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Volumn 29, Issue 5, 2006, Pages 286-293

LRRK2 in Parkinson's disease: protein domains and functional insights

Author keywords

[No Author keywords available]

Indexed keywords

LEUCINE RICH REPEAT KINASE 2; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 33646151866     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2006.03.006     Document Type: Review
Times cited : (416)

References (79)
  • 1
    • 0034643838 scopus 로고    scopus 로고
    • de Rijk, M.C. et al. (2000) Prevalence of Parkinson's disease in Europe: a collaborative study of population-based cohorts. Neurologic Diseases in the Elderly Research Group. Neurology 54 (11, Suppl. 5), S21-S23
  • 2
    • 0038727936 scopus 로고    scopus 로고
    • Description of Parkinson's disease as a clinical syndrome
    • Fahn S. Description of Parkinson's disease as a clinical syndrome. Ann. N. Y. Acad. Sci. 991 (2003) 1-14
    • (2003) Ann. N. Y. Acad. Sci. , vol.991 , pp. 1-14
    • Fahn, S.1
  • 3
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • Cookson M.R. The biochemistry of Parkinson's disease. Annu. Rev. Biochem. 74 (2005) 29-52
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 4
    • 20744435383 scopus 로고    scopus 로고
    • Molecular pathophysiology of Parkinson's disease
    • Moore D.J., et al. Molecular pathophysiology of Parkinson's disease. Annu. Rev. Neurosci. 28 (2005) 57-87
    • (2005) Annu. Rev. Neurosci. , vol.28 , pp. 57-87
    • Moore, D.J.1
  • 5
    • 8844266996 scopus 로고    scopus 로고
    • Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease
    • Paisan-Ruiz C., et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron 44 (2004) 595-600
    • (2004) Neuron , vol.44 , pp. 595-600
    • Paisan-Ruiz, C.1
  • 6
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
    • Zimprich A., et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 44 (2004) 601-607
    • (2004) Neuron , vol.44 , pp. 601-607
    • Zimprich, A.1
  • 7
    • 18244394793 scopus 로고    scopus 로고
    • Clinical features of LRRK2-associated Parkinson's disease in central Norway
    • Aasly J.O., et al. Clinical features of LRRK2-associated Parkinson's disease in central Norway. Ann. Neurol. 57 (2005) 762-765
    • (2005) Ann. Neurol. , vol.57 , pp. 762-765
    • Aasly, J.O.1
  • 8
    • 33644822969 scopus 로고    scopus 로고
    • Type and frequency of mutations in the LRRK2 gene in familial and sporadic Parkinson's disease
    • Berg D., et al. Type and frequency of mutations in the LRRK2 gene in familial and sporadic Parkinson's disease. Brain 128 (2005) 3000-3011
    • (2005) Brain , vol.128 , pp. 3000-3011
    • Berg, D.1
  • 9
    • 28544441181 scopus 로고    scopus 로고
    • Mutations in the gene LRRK2 encoding dardarin (PARK8) cause familial Parkinson's disease: clinical, pathological, olfactory and functional imaging and genetic data
    • Khan N.L., et al. Mutations in the gene LRRK2 encoding dardarin (PARK8) cause familial Parkinson's disease: clinical, pathological, olfactory and functional imaging and genetic data. Brain 128 (2005) 2786-2796
    • (2005) Brain , vol.128 , pp. 2786-2796
    • Khan, N.L.1
  • 10
    • 28344457936 scopus 로고    scopus 로고
    • Lrrk2 pathogenic substitutions in Parkinson's disease
    • Mata I.F., et al. Lrrk2 pathogenic substitutions in Parkinson's disease. Neurogenetics 6 (2005) 171-177
    • (2005) Neurogenetics , vol.6 , pp. 171-177
    • Mata, I.F.1
  • 11
    • 24644497562 scopus 로고    scopus 로고
    • LRRK2 mutations in Parkinson disease
    • Farrer M., et al. LRRK2 mutations in Parkinson disease. Neurology 65 (2005) 738-740
