Aggresomes, inclusion bodies and protein aggregation. Export

@article{citeulike:3251713, abstract = {Intracellular and extracellular accumulation of aggregated protein are linked to many diseases, including ageing-related neurodegeneration and systemic amyloidosis. Cells avoid accumulating potentially toxic aggregates by mechanisms including the suppression of aggregate formation by molecular chaperones and the degradation of misfolded proteins by proteasomes. Once formed, aggregates tend to be refractory to proteolysis and to accumulate in inclusion bodies. This accumulation has been assumed to be a diffusion-limited process, but recent studies suggest that, in animal cells, aggregated proteins are specifically delivered to inclusion bodies by dynein-dependent retrograde transport on microtubules. This microtubule-dependent inclusion body is called an aggresome.}, address = {Dept of Biological Sciences, Stanford University, Stanford, CA 94305-5020, USA. kopito@stanford.edu}, author = {Kopito, R. R.}, citeulike-article-id = {3251713}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11121744}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11121744}, issn = {0962-8924}, journal = {Trends in cell biology}, keywords = {aggregation, inclusions, proteinfolding, review}, month = {December}, number = {12}, pages = {524--530}, posted-at = {2008-09-13 13:43:01}, priority = {2}, title = {Aggresomes, inclusion bodies and protein aggregation.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11121744}, volume = {10}, year = {2000} }

TY - JOUR ID - citeulike:3251713 L3 - citeulike-article-id:3251713 N2 - Intracellular and extracellular accumulation of aggregated protein are linked to many diseases, including ageing-related neurodegeneration and systemic amyloidosis. Cells avoid accumulating potentially toxic aggregates by mechanisms including the suppression of aggregate formation by molecular chaperones and the degradation of misfolded proteins by proteasomes. Once formed, aggregates tend to be refractory to proteolysis and to accumulate in inclusion bodies. This accumulation has been assumed to be a diffusion-limited process, but recent studies suggest that, in animal cells, aggregated proteins are specifically delivered to inclusion bodies by dynein-dependent retrograde transport on microtubules. This microtubule-dependent inclusion body is called an aggresome. IS - 12 JF - Trends in cell biology SN - 0962-8924 AD - Dept of Biological Sciences, Stanford University, Stanford, CA 94305-5020, USA. kopito@stanford.edu EP - 530 TI - Aggresomes, inclusion bodies and protein aggregation. VL - 10 SP - 524 KW - aggregation KW - inclusions KW - proteinfolding KW - review AU - Kopito, RR PY - 2000/12// UR - http://view.ncbi.nlm.nih.gov/pubmed/11121744 ER -