-
1
-
-
33750459730
-
Parkinsonism genes: culprits and clues
-
Abeliovich A., Flint B.M. Parkinsonism genes: culprits and clues. J Neurochem 2006, 99:1062-1072.
-
(2006)
J Neurochem
, vol.99
, pp. 1062-1072
-
-
Abeliovich, A.1
Flint, B.M.2
-
2
-
-
68949125734
-
Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease
-
Biskup S., West A.B. Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease. Biochim Biophys Acta 2009, 1792:625-633.
-
(2009)
Biochim Biophys Acta
, vol.1792
, pp. 625-633
-
-
Biskup, S.1
West, A.B.2
-
3
-
-
79952918505
-
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2
-
Deng X., Dzamko N., Prescott A., Davies P., Liu Q., Yang Q., et al. Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2. Nat Chem Biol 2011, 7:203-205.
-
(2011)
Nat Chem Biol
, vol.7
, pp. 203-205
-
-
Deng, X.1
Dzamko, N.2
Prescott, A.3
Davies, P.4
Liu, Q.5
Yang, Q.6
-
4
-
-
77956655427
-
Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization
-
Dzamko N., Deak M., Hentati F., Reith A.D., Prescott A.R., Alessi D.R., et al. Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization. Biochem J 2010, 430:405-413.
-
(2010)
Biochem J
, vol.430
, pp. 405-413
-
-
Dzamko, N.1
Deak, M.2
Hentati, F.3
Reith, A.D.4
Prescott, A.R.5
Alessi, D.R.6
-
5
-
-
84862497413
-
The IkappaB kinase family phosphorylates the Parkinson's disease kinase LRRK2 at Ser935 and Ser910 during Toll-like receptor signaling
-
Dzamko N., Inesta-Vaquera F., Zhang J., Xie C., Cai H., Arthur S., et al. The IkappaB kinase family phosphorylates the Parkinson's disease kinase LRRK2 at Ser935 and Ser910 during Toll-like receptor signaling. PLoS One 2012, 7:e39132.
-
(2012)
PLoS One
, vol.7
-
-
Dzamko, N.1
Inesta-Vaquera, F.2
Zhang, J.3
Xie, C.4
Cai, H.5
Arthur, S.6
-
6
-
-
0030329981
-
SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
-
Frank R., Overwin H. SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Methods Mol Biol 1996, 66:149-169.
-
(1996)
Methods Mol Biol
, vol.66
, pp. 149-169
-
-
Frank, R.1
Overwin, H.2
-
7
-
-
68949218403
-
Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability - a point of convergence in parkinsonian neurodegeneration?
-
Gillardon F. Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability - a point of convergence in parkinsonian neurodegeneration?. J Neurochem 2009, 110:1514-1522.
-
(2009)
J Neurochem
, vol.110
, pp. 1514-1522
-
-
Gillardon, F.1
-
8
-
-
37048999786
-
A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes
-
Gloeckner C.J., Boldt K., Schumacher A., Roepman R., Ueffing M. A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics 2007, 7:4228-4234.
-
(2007)
Proteomics
, vol.7
, pp. 4228-4234
-
-
Gloeckner, C.J.1
Boldt, K.2
Schumacher, A.3
Roepman, R.4
Ueffing, M.5
-
9
-
-
31144443248
-
The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
-
Gloeckner C.J., Kinkl N., Schumacher A., Braun R.J., O'Neill E., Meitinger T., et al. The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum Mol Genet 2006, 15:223-232.
-
(2006)
Hum Mol Genet
, vol.15
, pp. 223-232
-
-
Gloeckner, C.J.1
Kinkl, N.2
Schumacher, A.3
Braun, R.J.4
O'Neill, E.5
Meitinger, T.6
-
10
-
-
47749114984
-
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., et al. The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. J Biol Chem 2008, 283:16906-16914.
-
(2008)
J Biol Chem
, vol.283
, pp. 16906-16914
-
-
Greggio, E.1
Zambrano, I.2
Kaganovich, A.3
Beilina, A.4
Taymans, J.M.5
Daniels, V.6
-
11
-
-
0037013143
-
The conformational plasticity of protein kinases
-
Huse M., Kuriyan J. The conformational plasticity of protein kinases. Cell 2002, 109:275-282.
-
(2002)
Cell
, vol.109
, pp. 275-282
-
-
Huse, M.1
Kuriyan, J.2
-
12
-
-
84855952177
-
Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form
-
Ito G., Iwatsubo T. Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form. Biochem J 2012, 441:987-994.
-
(2012)
Biochem J
, vol.441
, pp. 987-994
-
-
Ito, G.1
Iwatsubo, T.2
-
13
-
-
72749105819
-
Identification of the autophosphorylation sites of LRRK2
-
Kamikawaji S., Ito G., Iwatsubo T. Identification of the autophosphorylation sites of LRRK2. Biochemistry 2009, 48:10963-10975.
