The small heat shock proteins and their clients Export

@article{Nakamoto2007, abstract = {Abstract.\ \ Small heat shock proteins are ubiquitous proteins found throughout all kingdoms. One of the most notable features is their large oligomeric structures with conserved structural organization. It is well documented that small heat shock proteins can capture unfolding proteins to form stable complexes and prevent their irreversible aggregation. In addition, small heat shock proteins coaggregate with aggregation-prone proteins for subsequent, efficient disaggregation of the protein aggregates. The release of substrate proteins from the transient reservoirs, i.e. complexes and aggregates with small heat shock proteins, and their refolding require cooperation with ATP-dependent chaperone systems. The amphitropic small heat shock proteins were shown to associate with membranes, although they do not contain transmembrane domains or signal sequences. Recent studies indicate that small heat shock proteins play an important role in membrane quality control and thereby potentially contribute to the maintenance of membrane integrity especially under stress conditions.}, author = {Nakamoto, H. and V\'{\i}gh, L.}, citeulike-article-id = {1151250}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/s00018-006-6321-2}, citeulike-linkout-1 = {http://www.ingentaconnect.com/content/klu/18/2007/00000064/00000024/00006321}, citeulike-linkout-2 = {http://www.springerlink.com/content/n5u87774067r4r01}, day = {20}, doi = {10.1007/s00018-006-6321-2}, issn = {1420-682X}, journal = {Cellular and Molecular Life Sciences}, keywords = {heat, hsf, hsp70, hsp90, review, shock}, month = {February}, number = {3}, pages = {294--306}, posted-at = {2009-10-06 10:39:13}, priority = {2}, publisher = {Springer}, title = {The small heat shock proteins and their clients}, url = {http://dx.doi.org/10.1007/s00018-006-6321-2}, volume = {64}, year = {2007} }

TY - JOUR ID - Nakamoto2007 L3 - citeulike-article-id:1151250 N2 - Abstract.  Small heat shock proteins are ubiquitous proteins found throughout all kingdoms. One of the most notable features is their large oligomeric structures with conserved structural organization. It is well documented that small heat shock proteins can capture unfolding proteins to form stable complexes and prevent their irreversible aggregation. In addition, small heat shock proteins coaggregate with aggregation-prone proteins for subsequent, efficient disaggregation of the protein aggregates. The release of substrate proteins from the transient reservoirs, i.e. complexes and aggregates with small heat shock proteins, and their refolding require cooperation with ATP-dependent chaperone systems. The amphitropic small heat shock proteins were shown to associate with membranes, although they do not contain transmembrane domains or signal sequences. Recent studies indicate that small heat shock proteins play an important role in membrane quality control and thereby potentially contribute to the maintenance of membrane integrity especially under stress conditions. IS - 3 JF - Cellular and Molecular Life Sciences SN - 1420-682X EP - 306 TI - The small heat shock proteins and their clients PB - Springer VL - 64 SP - 294 KW - heat KW - hsf KW - hsp70 KW - hsp90 KW - review KW - shock AU - Nakamoto, H AU - Vígh, L PY - 2007/02/20/ UR - http://dx.doi.org/10.1007/s00018-006-6321-2 ER -