Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction

Biochemical and Biophysical Research Communications

Volumn 424, Issue 3, 2012, Pages 597-603

  Choi, Hee soon ^a   Liew, Hyunjeong ^a   Jang, Ahram ^a   Kim, Yun Mi ^a   Lashuel, Hilal ^b   Suh, Yoo Hun ^a  

^a Seoul National University   (South Korea)

^b EPFL   (Switzerland)

Author keywords

Synuclein; HSC70; Lysosome; Phosphorylation; Proteasome

Indexed keywords

ALPHA SYNUCLEIN; FOCAL ADHESION KINASE; FOCAL ADHESION KINASE PP125; HEAT SHOCK PROTEIN 70; PROTEASOME; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR; TYROSINE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELL DEATH; CONTROLLED STUDY; HUMAN; HUMAN CELL; LYSOSOME; MALE; MOUSE; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION;

ALPHA-SYNUCLEIN; ANIMALS; CELL LINE; DISEASE MODELS, ANIMAL; DOPAMINERGIC NEURONS; FOCAL ADHESION PROTEIN-TYROSINE KINASES; HSC70 HEAT-SHOCK PROTEINS; MALE; MICE; MICE, INBRED C57BL; NEUROPROTECTIVE AGENTS; PARKINSON DISEASE; PHOSPHORYLATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1; TYROSINE;

ANIMALIA;

EID: 84864741214     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.06.159     Document Type: Article

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