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Volumn 430, Issue 3, 2010, Pages

14-3-3 proteins are promising LRRK2 interactors

Author keywords

14 3 3 protein; Leucine rich repeat kinase 2 (LRRK2); Parkinson's disease; Phosphorylation; Protein protein interaction

Indexed keywords

LEUCINE RICH REPEAT KINASE 2; PROTEIN 14 3 3; SERINE; GREEN FLUORESCENT PROTEIN; LRRK2 PROTEIN, MOUSE; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE;

EID: 77956704554     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101200     Document Type: Note
Times cited : (20)

References (10)
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    • The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development
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    • Morrison, D.K.1
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    • The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation
    • Greggio, E., Zambrano, I., Kaganovich, A., Beilina, A., Taymans, J.-M., Daniels, V., Lewis, P., Jain, S., Ding, J., Syed, A. et al. (2008) The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. J. Biol. Chem. 283, 16906-16914
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    • Greggio, E.1    Zambrano, I.2    Kaganovich, A.3    Beilina, A.4    Taymans, J.-M.5    Daniels, V.6    Lewis, P.7    Jain, S.8    Ding, J.9    Syed, A.10
  • 8
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    • Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization
    • Sen, S., Webber, P. J. and West, A. B. (2009) Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. J. Biol. Chem. 284, 36346-36356
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    • Sen, S.1    Webber, P.J.2    West, A.B.3
  • 9
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    • Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation
    • Berger, Z., Smith, K. A. and Lavoie, M. J. (2010) Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation. Biochemistry 49, 5511-5523
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    • Gloeckner, C. J., Boldt, K., von Zweydorf, F., Helm, S., Wiesent, L., Sarioglu, H. and Ueffing, M. (2010) Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. J. Proteome Res. 9, 1738-1745
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.