    • (2005) Neurology , vol.65 , pp. 738-740
    • Farrer, M.1
  • 12
    • 24644486896 scopus 로고    scopus 로고
    • A clinic-based study of the LRRK2 gene in Parkinson disease yields new mutations
    • Zabetian C.P., et al. A clinic-based study of the LRRK2 gene in Parkinson disease yields new mutations. Neurology 65 (2005) 741-744
    • (2005) Neurology , vol.65 , pp. 741-744
    • Zabetian, C.P.1
  • 13
    • 31344432937 scopus 로고    scopus 로고
    • LRRK2 G2019S as a cause of Parkinson's disease in North African Arabs
    • Lesage S., et al. LRRK2 G2019S as a cause of Parkinson's disease in North African Arabs. N. Engl. J. Med. 354 (2006) 422-423
    • (2006) N. Engl. J. Med. , vol.354 , pp. 422-423
    • Lesage, S.1
  • 14
    • 22544465257 scopus 로고    scopus 로고
    • LRRK2 haplotype analyses in European and North African families with Parkinson disease: a common founder for the G mutation dating from the 13th century
    • Lesage S., et al. LRRK2 haplotype analyses in European and North African families with Parkinson disease: a common founder for the G mutation dating from the 13th century. Am. J. Hum. Genet. 77 (2005) 330-332
    • (2005) Am. J. Hum. Genet. , vol.77 , pp. 330-332
    • Lesage, S.1
  • 15
    • 31344439221 scopus 로고    scopus 로고
    • LRRK2 G2019S as a cause of Parkinson's disease in Ashkenazi Jews
    • Ozelius L.J., et al. LRRK2 G2019S as a cause of Parkinson's disease in Ashkenazi Jews. N. Engl. J. Med. 354 (2006) 424-425
    • (2006) N. Engl. J. Med. , vol.354 , pp. 424-425
    • Ozelius, L.J.1
  • 16
    • 19944431081 scopus 로고    scopus 로고
    • A frequent LRRK2 gene mutation associated with autosomal dominant Parkinson's disease
    • Di Fonzo A., et al. A frequent LRRK2 gene mutation associated with autosomal dominant Parkinson's disease. Lancet 365 (2005) 412-415
    • (2005) Lancet , vol.365 , pp. 412-415
    • Di Fonzo, A.1
  • 17
    • 20144387207 scopus 로고    scopus 로고
    • Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations
    • Kachergus J., et al. Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations. Am. J. Hum. Genet. 76 (2005) 672-680
    • (2005) Am. J. Hum. Genet. , vol.76 , pp. 672-680
    • Kachergus, J.1
  • 18
    • 19944432606 scopus 로고    scopus 로고
    • Genetic screening for a single common LRRK2 mutation in familial Parkinson's disease
    • Nichols W.C., et al. Genetic screening for a single common LRRK2 mutation in familial Parkinson's disease. Lancet 365 (2005) 410-412
    • (2005) Lancet , vol.365 , pp. 410-412
    • Nichols, W.C.1
  • 19
    • 19944432921 scopus 로고    scopus 로고
    • A common LRRK2 mutation in idiopathic Parkinson's disease
    • Gilks W.P., et al. A common LRRK2 mutation in idiopathic Parkinson's disease. Lancet 365 (2005) 415-416
    • (2005) Lancet , vol.365 , pp. 415-416
    • Gilks, W.P.1
  • 20
    • 32044466285 scopus 로고    scopus 로고
    • Lrrk2 and Lewy body disease
    • Ross O.A., et al. Lrrk2 and Lewy body disease. Ann. Neurol. 59 (2006) 388-393
    • (2006) Ann. Neurol. , vol.59 , pp. 388-393
    • Ross, O.A.1
  • 21
    • 0031460466 scopus 로고    scopus 로고
    • German-Canadian family (Family A) with parkinsonism, amyotrophy, and dementia - longitudinal observations
    • Wszolek Z., et al. German-Canadian family (Family A) with parkinsonism, amyotrophy, and dementia - longitudinal observations. Parkinsonism Relat. Disord. 3 (1997) 125-139
    • (1997) Parkinsonism Relat. Disord. , vol.3 , pp. 125-139
    • Wszolek, Z.1
  • 22
    • 32044458576 scopus 로고    scopus 로고
    • LRRK2: a common pathway for parkinsonism, pathogenesis and prevention?
