Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation.
about
Picornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virusThe structures of nonprotein-coding RNAs that drive internal ribosome entry site functionInsights into the Biology of IRES Elements through Riboproteomic ApproachesCrystallographic Analysis of Polypyrimidine Tract-Binding Protein-Raver1 Interactions Involved in Regulation of Alternative SplicingNuclear proteins hijacked by mammalian cytoplasmic plus strand RNA virusesActivation of picornaviral IRESs by PTB shows differential dependence on each PTB RNA-binding domainThe mechanism of translation initiation on Type 1 picornavirus IRESsPolypyrimidine tract binding protein functions as a negative regulator of feline calicivirus translationPolypyrimidine tract-binding protein stimulates the poliovirus IRES by modulating eIF4G binding.PTBP1 is required for embryonic development before gastrulation.PTBP1 is required for glucose-stimulated cap-independent translation of insulin granule proteins and Coxsackieviruses in beta cellsStress-inducible alternative translation initiation of human cytomegalovirus latency protein pUL138.40S recruitment in the absence of eIF4G/4A by EMCV IRES refines the model for translation initiation on the archetype of Type II IRESshnRNP Q and PTB modulate the circadian oscillation of mouse Rev-erb alpha via IRES-mediated translation.A cytoplasmic RNA virus generates functional viral small RNAs and regulates viral IRES activity in mammalian cellsCommon conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors.Far upstream element binding protein 1 binds the internal ribosomal entry site of enterovirus 71 and enhances viral translation and viral growth.A distinct class of internal ribosomal entry site in members of the Kobuvirus and proposed Salivirus and Paraturdivirus genera of the Picornaviridae.Neuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2.The current status of vertebrate cellular mRNA IRESsPolypyrimidine tract binding protein 1 protects mRNAs from recognition by the nonsense-mediated mRNA decay pathway.Cell type specificity and structural determinants of IRES activity from the 5' leaders of different HIV-1 transcriptsHigh-affinity interaction of hnRNP A1 with conserved RNA structural elements is required for translation and replication of enterovirus 71.RNA-binding proteins impacting on internal initiation of translation.U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression.Defining the roles and interactions of PTB.Viral subversion of host functions for picornavirus translation and RNA replication.New insights into functional roles of the polypyrimidine tract-binding protein.Human polypyrimidine tract-binding protein interacts with mitochondrial tRNA(Thr) in the cytosol.Secondary RNA structure and nucleotide specificity contribute to internal initiation mediated by the human tau 5' leader.The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES.Designing synthetic RNAs to determine the relevance of structural motifs in picornavirus IRES elements.Polypyrimidine tract-binding protein binds to the 5' untranslated region of the mouse mammary tumor virus mRNA and stimulates cap-independent translation initiation.Structural modeling of protein-RNA complexes using crosslinking of segmentally isotope-labeled RNA and MS/MSSequence features of viral and human Internal Ribosome Entry Sites predictive of their activity.Structural insights into the targeting of mRNA GU-rich elements by the three RRMs of CELF1.The organization of RNA contacts by PTB for regulation of FAS splicing.In silico analysis of IRES RNAs of foot-and-mouth disease virus and related picornaviruses.Viral internal ribosomal entry sites: four classes for one goal.The devil is in the domain: understanding protein recognition of multiple RNA targets.
P2860
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P2860
Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Polypyrimidine tract binding p ...... sites in a unique orientation.
@en
Polypyrimidine tract binding p ...... sites in a unique orientation.
@nl
type
label
Polypyrimidine tract binding p ...... sites in a unique orientation.
@en
Polypyrimidine tract binding p ...... sites in a unique orientation.
@nl
prefLabel
Polypyrimidine tract binding p ...... sites in a unique orientation.
@en
Polypyrimidine tract binding p ...... sites in a unique orientation.
@nl
P2093
P50
P1433
P1476
Polypyrimidine tract binding p ...... sites in a unique orientation.
@en
P2093
Panagiota Kafasla
Richard J Jackson
Tuija A A Pöyry
P304
P356
10.1016/J.MOLCEL.2009.04.015
P577
2009-06-01T00:00:00Z