(Q37351795)

19 August 2017

A thermodynamic coupling mechanism for GroEL-mediated unfolding (English)

1 reference

19 August 2017

3

Schmid FX

1 reference

19 August 2017

Walter S

1

1 reference

PMCID

38444

19 August 2017

Lorimer GH

series ordinal

2

1 reference

PMCID

38444

19 August 2017

language of work or name

English

0 references

publication date

1 September 1996

1 reference

Proceedings of the National Academy of Sciences of the United States of America

19 August 2017

1 reference

19 August 2017

93

1 reference

19 August 2017

9425-9430

1 reference

19 August 2017

18

1 reference

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

19 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Preferential binding of an unfolded protein to DsbA.

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Three-state analysis of sperm whale apomyoglobin folding

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Residues in chaperonin GroEL required for polypeptide binding and release

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Calculation of protein extinction coefficients from amino acid sequence data

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Conformational stability of ribonuclease T1. I. Thermal denaturation and effects of salts

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Folding and association of proteins

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

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

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Ribonuclease T1, Structure and function

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

The bonds that tie: catalyzed disulfide bond formation

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Molecular chaperone functions of heat-shock proteins

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Role of the Cys 2-Cys 10 disulfide bond for the structure, stability, and folding kinetics of ribonuclease T1.

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Kinetics of unfolding and refolding of proteins. I. Mathematical analysis.

26 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Folding of dihydrofolate reductase from Escherichia coli.

26 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeast

26 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate

26 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

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

26 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Nature and consequences of GroEL-protein interactions.

2 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

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

2 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=38444

Refolding of barnase in the presence of GroE

3 December 2018

1 reference

12 December 2020

Intact disulfide bonds decelerate the folding of ribonuclease T1

1 reference

12 December 2020

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

1 reference

12 December 2020

Protein disulphide isomerase: building bridges in protein folding

1 reference

12 December 2020

Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding

1 reference

12 December 2020

Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1

1 reference

12 December 2020

Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1

1 reference

12 December 2020

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

1 reference

12 December 2020

Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds

1 reference

12 December 2020

Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation

1 reference

12 December 2020

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

1 reference

12 December 2020

Labeling of proteins by reductive methylation using sodium cyanoborohydride

1 reference

12 December 2020

Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation

1 reference

12 December 2020

Specific protein-nucleic acid recognition in ribonuclease T1–2′-guanylic acid complex: an X-ray study

1 reference

12 December 2020

Reassociation of dimeric cytoplasmic malate dehydrogenase is determined by slow and very slow folding reactions

1 reference

12 December 2020

Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli

1 reference

12 December 2020

A purification method for labile variants of ribonuclease T1

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.93.18.9425

1 reference

19 August 2017

0 references

1 reference

19 August 2017

1 reference

PMCID

38444