    • Taylor J.P., et al. LRRK2: a common pathway for parkinsonism, pathogenesis and prevention?. Trends Mol. Med. 12 (2006) 76-82
    • (2006) Trends Mol. Med. , vol.12 , pp. 76-82
    • Taylor, J.P.1
  • 23
    • 33646146878 scopus 로고    scopus 로고
    • Anatomical localization of leucine-rich repeat kinase 2 in mouse brain
    • 10.1016/j.neuroscience.2006.01.017 (http://www.sciencedirect.com/science/journal/03064522)
    • Melrose H., et al. Anatomical localization of leucine-rich repeat kinase 2 in mouse brain. Neuroscience (2006). http://www.sciencedirect.com/science/journal/03064522 10.1016/j.neuroscience.2006.01.017 (http://www.sciencedirect.com/science/journal/03064522)
    • (2006) Neuroscience
    • Melrose, H.1
  • 24
    • 33644934224 scopus 로고    scopus 로고
    • LRRK2 is expressed in areas affected by Parkinson's disease in the adult mouse brain
    • Simon-Sanchez J., et al. LRRK2 is expressed in areas affected by Parkinson's disease in the adult mouse brain. Eur. J. Neurosci. 23 (2006) 659-666
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 659-666
    • Simon-Sanchez, J.1
  • 25
    • 32244443107 scopus 로고    scopus 로고
    • LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain
    • Korr D., et al. LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain. Cell. Signal. 18 (2006) 910-920
    • (2006) Cell. Signal. , vol.18 , pp. 910-920
    • Korr, D.1
  • 27
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning G., et al. The protein kinase complement of the human genome. Science 298 (2002) 1912-1934
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1
  • 28
    • 0035783061 scopus 로고    scopus 로고
    • Protein repeats: structures, functions, and evolution
    • Andrade M.A., et al. Protein repeats: structures, functions, and evolution. J. Struct. Biol. 134 (2001) 117-131
    • (2001) J. Struct. Biol. , vol.134 , pp. 117-131
    • Andrade, M.A.1
  • 29
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah B.J., et al. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90 (1997) 859-869
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1
  • 30
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 31
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B., et al. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15 (2004) 661-675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1
  • 32
    • 85101729313 scopus 로고    scopus 로고
    • LRRK2 mutations and Parkinsonism
    • Toft M., et al. LRRK2 mutations and Parkinsonism. Lancet 365 (2005) 1229-1230
    • (2005) Lancet , vol.365 , pp. 1229-1230
    • Toft, M.1
  • 33
    • 16444380313 scopus 로고    scopus 로고
    • LRRK2 mutations and Parkinsonism
    • Albrecht M. LRRK2 mutations and Parkinsonism. Lancet 365 (2005) 1230
    • (2005) Lancet , vol.365 , pp. 1230
    • Albrecht, M.1
  • 34
    • 27744446035 scopus 로고    scopus 로고
    • The LRRK2 I2012T, G2019S, and I2020T mutations are rare in Taiwanese patients with sporadic Parkinson's disease
    • Lu C.S., et al. The LRRK2 I2012T, G2019S, and I2020T mutations are rare in Taiwanese patients with sporadic Parkinson's disease. Parkinsonism Relat. Disord. 11 (2005) 521-522
    • (2005) Parkinsonism Relat. Disord. , vol.11 , pp. 521-522
    • Lu, C.S.1
  • 35
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • West A.B., et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 16842-16847
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16842-16847
    • West, A.B.1
  • 36
    • 31144443248 scopus 로고    scopus 로고
    • The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
    • Gloeckner C.J., et al. The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum. Mol. Genet. 15 (2006) 223-232
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 223-232
    • Gloeckner, C.J.1
  • 37
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: crucial integrators of cellular stress
    • Meylan E., and Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 30 (2005) 151-159
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 38
    • 20444418706 scopus 로고    scopus 로고
