The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation - Wikidata - awgldk - TriplyDB

The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation

The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation

http://www.wikidata.org/entity/Q24324345

about

Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow ER-Golgi export GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2 Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7 Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle Thiol peroxidases ameliorate LRRK2 mutant-induced mitochondrial and dopaminergic neuronal degeneration in Drosophila Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease Heterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implications Pathogenic Parkinson's disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation G2385R and I2020T Mutations Increase LRRK2 GTPase Activity Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity.Heat shock proteins in neurodegenerative disorders and aging Parkinson's disease-implicated kinases in the brain; insights into disease pathogenesis.The LRRK2 G2385R variant is a partial loss-of-function mutation that affects synaptic vesicle trafficking through altered protein interactions.Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistribution Genetic variants ofLRRK2 in Taiwanese Parkinson's disease Lack of correlation between the kinase activity of LRRK2 harboring kinase-modifying mutations and its phosphorylation at Ser910, 935, and Ser955.Activation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 Mutations.Cellular effects of LRRK2 mutations.LRRK2: an éminence grise of Wnt-mediated neurogenesis?The function of orthologues of the human Parkinson's disease gene LRRK2 across species: implications for disease modelling in preclinical research.LRRK2: cause, risk, and mechanism.Deciphering the function of leucine-rich repeat kinase 2 and targeting its dysfunction in disease.Prediction of the repeat domain structures and impact of parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2).Structural biology of the LRRK2 GTPase and kinase domains: implications for regulation.The association between the LRRK2 G2385R variant and the risk of Parkinson's disease: a meta-analysis based on 23 case-control studies.LRRK2 pathobiology in Parkinson's disease.Cellular processes associated with LRRK2 function and dysfunction LRRK2 Pathways Leading to Neurodegeneration.GTP binding and intramolecular regulation by the ROC domain of Death Associated Protein Kinase 1.In silico, in vitro and cellular analysis with a kinome-wide inhibitor panel correlates cellular LRRK2 dephosphorylation to inhibitor activity on LRRK2.A Link between Autophagy and the Pathophysiology of LRRK2 in Parkinson's Disease.The genetic architecture of mitochondrial dysfunction in Parkinson's disease.Mechanisms of Mutant LRRK2 Neurodegeneration.LRRK2 G2019S-induced mitochondrial DNA damage is LRRK2 kinase dependent and inhibition restores mtDNA integrity in Parkinson's disease.Molecular Insights and Functional Implication of LRRK2 Dimerization.LRRK2 Phosphorylation.The LRRK2 Variant E193K Prevents Mitochondrial Fission Upon MPP+ Treatment by Altering LRRK2 Binding to DRP1.

P2860

b51faa01514fd70f759452eba436626eaaae4f3b ecdf0f6cc9838d4fe6a1d250e3ca32ad1b4801ce

