O‐GlcNAcylation of TDP‐43 suppresses proteinopathies and promotes TDP‐43’s mRNA splicing activity
Published 2021 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
O‐GlcNAcylation of TDP‐43 suppresses proteinopathies and promotes TDP‐43’s mRNA splicing activity
Authors
Keywords
-
Journal
EMBO REPORTS
Volume -, Issue -, Pages -
Publisher
EMBO
Online
2021-04-16
DOI
10.15252/embr.202051649
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- ALS-implicated protein TDP-43 sustains levels of STMN2, a mediator of motor neuron growth and repair
- (2019) Joseph R. Klim et al. NATURE NEUROSCIENCE
- Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration
- (2019) Ze’ev Melamed et al. NATURE NEUROSCIENCE
- Glycolysis upregulation is neuroprotective as a compensatory mechanism in ALS
- (2019) Ernesto Manzo et al. eLife
- RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy
- (2019) Han-Jou Chen et al. BRAIN
- NPGPx-Mediated Adaptation to Oxidative Stress Protects Motor Neurons from Degeneration in Aging by Directly Modulating O-GlcNAcase
- (2019) Yung-Lin Hsieh et al. Cell Reports
- Identification of a subnuclear body involved in sequence-specific cytokine RNA processing
- (2015) Sungwook Lee et al. Nature Communications
- An acetylation switch controls TDP-43 function and aggregation propensity
- (2015) Todd J. Cohen et al. Nature Communications
- O-GlcNAc and neurodegeneration: biochemical mechanisms and potential roles in Alzheimer's disease and beyond
- (2014) Scott A. Yuzwa et al. CHEMICAL SOCIETY REVIEWS
- CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration
- (2013) Nicole F. Liachko et al. ANNALS OF NEUROLOGY
- TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo
- (2013) Darshana K. Choksi et al. HUMAN MOLECULAR GENETICS
- Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
- (2013) Shuo-Chien Ling et al. NEURON
- ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43
- (2013) E. S. Arnold et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations
- (2012) J. G. Daigle et al. HUMAN MOLECULAR GENETICS
- Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation
- (2012) Scott A Yuzwa et al. Nature Chemical Biology
- Reduced protein O-glycosylation in the nervous system of the mutant SOD1 transgenic mouse model of amyotrophic lateral sclerosis
- (2012) Xiaoyang Shan et al. NEUROSCIENCE LETTERS
- Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing
- (2011) Mei-Xia Che et al. FASEB JOURNAL
- Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS
- (2011) Patricia S. Estes et al. HUMAN MOLECULAR GENETICS
- The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span
- (2011) Ji-Wu Wang et al. JOURNAL OF CLINICAL INVESTIGATION
- Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
- (2011) Lionel M. Igaz et al. JOURNAL OF CLINICAL INVESTIGATION
- Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
- (2011) Magdalini Polymenidou et al. NATURE NEUROSCIENCE
- Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
- (2011) James R Tollervey et al. NATURE NEUROSCIENCE
- Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
- (2011) Edward B. Lee et al. NATURE REVIEWS NEUROSCIENCE
- Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies
- (2011) Yohei Iguchi et al. NEUROBIOLOGY OF DISEASE
- TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
- (2011) Todd J. Cohen et al. TRENDS IN MOLECULAR MEDICINE
- Cytoplasmic Mislocalization of TDP-43 Is Toxic to Neurons and Enhanced by a Mutation Associated with Familial Amyotrophic Lateral Sclerosis
- (2010) S. J. Barmada et al. JOURNAL OF NEUROSCIENCE
- A Drosophila model for TDP-43 proteinopathy
- (2010) Y. Li et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo
- (2009) Edor Kabashi et al. HUMAN MOLECULAR GENETICS
- Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
- (2009) G. S. Pesiridis et al. HUMAN MOLECULAR GENETICS
- Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
- (2009) Y.-J. Zhang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
- (2008) Masato Hasegawa et al. ANNALS OF NEUROLOGY
- A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
- (2008) Scott A Yuzwa et al. Nature Chemical Biology
- A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
- (2008) B. S. Johnson et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
- (2008) J. Sreedharan et al. SCIENCE
- Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
- (2007) Emanuele Buratti Frontiers in Bioscience-Landmark
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started