LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations
about
LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowthParkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3An early endosome regulator, Rab5b, is an LRRK2 kinase substrateLRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25LRRK2 phosphorylates novel tau epitopes and promotes tauopathyMutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neuronsCurrent understanding of LRRK2 in Parkinson's disease: biochemical and structural features and inhibitor designPhosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPasesG2385R and I2020T Mutations Increase LRRK2 GTPase ActivityLeucine-rich repeat kinase 2 for beginners: six key questions.Regulation of DJ-1 by Glutaredoxin 1 in Vivo: Implications for Parkinson's Disease.Ursocholanic acid rescues mitochondrial function in common forms of familial Parkinson's disease.Leucine-Rich Repeat Kinase 2 (LRRK2) phosphorylates p53 and induces p21(WAF1/CIP1) expressionTherapeutic effects of microRNA-582-5p and -3p on the inhibition of bladder cancer progression.Development of inducible leucine-rich repeat kinase 2 (LRRK2) cell lines for therapeutics development in Parkinson's disease.Phosphorylation of LRRK2: from kinase to substrate.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).The Role of α-Synuclein and LRRK2 in Tau Phosphorylation.I2020T mutant LRRK2 iPSC-derived neurons in the Sagamihara family exhibit increased Tau phosphorylation through the AKT/GSK-3β signaling pathway.Leucine-rich repeat kinase 2 exacerbates neuronal cytotoxicity through phosphorylation of histone deacetylase 3 and histone deacetylation.Development of an enzyme-linked immunosorbent assay for detection of cellular and in vivo LRRK2 S935 phosphorylation.Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN-1.LRRK2: dropping (kinase) inhibitions and seeking an (immune) response.Genetic dissection reveals that Akt is the critical kinase downstream of LRRK2 to phosphorylate and inhibit FOXO1, and promotes neuron survival.
P2860
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P2860
LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
LRRK2 directly phosphorylates ...... s disease-associated mutations
@ast
LRRK2 directly phosphorylates ...... s disease-associated mutations
@en
LRRK2 directly phosphorylates ...... s disease-associated mutations
@en-gb
LRRK2 directly phosphorylates ...... s disease-associated mutations
@nl
type
label
LRRK2 directly phosphorylates ...... s disease-associated mutations
@ast
LRRK2 directly phosphorylates ...... s disease-associated mutations
@en
LRRK2 directly phosphorylates ...... s disease-associated mutations
@en-gb
LRRK2 directly phosphorylates ...... s disease-associated mutations
@nl
prefLabel
LRRK2 directly phosphorylates ...... s disease-associated mutations
@ast
LRRK2 directly phosphorylates ...... s disease-associated mutations
@en
LRRK2 directly phosphorylates ...... s disease-associated mutations
@en-gb
LRRK2 directly phosphorylates ...... s disease-associated mutations
@nl
P2093
P2860
P3181
P1433
P1476
LRRK2 directly phosphorylates ...... s disease-associated mutations
@en
P2093
Etsuro Ohta
Fumitaka Kawakami
Fumiya Obata
Makoto Kubo
P2860
P304
P3181
P356
10.1016/J.FEBSLET.2011.05.044
P407
P577
2011-07-21T00:00:00Z