    • MAPK kinase kinases (MKKKs) as a target class for small-molecule inhibition to modulate signaling networks and gene expression
    • Johnson G.L., et al. MAPK kinase kinases (MKKKs) as a target class for small-molecule inhibition to modulate signaling networks and gene expression. Curr. Opin. Chem. Biol. 9 (2005) 325-331
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 325-331
    • Johnson, G.L.1
  • 39
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson G.L., and Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 298 (2002) 1911-1912
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 40
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-κB but not Fas/APO-1-initiated apoptosis
    • Ting A.T., et al. RIP mediates tumor necrosis factor receptor 1 activation of NF-κB but not Fas/APO-1-initiated apoptosis. EMBO J. 15 (1996) 6189-6196
    • (1996) EMBO J. , vol.15 , pp. 6189-6196
    • Ting, A.T.1
  • 41
    • 8444238236 scopus 로고    scopus 로고
    • The RAF proteins take centre stage
    • Wellbrock C., et al. The RAF proteins take centre stage. Nat. Rev. Mol. Cell Biol. 5 (2004) 875-885
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 875-885
    • Wellbrock, C.1
  • 42
    • 0036731701 scopus 로고    scopus 로고
    • Mixed-lineage kinase control of JNK and p38 MAPK pathways
    • Gallo K.A., and Johnson G.L. Mixed-lineage kinase control of JNK and p38 MAPK pathways. Nat. Rev. Mol. Cell Biol. 3 (2002) 663-672
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 663-672
    • Gallo, K.A.1    Johnson, G.L.2
  • 43
    • 1342344813 scopus 로고    scopus 로고
    • Mixed-lineage kinases: a target for the prevention of neurodegeneration
    • Wang L.H., et al. Mixed-lineage kinases: a target for the prevention of neurodegeneration. Annu. Rev. Pharmacol. Toxicol. 44 (2004) 451-474
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 451-474
    • Wang, L.H.1
  • 44
    • 0036684674 scopus 로고    scopus 로고
    • Untying the regulation of the Raf-1 kinase
    • Dhillon A.S., and Kolch W. Untying the regulation of the Raf-1 kinase. Arch. Biochem. Biophys. 404 (2002) 3-9
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 3-9
    • Dhillon, A.S.1    Kolch, W.2
  • 45
    • 0035860701 scopus 로고    scopus 로고
    • Function of the Rho family GTPases in Ras-stimulated Raf activation
    • Li W., et al. Function of the Rho family GTPases in Ras-stimulated Raf activation. J. Biol. Chem. 276 (2001) 34728-34737
    • (2001) J. Biol. Chem. , vol.276 , pp. 34728-34737
    • Li, W.1
  • 46
    • 30044441291 scopus 로고    scopus 로고
    • Cdc42 induces activation loop phosphorylation and membrane targeting of mixed lineage kinase 3
    • Du Y., et al. Cdc42 induces activation loop phosphorylation and membrane targeting of mixed lineage kinase 3. J. Biol. Chem. 280 (2005) 42984-42993
    • (2005) J. Biol. Chem. , vol.280 , pp. 42984-42993
    • Du, Y.1
  • 47
    • 0032484215 scopus 로고    scopus 로고
    • Dimerization via tandem leucine zippers is essential for the activation of the mitogen-activated protein kinase kinase kinase, MLK-3
    • Leung I.W., and Lassam N. Dimerization via tandem leucine zippers is essential for the activation of the mitogen-activated protein kinase kinase kinase, MLK-3. J. Biol. Chem. 273 (1998) 32408-32415
    • (1998) J. Biol. Chem. , vol.273 , pp. 32408-32415
    • Leung, I.W.1    Lassam, N.2
  • 48
    • 0034623051 scopus 로고    scopus 로고
    • Zipper-mediated oligomerization of the mixed lineage kinase SPRK/MLK-3 is not required for its activation by the GTPase cdc42 but is necessary for its activation of the JNK pathway
    • Vacratsis P.O., and Gallo K.A. Zipper-mediated oligomerization of the mixed lineage kinase SPRK/MLK-3 is not required for its activation by the GTPase cdc42 but is necessary for its activation of the JNK pathway. J. Biol. Chem. 275 (2000) 27893-27900
    • (2000) J. Biol. Chem. , vol.275 , pp. 27893-27900
    • Vacratsis, P.O.1    Gallo, K.A.2
  • 49
    • 0034986111 scopus 로고    scopus 로고
    • Stenmark, H. and Olkkonen, V.M. (2001) The Rab GTPase family. Genome Biol. 2reviews3007.1-reviews3007.7
