Cleavage of polypeptide chain initiation factor eIF4GI during apoptosis in lymphoma cells: characterisation of an internal fragment generated by caspase-3-mediated cleavage.
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The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins.Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g)RoXaN, a novel cellular protein containing TPR, LD, and zinc finger motifs, forms a ternary complex with eukaryotic initiation factor 4G and rotavirus NSP3Poly(A)-binding protein interaction with elF4G stimulates picornavirus IRES-dependent translationStructural Analysis of the DAP5 MIF4G Domain and Its Interaction with eIF4ADisruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavagesFunctional analysis of individual binding activities of the scaffold protein eIF4GCaspase cleavage of initiation factor 4E-binding protein 1 yields a dominant inhibitor of cap-dependent translation and reveals a novel regulatory motifMass spectrometric analysis of the N terminus of translational initiation factor eIF4G-1 reveals novel isoforms.Translation initiation factor modifications and the regulation of protein synthesis in apoptotic cells.Eukaryotic translation initiation factor 4GI and p97 promote cellular internal ribosome entry sequence-driven translationCap-independent translation promotes C. elegans germ cell apoptosis through Apaf-1/CED-4 in a caspase-dependent mechanismTranslational regulation in cell stress and apoptosis. Roles of the eIF4E binding proteins.Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN.Specific isoforms of translation initiation factor 4GI show differences in translational activityA continuous-exchange cell-free protein synthesis system based on extracts from cultured insect cells.Ischemia-induced calpain activation causes eukaryotic (translation) initiation factor 4G1 (eIF4GI) degradation, protein synthesis inhibition, and neuronal deathThe eIF4G-homolog p97 can activate translation independent of caspase cleavageInitiation factor modifications in the preapoptotic phase.Memory CD4+ T-cell-mediated protection depends on secondary effectors that are distinct from and superior to primary effectors.Regulation of translation is required for dendritic cell function and survival during activation.Re-programming of translation following cell stress allows IRES-mediated translation to predominate.Direct ribosomal binding by a cellular inhibitor of translation.Global decay of mRNA is a hallmark of apoptosis in aging Xenopus eggs.IRES mediated translational regulation of p53 isoforms.RPPA-based protein profiling reveals eIF4G overexpression and 4E-BP1 serine 65 phosphorylation as molecular events that correspond with a pro-survival phenotype in chronic lymphocytic leukemia.A researcher's guide to the galaxy of IRESs.Caspase-mediated cleavage and DNase activity of the translation initiation factor 3, subunit G (eIF3g).Multiple isoforms of the translation initiation factor eIF4GII are generated via use of alternative promoters, splice sites and a non-canonical initiation codon.Protein factor requirements of the Apaf-1 internal ribosome entry segment: roles of polypyrimidine tract binding protein and upstream of N-ras.Multiple eIF4GI-specific protease activities present in uninfected and poliovirus-infected cells.The multifaceted poliovirus 2A protease: regulation of gene expression by picornavirus proteases.Translation of eukaryotic translation initiation factor 4GI (eIF4GI) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection.Translational induction of the inhibitor of apoptosis protein HIAP2 during endoplasmic reticulum stress attenuates cell death and is mediated via an inducible internal ribosome entry site element.Distinct regulation of internal ribosome entry site-mediated translation following cellular stress is mediated by apoptotic fragments of eIF4G translation initiation factor family members eIF4GI and p97/DAP5/NAT1.Proteasome inhibitors and immunosuppressive drugs promote the cleavage of eIF4GI and eIF4GII by caspase-8-independent mechanisms in Jurkat T cell lines.Phosphorylation of eIF4GII and 4E-BP1 in response to nocodazole treatment: a reappraisal of translation initiation during mitosis.A novel mechanism for Bcr-Abl action: Bcr-Abl-mediated induction of the eIF4F translation initiation complex and mRNA translation.Regulation of the phosphorylation and integrity of protein synthesis initiation factor eIF4GI and the translational repressor 4E-BP1 by p53.Myofibrillogenesis regulator 1 (MR-1): a potential therapeutic target for cancer and PNKD.
P2860
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P2860
Cleavage of polypeptide chain initiation factor eIF4GI during apoptosis in lymphoma cells: characterisation of an internal fragment generated by caspase-3-mediated cleavage.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Cleavage of polypeptide chain ...... y caspase-3-mediated cleavage.
@en
type
label
Cleavage of polypeptide chain ...... y caspase-3-mediated cleavage.
@en
prefLabel
Cleavage of polypeptide chain ...... y caspase-3-mediated cleavage.
@en
P2093
P2860
P356
P1476
Cleavage of polypeptide chain ...... y caspase-3-mediated cleavage.
@en
P2093
Clemens MJ
Marissen WE
P2860
P2888
P304
P356
10.1038/SJ.CDD.4400699
P577
2000-07-01T00:00:00Z
P5875
P6179
1033600721