Opposing activities protect against age-onset proteotoxicity. Export

@article{citeulike:1361304, abstract = {Aberrant protein aggregation is a common feature of late-onset neurodegenerative diseases, including Alzheimer's disease, which is associated with the misassembly of the Abeta(1-42) peptide. Aggregation-mediated Abeta(1-42) toxicity was reduced in Caenorhabditis elegans when aging was slowed by decreased insulin/insulin growth factor-1-like signaling (IIS). The downstream transcription factors, heat shock factor 1, and DAF-16 regulate opposing disaggregation and aggregation activities to promote cellular survival in response to constitutive toxic protein aggregation. Because the IIS pathway is central to the regulation of longevity and youthfulness in worms, flies, and mammals, these results suggest a mechanistic link between the aging process and aggregation-mediated proteotoxicity.}, address = {Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.}, author = {Cohen, Ehud and Bieschke, Jan and Perciavalle, Rhonda M. and Kelly, Jeffery W. and Dillin, Andrew}, citeulike-article-id = {1361304}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1124646}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/313/5793/1604}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/16902091}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=16902091}, citeulike-linkout-4 = {http://www.wormbase.org/db/misc/paper?name=WBPaper00028353}, day = {15}, doi = {10.1126/science.1124646}, issn = {1095-9203}, journal = {Science (New York, N.Y.)}, keywords = {abeta1-42, aging, alzheimers, daf-16, daf-2, hsf-1, promoter}, month = {September}, number = {5793}, pages = {1604--1610}, posted-at = {2007-06-04 03:30:00}, priority = {5}, title = {Opposing activities protect against age-onset proteotoxicity.}, url = {http://dx.doi.org/10.1126/science.1124646}, volume = {313}, year = {2006} }

TY - JOUR ID - citeulike:1361304 L3 - citeulike-article-id:1361304 N2 - Aberrant protein aggregation is a common feature of late-onset neurodegenerative diseases, including Alzheimer's disease, which is associated with the misassembly of the Abeta(1-42) peptide. Aggregation-mediated Abeta(1-42) toxicity was reduced in Caenorhabditis elegans when aging was slowed by decreased insulin/insulin growth factor-1-like signaling (IIS). The downstream transcription factors, heat shock factor 1, and DAF-16 regulate opposing disaggregation and aggregation activities to promote cellular survival in response to constitutive toxic protein aggregation. Because the IIS pathway is central to the regulation of longevity and youthfulness in worms, flies, and mammals, these results suggest a mechanistic link between the aging process and aggregation-mediated proteotoxicity. IS - 5793 JF - Science (New York, N.Y.) SN - 1095-9203 AD - Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. EP - 1610 TI - Opposing activities protect against age-onset proteotoxicity. VL - 313 SP - 1604 KW - abeta1-42 KW - aging KW - alzheimers KW - daf-16 KW - daf-2 KW - hsf-1 KW - promoter AU - Cohen, Ehud AU - Bieschke, Jan AU - Perciavalle, Rhonda AU - Kelly, Jeffery AU - Dillin, Andrew PY - 2006/09/15/ UR - http://dx.doi.org/10.1126/science.1124646 ER -