(Q42147515)

17 October 2017

Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase (English)

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17 October 2017

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Miller AD

1

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17 October 2017

Maghlaoui K

2

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17 October 2017

Albanese G

3

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17 October 2017

Kleinjan DA

4

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17 October 2017

Smith C

5

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17 October 2017

language of work or name

English

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publication date

1 April 1993

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17 October 2017

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17 October 2017

291 ( Pt 1)

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17 October 2017

139-144

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

17 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Selective chemical modification of malate dehydrogenase. N-ethylmaleimide modification of active center sulfhydryl residues

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Purification and properties of the groES morphogenetic protein of Escherichia coli

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

The Escherichia coli groE chaperonins

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Protein folding in the cell

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

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

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

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

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60.

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

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

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

GroE prevents the accumulation of early folding intermediates of pre-beta-lactamase without changing the folding pathway.

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation.

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

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

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

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

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

17 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1132492

Physicochemical properties of pig and horse heart mitochondrial malate dehydrogenase

17 August 2018

1 reference

12 December 2020

Quaternary structure, subunit activity, and in vitro association of porcine mitochondrial malic dehydrogenase

1 reference

12 December 2020

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

1 reference

12 December 2020

The three-dimensional structure of porcine heart mitochondrial malate dehydrogenase at 3.0-A resolution

1 reference

12 December 2020

GroE facilitates refolding of citrate synthase by suppressing aggregation

1 reference

12 December 2020

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1 reference

12 December 2020

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1 reference

12 December 2020

Identifiers

DOI

10.1042/BJ2910139

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17 October 2017

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17 October 2017

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