Cleavage of eukaryotic translation initiation factor 4GII correlates with translation inhibition during apoptosis (Q33933174)

30 July 2017

Cleavage of eukaryotic translation initiation factor 4GII correlates with translation inhibition during apoptosis (English)

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30 July 2017

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Marissen WE

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30 July 2017

Gradi A

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30 July 2017

Sonenberg N

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30 July 2017

Lloyd RE

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30 July 2017

1 December 2000

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Cell Death & Differentiation

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30 July 2017

1234-1243

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https://scigraph.springernature.com/pub.10.1038/sj.cdd.4400750

30 July 2017

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Potassium deprivation-induced apoptosis of cerebellar granule neurons: a sequential requirement for new mRNA and protein synthesis, ICE-like protease activity, and reactive oxygen species.

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Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation

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Poliovirus 2A protease induces apoptotic cell death

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Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells

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A novel functional human eukaryotic translation initiation factor 4G

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TIF4631 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

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Proteolysis of human eukaryotic translation initiation factor eIF4GII, but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection

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Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI.

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In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains

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A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation

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7 January 2021

Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis

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7 January 2021

Caspase-3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis

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7 January 2021

Substrate specificities of caspase family proteases

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7 January 2021

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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7 January 2021

Changes in integrity and association of eukaryotic protein synthesis initiation factors during apoptosis

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Identification of caspase 3-mediated cleavage and functional alteration of eukaryotic initiation factor 2alpha in apoptosis

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Caspase-mediated cleavage of eukaryotic translation initiation factor subunit 2alpha

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The large subunit of replication factor C is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during Fas-mediated apoptosis

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7 January 2021

The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E.

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7 January 2021

Translation driven by an eIF4G core domain in vivo

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7 January 2021

Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region

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7 January 2021

Identifiers

DOI

10.1038/SJ.CDD.4400750

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30 July 2017

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