Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.
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Spatio-temporal Dynamics and Mechanisms of Stress Granule AssemblyStructure, dynamics and RNA binding of the multi-domain splicing factor TIA-1T-cell intracellular antigens in health and diseaseA Structure-free Method for Quantifying Conformational Flexibility in proteins.Topoisomerase 3β is the major topoisomerase for mRNAs and linked to neurodevelopment and mental dysfunction.TIA-1 RRM23 binding and recognition of target oligonucleotides.GraphProt: modeling binding preferences of RNA-binding proteins.The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain.RNA recognition and stress granule formation by TIA proteins.Alternative splicing of TIA-1 in human colon cancer regulates VEGF isoform expression, angiogenesis, tumour growth and bevacizumab resistance.Boric acid induces cytoplasmic stress granule formation, eIF2α phosphorylation, and ATF4 in prostate DU-145 cells.Distinct binding properties of TIAR RRMs and linker region.RNA binding of T-cell intracellular antigen-1 (TIA-1) C-terminal RNA recognition motif is modified by pH conditions.Pick one, but be quick: 5' splice sites and the problems of too many choices.A Non-Invasive NMR Method Based on Histidine Imidazoles to Analyze the pH-Modulation of Protein-Nucleic Acid Interfaces.Deciphering the protein-RNA recognition code: combining large-scale quantitative methods with structural biology.Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicingSelection preserves Ubiquitin Specific Protease 4 alternative exon skipping in therian mammals.KSHV inhibits stress granule formation by viral ORF57 blocking PKR activation.KH-type splicing regulatory protein is involved in esophageal squamous cell carcinoma progression.Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.Linking hnRNP Function to ALS and FTD Pathology.Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins
P2860
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P2860
Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Three RNA recognition motifs p ...... he pro-apoptotic factor TIA-1.
@ast
Three RNA recognition motifs p ...... he pro-apoptotic factor TIA-1.
@en
type
label
Three RNA recognition motifs p ...... he pro-apoptotic factor TIA-1.
@ast
Three RNA recognition motifs p ...... he pro-apoptotic factor TIA-1.
@en
prefLabel
Three RNA recognition motifs p ...... he pro-apoptotic factor TIA-1.
@ast
Three RNA recognition motifs p ...... he pro-apoptotic factor TIA-1.
@en
P2860
P1476
Three RNA recognition motifs p ...... he pro-apoptotic factor TIA-1.
@en
P2093
Jason Heath
William J Bauer
P2860
P304
P356
10.1016/J.JMB.2011.11.040
P407
P577
2011-12-02T00:00:00Z