P248

Q24293453-EC406492-3905-4CBE-9A86-6090868A2BB4 Q24298093-7FB82144-3F44-4AF9-BE27-0B8F637791C7 Q24300605-7944C9B1-7DF6-4BA9-A51A-7763A718D42B Q24303851-5BFACBB5-922A-44D2-8570-0D058FB2DA28 Q24306167-8A8CA68F-C446-4A11-8EEC-3C45580902C1 Q24309417-45ED509C-9695-4F6B-91AC-6DEA15298EF2 Q24317158-ECA01809-92D2-44E6-9223-36020F059410 Q24322678-10EF2852-D281-4719-9DCB-308EFFC31BE9 Q24336432-4708FDCB-3417-42C6-82B0-39C3EEA2814A Q27013695-EBE51AC0-29FF-4AAB-BF83-2EAFBC163B63 Q28115231-2C3FB642-97CF-44D7-B164-9CFC56B8A0A5 Q29347540-F5EE2C2C-4650-48CD-85E9-6D4690CD8304 Q29347547-AA866F79-FA68-43CF-83D9-0F36DEB57B93 Q30414556-4F1586AD-3652-4175-A6BC-EC29AEA5B8FE Q33797449-7F016B30-C01B-4541-BA50-2A7F8F69FE33 Q33905778-863A07AF-C805-4185-9101-F69A22D2EB14 Q33985278-B74C1C72-BB3B-4124-8F02-144E27B52C9C Q35067666-53C718BF-2F2C-442A-8D3D-5B74024213AF Q35170220-D19EC769-FF6B-4340-8C8A-D8C8D30F4622 Q36188579-3C5CD6CE-6975-4F5C-B61D-56F96A0DB6A0 Q36325683-F374E62A-70ED-4B6A-90A4-B667B60C5EBE Q36888947-2DE94C17-145E-47D9-88DA-D320B5F75554 Q37513500-2160EA09-9929-45B4-8FAB-0025BEFFEA0D Q37635000-F5F24AB0-5096-46E1-AA3A-EFF3B019178F Q38044425-35FCF971-9540-4377-9EF2-620995CEB08B Q38182492-5A0470E7-6342-4239-9783-6AEB6CDAE3A9 Q38213378-BD767445-842C-4152-8289-C1EE94DD3B3C Q38229792-F0A9BDE2-C2E5-4648-959A-BCB270DF18E3 Q38253871-4A38B6E2-BE3B-4B88-A0A4-DB7BC9AE12B5 Q38433725-B5935BD9-0964-40EF-99F1-CB53D832B304 Q38501861-52767A9A-C196-4244-8B75-EDB67486A4A7 Q39269900-BE57AAA3-A40A-4146-AEA9-1ED95A4E58D4 Q40188432-D077D366-2134-42D9-855E-18B7C94D57E4 Q41776543-4505A9B1-FD8A-4100-873E-60A31DB5C439 Q47646796-9826A06A-B703-4C04-89A7-338D6D6AEE0F Q48239635-8D85C645-7334-445E-9E09-592B7FB1CBE2 Q48560989-0FE62821-73BD-4730-BD66-33367A1B4C7B Q51082151-EBA2543D-4F21-4802-BC9C-D0E9EA15E553 Q51082156-12856BA4-03AA-4481-A65D-BD9CEBDC50B7 Q52355227-9941F886-B105-450B-A300-BE286C8CE0B1

