Cargando…

Correction: Phosphorylation-Dependent 14-3-3 Binding to LRRK2 Is Impaired by Common Mutations of Familial Parkinson's Disease

Detalles Bibliográficos
Autores principales:	Li, Xianting, Wang, Qing Jun, Pan, Nina, Lee, Sangkyu, Zhao, Yingming, Chait, Brian T., Yue, Zhenyu
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2011
Materias:	Correction
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3144976/ http://dx.doi.org/10.1371/annotation/e66e7e90-9503-46b8-91f9-abe4d5056ba1

Ejemplares similares

Phosphorylation-Dependent 14-3-3 Binding to LRRK2 Is Impaired by Common Mutations of Familial Parkinson's Disease
por: Li, Xianting, et al.
Publicado: (2011)

PAK6 Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2
por: Civiero, Laura, et al.
Publicado: (2017)

14-3-3 phosphorylation inhibits 14-3-3θ’s ability to regulate LRRK2 kinase activity
por: Pattanayak, Rudradip, et al.
Publicado: (2023)

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization
por: Nichols, R. Jeremy, et al.
Publicado: (2010)

RAB3 phosphorylation by pathogenic LRRK2 impairs trafficking of synaptic vesicle precursors
por: Dou, Dan, et al.
Publicado: (2023)

Arsenite Stress Down-regulates Phosphorylation and 14-3-3 Binding of Leucine-rich Repeat Kinase 2 (LRRK2), Promoting Self-association and Cellular Redistribution
por: Mamais, Adamantios, et al.
Publicado: (2014)

Short- and Long-Term Effects of LRRK2 on Axon and Dendrite Growth
por: Sepulveda, Bryan, et al.
Publicado: (2013)

Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms
por: Malik, Asad U., et al.
Publicado: (2021)

Trafficking of the glutamate transporter is impaired in LRRK2-related Parkinson’s disease
por: Iovino, Ludovica, et al.
Publicado: (2022)

Parkinson-Related LRRK2 Mutation R1628P Enables Cdk5 Phosphorylation of LRRK2 and Upregulates Its Kinase Activity
por: Shu, Yang, et al.
Publicado: (2016)

Structural basis for Parkinson’s disease-linked LRRK2’s binding to microtubules
por: Snead, David M., et al.
Publicado: (2022)

Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism
por: Taymans, Jean-Marc, et al.
Publicado: (2014)

Progress in LRRK2-Associated Parkinson’s Disease Animal Models
por: Seegobin, Steven P., et al.
Publicado: (2020)

An Assessment of LRRK2 Serine 935 Phosphorylation in Human Peripheral Blood Mononuclear Cells in Idiopathic Parkinson’s Disease and G2019S LRRK2 Cohorts
por: Padmanabhan, Shalini, et al.
Publicado: (2020)

LRRK2 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding
por: Taymans, Jean-Marc, et al.
Publicado: (2011)

LRRK2 Phosphorylation, More Than an Epiphenomenon
por: Marchand, Antoine, et al.
Publicado: (2020)

GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2
por: Blanca Ramírez, Marian, et al.
Publicado: (2017)

Models for LRRK2-Linked Parkinsonism
por: Li, Tianxia, et al.
Publicado: (2011)

The role of the LRRK2 gene in Parkinsonism
por: Li, Jie-Qiong, et al.
Publicado: (2014)

LRRK2 and Proteostasis in Parkinson’s Disease
por: Pérez-Carrión, María Dolores, et al.
Publicado: (2022)

Targeting LRRK2 in Parkinson’s disease
por: Xiao, Bin, et al.
Publicado: (2022)

PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2-mediated phosphorylation at Threonine72
por: Vieweg, Sophie, et al.
Publicado: (2020)

‘Up with the LRRK’: a phosphorylated Rab10 assay for evaluation of LRRK2 activity and inhibitor engagement
por: Eyers, Patrick A.
Publicado: (2016)

Cognitive Impairments in LRRK2-Related Parkinson's Disease: A Study in Chinese Individuals
por: Zheng, Yifan, et al.
Publicado: (2015)

The Role of α-Synuclein and LRRK2 in Tau Phosphorylation
por: Kawakami, Fumitaka, et al.
Publicado: (2015)

Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization
por: Dzamko, Nicolas, et al.
Publicado: (2010)

Analysis of DNM3 and VAMP4 as genetic modifiers of LRRK2 Parkinson’s disease
por: Brown, Emmeline E., et al.
Publicado: (2021)

The Parkinson's Disease Associated LRRK2 Exhibits Weaker In Vitro Phosphorylation of 4E-BP Compared to Autophosphorylation
por: Kumar, Azad, et al.
Publicado: (2010)

Interrogating Parkinson's disease LRRK2 kinase pathway activity by assessing Rab10 phosphorylation in human neutrophils
por: Fan, Ying, et al.
Publicado: (2018)

Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation
por: Madero-Pérez, Jesús, et al.
Publicado: (2018)

Accurate MS-based Rab10 Phosphorylation Stoichiometry Determination as Readout for LRRK2 Activity in Parkinson's Disease
por: Karayel, Özge, et al.
Publicado: (2020)

The IkappaB Kinase Family Phosphorylates the Parkinson’s Disease Kinase LRRK2 at Ser935 and Ser910 during Toll-Like Receptor Signaling
por: Dzamko, Nicolas, et al.
Publicado: (2012)

Rare variants in LRRK1 and Parkinson's disease
por: Schulte, Eva C., et al.
Publicado: (2013)

The Role of LRRK2 in Neurodegeneration of Parkinson Disease
por: Rui, Qin, et al.
Publicado: (2018)

LRRK2 and the Endolysosomal System in Parkinson’s Disease
por: Erb, Madalynn L., et al.
Publicado: (2020)

LRRK2 at the Crossroad of Aging and Parkinson’s Disease
por: Hur, Eun-Mi, et al.
Publicado: (2021)

Pathological Functions of LRRK2 in Parkinson’s Disease
por: Jeong, Ga Ram, et al.
Publicado: (2020)

Modeling Parkinson’s disease in LRRK2 rodents
por: Domenicale, Chiara, et al.
Publicado: (2023)

Functional Analyses of Two Novel LRRK2 Pathogenic Variants in Familial Parkinson′s Disease
por: Coku, Ilda, et al.
Publicado: (2022)

Phosphorylation of S776 and 14-3-3 Binding Modulate Ataxin-1 Interaction with Splicing Factors
por: de Chiara, Cesira, et al.
Publicado: (2009)

Cannot write session to /tmp/vufind_sessions/sess_lvut5lou493jv2ski4iikq1jcp