The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids
about
TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNATrinucleotide expansion in disease: why is there a length threshold?Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation.Structural Dynamics of Human Argonaute2 and Its Interaction with siRNAs Designed to Target Mutant tdp43.Cytoplasmic Relocalization of TAR DNA-Binding Protein 43 Is Not Sufficient to Reproduce Cellular Pathologies Associated with ALS In vitro.An acetylation switch controls TDP-43 function and aggregation propensity.The Role of TDP-43 in Alzheimer's Disease.The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity.TDP-43/FUS in motor neuron disease: Complexity and challenges.Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program.A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43.Predicted RNA Binding Proteins Pes4 and Mip6 Regulate mRNA Levels, Translation, and Localization during Sporulation in Budding Yeast.Comparative analysis of thermal unfolding simulations of RNA recognition motifs (RRMs) of TAR DNA-binding protein 43 (TDP-43).Regulatory Role of RNA Chaperone TDP-43 for RNA Misfolding and Repeat-Associated Translation in SCA31.Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.The proteinopathy of D169G and K263E mutants at the RNA Recognition Motif (RRM) domain of tar DNA-binding protein (tdp43) causing neurological disorders: A computational study.Streptococcus pneumoniae Genome-wide Identification and Characterization of BOX Element-binding Domains.Analysis of the substrate recognition state of TDP-43 to single-stranded DNA using fluorescence correlation spectroscopy.Linking hnRNP Function to ALS and FTD Pathology.
P2860
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P2860
The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids
description
2014 nî lūn-bûn
@nan
2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@ast
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@en
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@nl
type
label
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@ast
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@en
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@nl
prefLabel
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@ast
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@en
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@nl
P2093
P2860
P356
P1476
The crystal structure of TDP-4 ...... UG- and TG-rich nucleic acids
@en
P2093
Chien-Hao Chiang
Lyudmila G Doudeva
Pan-Hsien Kuo
Yi-Ting Wang
P2860
P304
P356
10.1093/NAR/GKT1407
P407
P50
P577
2014-04-01T00:00:00Z