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Open AccessJournal ArticleDOI

The Product of par-4, a Gene Induced during Apoptosis, Interacts Selectively with the Atypical Isoforms of Protein Kinase C

TLDR
Results are shown here demonstrating that the expression of par-4 in NIH-3T3 cells induces morphological changes typical of apoptosis, which are abrogated by cotransfection of either wild-type zeta PKC or lambda/LPKC, but not by their respective kinase-inactive mutants.
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This article is published in Cell.The article was published on 1996-09-06 and is currently open access. It has received 377 citations till now. The article focuses on the topics: Protein kinase C & PAWR.

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Cellular survival: a play in three Akts

TL;DR: The mechanisms by which survival factors regulate the PI3K/c-Akt cascade, the evidence that activation of the PI 3K/ c-AKT pathway promotes cell survival, and the current spectrum of c- akt targets and their roles in mediating c- Akt-dependent cell survival are reviewed.
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The PI 3-kinase/Akt signaling pathway delivers an anti-apoptotic signal.

TL;DR: The results suggest that uncoupling of survival and mitogenesis can be explained by differing abilities of distinct mitogens to efficiently induce the PI 3-kinase/Akt signaling pathway.
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Serine/threonine protein kinases and apoptosis.

TL;DR: This minireview will focus on the role of protein kinases in apoptosis, which has been implicated both in the upstream induction phase of apoptosis and in the downstream execution stage, as the direct targets for caspases.
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New insights into the regulation of protein kinase C and novel phorbol ester receptors

TL;DR: It is speculated that some of the biological responses elicited by phorbol esters or by activation of receptors coupled to elevation in DAG levels could be mediated by PKC‐independent pathways.
References
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Journal ArticleDOI

Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis

TL;DR: The effects of dominant-interfering or constitutively activated forms of various components of the JNK-p38 and ERK signaling pathways demonstrated that activation of JNK and p38 and concurrent inhibition of ERK are critical for induction of apoptosis in these cells.
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Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C

TL;DR: It is becoming clear that agonist-induced hydrolysis of other membrane phospholipids, particularly choline phospholipsids, by phospholIPase D and phospholiptase A2 may also take part in cell signaling.
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FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis

TL;DR: Findings suggest that FADD may play an important role in the proximal signal transduction of Fas, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8.
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The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase

TL;DR: It is shown that Akt and the Akt-related kinase AKT2 are activated by PDGF, and it is suggested that the AkT PH domain may be a mediator of PI 3-kinase signaling.
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TRADD–TRAF2 and TRADD–FADD Interactions Define Two Distinct TNF Receptor 1 Signal Transduction Pathways

TL;DR: It is shown that TRADD directly interacts with TRAF2 and FADD, signal transducers that activate NF-kappa B and induce apoptosis, respectively, and these two TNFR1-TRADD signaling cascades appear to bifurcate at TRADD.
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