about
The dictyostelium kinome--analysis of the protein kinases from a simple model organism.Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domainBiochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimersHeterodimerization of Lrrk1-Lrrk2: Implications for LRRK2-associated Parkinson diseaseLRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complexThe R1441C mutation of LRRK2 disrupts GTP hydrolysisInsight into the mode of action of the LRRK2 Y1699C pathogenic mutantGTP binding controls complex formation by the human ROCO protein MASL1GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signallingMutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathwaysMutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal deathActivation Mechanism of LRRK2 and Its Cellular Functions in Parkinson's DiseaseLRRK2 as a Potential Genetic Modifier of Synucleinopathies: Interlacing the Two Major Genetic Factors of Parkinson's DiseaseTen years and counting: moving leucine-rich repeat kinase 2 inhibitors to the clinicStructure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPaseStructure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinaseRoco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutationsRevisiting the Roco G-protein cycleLeucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brainTargeted disruption of leucine-rich repeat kinase 1 but not leucine-rich repeat kinase 2 in mice causes severe osteopetrosisEnhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019SLRRK2 phosphorylation level correlates with abnormal motor behaviour in an experimental model of levodopa-induced dyskinesiasProtective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity.LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activityThe LRRK2-related Roco kinase Roco2 is regulated by Rab1A and controls the actin cytoskeletonDynamic and redundant regulation of LRRK2 and LRRK1 expression.The R1441C mutation alters the folding properties of the ROC domain of LRRK2.Leucine-rich repeat kinase 2 (LRRK2): a key player in the pathogenesis of Parkinson's diseaseIdentification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations.Leucine-rich repeat kinase 2: a new player with a familiar theme for Parkinson's disease pathogenesis.GST P1, a novel downstream regulator of LRRK2, G2019S-induced neuronal cell death.A QUICK screen for Lrrk2 interaction partners--leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics.Mitochondrial dysfunction in Parkinson's disease: pathogenesis and neuroprotection.Novel ethyl methanesulfonate (EMS)-induced null alleles of the Drosophila homolog of LRRK2 reveal a crucial role in endolysosomal functions and autophagy in vivo.FIH-1 disrupts an LRRK1/EGFR complex to positively regulate keratinocyte migration.Expression analysis of Lrrk1, Lrrk2 and Lrrk2 splice variants in mice.Models for LRRK2-Linked Parkinsonism.Evolution and diversity of the Ras superfamily of small GTPases in prokaryotesTemporal expression of mutant LRRK2 in adult rats impairs dopamine reuptakeA comparative study of Lrrk2 function in primary neuronal cultures.
P2860
Q21145270-2FFE69AA-1413-4E73-B389-DA3FB2DF5375Q24293453-7B8F2098-2BA4-497D-8FC5-362B8B761C5DQ24298093-EFB58D82-8574-4C2C-9C3B-B8FBFCB577B8Q24298781-557118B5-F269-43D9-90D0-0A6F4FA3C5F8Q24298891-436866AC-B5AE-47EE-A440-7C7A80C06573Q24303406-7A671A26-647E-47BA-83F5-8CDD0148CF90Q24306788-3B24D772-70E1-433B-9061-72D94E0EE9F1Q24310620-75725C4A-E549-4126-A5D0-33C04FDBE59AQ24311806-3018F396-9624-489A-98A0-E08410220956Q24316917-8C5D2B1F-9569-45A6-90EC-8080C804581AQ24323228-C54348DA-92D7-4CE9-9AFA-864A81DAD39FQ26746897-3402E5FC-A9C8-4716-A19B-3D7838F540E9Q26861279-75939FDF-4525-4296-804B-F809838739DEQ27007413-48A63864-A2C4-4945-B9BB-3255D4AEF09AQ27649733-46B9F7F7-01ED-4865-8C1A-1A00927781ACQ27651307-E1F164D7-372F-4FBB-A2DA-5C08A63C885AQ27681111-6C82E197-4236-4DAA-823B-D51C41D13FF8Q27695715-F140CE53-C738-4B19-B432-0EC6D3CFB766Q28267434-A2BE2A16-A643-46E0-A054-4A93EFEA18EBQ28505157-E6E7E4A8-C7B8-4F78-A33E-E04C89068876Q28589899-3D535C21-8AF5-4787-8374-33353CB7C1C9Q28602836-9A050C74-2F17-4D25-90AA-9E0B1DA4A986Q29347547-D255368C-7C79-49CE-B3EE-F5C3F960BF62Q29615144-70D006E7-472F-4D3B-9055-A0F422E5FA21Q30501999-C5E048E0-1D94-407B-9AFF-DB8C26865874Q33307626-39B732B8-A7A0-44F2-AB2A-ED575D900A26Q33758163-01499728-8C3B-4545-BEC7-93EC1E51C18BQ33812599-0DFF1D64-F82A-4A6C-98E4-9FE9975D2320Q33942173-D757DDDC-BF22-4896-887D-11D3F05AE33AQ34133422-668CCD78-91C2-4815-AA47-42BF5A0F52DCQ34240711-053754C1-C635-402C-9643-EF41200578BDQ34454883-66521D0E-5A74-4B37-A281-6CD7D1455563Q34460675-7E9D41CB-3AD8-4A0B-A959-C024E08AA8FFQ34637362-14404BF6-F7D1-4837-A956-71E5A857075AQ34646937-74852457-E33A-429B-B665-B5F97FCB030CQ34723024-61AA9907-0DD3-43B8-AB67-0075CDB3DF15Q34986076-13DD0108-851A-48B8-90B6-B201AAB0EDF7Q35047500-C5D4E5AF-614C-451D-8C53-517C588AA44BQ35059247-C43709AF-53AF-4FAC-B68C-09CB62951951Q35176338-479D3FD9-32F4-43F4-BAE5-6E61872E5364
P2860
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Roc, a Ras/GTPase domain in complex proteins.
@ast
Roc, a Ras/GTPase domain in complex proteins.
@en
Roc, a Ras/GTPase domain in complex proteins.
@nl
type
label
Roc, a Ras/GTPase domain in complex proteins.
@ast
Roc, a Ras/GTPase domain in complex proteins.
@en
Roc, a Ras/GTPase domain in complex proteins.
@nl
prefLabel
Roc, a Ras/GTPase domain in complex proteins.
@ast
Roc, a Ras/GTPase domain in complex proteins.
@en
Roc, a Ras/GTPase domain in complex proteins.
@nl
P1476
Roc, a Ras/GTPase domain in complex proteins.
@en
P2093
Leonard Bosgraaf
Peter J M Van Haastert
P356
10.1016/J.BBAMCR.2003.08.008
P407
P577
2003-12-01T00:00:00Z