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.
|
Colección: | Advances in protein chemistry ;
v. 59. |
Temas: | |
Acceso en línea: | Texto completo Texto completo Texto completo |
MARC
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245 | 0 | 0 | |a Protein Folding in the Cell / |c edited by Arthur Horwich. |
264 | 1 | |a San Diego : |b Academic Press, |c 2002. | |
300 | |a 1 online resource (xiii, 491 pages, 4 unnumbered leaves of plates) : |b illustrations (some color) | ||
336 | |a text |b txt |2 rdacontent | ||
337 | |a computer |b c |2 rdamedia | ||
338 | |a online resource |b cr |2 rdacarrier | ||
490 | 1 | |a Advances in protein chemistry, |x 0065-3233 ; |v v. 59 | |
546 | |a Text in English. | ||
550 | |a Made available through: Science Direct. | ||
504 | |a Includes bibliographical references and index. | ||
505 | 0 | |a 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]. | |
520 | |a 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 information. Topics covered include a review of the structure and mechanism of the major chaperone components, prion formation in yeast, and the use of microarrays in studying stress response. Outlines preceding each chapter allow the reader to quickly access the subjects of greatest interest. The. | ||
650 | 0 | |a Protein folding. | |
650 | 2 | |a Protein Folding |0 (DNLM)D017510 | |
650 | 6 | |a Prot�eines |x Repliement. |0 (CaQQLa)201-0217303 | |
650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
650 | 7 | |a Protein folding |2 fast |0 (OCoLC)fst01079687 | |
650 | 1 | 7 | |a Eiwitvouwing. |2 gtt |
700 | 1 | |a Horwich, Arthur, |e editor. | |
776 | 0 | 8 | |i Print version: |t Protein folding in the cell (print) |w (DLC) 49237060 |
830 | 0 | |a Advances in protein chemistry ; |v v. 59. | |
856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780120342594 |z Texto completo |
856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00653233/59 |z Texto completo |
856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00653233 |z Texto completo |