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Literature DB >> 10753820

Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.

Abstract

Newly solved chaperone structures include the thermosome, a group II chaperonin, and a small heat-shock protein. Novel ideas on chaperone mechanism are presented in the forced unfolding hypothesis of GroEL action. Structures of chaperone-pilin complexes reveal the mechanism of chaperone interaction in bacterial pilus assembly and there have been major advances in understanding the structure and function of Hsp100 unfoldases.

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Year: 2000 PMID： 10753820 DOI： 10.1016/s0959-440x(00)00074-9

Source DB: PubMed Journal: Curr Opin Struct Biol ISSN： 0959-440X Impact factor: 6.809

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Cited

35 in total

1. Mutational studies on HslU and its docking mode with HslV.

Authors: H K Song; C Hartmann; R Ramachandran; M Bochtler; R Behrendt; L Moroder; R Huber
Journal: Proc Natl Acad Sci U S A Date: 2000-12-19 Impact factor: 11.205

2. Arabidopsis thaliana type I and II chaperonins.

Authors: J E Hill; S M Hemmingsen
Journal: Cell Stress Chaperones Date: 2001-07 Impact factor: 3.667

3. A genomics approach to the chaperone network of Arabidopsis thaliana.

Authors: L Nover; J A Miernyk
Journal: Cell Stress Chaperones Date: 2001-07 Impact factor: 3.667

4. A high-speed atomic force microscope for studying biological macromolecules.

Authors: T Ando; N Kodera; E Takai; D Maruyama; K Saito; A Toda
Journal: Proc Natl Acad Sci U S A Date: 2001-10-09 Impact factor: 11.205

5. The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding.

Authors: Andre Silvanovich; Min-Gang Li; Madeline Serr; Sarah Mische; Thomas S Hays
Journal: Mol Biol Cell Date: 2003-04 Impact factor: 4.138

Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.

1. Mutational studies on HslU and its docking mode with HslV.

2. Arabidopsis thaliana type I and II chaperonins.

3. A genomics approach to the chaperone network of Arabidopsis thaliana.

4. A high-speed atomic force microscope for studying biological macromolecules.

5. The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding.

6. Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.

Review 7. Chaperonin 60 unfolds its secrets of cellular communication.

8. The unfolding action of GroEL on a protein substrate.

9. J domain co-chaperone specificity defines the role of BiP during protein translocation.

10. Structure of an Hsp90-Cdc37-Cdk4 complex.