Protein Folding in the Cell /
This volume of Advances in Protein Chemistry provides a broad, yet deep look at the cellular components that assist protein folding in the cell. This area of research is relatively new--10 years ago these components were barely recognized, so this book is a particularly timely compilation of current...
Clasificación: | Libro Electrónico |
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Otros Autores: | |
Formato: | Electrónico eBook |
Idioma: | Inglés |
Publicado: |
San Diego :
Academic Press,
2002.
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Colección: | Advances in protein chemistry ;
v. 59. |
Temas: | |
Acceso en línea: | Texto completo Texto completo Texto completo |
Tabla de Contenidos:
- Hsp70 chaperone machines / Matthias P. Mayer [and others]
- Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding / Helen R. Saibil, Arthur L. Horwich, and Wayne A. Fenton
- Type II chaperonins, prefoldin, and the tubulin-specific chaperones / Nicholas J. Cowan and Sally A. Lewis
- Structure and function of the small heat shock protein/[alpha]-crystallin family of molecular chaperones / Rob van Montfort, Christine Slingsby, and Elizabeth Vierling
- Structure, function, and mechanism of the Hsp90 molecular chaperone / Laurence H. Pearl and Chrisostomos Prodromou
- The proteasome: a supramolecular assembly designed for controlled proteolysis / Peter Zwickl [and others]
- Hsp70 proteins in protein translocation / Michael T. Ryan and Nikolaus Pfanner
- Protyl isomerases / Franz X. Schmid
- Catalysis of disulfide bond formation and isomerization in Escherichia coli / Martin W. Bader and James C.A. Bardwell
- N-glycan processing and glycoprotein folding / E. Sergio Trombetta and Armando J. Parodi
- Functional genomic approaches to understanding molecular chaperones and stress responses / Kevin J. Travers, Christopher K. Patil, and Jonathan S. Weissman
- The yeast prion (PSI): molecular insights and functional consequences / Tricia R. Serio and Susan L. Lindquist
- Clp ATPases and their role in protein unfolding and degradation / Joel R. Hoskins [and others].