Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
about
Ubiquilin-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-43Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseDoes a loss of TDP-43 function cause neurodegeneration?Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregationMolecular basis of UG-rich RNA recognition by the human splicing factor TDP-43TDP-43 identified from a genome wide RNAi screen for SOD1 regulatorsKnockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43.Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.Wild type human TDP-43 potentiates ALS-linked mutant TDP-43 driven progressive motor and cortical neuron degeneration with pathological features of ALS.The localization of hnRNP A2/B1 in nuclear matrix and the aberrant expression during the RA-induced differentiation of human neuroblastoma SK-N-SH cells.Kinase Inhibitor Screening Identifies Cyclin-Dependent Kinases and Glycogen Synthase Kinase 3 as Potential Modulators of TDP-43 Cytosolic Accumulation during Cell Stress.TDP-43 regulates its mRNA levels through a negative feedback loop.TDP-43 regulates Drosophila neuromuscular junctions growth by modulating Futsch/MAP1B levels and synaptic microtubules organizationTAR DNA-binding protein 43 in neurodegenerative disease.The influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.Neurotoxic effects of TDP-43 overexpression in C. elegans.Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor.TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1.C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stressAlteration of POLDIP3 splicing associated with loss of function of TDP-43 in tissues affected with ALSReview: transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration.Targeting RNA binding proteins involved in neurodegeneration.A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport.UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination.Regulation of autophagy by neuropathological protein TDP-43.Altered RNA metabolism and amyotrophic lateral sclerosisGains or losses: molecular mechanisms of TDP43-mediated neurodegeneration.The hnRNP-Htt axis regulates necrotic cell death induced by transcriptional repression through impaired RNA splicing.Augmented quantal release of acetylcholine at the vertebrate neuromuscular junction following tdp-43 depletion.Long non-coding RNA gadd7 interacts with TDP-43 and regulates Cdk6 mRNA decay.Misregulation of human sortilin splicing leads to the generation of a nonfunctional progranulin receptor.Spliceosome integrity is defective in the motor neuron diseases ALS and SMA.TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD.A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defectsMutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones.
P2860
Q24337496-3E230AB2-54C1-4097-95CD-4DE01E513E3EQ24338199-EA8BE806-AD07-4EDD-82FD-61E37DE4B3C1Q24594172-32E94FFF-415D-4215-BBBC-CAECE157B9FEQ26753190-0A6D1FB8-BEA0-4F4A-929D-41FDF1432528Q27026848-63F5367D-197B-4D92-9363-57F0C0925245Q27325625-B40A0F90-3F54-4E67-B6A0-9B74E315E568Q27687574-938C6620-357D-4FE4-BCCB-964AF3D93BB0Q28482611-ADD9D403-78CB-446A-94A4-B0DA81CE28C9Q30492839-5680752C-BEFC-48A3-8AFC-7C53636577FBQ30536540-8A0A1732-4AAD-4CCA-9B42-86C9E749D332Q30538184-6239C944-4C3A-4FDB-BC2C-E8E80B411EA5Q30655551-5D343A7F-69AF-40DD-A0C7-54C6492EF706Q30999965-D6E482FF-3A85-4EF1-B176-8F2AF43EC9F7Q31122876-86B451EC-5617-4F4A-97C4-560F5C28A4ECQ33763346-A0C28AB6-3FB1-4E43-8D7B-EA3755C97A56Q33849007-4D238336-DC9C-4FC2-A5E2-B8E8221BAC20Q33941040-58B46435-C87E-420E-B18B-64869E0D341AQ33999609-D7F68F69-53D0-455A-A4E0-FB3136A8FD39Q34013543-785CA690-E82A-4A88-99C6-F740A42F515FQ34074385-7D215481-EAD0-42D8-9651-9B049CB66262Q34155890-326FABB8-F3D2-40E3-8FFE-687BB513F582Q34160352-F919D45D-0FD0-4E74-88E5-55BF041E2014Q34206209-5EFE96BD-55D9-4E1A-A459-AAA852DC7F23Q34382817-5051947D-4241-4537-BF83-210F447C4B19Q34642738-A9A2C67D-BFE9-4710-BE59-8C55C92C314EQ34954162-CB5A4900-E8BB-4CF2-BEFC-D5A39D3AB8C9Q34998181-986AB67C-3586-45CD-86D9-B9BE5BBA6D94Q35168278-3A3C374C-9F58-481E-B29A-7D68E4443AC3Q35639841-64695AF8-8E7F-4BD2-A31E-003B70D7B51DQ35732120-1E0607BE-8D91-48E0-A712-E3F832630001Q35773678-EE1893EA-DEF7-4BF3-9864-63027FC2BA33Q36002020-883331D9-40B4-428F-B0EB-B018CA9FF60DQ36363305-44E98D9D-05C9-4BED-A7DB-CF663E39FB41Q36440463-D956198B-61AD-4288-9336-857B74B35CCFQ36504281-24FD52F1-F553-4B94-B7CF-C6E0DA95C0CAQ36602121-9B1D1BC0-6812-4A1B-BF23-A261788A5E7FQ36781316-16E8A69B-AE53-4B3A-91AF-96CC02DBCCC1Q37036144-ED746A11-D312-4822-9F5E-AEE69D28B4A9Q37379471-8F9D42C5-15ED-4841-9448-C68DE8CD21DBQ37380181-FC66A8C2-5F5C-42CC-A26C-F69BC503CF7B
P2860
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 08 May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
@en
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo.
@nl
type
label
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
@en
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo.
@nl
prefLabel
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
@en
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo.
@nl
P2093
P2860
P356
P1476
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
@en
P2093
Andrea D'Ambrogio
Corrado Guarnaccia
Cristiana Stuani
Francisco E Baralle
Youhna M Ayala
P2860
P304
P356
10.1093/NAR/GKP342
P407
P577
2009-05-08T00:00:00Z