Refolding of proteins by hexadecamers and monomers of the α and β subunits of group II chaperonin from the hyperthermophilic archaeum Thermococcus strain KS-1-Reference-Cited by-同舟云学术

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Refolding of proteins by hexadecamers and monomers of the α and β subunits of group II chaperonin from the hyperthermophilic archaeum Thermococcus strain KS-1

Published:2004-04 Issue:1 Volume:18 Page:73-79
ISSN:1369-703X
Container-title:Biochemical Engineering Journal
language:en
Short-container-title:Biochemical Engineering Journal

Author:

Kohda Jiro,Yamada Tadanori,Yoshida Takao,Maruyama Tadashi,Yohda Masafumi,Fukuda Hideki,Kondo Akihiko

Publisher

Elsevier BV

Subject

Biomedical Engineering,Environmental Engineering,Bioengineering,Biotechnology

Reference32 articles.

1. Protein folding in the cell;Gething;Nature,1992

2. Molecular chaperones in cellular protein folding;Hartl;Nature,1996

3. Chaperone-mediated protein folding;Fink;Physiol. Rev.,1999

4. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein complex polypeptide-1;Trent;Nature,1991

5. Conformational cycle of the archeosome, a TCP1-like chaperonin from Sulfolobus shibatae;Quaite-Randall;J. Biol. Chem.,1995

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1. Determination of eugenol diffusion through LLDPE using FTIR-ATR flow cell and HPLC techniques;Polymer;2009-03

2. Determination of the Diffusivity of a Hydrophilic Migratory Additive in Ipp Films;Journal of Plastic Film & Sheeting;2007-07

3. Stabilization of free and immobilized enzymes using hyperthermophilic chaperonin;Journal of Bioscience and Bioengineering;2006-02

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