Leucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brain

Journal of Neurochemistry

Volumn 135, Issue 6, 2015, Pages 1242-1256

  Civiero, Laura ^a   Cirnaru, Maria Daniela ^b   Beilina, Alexandra ^c   Rodella, Umberto ^a   Russo, Isabella ^a   Belluzzi, Elisa ^a   Lobbestael, Evy ^d   Reyniers, Lauran ^d   Hondhamuni, Geshanthi ^e   Lewis, Patrick A ^e,f   Van Den Haute, Chris ^d,g   Baekelandt, Veerle ^d   Bandopadhyay, Rina ^e   Bubacco, Luigi ^a   Piccoli, Giovanni ^b   Cookson, Mark R ^c   Taymans, Jean Marc ^d,h   Greggio, Elisa ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b VITA SALUTE SAN RAFFAELE UNIVERSITY   (Italy)

^c NATIONAL INSTITUTE ON AGING   (United States)

^d UNIVERSITY OF LEUVEN   (Belgium)

^e UNIVERSITY COLLEGE LONDON   (United Kingdom)

^f UNIVERSITY OF READING   (United Kingdom)

^g KU LEUVEN   (Belgium)

^h JEAN PIERRE AUBERT RESEARCH CENTER   (France)

Author keywords

LRRK2; neurodegeneration; neuronal cyto skeleton; p21 activated kinases; Parkinson's disease

Indexed keywords

GLUTATHIONE TRANSFERASE; LEUCINE RICH REPEAT KINASE 2; P21 ACTIVATED KINASE 6; PROTEIN CDC42; RAC1 PROTEIN; LEUCINE; LRRK2 PROTEIN, HUMAN; LRRK2 PROTEIN, MOUSE; P21 ACTIVATED KINASE; PAK6 PROTEIN, HUMAN; PAK6 PROTEIN, MOUSE; PROTEIN SERINE THREONINE KINASE;

ACTIN FILAMENT; ADULT; AGED; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BRAIN; CELL STRUCTURE; CONTROLLED STUDY; FEMALE; HUMAN; HUMAN CELL; HUMAN TISSUE; IN VIVO STUDY; MALE; MOUSE; NERVE DEGENERATION; NERVE FIBER GROWTH; NEURITE; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; REGULATORY MECHANISM; SEQUENCE ANALYSIS; VERY ELDERLY; ANIMAL; GENETICS; MAMMAL; METABOLISM; MUTATION;

ACTIN CYTOSKELETON; ANIMALS; BRAIN; HUMANS; LEUCINE; LEUCINE-RICH REPEAT SERINE-THREONINE PROTEIN KINASE-2; MAMMALS; MICE; MUTATION; NEURITES; P21-ACTIVATED KINASES; PARKINSON DISEASE; PROTEIN-SERINE-THREONINE KINASES;

EID: 84955212896     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13369     Document Type: Article

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