Structural insights into TDP-43 in nucleic-acid binding and domain interactions
about
Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linkingMolecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of functionUbiquilin-2 (UBQLN2) binds with high affinity to the C-terminal region of TDP-43 and modulates TDP-43 levels in H4 cells: characterization of inhibition by nucleic acids and 4-aminoquinolinesTDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNATARDBP mutation analysis in TDP-43 proteinopathies and deciphering the toxicity of mutant TDP-43A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusionsThe extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivoPathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersThe structure, function and evolution of proteins that bind DNA and RNADoes a loss of TDP-43 function cause neurodegeneration?Interaction of RNA with a C-terminal fragment of the amyotrophic lateral sclerosis-associated TDP43 reduces cytotoxicityCrystal Structure of the RNA Recognition Motif of Yeast Translation Initiation Factor eIF3b Reveals Differences to Human eIF3bPub1p C-Terminal RRM Domain Interacts with Tif4631p through a Conserved Region Neighbouring the Pab1p Binding SiteThe crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acidsMolecular basis of UG-rich RNA recognition by the human splicing factor TDP-43Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexesTDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degenerationThe dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation.Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasmNovel monoclonal antibodies to normal and pathologically altered human TDP-43 proteins.Mitochondrial dysfunction and decrease in body weight of a transgenic knock-in mouse model for TDP-43.Development of a novel nonradiometric assay for nucleic acid binding to TDP-43 suitable for high-throughput screening using AlphaScreen technology.TDP-43 suppresses tau expression via promoting its mRNA instability.TDP-43 regulates its mRNA levels through a negative feedback loop.The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanismNeuronal function and dysfunction of Drosophila dTDPDeletion of TDP-43 down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism.Dual vulnerability of TDP-43 to calpain and caspase-3 proteolysis after neurotoxic conditions and traumatic brain injuryTDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor.Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA.Coaggregation of RNA-binding proteins in a model of TDP-43 proteinopathy with selective RGG motif methylation and a role for RRM1 ubiquitinationDisease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-lifeConserved acidic amino acid residues in a second RNA recognition motif regulate assembly and function of TDP-43.An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution.Review: transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration.Inhibition of TDP-43 aggregation by nucleic acid bindingA "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport.Aberrant RNA homeostasis in amyotrophic lateral sclerosis: potential for new therapeutic targets?Aging--RNA in development and disease.Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration.
P2860
Q24300438-361E9752-B8AB-43EA-8E14-C76991F754E3Q24314515-D1391017-0989-4CC5-8488-F78749294BFBQ24337496-534ADC0D-366B-4753-988A-B4F243470ECFQ24338199-6A16C55F-76F9-40D3-AEB2-29108EB26E40Q24594172-A6CFAD21-E3D0-4178-9D09-3C39A72DD307Q24632492-18C10DFF-1642-4973-8461-2C3672854415Q26751400-E11BBDD0-3429-4B76-9684-C99EBF063D86Q26828357-61C259C6-97B4-45CE-89FF-5B377FE2DBDAQ27003938-37312AA5-809C-40F6-A127-D549EF7F498BQ27026848-F5229521-48E1-4557-8C82-3B80524C617FQ27301865-04222116-CF30-405B-AED5-A9E78A680392Q27664645-B95185EA-0800-404F-ADDE-91314336A3D4Q27674307-CD6B0EF3-1840-45C5-841A-9219C2E65F79Q27681463-708173B7-B0DF-4BA9-B94C-C8E796122137Q27687574-07F53185-FC76-4419-A542-0D38CAD639E2Q28297716-52AFB325-9673-492A-8F9B-BFFFB1FA35DFQ30493749-496A2692-0E24-402A-B9AF-C11BAE9DAA5EQ30541099-B0683CDE-9D8E-4EA5-B748-3744B1667120Q30559680-504AB00C-255C-46EA-A713-CE1CF95AC4C5Q33622382-AE516C61-1575-42D2-9274-7233C3B1C318Q33675871-556F4451-7A71-4DC7-B27F-9A601D30ED8CQ33696882-6CA06794-9481-4601-B55E-D313655B009CQ33740999-F4FA343C-B3AC-452E-8664-6919FB2A402BQ33763346-3CF75C4D-0AE8-47F7-8539-D2108690B8DAQ33786698-E3AD02F0-7529-4DA7-816E-906F7C0F39CAQ33932740-63B85627-C8BF-40E7-804C-C3C9D5479EE3Q34136356-49A5A6F6-AF95-4201-8C36-6F5FC545634AQ34153412-AB9AC757-3B17-474A-9C26-B5906A6104DAQ34155890-9C6C1543-58AC-44BD-862F-13D25A5DF063Q34232143-B89E5CBB-6C2C-408E-B8C7-ACA915143553Q34285952-7C8EE927-4E2F-4933-AAB1-51E67FB1927FQ34408072-7342B748-80A4-47B0-82A2-9B69A7E69846Q34541179-F108FB70-BC07-4E14-82A7-5EA1BF67504CQ34575728-D62077CE-B874-49C1-B084-2E4DA5625316Q34642738-2F2ADD2F-82BD-45D6-BEB4-CB67E2C498F6Q34758540-95BFBB72-3D24-4A59-8325-48117508BC98Q34998181-F2157073-3EFE-407C-B81F-0BBB6C257C62Q35019375-394CF57C-56E4-4BB5-B94C-BAB7D8A753E0Q35605882-B89048E4-E21B-4E77-87CA-F2F79D6975E5Q35773678-48879BFD-0D18-4778-B47D-EA3251F2B0E4
P2860
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@ast
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@en
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@nl
type
label
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@ast
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@en
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@nl
prefLabel
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@ast
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@en
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@nl
P2093
P2860
P3181
P356
P1476
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
@en
P2093
Che-Kun James Shen
Hanna S Yuan
Lyudmila G Doudeva
Pan-Hsien Kuo
Yi-Ting Wang
P2860
P304
P3181
P356
10.1093/NAR/GKP013
P407
P577
2009-04-01T00:00:00Z