-
(2009)
Biochemistry
, vol.48
, pp. 10963-10975
-
-
Kamikawaji, S.1
Ito, G.2
Iwatsubo, T.3
-
14
-
-
77649328234
-
The Parkinson's disease associated LRRK2 exhibits weaker in vitro phosphorylation of 4E-BP compared to autophosphorylation
-
Kumar A., Greggio E., Beilina A., Kaganovich A., Chan D., Taymans J.M., et al. The Parkinson's disease associated LRRK2 exhibits weaker in vitro phosphorylation of 4E-BP compared to autophosphorylation. PLoS One 2010, 5:e8730.
-
(2010)
PLoS One
, vol.5
-
-
Kumar, A.1
Greggio, E.2
Beilina, A.3
Kaganovich, A.4
Chan, D.5
Taymans, J.M.6
-
15
-
-
77956529777
-
Reevaluation of phosphorylation sites in the Parkinson disease-associated leucine-rich repeat kinase 2
-
Li X., Moore D.J., Xiong Y., Dawson T.M., Dawson V.L. Reevaluation of phosphorylation sites in the Parkinson disease-associated leucine-rich repeat kinase 2. J Biol Chem 2010, 285:29569-29576.
-
(2010)
J Biol Chem
, vol.285
, pp. 29569-29576
-
-
Li, X.1
Moore, D.J.2
Xiong, Y.3
Dawson, T.M.4
Dawson, V.L.5
-
16
-
-
33646151866
-
LRRK2 in Parkinson's disease: protein domains and functional insights
-
Mata I.F., Wedemeyer W.J., Farrer M.J., Taylor J.P., Gallo K.A. LRRK2 in Parkinson's disease: protein domains and functional insights. Trends Neurosci 2006, 29:286-293.
-
(2006)
Trends Neurosci
, vol.29
, pp. 286-293
-
-
Mata, I.F.1
Wedemeyer, W.J.2
Farrer, M.J.3
Taylor, J.P.4
Gallo, K.A.5
-
17
-
-
67149108177
-
Update on the functional biology of LRRK2
-
Melrose H. Update on the functional biology of LRRK2. Future Neurol 2008, 3:669-681.
-
(2008)
Future Neurol
, vol.3
, pp. 669-681
-
-
Melrose, H.1
-
18
-
-
70350653779
-
Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease
-
Nichols R.J., Dzamko N., Hutti J.E., Cantley L.C., Deak M., Moran J., et al. Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease. Biochem J 2009, 424:47-60.
-
(2009)
Biochem J
, vol.424
, pp. 47-60
-
-
Nichols, R.J.1
Dzamko, N.2
Hutti, J.E.3
Cantley, L.C.4
Deak, M.5
Moran, J.6
-
19
-
-
77956674229
-
14-3-3 Binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization
-
Nichols R.J., Dzamko N., Morrice N.A., Campbell D.G., Deak M., Ordureau A., et al. 14-3-3 Binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization. Biochem J 2010, 430:393-404.
-
(2010)
Biochem J
, vol.430
, pp. 393-404
-
-
Nichols, R.J.1
Dzamko, N.2
Morrice, N.A.3
Campbell, D.G.4
Deak, M.5
Ordureau, A.6
-
20
-
-
4444353636
-
Regulation of protein kinases; controlling activity through activation segment conformation
-
Nolen B., Taylor S., Ghosh G. Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 2004, 15:661-675.
-
(2004)
Mol Cell
, vol.15
, pp. 661-675
-
-
Nolen, B.1
Taylor, S.2
Ghosh, G.3
-
21
-
-
84866429101
-
Sequences located within the n-terminus of the PD-Linked LRRK2 lead to increased aggregation and attenuation of 6-hydroxydopamine-induced cell death
-
Pandey N., Fahey M.T., Jong Y.J., O'Malley K.L. Sequences located within the n-terminus of the PD-Linked LRRK2 lead to increased aggregation and attenuation of 6-hydroxydopamine-induced cell death. PLoS One 2012, 7:e45149.
-
(2012)
PLoS One
, vol.7
-
-
Pandey, N.1
Fahey, M.T.2
Jong, Y.J.3
O'Malley, K.L.4
-
22
-
-
73649120624
-
Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization
-
Sen S., Webber P.J., West A.B. Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. J Biol Chem 2009, 284:36346-36356.
-
(2009)
J Biol Chem
, vol.284
, pp. 36346-36356
-
-
Sen, S.1
Webber, P.J.2
West, A.B.3
-
23
-
-
77649105209
-
Mechanisms in dominant Parkinsonism: the toxic triangle of LRRK2, alpha-synuclein, and tau
-
Taymans J.M., Cookson M.R. Mechanisms in dominant Parkinsonism: the toxic triangle of LRRK2, alpha-synuclein, and tau. Bioessays 2010, 32:227-235.
-
(2010)
Bioessays
, vol.32
, pp. 227-235
-
-
Taymans, J.M.1
Cookson, M.R.2
-
24
-
-
41549144503
-
The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2
-
Wang L., Xie C., Greggio E., Parisiadou L., Shim H., Sun L., et al. The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2. J Neurosci 2008, 28:3384-3391.
-
(2008)
J Neurosci
, vol.28
, pp. 3384-3391
-
-
Wang, L.1
Xie, C.2
Greggio, E.3
Parisiadou, L.4
Shim, H.5
Sun, L.6
|