Isolation and structural characterization of cap-binding proteins from poliovirus-infected HeLa cells.
about
Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4EInhibition of translation in cells infected with a poliovirus 2Apro mutant correlates with phosphorylation of the alpha subunit of eucaryotic initiation factor 2RNA-protein interactions in regulation of picornavirus RNA translationTIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function.Purification and partial characterization of poliovirus protease 2A by means of a functional assayCap-independent translation initiation in Xenopus oocytesRelationship of eukaryotic initiation factor 3 to poliovirus-induced p220 cleavage activityThe adenovirus tripartite leader may eliminate the requirement for cap-binding protein complex during translation initiationPoliovirus protease 3C (P3-7c) does not cleave P220 of the eucaryotic mRNA cap-binding protein complex.Restriction of translation of capped mRNA in vitro as a model for poliovirus-induced inhibition of host cell protein synthesis: relationship to p220 cleavageMonoclonal antibody-aided characterization of cellular p220 in uninfected and poliovirus-infected HeLa cells: subcellular distribution and identification of conformers.Poliovirus mutant that does not selectively inhibit host cell protein synthesis.General RNA-binding proteins have a function in poly(A)-binding protein-dependent translationRequirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap.Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells.Initiation of protein synthesis in mammalian cellsThe eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase.Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C proteases.Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection.
P2860
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P2860
Isolation and structural characterization of cap-binding proteins from poliovirus-infected HeLa cells.
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
1985年论文
@zh
1985年论文
@zh-cn
name
Isolation and structural chara ...... oliovirus-infected HeLa cells.
@en
type
label
Isolation and structural chara ...... oliovirus-infected HeLa cells.
@en
prefLabel
Isolation and structural chara ...... oliovirus-infected HeLa cells.
@en
P2093
P2860
P1433
P1476
Isolation and structural chara ...... oliovirus-infected HeLa cells.
@en
P2093
P2860
P304
P407
P577
1985-05-01T00:00:00Z