Structure, tissue distribution and genomic organization of the murine RRM-type RNA binding proteins TIA-1 and TIAR.
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Fas-activated serine/threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicingCell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication.U1 snRNP-dependent function of TIAR in the regulation of alternative RNA processing of the human calcitonin/CGRP pre-mRNAThe p53-dependent apoptotic pathway of breast cancer cells (BC-M1) induced by the bis-type bioreductive compound aziridinylnaphthoquinoneRole of stress granules and RNA-binding proteins in neurodegeneration: a mini-reviewInteraction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assemblyMutation of Mapped TIA-1/TIAR Binding Sites in the 3' Terminal Stem-Loop of West Nile Virus Minus-Strand RNA in an Infectious Clone Negatively Affects Genomic RNA AmplificationStructure of the central RNA recognition motif of human TIA-1 at 1.95Å resolutionT-cell intracellular antigens in health and diseaseTIA proteins are necessary but not sufficient for the tissue-specific splicing of the myosin phosphatase targeting subunit 1Welander distal myopathy is caused by a mutation in the RNA-binding protein TIA1Alternative pre-mRNA splicing regulation in cancer: pathways and programs unhingedCompetition of PTB with TIA proteins for binding to a U-rich cis-element determines tissue-specific splicing of the myosin phosphatase targeting subunit 1The splicing factor ASF/SF2 is associated with TIA-1-related/TIA-1-containing ribonucleoproteic complexes and contributes to post-transcriptional repression of gene expressionTIA-1 is a translational silencer that selectively regulates the expression of TNF-alphaRNA-binding protein TIAR is essential for primordial germ cell developmentThe RNA-binding protein TIA-1 is a novel mammalian splicing regulator acting through intron sequences adjacent to a 5' splice siteThe pivotal roles of TIA proteins in 5' splice-site selection of alu exons and across evolutionTissue- and age-dependent expression of RNA-binding proteins that influence mRNA turnover and translationPost-transcriptional regulation of tumour necrosis factor alpha production.TIA1 prevents skipping of a critical exon associated with spinal muscular atrophy.Different modes of interaction by TIAR and HuR with target RNA and DNANuclear protein TIA-1 regulates COL2A1 alternative splicing and interacts with precursor mRNA and genomic DNA.A systematic analysis of intronic sequences downstream of 5' splice sites reveals a widespread role for U-rich motifs and TIA1/TIAL1 proteins in alternative splicing regulation.RNA recognition and stress granule formation by TIA proteins.Visibly stressed: the role of eIF2, TIA-1, and stress granules in protein translation.Control of mRNA stability by SAPKs.Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.An essential function of the SRC-3 coactivator in suppression of cytokine mRNA translation and inflammatory response.Convergence of stress granules and protein aggregates in hippocampal cornu ammonis 1 at later reperfusion following global brain ischemiaThe translational repressor T-cell intracellular antigen-1 (TIA-1) is a key modulator of Th2 and Th17 responses driving pulmonary inflammation induced by exposure to house dust mite.Rabies Virus Infection Induces the Formation of Stress Granules Closely Connected to the Viral Factories.Distinct binding properties of TIAR RRMs and linker region.Inflammation: cytokines and RNA-based regulation.RBP45 and RBP47, two oligouridylate-specific hnRNP-like proteins interacting with poly(A)+ RNA in nuclei of plant cells.Molecular characterization of a TIA-1-like RNA-binding protein in cells derived from the fall armyworm Spodoptera frugiperda (Lepidoptera: Noctuidae).Genome-wide analysis of TIAR RNA ligands in mouse macrophages before and after LPS stimulation.TIA-1 Is a Functional Prion-Like Protein.Maintenance of the Innate Seizure Threshold by Cyclooxygenase-2 is Not Influenced by the Translational Silencer, T-cell Intracellular Antigen-1.Unraveling the Pathways to Neuronal Homeostasis and Disease: Mechanistic Insights into the Role of RNA-Binding Proteins and Associated Factors
P2860
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P2860
Structure, tissue distribution and genomic organization of the murine RRM-type RNA binding proteins TIA-1 and TIAR.
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
name
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@ast
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@en
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@nl
type
label
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@ast
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@en
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@nl
prefLabel
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@ast
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@en
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@nl
P2093
P2860
P356
P1476
Structure, tissue distribution ...... nding proteins TIA-1 and TIAR.
@en
P2093
P2860
P304
P356
10.1093/NAR/24.19.3829
P407
P577
1996-10-01T00:00:00Z