Lysine-rich histone (H1) is a lysyl substrate of tissue transglutaminase: Possible involvement of transglutaminase in the formation of nuclear aggregates in (CAG)(n)/Q(n) expansion diseases

Developmental Neuroscience

Volumn 22, Issue 5-6, 2000, Pages 404-417

  Cooper, Arthur J L ^a   Wang, Jianping ^a   Pasternack, Ralf ^b   Fuchsbauer, Hans Lothar ^b   Sheu, Rex K F ^a   Blass, John P ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

^b Fachbereich Chemische Technologie   (Germany)

Author keywords

CAG repeats; Glutaminyl donors; Histone H1; Lysyl donors; Neurodegenerative diseases; Polyglutamine domains; Tissue transglutaminase

Indexed keywords

1 N (CARBOBENZOXYGLUTAMINYLGLYCYL) 5 N (5'N'N' DIMETHYLAMINONAPHTHALENESULFONYL) DIAMIDOPENTANE; BETA ENDORPHIN; CALCIUM ION; CASEIN; DIMETHYLCASEIN; DODECYL SULFATE SODIUM; HISTONE H1; LYSINE; NAPHTHALENE DERIVATIVE; NEUROPEPTIDE; PENTANE; POLYGLUTAMINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL NUCLEUS; CHROMATIN; CONTROLLED STUDY; CYTOSOL; DEGENERATIVE DISEASE; ENZYME ACTIVITY; FLUORESCENCE; GEL ELECTROPHORESIS; GENE MUTATION; GENOME; GUINEA PIG; HUNTINGTON CHOREA; NERVE CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STREPTOVERTICILLIUM;

EID: 0033671963     PISSN: 03785866     EISSN: None     Source Type: Journal    
DOI: 10.1159/000017470     Document Type: Article

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