Interaction of a cellular 57-kilodalton protein with the internal translation initiation site of foot-and-mouth disease virus.
about
Determination of functional domains in polypyrimidine-tract-binding proteinStructural organization of a viral IRES depends on the integrity of the GNRA motif.Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM foldBiological function of Foot-and-mouth disease virus non-structural proteins and non-coding elementsPicornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virusIn vivo and in vitro identification of structural and sequence elements of the human parechovirus 5' untranslated region required for internal initiationInteraction of polypyrimidine tract-binding protein with the 5' noncoding region of the hepatitis C virus RNA genome and its functional requirement in internal initiation of translationFunctional involvement of polypyrimidine tract-binding protein in translation initiation complexes with the internal ribosome entry site of foot-and-mouth disease virusThe cellular polypeptide p57 (pyrimidine tract-binding protein) binds to multiple sites in the poliovirus 5' nontranslated regionA small yeast RNA selectively inhibits internal initiation of translation programmed by poliovirus RNA: specific interaction with cellular proteins that bind to the viral 5'-untranslated regionRNA-protein interactions in regulation of picornavirus RNA translationBridging IRES elements in mRNAs to the eukaryotic translation apparatusLa autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysateExploring IRES region accessibility by interference of foot-and-mouth disease virus infectivity.Transient expression of cellular polypyrimidine-tract binding protein stimulates cap-independent translation directed by both picornaviral and flaviviral internal ribosome entry sites In vivo.Identification and characterization of a cis-acting replication element (cre) adjacent to the internal ribosome entry site of foot-and-mouth disease virus.Differential utilization of poly(rC) binding protein 2 in translation directed by picornavirus IRES elements.Computational modeling of eukaryotic mRNA turnover.Foot-and-mouth disease.Mutational analysis of the J-K stem-loop region of the encephalomyocarditis virus IRES.A cytoplasmic 57-kDa protein that is required for translation of picornavirus RNA by internal ribosomal entry is identical to the nuclear pyrimidine tract-binding protein.Encephalomyocarditis virus internal ribosomal entry site RNA-protein interactions.RNA-binding proteins impacting on internal initiation of translation.Cell proteins bind to a linear polypyrimidine-rich sequence within the 5'-untranslated region of rhinovirus 14 RNA.Cell type-specific proteins which interact with the 5' nontranslated region of hepatitis A virus RNA.Identification of an essential region for internal initiation of translation in the aphthovirus internal ribosome entry site and implications for viral evolutionGemin5: A Multitasking RNA-Binding Protein Involved in Translation Control.Structural basis for the biological relevance of the invariant apical stem in IRES-mediated translation.La autoantigen enhances translation of BiP mRNAInteraction of eukaryotic initiation factor eIF4B with the internal ribosome entry site of foot-and-mouth disease virus is independent of the polypyrimidine tract-binding protein.Interaction of cellular proteins with the 5' end of Norwalk virus genomic RNA.Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3C(pro)Interaction of eukaryotic initiation factor eIF-4B with a picornavirus internal translation initiation site.Sequences within a small yeast RNA required for inhibition of internal initiation of translation: interaction with La and other cellular proteins influences its inhibitory activity.Conserved structural motifs located in distal loops of aphthovirus internal ribosome entry site domain 3 are required for internal initiation of translation.Designing synthetic RNAs to determine the relevance of structural motifs in picornavirus IRES elements.trans complementation by RNA of defective foot-and-mouth disease virus internal ribosome entry site elements.Internal translation initiation on poliovirus RNA: further characterization of La function in poliovirus translation in vitro.A single nucleotide substitution in the internal ribosome entry site of foot-and-mouth disease virus leads to enhanced cap-independent translation in vivo.Three different cellular proteins bind to complementary sites on the 5'-end-positive and 3'-end-negative strands of mouse hepatitis virus RNA.
P2860
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P2860
Interaction of a cellular 57-kilodalton protein with the internal translation initiation site of foot-and-mouth disease virus.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
Interaction of a cellular 57-k ...... foot-and-mouth disease virus.
@en
type
label
Interaction of a cellular 57-k ...... foot-and-mouth disease virus.
@en
prefLabel
Interaction of a cellular 57-k ...... foot-and-mouth disease virus.
@en
P2860
P1433
P1476
Interaction of a cellular 57-k ...... foot-and-mouth disease virus.
@en
P2860
P304
P407
P577
1991-12-01T00:00:00Z