๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Small heat shock proteins: molecular structure and chaperone function

โœ Scribed by Y. Sun; T. H. MacRae

Publisher
Springer
Year
2005
Tongue
English
Weight
426 KB
Volume
62
Category
Article
ISSN
1420-682X

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

Heat causes oligomeric disassembly and i
Heat causes oligomeric disassembly and increases the chaperone activity of small heat shock proteins from sugarcane
โœ Ana O. Tiroli-Cepeda; Carlos H.I. Ramos ๐Ÿ“‚ Article ๐Ÿ“… 2010 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 875 KB

Small heat shock proteins (sHsp) constitute an important chaperone family linked to conformational diseases. In plants, sHsps prevent protein aggregation by acting as thermosensors and to enhance cell stress tolerance. SsHsp17.2 and SsHsp17.9 are the most highly expressed class I sHsps in sugarcane.

N-terminal control of small heat shock p
N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function
โœ Cheryl Eifert; Michael R. Burgio; Pauline M. Bennett; John C. Salerno; Jane F. K ๐Ÿ“‚ Article ๐Ÿ“… 2005 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 842 KB

The small heat shock protein superfamily is composed of proteins from throughout the phylogenetic spectrum that are induced upon environmental stress. Their structural stability under stress derives in large part from the central region of the proteins, which forms two beta sheets held together by h