Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
about
Parallel manifestations of neuropathologies in the enteric and central nervous systemsPathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersThe function of RNA-binding proteins at the synapse: implications for neurodegenerationHistone methylation restrains the expression of subtype-specific genes during terminal neuronal differentiation in Caenorhabditis elegansHyperphosphorylation as a defense mechanism to reduce TDP-43 aggregationTDP-43 aggregation in neurodegeneration: are stress granules the key?DNAJB6 Myopathies: Focused Review on an Emerging and Expanding Group of MyopathiesTDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets.Identification of genetic modifiers of TDP-43 neurotoxicity in DrosophilaStress and aging induce distinct polyQ protein aggregation statesALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43.The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation.Selective forelimb impairment in rats expressing a pathological TDP-43 25 kDa C-terminal fragment to mimic amyotrophic lateral sclerosis.Protein misfolding specifies recruitment to cytoplasmic inclusion bodiesOverexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLSMyopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Inhibition of TDP-43 aggregation by nucleic acid bindingRNP2 of RNA recognition motif 1 plays a central role in the aberrant modification of TDP-43.TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNATargeting RNA binding proteins involved in neurodegeneration.Casein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins.UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination.Heterologous aggregates promote de novo prion appearance via more than one mechanism.TDP-43-based animal models of neurodegeneration: new insights into ALS pathology and pathophysiology.Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration.Exome sequencing reveals DNAJB6 mutations in dominantly-inherited myopathy.ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effectsTwo mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation.FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis.Genome-Wide Identification and Characterization of bZIP Transcription Factors in Brassica oleracea under Cold StressStructural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion.A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defectsLentiviral vector-mediated overexpression of mutant ataxin-7 recapitulates SCA7 pathology and promotes accumulation of the FUS/TLS and MBNL1 RNA-binding proteinsRNA-binding proteins in neurodegenerative disease: TDP-43 and beyond.Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones.
P2860
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P2860
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@ast
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@en
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@nl
type
label
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@ast
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@en
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@nl
prefLabel
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@ast
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@en
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.
@nl
P2093
P2860
P356
P1476
Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43
@en
P2093
Conrad C Weihl
Iga Wegorzewska
Jieya Shao
Marc I Diamond
Maria Udan
Robert H Baloh
Shaughn Bell
P2860
P304
26304-26314
P356
10.1074/JBC.M110.125039
P407
P577
2010-06-16T00:00:00Z