Cysteine cathepsins are essential in lysosomal degradation of α-synuclein

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 30, 2015, Pages 9322-9327

  McGlinchey, Ryan P ^a   Lee, Jennifer C ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

Amyloid; Lysosomes; Mass spectrometry; Parkinson's disease; Protein lipid interactions

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; ASPARTIC PROTEINASE; CATHEPSIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN L; CYSTEINE; LEUPEPTIN; LYSOSOME ENZYME; PEPSTATIN; PHOSPHOLIPID; PROTEINASE; PEPTIDE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BRAIN TISSUE; CLINICAL EVALUATION; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; LIQUID CHROMATOGRAPHY; LIVER PARENCHYMA; LYSOSOME; MASS SPECTROMETRY; MOUSE; NONHUMAN; PEPTIDE MAPPING; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; SEQUENCE ANALYSIS; ANIMAL; BRAIN; CHEMISTRY; CIRCULAR DICHROISM; DEGENERATIVE DISEASE; LIVER; METABOLISM; PARKINSON DISEASE;

ALPHA-SYNUCLEIN; ANIMALS; BRAIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN L; CHROMATOGRAPHY, LIQUID; CIRCULAR DICHROISM; CYSTEINE; HUMANS; LIVER; LYSOSOMES; MASS SPECTROMETRY; MICE; NEURODEGENERATIVE DISEASES; PARKINSON DISEASE; PEPTIDE MAPPING; PEPTIDES; PHOSPHOLIPIDS;

EID: 84938118051     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1500937112     Document Type: Article

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