Prolyl-isomerase Pin1 accumulates in Lewy bodies of Parkinson Disease and facilitates formation of α-synuclein inclusions

Journal of Biological Chemistry

Volumn 281, Issue 7, 2006, Pages 4117-4125

  Ryo, Akihide ^a   Togo, Takashi ^a   Nakai, Toshiki ^a   Hirai, Akiko ^a   Nishi, Mayuko ^a   Yamaguchi, Akira ^a   Suzuki, Kyoko ^a   Hirayasu, Yoshio ^a   Kobayashi, Hideki ^b   Perrem, Kilian ^c   Liou, Yih Cherng ^d   Aoki, Ichiro ^a  

^a YOKOHAMA CITY UNIVERSITY   (Japan)

^b KYUSHU UNIVERSITY   (Japan)

^c ROYAL COLLEGE OF SURGEONS IN IRELAND   (Ireland)

^d NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN; DISEASES; ENZYME KINETICS; ENZYMES; MATHEMATICAL MODELS; MOLECULAR BIOLOGY; TISSUE;

LEWY BODIES (LB); NEURODEGENERATIVE DISORDER; PARKINSON DISEASE; SYNUCLEIN INCLUSIONS;

NEUROLOGY;

ALPHA SYNUCLEIN; ISOMERASE; PIN 1 ENZYME; PROLINE; SERINE; UNCLASSIFIED DRUG; CARRIER PROTEIN; CASEIN KINASE II; NERVE PROTEIN; NIMA INTERACTING PEPTIDYLPROLYL ISOMERASE; NIMA-INTERACTING PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE; SNCAIP PROTEIN, HUMAN;

ANIMAL CELL; ARTICLE; CELL INCLUSION; CONTROLLED STUDY; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; ISOMERIZATION; LEWY BODY; MOLECULAR MODEL; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CELL STRAIN COS1; CERCOPITHECUS; HALF LIFE TIME; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; PHYSIOLOGY; SOLUBILITY;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CARRIER PROTEINS; CASEIN KINASE II; CERCOPITHECUS AETHIOPS; COS CELLS; HALF-LIFE; HUMANS; LEWY BODIES; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PARKINSON DISEASE; PEPTIDYLPROLYL ISOMERASE; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; SOLUBILITY;

EID: 33645238274     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M507026200     Document Type: Article

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