Corrigendum: Increased cytoplasmic TDP-43 reduces global protein synthesis by interacting with RACK1 on polyribosomes (original) (raw)

Increased Cytoplasmic TDP-43 Reduces Global Protein Synthesis by Interacting with RACK1 on Polyribosomes

Marcello Ceci

Human Molecular Genetics, 2017

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Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates

Peter ofosu Antwi crouch

Neurochemistry International, 2012

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TDP-43 Autoregulation: Implications for Disease

Emanuele Buratti

Journal of Molecular Neuroscience, 2011

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TDP-43 aggregation mirrors TDP-43 knockdown, affecting the expression levels of a common set of proteins

Emanuele Buratti

Scientific Reports, 2016

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TDP-43 regulates its mRNA levels through a negative feedback loop

Emanuele Buratti

The EMBO Journal, 2011

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Rsp5/NEDD4 and ESCRT regulate TDP-43 toxicity and turnover via an endolysosomal clearance mechanism

Lucas Marmorale

bioRxiv (Cold Spring Harbor Laboratory), 2022

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TDP-43: gumming up neurons through protein-protein and protein-RNA interactions

Emanuele Buratti

2012

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TDP-43 dysfunction results in R-loop accumulation and DNA replication defects

Annabel Quinet

Journal of Cell Science

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Functional implication of ubiquitinating and deubiquitinating mechanisms in TDP-43 proteinopathies

Nuoc Tran

2022

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RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy

Elsa Zacco

Brain, 2019

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Structural Insights Into TDP-43 and Effects of Post-translational Modifications

niloufar mollasalehi

Frontiers in Molecular Neuroscience

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The structural integrity of TDP-43 N-terminus is required for efficient aggregate entrapment and consequent loss of protein function

Emanuele Buratti

Prion, 2015

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Global Analysis of TDP-43 Interacting Proteins Reveals Strong Association with RNA Splicing and Translation Machinery

Raghu Chitta

Journal of Proteome Research, 2010

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TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1

xuan song

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Structural determinants of the cellular localization and shuttling of TDP-43

Emanuele Buratti

Journal of Cell Science, 2008

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TDP-43 post-translational modifications in health and disease

Emanuele Buratti

Expert Opinion on Therapeutic Targets, 2018

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TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules

Jocelyn Cote

Human Molecular Genetics, 2008

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Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies

Manuela Neumann

Journal of Biological Chemistry, 2009

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RACK1 Specifically Regulates Translation through Its Binding to Ribosomes

Piera Calamita

Molecular and Cellular Biology, 2018

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TDP-43 regulates the mammalian spinogenesis through translational repression of Rac1

信忠 鄭

Acta Neuropathologica, 2012

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Spatial proteomics reveal that the protein phosphatase PTP1B interacts with and may modify tyrosine phosphorylation of the rhomboid protease RHBDL4

Kyojiro N Ikeda

Journal of Biological Chemistry

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Chaperone Mediated Autophagy Degrades TDP-43 Protein and Is Affected by TDP-43 Aggregation

Javiera Rios

Frontiers in Molecular Neuroscience, 2020

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Distinct pathways leading to TDP-43-induced cellular dysfunctions

Masato Hosokawa

Human Molecular Genetics, 2014

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Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

Emanuele Buratti

Proceedings of the National Academy of Sciences, 2009

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ALS-Associated TDP-43 Induces Endoplasmic Reticulum Stress, Which Drives Cytoplasmic TDP-43 Accumulation and Stress Granule Formation

Sonam Parakh, Kai Soo, Bradley Turner, Julie Atkin

PLoS ONE, 2013

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