Toxic and non-toxic aggregates from the SBMA and normal forms of androgen receptor have distinct oligomeric structures

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1822, Issue 6, 2012, Pages 1070-1078

  Jochum, Tobias ^a   Ritz, Manuela E ^a   Schuster, Christoph ^a   Funderburk, Sarah F ^a,c   Jehle, Katja ^a   Schmitz, Katja ^b   Brinkmann, Falko ^a   Hirtz, Michael ^a   Moss, David ^a   Cato, Andrew C B ^a  

^a KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c IMsci   (United States)

Author keywords

Aggregation; Androgen receptor; Melatonin; Neurodegeneration; Polyglutamine; SBMA

Indexed keywords

ALANINE; ANDROGEN RECEPTOR; GLUTAMINE; MELATONIN; OLIGOMER; SERINE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; ATOMIC FORCE MICROSCOPY; CYTOTOXICITY; DROSOPHILA; KENNEDY DISEASE; MOTONEURON; MUTATIONAL ANALYSIS; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; STRUCTURE ANALYSIS; TOXICITY TESTING;

ANIMALS; BULBO-SPINAL ATROPHY, X-LINKED; CELLS, CULTURED; DISEASE MODELS, ANIMAL; DROSOPHILA; HUMANS; MELATONIN; MICROSCOPY, ATOMIC FORCE; NEURONS; PEPTIDES; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEOSTASIS DEFICIENCIES; RECEPTORS, ANDROGEN;

HEXAPODA;

EID: 84859485246     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2012.02.006     Document Type: Article

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