  • 50
    • 0034175984 scopus 로고    scopus 로고
    • Understanding Ras: 'it ain't over 'til it's over'
    • Shields J.M., et al. Understanding Ras: 'it ain't over 'til it's over'. Trends Cell Biol. 10 (2000) 147-154
    • (2000) Trends Cell Biol. , vol.10 , pp. 147-154
    • Shields, J.M.1
  • 51
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • Jaffe A.B., and Hall A. Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21 (2005) 247-269
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 52
    • 10944244704 scopus 로고    scopus 로고
    • Rho signalling at a glance
    • Schwartz M. Rho signalling at a glance. J. Cell Sci. 117 (2004) 5457-5458
    • (2004) J. Cell Sci. , vol.117 , pp. 5457-5458
    • Schwartz, M.1
  • 53
    • 29444437871 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration
    • Smith W.W., et al. Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 18676-18681
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18676-18681
    • Smith, W.W.1
  • 55
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T., et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392 (1998) 605-608
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1
  • 56
    • 9644257142 scopus 로고    scopus 로고
    • Ubiquitin, proteasome and parkin
    • Tanaka K., et al. Ubiquitin, proteasome and parkin. Biochim. Biophys. Acta 1695 (2004) 235-247
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 235-247
    • Tanaka, K.1
  • 57
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte E.M., et al. Detecting protein function and protein-protein interactions from genome sequences. Science 285 (1999) 751-753
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1
  • 58
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi L.K., et al. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 13 (2004) 1435-1448
    • (2004) Protein Sci. , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1
  • 59
    • 0033598382 scopus 로고    scopus 로고
    • Functional evaluation of tumour-specific variants of p16INK4a/CDKN2A: correlation with protein structure information
    • Ruas M., et al. Functional evaluation of tumour-specific variants of p16INK4a/CDKN2A: correlation with protein structure information. Oncogene 18 (1999) 5423-5434
    • (1999) Oncogene , vol.18 , pp. 5423-5434
    • Ruas, M.1
  • 60
    • 0032541623 scopus 로고    scopus 로고
    • Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a
    • Russo A.A., et al. Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. Nature 395 (1998) 237-243
    • (1998) Nature , vol.395 , pp. 237-243
    • Russo, A.A.1
  • 61
    • 16044362074 scopus 로고    scopus 로고
    • Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia
    • Joutel A., et al. Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia. Nature 383 (1996) 707-710
    • (1996) Nature , vol.383 , pp. 707-710
    • Joutel, A.1
  • 62
    • 0142210110 scopus 로고    scopus 로고
    • Structure and stability of the ankyrin domain of the Drosophila Notch receptor
    • Zweifel M.E., et al. Structure and stability of the ankyrin domain of the Drosophila Notch receptor. Protein Sci. 12 (2003) 2622-2632
    • (2003) Protein Sci. , vol.12 , pp. 2622-2632
    • Zweifel, M.E.1
  • 63
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B., and Kajava A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11 (2001) 725-732
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 64
    • 27144517403 scopus 로고    scopus 로고
    • Analysis of LRRK2 functional domains in nondominant Parkinson disease
    • Skipper L., et al. Analysis of LRRK2 functional domains in nondominant Parkinson disease. Neurology 65 (2005) 1319-1321
    • (2005) Neurology , vol.65 , pp. 1319-1321
    • Skipper, L.1
  • 65
    • 0034490962 scopus 로고    scopus 로고
    • Thirty-plus functional families from a single motif
    • Yu L., et al. Thirty-plus functional families from a single motif. Protein Sci. 9 (2000) 2470-2476
    • (2000) Protein Sci. , vol.9 , pp. 2470-2476
    • Yu, L.1
  • 66
