Title |
Ubiquitination is involved in secondary growth, not initial formation of polyglutamine protein aggregates in C. elegans
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Published in |
BMC Molecular and Cell Biology, April 2012
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DOI | 10.1186/1471-2121-13-10 |
Pubmed ID | |
Authors |
Gregory A Skibinski, Lynn Boyd |
Abstract |
Protein misfolding and subsequent aggregation are hallmarks of several human diseases. The cell has a variety of mechanisms for coping with misfolded protein stress, including ubiquitin-mediated protein degradation. In fact, the presence of ubiquitin at protein aggregates is a common feature of protein misfolding diseases. Ubiquitin conjugating enzymes (UBCs) are part of the cascade of enzymes responsible for the regulated attachment of ubiquitin to protein substrates. The specific UBC used during ubiquitination can determine the type of polyubiquitin chain linkage, which in turn plays an important role in determining the fate of the ubiquitinated protein. Thus, UBCs may serve an important role in the cellular response to misfolded proteins and the fate of protein aggregates. |
X Demographics
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United States | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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Brazil | 1 | 3% |
Unknown | 33 | 97% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 10 | 29% |
Student > Ph. D. Student | 9 | 26% |
Student > Master | 4 | 12% |
Student > Doctoral Student | 3 | 9% |
Student > Bachelor | 3 | 9% |
Other | 3 | 9% |
Unknown | 2 | 6% |
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Medicine and Dentistry | 2 | 6% |
Other | 5 | 15% |
Unknown | 2 | 6% |