LRRK2 I2020T mutation is associated with tau pathology

scientific article published on 22 April 2012

LRRK2 I2020T mutation is associated with tau pathology is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/J.PARKRELDIS.2012.03.024
P698PubMed publication ID22525366

P50authorTaku HatanoQ42320293
Nobutaka HattoriQ64780524
P2093author name stringShigeto Sato
Shin-Ichiro Kubo
Fumihiko Sakai
Kazuko Hasegawa
Saburo Yagishita
Satoshi Imai
Toshiki Uchihara
Hisayuki Kowa
Sachiko Ujiie
P433issue7
P921main subjectpathologyQ7208
P1104number of pages5
P304page(s)819-823
P577publication date2012-04-22
P1433published inParkinsonism and Related DisordersQ15762600
P1476titleLRRK2 I2020T mutation is associated with tau pathology
P478volume18

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cites work (P2860)
Q99711175A Critical LRRK at the Synapse? The Neurobiological Function and Pathophysiological Dysfunction of LRRK2
Q92586724Advances in the Genetics of Parkinson's Disease: A Guide for the Clinician
Q38121773Advances in the genetics of Parkinson disease
Q46441393Analysis of neurodegenerative Mendelian genes in clinically diagnosed Alzheimer Disease
Q37590635Back to the tubule: microtubule dynamics in Parkinson's disease
Q36325683Cellular effects of LRRK2 mutations
Q33593798ERKed by LRRK2: a cell biological perspective on hereditary and sporadic Parkinson's disease
Q29347540G2385R and I2020T Mutations Increase LRRK2 GTPase Activity
Q94586186Genetic perspective on the synergistic connection between vesicular transport, lysosomal and mitochondrial pathways associated with Parkinson's disease pathogenesis
Q38233866Genetics and genomics of Parkinson's disease
Q27013695Heterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implications
Q38865951I2020T mutant LRRK2 iPSC-derived neurons in the Sagamihara family exhibit increased Tau phosphorylation through the AKT/GSK-3β signaling pathway
Q30587398Identification of a Japanese family with LRRK2 p.R1441G-related Parkinson's disease
Q51082143Interaction of LRRK2 and α-Synuclein in Parkinson's Disease.
Q98177378LRRK2 and Protein Aggregation in Parkinson's Disease: Insights From Animal Models
Q24338188LRRK2 phosphorylates novel tau epitopes and promotes tauopathy
Q36888947LRRK2: an éminence grise of Wnt-mediated neurogenesis?
Q37635000LRRK2: cause, risk, and mechanism
Q48264748Lack of exacerbation of neurodegeneration in a double transgenic mouse model of mutant LRRK2 and tau.
Q24338942Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3β
Q39104616Parkinson's disease-associated DJ-1 mutations increase abnormal phosphorylation of tau protein through Akt/GSK-3β pathways
Q48177425Pathological and Clinical Spectrum of Progressive Supranuclear Palsy: With Special Reference to Astrocytic Tau Pathology
Q21131229Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism
Q59099056Physiological and pathological functions of LRRK2: implications from substrate proteins
Q38214594Protein phosphorylation in neurodegeneration: friend or foe?
Q60141582Proteomic analysis reveals co-ordinated alterations in protein synthesis and degradation pathways in LRRK2 knockout mice
Q38160939Targeting leucine-rich repeat kinase 2 in Parkinson's disease
Q38482479The Role of α-Synuclein and LRRK2 in Tau Phosphorylation
Q38229792The association between the LRRK2 G2385R variant and the risk of Parkinson's disease: a meta-analysis based on 23 case-control studies
Q38111307The neurobiology of LRRK2 and its role in the pathogenesis of Parkinson's disease
Q26991986The regulation and deregulation of Wnt signaling by PARK genes in health and disease
Q38520438Type II kinase inhibitors show an unexpected inhibition mode against Parkinson's disease-linked LRRK2 mutant G2019S.

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