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • Nash P., et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414 (2001) 514-521
    • (2001) Nature , vol.414 , pp. 514-521
    • Nash, P.1
  • 67
    • 3042592410 scopus 로고    scopus 로고
    • The use of in vitro peptide-library screens in the analysis of phosphoserine/threonine-binding domain structure and function
    • Yaffe M.B., and Smerdon S.J. The use of in vitro peptide-library screens in the analysis of phosphoserine/threonine-binding domain structure and function. Annu. Rev. Biophys. Biomol. Struct. 33 (2004) 225-244
    • (2004) Annu. Rev. Biophys. Biomol. Struct. , vol.33 , pp. 225-244
    • Yaffe, M.B.1    Smerdon, S.J.2
  • 68
    • 3242733049 scopus 로고    scopus 로고
    • Interaction of Gβγ with RACK1 and other WD40 repeat proteins
    • Chen S., et al. Interaction of Gβγ with RACK1 and other WD40 repeat proteins. J. Mol. Cell. Cardiol. 37 (2004) 399-406
    • (2004) J. Mol. Cell. Cardiol. , vol.37 , pp. 399-406
    • Chen, S.1
  • 69
    • 0038054300 scopus 로고    scopus 로고
    • Structural fingerprints of the Ras-GTPase activating proteins neurofibromin and p120GAP
    • Ahmadian M.R., et al. Structural fingerprints of the Ras-GTPase activating proteins neurofibromin and p120GAP. J. Mol. Biol. 329 (2003) 699-710
    • (2003) J. Mol. Biol. , vol.329 , pp. 699-710
    • Ahmadian, M.R.1
  • 70
    • 0033179296 scopus 로고    scopus 로고
    • GEFs: structural basis for their activation of small GTP-binding proteins
    • Cherfils J., and Chardin P. GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem. Sci. 24 (1999) 306-311
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 306-311
    • Cherfils, J.1    Chardin, P.2
  • 71
    • 24644431901 scopus 로고    scopus 로고
    • LRRK2 gene in Parkinson disease
    • Paisan-Ruiz C., et al. LRRK2 gene in Parkinson disease. Neurology 65 (2005) 696-700
    • (2005) Neurology , vol.65 , pp. 696-700
    • Paisan-Ruiz, C.1
  • 72
    • 21144451648 scopus 로고    scopus 로고
    • LRRK2 R1441G in Spanish patients with Parkinson's disease
    • Mata I.F., et al. LRRK2 R1441G in Spanish patients with Parkinson's disease. Neurosci. Lett. 382 (2005) 309-311
    • (2005) Neurosci. Lett. , vol.382 , pp. 309-311
    • Mata, I.F.1
  • 73
    • 30344450900 scopus 로고    scopus 로고
    • Parkinson's disease and LRRK2: Frequency of a common mutation in U.S. movement disorder clinics
    • Kay D.M., et al. Parkinson's disease and LRRK2: Frequency of a common mutation in U.S. movement disorder clinics. Mov Disord. (2005)
    • (2005) Mov Disord.
    • Kay, D.M.1
  • 74
    • 20444420103 scopus 로고    scopus 로고
    • An LRRK2 mutation as a cause for the parkinsonism in the original PARK8 family
    • Funayama M., et al. An LRRK2 mutation as a cause for the parkinsonism in the original PARK8 family. Ann. Neurol. 57 (2005) 918-921
    • (2005) Ann. Neurol. , vol.57 , pp. 918-921
    • Funayama, M.1
  • 75
    • 26444613397 scopus 로고    scopus 로고
    • Escaping Parkinson's disease: a neurologically healthy octogenarian with the LRRK2 G2019S mutation
    • Kay D.M., et al. Escaping Parkinson's disease: a neurologically healthy octogenarian with the LRRK2 G2019S mutation. Mov. Disord. 20 (2005) 1077-1078
    • (2005) Mov. Disord. , vol.20 , pp. 1077-1078
    • Kay, D.M.1
  • 76
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: a simple approach to improve protein structure predictions
    • Ginalski K., et al. 3D-Jury: a simple approach to improve protein structure predictions. Bioinformatics 19 (2003) 1015-1018
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1
  • 77
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 78
    • 23144463912 scopus 로고    scopus 로고
    • FFAS03: a server for profile-profile sequence alignments
    • Jaroszewski L., et al. FFAS03: a server for profile-profile sequence alignments. Nucleic Acids Res. 33 (2005) W284-W288
    • (2005) Nucleic Acids Res. , vol.33
    • Jaroszewski, L.1
  • 79
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., et al. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.