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cellular eukaryotic translation initiation factor 4G + H2O
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cellular eukaryotic translation initiation factor eIF4GI + H2O
peptides
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cellular eukaryotic translation initiation factor eIF4GII + H2O
peptides
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CVB1 protein + H2O
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death-associated protein 5 + H2O
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DAP5
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eIF4G + H2O
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eukaryotic initiation factor-4G
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eIF4G + H2O
fragments of eIF4G
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eIF4GI + H2O
fragments of eIF4GI
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eukaryotic initiation factor 4G + H2O
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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eukaryotic translation initiation factor 4G + H2O
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eukaryotic translation initiation factor 4G I + H2O
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eukaryotic translation initiation factor 4G II + H2O
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eukaryotic translation initiation factor 4gamma + H2O
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EV-A71 viral polyprotein + H2O
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Grb2-associated binding protein 1 + H2O
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GAB1 is cleaved during CV-B3 infection by viral proteinase 2A
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Grb2-associated binding protein 2 + H2O
GAB2-N1-237 + GAB2-C238-676
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GAB2 is cleaved at G238 during CV-B3 infection by viral proteinase 2A, generating two cleaved fragments of GAB2-N1-237 and GAB2-C238-676
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HRV 3Cpro precursor 3CD + H2O
3Cpro + 3Dpro
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activation of 3C protease, EC 3.4.22.28, of human rhinovirus A-16
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human eukaryotic translation initiation factor 4 G I + H2O
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human eIF4GI
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human eukaryotic translation initiation factor 4 G II + H2O
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human eIF4GII
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nuclear factor of activated T cells 5/tonicity enhancer binding protein
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NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, inactivation of NFAT5
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picornavirus polyprotein + H2O
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intramolecular reaction, processing begins before synthesis of the polyprotein is complete, cleavage separates capsid protein precursor and noncapsid protein precursor
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poliovirus polypeptide + H2O
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poly(A) binding protein + H2O
fragments of poly(A) binding protein
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contains 1 cleavage site for 2A proteinase within the proline-rich linker domain
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serum response factor + H2O
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additional information
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cytokeratin 8 + H2O
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cytokeratin 8 + H2O
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the cleavage results in removal of 14 amino acids from the N-terminal head domain of cytokeratin 8. Cleavage occurs late in the infection cycle at the time of the onset of the cytopathic effect
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dystrophin + H2O
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the protease cleaves dystrophin in coxsackievirus B3-infected myocytes. The cleavage functionally impairs dystrophin
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dystrophin + H2O
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functional impairment and morphological disruption of dystrophin
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dystrophin + H2O
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eukaryotic initiation factor 4G + H2O
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eukaryotic initiation factor 4G + H2O
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eukaryotic initiation factor 4G + H2O
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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turns off host-cell protein synthesis
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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involved in shut-off in translation of cellular mRNAs upon viral infection, induces cleavage of eukaryotic initiation factor (eIF)4gamma component (i.e. p220) of eIF-4, formerly eIF-4F
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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turns off host-cell protein synthesis
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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turns off host-cell protein synthesis
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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turns off host-cell protein synthesis
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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turns off host-cell protein synthesis
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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involved in shut-off in translation of cellular mRNAs upon viral infection, induces cleavage of eukaryotic initiation factor (eIF)4gamma component (i.e. p220) of eIF-4, formerly eIF-4F
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eukaryotic translation initiation factor 4F p220 subunit + H2O
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turns off host-cell protein synthesis
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eukaryotic translation initiation factor 4G + H2O
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eIF4G
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eukaryotic translation initiation factor 4G + H2O
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eIF4G
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eukaryotic translation initiation factor 4G + H2O
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eIF4G
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eukaryotic translation initiation factor 4G + H2O
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eIF4G
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eukaryotic translation initiation factor 4G + H2O
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Enterovirus A71 BrCR
eIF4G
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eukaryotic translation initiation factor 4G + H2O
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eIF4G
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eukaryotic translation initiation factor 4G + H2O
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eIF4G
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MAVS + H2O
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a cellular protein
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MAVS + H2O
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a cellular protein
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MAVS + H2O
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a cellular protein
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MAVS + H2O
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a cellular protein
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MDA5 + H2O
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a cellular protein
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MDA5 + H2O
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a cellular protein
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MDA5 + H2O
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a cellular protein
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MDA5 + H2O
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a cellular protein
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poliovirus polypeptide + H2O
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involved in primary processing of poliovirus
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poliovirus polypeptide + H2O
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involved in primary processing of poliovirus
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poliovirus polypeptide + H2O
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involved in primary processing of poliovirus
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poliovirus polypeptide + H2O
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immediately after polypeptide 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent chain is cleaved intramolecularly
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poliovirus polypeptide + H2O
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together with 3C protease
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poliovirus polypeptide + H2O
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involved in primary processing of poliovirus
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additional information
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2Apro cleaves eIF4G, separating the domains of eIF4GI or eIF4GII that bind to eIF4E (and mRNA) and eIF3 (and the 40S ribosome) and inhibits de novo translation initiation by interfering with the ribosome mRNA binding step
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additional information
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DAP5 is cleaved during CVB3 infection in tissue culture and in mouse heart
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additional information
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in vivo assays by expression of GAB2 proteins in virus-infected HeLa cells
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additional information
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enzyme, or its polyprotein precursors, are required to stabilize viral RNA and prolong translation. Enzyme activity stimulates negative-strand initiation by approximately fivefold, but has no effect on stability. Stimulation of negative-strand synthesis is independent of the effect on stability and translation
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additional information
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2Apro processes the viral polyprotein, and it cleaves a variety of host proteins, including the translation proteins eIF4GI, eIF4GII and poly(A)-binding protein
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additional information
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important cellular substrate for 2Apro is eIF4G, cleavage of this translation protein leads to inhibition of host protein synthesis during picornavirus infection
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additional information
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inhibitory role for 2Apro in the most downstream event in interferon signaling, the antiviral activities of interferon-stimulated genes
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additional information
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picornaviral 2A sequences are used to express transgenes in oncolytic adenoviruses
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additional information
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proteinase 2Apro is essential for enterovirus replication in type I interferon-treated cells
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additional information
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ribosome skipping is a mechanism that allows translation of multiple proteins from a single mRNA, it is based on the use of a picornaviral 2A sequence that causes the ribosome to continue translation after skipping the formation of one peptide bond
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