(Q41763175)

English

The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form

scientific article published on August 1997

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Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form (English)

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

peptidyl-prolyl cis-trans isomerase

0 references

author name string

von Ahsen O

1

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

Tropschug M

2

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

Pfanner N

3

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

Rassow J

4

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

language of work or name

0 references

publication date

1 August 1997

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

The EMBO Journal

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

16

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

15

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

4568-4578

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

GroEL-mediated protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

The Escherichia coli trigger factor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Protein biogenesis: chaperones for nascent polypeptides

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Hsp60-independent protein folding in the matrix of yeast mitochondria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Role of the major heat shock proteins as molecular chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Specific incorporation of cyclophilin A into HIV-1 virions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Molecular chaperones and intracellular protein translocation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Cyclophilin catalyzes protein folding in yeast mitochondria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Cyclosporin A-binding protein (cyclophilin) of Neurospora crassa. One gene codes for both the cytosolic and mitochondrial forms.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Protein folding in the cell

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Cis-transisomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

A yeast cyclophilin gene essential for lactate metabolism at high temperature

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

The mechanism of action of cyclosporin A and FK506

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

Interaction of GroE with an all-beta-protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

6 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

18 August 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

18 August 2018

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

18 August 2018

Nature and consequences of GroEL-protein interactions.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

18 August 2018

Molecular Chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

18 August 2018

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1170083

2 December 2018

Folding intermediates of β-lactamase recognized by GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reassessment of the putative chaperone function of prolyl-cis/trans-isomerases

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A cyclophilin function in Hsp90-dependent signal transduction

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chaperone function of Hsp90-associated proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides

1 reference

https://pubmed.ncbi.nlm.nih.gov/9303301

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1093/EMBOJ/16.15.4568

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

ResearchGate publication ID

0 references

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