Sumoylation and human disease pathogenesis.
Sumoylation and human disease pathogenesis.
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DOI:
10.1016/j.tibs.2009.01.004
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发表时间:
2009-04
影响因子:
13.8
通讯作者:
Park-Sarge OK
中科院分区:
文献类型:
--
作者:
Sarge KD;Park-Sarge OK
Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are a number of proteins implicated in human diseases, including cancer, Huntington’s, Alzheimer’s, and Parkinson’s Diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. Recent reports reveal two new examples of human disease-associated proteins that are SUMO modified: amyloid precursor protein and lamin A. These findings point to a function for sumoylation in modulating Aβ peptide levels, suggesting a potential role in Alzheimer’s Disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.
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