Translational control of the antiapoptotic function of Ras. (Q40879734)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10811643%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

title

Translational control of the antiapoptotic function of Ras (English)

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6 November 2019

2

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6 November 2019

Peter B Bitterman

8

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6 November 2019

author name string

Polunovsky VA

1

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6 November 2019

Sonenberg N

3

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6 November 2019

Peterson M

4

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6 November 2019

Tan A

5

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6 November 2019

Rubins JB

6

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6 November 2019

Manivel JC

7

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6 November 2019

language of work or name

English

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publication date

1 August 2000

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Journal of Biological Chemistry

6 November 2019

published in

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6 November 2019

volume

275

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6 November 2019

issue

32

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6 November 2019

page(s)

24776-24780

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Increasing complexity of the Ras signaling pathway

6 November 2019

cites work

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Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB.

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Cellular survival: a play in three Akts

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Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

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NF-kappaB is a target of AKT in anti-apoptotic PDGF signalling

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Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death Machinery

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Regulation of cell death protease caspase-9 by phosphorylation

21 January 2018

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Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin

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4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway

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Target of rapamycin (TOR): balancing the opposing forces of protein synthesis and degradation

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eIF4E activity is regulated at multiple levels

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The mRNA 5' cap-binding protein eIF4E and control of cell growth

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Translational control of programmed cell death: eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated Myc.

21 January 2018

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Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function

21 January 2018

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PHAS-I as a link between mitogen-activated protein kinase and translation initiation

21 January 2018

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Activation of the translational suppressor 4E-BP1 following infection with encephalomyocarditis virus and poliovirus.

21 January 2018

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A Novel Functional Human Eukaryotic Translation Initiation Factor 4G

21 January 2018

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Targeted disruption of p70(s6k) defines its role in protein synthesis and rapamycin sensitivity

21 January 2018

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Continuous protein synthesis is required to maintain the probability of entry into S phase

21 January 2018

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Size control in animal development

21 January 2018

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A novel form of DAP5 protein accumulates in apoptotic cells as a result of caspase cleavage and internal ribosome entry site-mediated translation

21 January 2018

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Phosphorylation of Eukaryotic Translation Initiation Factor 2 Mediates Apoptosis in Response to Activation of the Double-stranded RNA-dependent Protein Kinase

21 January 2018

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

21 January 2018

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c-Myc protein synthesis is initiated from the internal ribosome entry segment during apoptosis.

21 January 2018

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Translational control: the cancer connection

21 January 2018

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Translational control of growth factor and proto-oncogene expression

21 January 2018

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Inhibition of Myc-dependent apoptosis by eukaryotic translation initiation factor 4E requires cyclin D1.

21 January 2018

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eIF4E expression in tumors: its possible role in progression of malignancies

21 January 2018

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PHAS/4E-BPs as regulators of mRNA translation and cell proliferation

21 January 2018

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Disruption of the Gene Encoding the Mitogen-regulated Translational Modulator PHAS-I in Mice

21 January 2018

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Activation of ribosomes in sea urchin eggs in response to fertilization

21 January 2018

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Degradation of eukaryotic polypeptide chain initiation factor (eIF) 4G in response to induction of apoptosis in human lymphoma cell lines

21 January 2018

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Cleavage of translation initiation factor 4G (eIF4G) during anti-Fas IgM-induced apoptosis does not require signalling through the p38 mitogen-activated protein (MAP) kinase

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