Histone H3 is aberrantly phosphorylated in glutamine-repeat diseases

Biochemical and Biophysical Research Communications

Volumn 302, Issue 1, 2003, Pages 144-149

  Yazawa, Ikuru ^a,b,d   Hazeki, Noriko ^c   Nakase, Hirofumi ^a   Kanazawa, Ichiro ^c   Tanaka, Masumi ^b  

^a TORANOMON HOSPITAL   (Japan)

^b Okinaka Memorial Institute for Medical Research   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Dentatorubral pallidoluysian atrophy; Glutamine repeat disease; Histone H3; Huntington's disease; Machado Joseph disease; Nuclear inclusion; Phosphorylation; Phosphoserine; Polyglutamine disease; Spinocerebellar ataxia 1

Indexed keywords

ANTIBODY; GLUTAMINE; HISTONE H3; NUCLEAR PROTEIN; PHOSPHOSERINE;

ADULT; AGED; ARTICLE; BRAIN TISSUE; CELL ISOLATION; CELL NUCLEUS INCLUSION BODY; CONTROLLED STUDY; CYTOPATHOLOGY; DENTATORUBROPALLIDOLUYSIAN ATROPHY; ENZYME BLOOD LEVEL; EXON; FLUORESCENCE ACTIVATED CELL SORTING; GENE EXPRESSION; HUMAN; HUMAN CELL; HUMAN TISSUE; HUNTINGTON CHOREA; IMMUNOHISTOCHEMISTRY; MACHADO JOSEPH DISEASE; NERVE CELL CULTURE; NUCLEOTIDE REPEAT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING; SPINOCEREBELLAR DEGENERATION;

ATAXIA;

EID: 0037470363     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00115-3     Document Type: Article

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