N-Terminal Fragments of Huntingtin Longer than Residue 170 form Visible Aggregates Independently to Polyglutamine Expansion | Zendy

Moore Z. Chen | Zendy; SueAnn Mok | Zendy; Angelique R. Ormsby | Zendy; Paul J. Muchowski | Zendy; Danny M. Hatters | Zendy

Open Access

N-Terminal Fragments of Huntingtin Longer than Residue 170 form Visible Aggregates Independently to Polyglutamine Expansion

Author(s) -

Moore Z. Chen,

SueAnn Mok,

Angelique R. Ormsby,

Paul J. Muchowski,

Danny M. Hatters

Publication year - 2017

Publication title -

journal of huntington s disease

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.081

H-Index - 24

eISSN - 1879-6400

pISSN - 1879-6397

DOI - 10.3233/jhd-160207

Subject(s) - huntingtin , amino acid , intracellular , exon , huntingtin protein , trinucleotide repeat expansion , chemistry , terminal (telecommunication) , biology , biophysics , biochemistry , gene , mutant , allele , telecommunications , computer science

A hallmark of Huntington's disease is the progressive aggregation of full length and N-terminal fragments of polyglutamine (polyQ)-expanded Huntingtin (Htt) into intracellular inclusions. The production of N-terminal fragments appears important for enabling pathology and aggregation; and hence the direct expression of a variety of N-terminal fragments are commonly used to model HD in animal and cellular models.

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