Publications by authors named "Charles W Bugg"

Pelvic inflammatory disease is a common disease that is associated with significant complications including infertility, chronic pelvic pain, ruptured tubo-ovarian abscess, and ectopic pregnancy. The diagnosis may be delayed when the presentation has nonspecific signs and symptoms. Even when it is properly identified, pelvic inflammatory disease is often treated suboptimally.

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Pelvic inflammatory disease is a common disease that is associated with significant complications including infertility, chronic pelvic pain, ruptured tubo-ovarian abscess, and ectopic pregnancy. The diagnosis may be delayed when the presentation has nonspecific signs and symptoms. Even when it is properly identified, pelvic inflammatory disease is often treated suboptimally.

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Article Synopsis
  • Misfolding and aggregation of the huntingtin protein is crucial in Huntington disease, but the specific structure of these aggregates and the misfolding process are not well understood.
  • The study used advanced techniques (spin labeling and EPR spectroscopy) to analyze the structure of the huntingtin exon 1 (HDx1) protein, particularly focusing on the behavior of its polyglutamine (polyQ) region during aggregation.
  • Findings reveal that while the N terminus of HDx1 becomes structured and interacts closely with other molecules, the C-terminal domain remains dynamic and less organized, suggesting different roles in the formation of protein fibrils associated with Huntington disease.
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Background: Proteolytic processing of mutant huntingtin (mHtt), the protein that causes Huntington's disease (HD), is critical for mHtt toxicity and disease progression. mHtt contains several caspase and calpain cleavage sites that generate N-terminal fragments that are more toxic than full-length mHtt. Further processing is then required for the degradation of these fragments, which in turn, reduces toxicity.

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Although expanded polyglutamine (polyQ) repeats are inherently toxic, causing at least nine neurodegenerative diseases, the protein context determines which neurons are affected. The polyQ expansion that causes Huntington's disease (HD) is in the first exon (HDx-1) of huntingtin (Htt). However, other parts of the protein, including the 17 N-terminal amino acids and two proline (polyP) repeat domains, regulate the toxicity of mutant Htt.

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