The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation

Journal of Biological Chemistry

Volumn 283, Issue 24, 2008, Pages 16906-16914

  Greggio, Elisa ^a,d   Zambrano, Ibardo ^a   Kaganovich, Alice ^a   Beilina, Alexandra ^a   Taymans, Jean Marc ^c   Daniëls, Veronique ^c   Lewis, Patrick ^a,e   Jain, Shushant ^a,f   Ding, Jinhui ^b   Syed, Ali ^a   Thomas, Kelly J ^a   Baekelandt, Veerle ^c   Cookson, Mark R ^a  

^a Neuronal Gene Expression Unit   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c UNIVERSITY OF LEUVEN   (Belgium)

^d NATIONAL INSTITUTE ON AGING   (United States)

^e UNIVERSITY COLLEGE LONDON   (United Kingdom)

^f VU UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION;

ACTIVATION LOOPS; C TERMINUSES; DO-MAINS; KINASE ACTIVATIONS; KINASE ACTIVITIES; KINASE INHIBITORS; MULTIDOMAIN PROTEINS; MULTIPLE DOMAINS; N TERMINUSES; NEURONAL TOXICITIES; PARKINSON DISEASES;

AMINO ACIDS;

LEUCINE RICH REPEAT KINASE 2; LRRK2 PROTEIN, MOUSE; PROTEIN SERINE THREONINE KINASE;

ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME REGULATION; ENZYME STABILITY; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; ANIMAL; BIOLOGICAL MODEL; BRAIN; CELL STRAIN COS1; CERCOPITHECUS; CHEMISTRY; DIMERIZATION; GENE EXPRESSION REGULATION; HUMAN; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; TWO HYBRID SYSTEM;

ANIMALS; BRAIN; CERCOPITHECUS AETHIOPS; COS CELLS; DIMERIZATION; GENE EXPRESSION REGULATION; HUMANS; MODELS, BIOLOGICAL; PARKINSON DISEASE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 47749114984     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M708718200     Document Type: Article

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