(Q50515011)

English

SDS-induced conformational changes and inactivation of the bacterial chaperonin GroEL.

scientific article published in August 1999

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

SDS-induced conformational changes and inactivation of the bacterial chaperonin GroEL. (English)

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

author name string

Li S

1

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

Wang LT

2

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

Zhou HM

3

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

publication date

1 August 1999

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

The Protein Journal

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

18

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

6

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

653-657

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

Positive cooperativity in the functioning of molecular chaperone GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Residual Structure in Urea-Denatured Chaperonin GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Unfolding, conformational change of active sites and inactivation of creatine kinase in SDS solutions

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Molecular chaperones in protein folding: the art of avoiding sticky situations

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

On the role of groES in the chaperonin-assisted folding reaction. Three case studies

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60)

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Inactivation and unfolding of aminoacylase during denaturation in sodium dodecyl sulfate solutions

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The interaction of sodium dodecyl sulfate and urea with cat-fish collagen solutions in acetate buffer: hydrodynamic and thermodynamic studies.

1 reference

https://pubmed.ncbi.nlm.nih.gov/10609640

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1023/A:1020650105969

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

Dimensions Publication ID

0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/10609640

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