AMSH is required to degrade ubiquitinated proteins in the central nervous system

Biochemical and Biophysical Research Communications

Volumn 408, Issue 4, 2011, Pages 582-588

  Suzuki, Shunya ^a   Tamai, Keiichi ^a,b   Watanabe, Masahiko ^c   Kyuuma, Masanao ^a   Ono, Masao ^a   Sugamura, Kazuo ^a,b   Tanaka, Nobuyuki ^a,b  

^a TOHOKU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b MIYAGI CANCER CENTER RESEARCH INSTITUTE   (Japan)

^c HOKKAIDO UNIVERSITY   (Japan)

Author keywords

AMSH; Hippocampus; Neurodegeneration; Ubiquitin

Indexed keywords

ASSOCIATED MOLECULE WITH SH3 DOMAIN OF STAM; CELL ENZYME; GLUTAMATE RECEPTOR; PROTEIN P18; PROTEIN P62; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BRAIN DAMAGE; CENTRAL NERVOUS SYSTEM; CONTROLLED STUDY; MOUSE; NONHUMAN; PERINATAL PERIOD; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; UBIQUITINATION;

ANIMALS; BRAIN; DISEASE MODELS, ANIMAL; ENDOPEPTIDASES; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT; MICE; MICE, MUTANT STRAINS; NEURODEGENERATIVE DISEASES; UBIQUITIN; UBIQUITIN THIOLESTERASE; UBIQUITINATED PROTEINS; UBIQUITINATION;

ANIMALIA; MUS;

EID: 79956200569     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.04.065     Document Type: Article

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