference

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22 October 2019

M Schmidt

2

1 reference

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22 October 2019

J Buchner

3

1 reference

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22 October 2019

T Suzuki

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7629128%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

R Dickson

6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7629128%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

G H Lorimer

7

1 reference

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22 October 2019

A Gatenby

8

1 reference

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22 October 2019

J Soll

9

1 reference

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22 October 2019

language of work or name

English

0 references

publication date

1 July 1995

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7629128%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

22 October 2019

published in

1 reference

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22 October 2019

volume

270

1 reference

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22 October 2019

page(s)

18158-18164

1 reference

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22 October 2019

issue

30

1 reference

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

22 October 2019

cites work

1 reference

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Protein folding in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

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.270.30.18158

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.270.30.18158

Purification and properties of groE, a host protein involved in bacteriophage assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.

21 January 2018

1 reference

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The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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

21 January 2018

1 reference

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Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

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.270.30.18158

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.270.30.18158

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Synthesis and assembly of large subunits into ribulose bisphosphate carboxylase/oxygenase in chloroplast extracts.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

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.270.30.18158

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

Accumulation, stability, and localization of a major chloroplast heat-shock protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Stromal factor plays an essential role in protein integration into thylakoids that cannot be replaced by unfolding or by heat shock protein Hsp70

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

Use of a scanning densitometer or an ELISA plate reader for measurement of nanogram amounts of protein in crude extracts from biological tissues

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Structure of holo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

Heat shock proteins of barley mitochondria and chloroplasts Identification of organellar hsp 10 and 12: putative chaperonin 10 homologues

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158

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.270.30.18158

Assembly of in Vitro-Synthesized Large Subunits into Ribulose Bisphosphate Carboxylase/Oxygenase Is Sensitive to CI-, Requires ATP, and Does Not Proceed When Large Subunits Are Synthesized at Temperatures [greater than or equal to]32[deg]C

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.18158

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.270.30.18158