P2860

The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation

http://www.wikidata.org/entity/Q24324345

description

2012 nî lūn-bûn

@nan

2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

The G2385R variant of leucine- ...... tial loss-of-function mutation

@ast

The G2385R variant of leucine- ...... tial loss-of-function mutation

@en

The G2385R variant of leucine- ...... tial loss-of-function mutation

@en-gb

The G2385R variant of leucine- ...... tial loss-of-function mutation

@nl

type

label

The G2385R variant of leucine- ...... tial loss-of-function mutation

@ast

The G2385R variant of leucine- ...... tial loss-of-function mutation

@en

The G2385R variant of leucine- ...... tial loss-of-function mutation

@en-gb

The G2385R variant of leucine- ...... tial loss-of-function mutation

@nl

prefLabel

The G2385R variant of leucine- ...... tial loss-of-function mutation

@ast

The G2385R variant of leucine- ...... tial loss-of-function mutation

@en

The G2385R variant of leucine- ...... tial loss-of-function mutation

@en-gb

The G2385R variant of leucine- ...... tial loss-of-function mutation

@nl

P1433

Q24324345-5506346F-F878-4F68-9F45-0B2730C9F1ED

P1476

Q24324345-7C6830AE-AFBD-4F65-9085-992433408FBF

P2093

Q24324345-1E9A0B41-3E1D-433A-9ADD-4AE2E759A1BD

Q24324345-30002A3E-7E44-4120-8B1A-EB75D805596E

Q24324345-3B27D640-0510-4DF7-99C6-8EF34E5E6F94

Q24324345-426158AB-5438-4D9A-BD56-DDAE683EE076

Q24324345-F43968DC-5F3B-4D0E-9BCC-AECF44F0FE14

Q24324345-F635BCB7-B8B6-497C-8474-7F012279598C

Q24324345-F91E8B34-C87A-4A15-9376-BBC9996C74E0

P2860

Q24324345-015A1529-9249-4C1B-913E-366AC745EBF7

Q24324345-05B00EEC-4AAD-4287-BD7D-D9FA1DB5DB40

Q24324345-13F750CD-69B0-451E-B705-4CCD43D51B26

Q24324345-16AC647D-1CA7-46EC-ADE7-A6D5EECD6C65

Q24324345-18D233A8-504F-487D-BD25-AE27E6527E82

Q24324345-1CCC1DBA-CBF2-4B7C-B46B-20936FB18741

Q24324345-1F48EBF1-33C1-4DE0-BCA9-0F0919C34333

Q24324345-1FA81BC7-BB9C-4F20-A444-477A50F419C3

Q24324345-24C2A828-4E49-4A14-8357-86DA41EAD591

Q24324345-32E12014-F8FC-454A-BCDF-1208ED36F793

P304

Q24324345-BD97FAF9-85D8-47FA-A602-A93FCCEE27D7

P31

Q24324345-7DF6C18B-CCC4-4BD5-89C0-80AFBBCD18C3

P3181

Q24324345-A76C81D6-74BC-42D3-8D4A-CE22B037FDEC

P356

Q24324345-42111DAB-B56F-4587-A7D1-5F23E8DA6384

P407

Q24324345-772B132E-54B4-4A15-B976-103BC31AE90A

P433

Q24324345-CE5E5374-D4D2-4BE5-8D36-885C5640BF5F

P478

Q24324345-ED69BE44-8EF7-439B-8C74-B36F3E077422

P50

Q24324345-24B5F91F-3C4D-4093-A7CB-561A670C8AD8

Q24324345-F08C9B7F-A00E-486B-85AF-7CE9A274BE27

P577

Q24324345-F4EBAF20-5724-417A-9DB8-89B6C0228984

P698

Q24324345-E84D5DA3-FDC0-42E0-86CE-05E25CC9D718

P921

Q24324345-4CE503E3-D02E-406B-AFF3-8DCCBF011EAE

Q24324345-B59761BB-C36F-409D-BABE-59B7E00CF5B7

P932

Q24324345-6A5775AA-4976-44D3-A3B0-B80CC3635671

P3181

P356

P1433

Biochemical Journal

P1476

The G2385R variant of leucine- ...... tial loss-of-function mutation

@en

P2093

Aleksandra Beylina

http://www.w3.org/2001/XMLSchema#string

Alice Kaganovich

http://www.w3.org/2001/XMLSchema#string

Dragan Maric

http://www.w3.org/2001/XMLSchema#string

Howard Jaffe

http://www.w3.org/2001/XMLSchema#string

Iakov N Rudenko

http://www.w3.org/2001/XMLSchema#string

Jinhui Ding

http://www.w3.org/2001/XMLSchema#string

Ruth Chia

http://www.w3.org/2001/XMLSchema#string

P2860

The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity

The R1441C mutation of LRRK2 disrupts GTP hydrolysis

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment

Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation

The familial Parkinsonism gene LRRK2 regulates neurite process morphology

The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation

Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

Is inhibition of kinase activity the only therapeutic strategy for LRRK2-associated Parkinson's disease?

P304

99-111

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1364119

http://www.w3.org/2001/XMLSchema#string

P356

10.1042/BJ20120637

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

446

http://www.w3.org/2001/XMLSchema#string

P50

P577

2012-08-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

22612223

http://www.w3.org/2001/XMLSchema#string

P921

Parkinson's disease

P932

4667980

http://www.w3.org/2001/XMLSchema#string