A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport.
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TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNAPathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersInteraction of RNA with a C-terminal fragment of the amyotrophic lateral sclerosis-associated TDP43 reduces cytotoxicityTDP-1/TDP-43 regulates stress signaling and age-dependent proteotoxicity in Caenorhabditis elegansTDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets.A 43-kDa TDP-43 species is present in aggregates associated with frontotemporal lobar degenerationOverexpression of ALS-associated p.M337V human TDP-43 in mice worsens disease features compared to wild-type human TDP-43 mice.Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasmDifferential roles of the ubiquitin proteasome system and autophagy in the clearance of soluble and aggregated TDP-43 speciesDistinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusionsKinase Inhibitor Screening Identifies Cyclin-Dependent Kinases and Glycogen Synthase Kinase 3 as Potential Modulators of TDP-43 Cytosolic Accumulation during Cell Stress.Novel monoclonal antibodies to normal and pathologically altered human TDP-43 proteins.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Coaggregation of RNA-binding proteins in a model of TDP-43 proteinopathy with selective RGG motif methylation and a role for RRM1 ubiquitinationInhibition of TDP-43 aggregation by nucleic acid bindingRNP2 of RNA recognition motif 1 plays a central role in the aberrant modification of TDP-43.Casein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins.Aberrant septin 11 is associated with sporadic frontotemporal lobar degeneration.Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration.Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice.Pharmacological Modulation of the N-End Rule Pathway and Its Therapeutic Implications.Amyotrophic lateral sclerosis and organ donation: is there risk of disease transmission?Prions and the potential transmissibility of protein misfolding diseasesThe truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation.Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43)Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion.Disease animal models of TDP-43 proteinopathy and their pre-clinical applications.Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43.TDP-43 autoregulation: implications for disease.RNA-binding proteins with prion-like domains in ALS and FTLD-U.Progranulin and TDP-43: mechanistic links and future directions.Protein misdirection inside and outside motor neurons in Amyotrophic Lateral Sclerosis (ALS): a possible clue for therapeutic strategiesCan regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation?Protein truncation as a common denominator of human neurodegenerative foldopathies.Old versus New Mechanisms in the Pathogenesis of ALS.Physiological functions and clinical implications of the N-end rule pathway.Prion-like propagation as a pathogenic principle in frontotemporal dementia.Robust cytoplasmic accumulation of phosphorylated TDP-43 in transgenic models of tauopathy.TDP-43 suppresses CGG repeat-induced neurotoxicity through interactions with HnRNP A2/B1.
P2860
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P2860
A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին 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
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@ast
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@en
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@nl
type
label
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@ast
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@en
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@nl
prefLabel
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@ast
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@en
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@nl
P2093
P2860
P356
P1476
A "two-hit" hypothesis for inc ...... crotubule-dependent transport.
@en
P2093
G Scott Pesiridis
Kalyan Tripathy
Selçuk Tanik
Virginia M-Y Lee
P2860
P304
18845-18855
P356
10.1074/JBC.M111.231118
P407
P577
2011-03-24T00:00:00Z