Ontology highlight
ABSTRACT:
SUBMITTER: Chaibva M
PROVIDER: S-EPMC4968481 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Chaibva Maxmore M Jawahery Sudi S Pilkington Albert W AW Arndt James R JR Sarver Olivia O Valentine Stephen S Matysiak Silvina S Legleiter Justin J
Biophysical journal 20160701 2
Huntington's disease (HD) is a genetic neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain near the N-terminus of the huntingtin (htt) protein. Expanded polyQ leads to htt aggregation. The first 17 amino acids (Nt(17)) in htt comprise a lipid-binding domain that undergoes a number of posttranslational modifications that can modulate htt toxicity and subcellular localization. As there are three lysines within Nt(17), we evaluated the impact of lysine acetylation on htt a ...[more]