Topic
ASK1
About: ASK1 is a research topic. Over the lifetime, 8203 publications have been published within this topic receiving 783320 citations. The topic is also known as: ASK1 & MAPKKK5.
Papers published on a yearly basis
1 / 2
Papers
TL;DR: Protein kinase C probably serves as a receptor for the tumour promoters and further exploration of the roles of this enzyme may provide clues for understanding the mechanism of cell growth and differentiation.
Abstract: Protein kinase C has a crucial role in signal transduction for a variety of biologically active substances which activate cellular functions and proliferation. When cells are stimulated, protein kinase C is transiently activated by diacylglycerol which is produced in the membrane during the signal-induced turnover of inositol phospholipids. Tumour-promoting phorbol esters, when intercalated into the cell membrane, may substitute for diacylglycerol and permanently activate protein kinase C. The enzyme probably serves as a receptor for the tumour promoters. Further exploration of the roles of this enzyme may provide clues for understanding the mechanism of cell growth and differentiation.
7,619 citations
TL;DR: Kinetic analysis indicates that TPA can substitute for diacylglycerol and greatly increases the affinity of the enzyme for Ca2+ as well as for phospholipid, and various phorbol derivatives which have been shown to be active in tumor promotion are also capable of activating this protein kinase in in vitro systems.
4,912 citations
TL;DR: Experiments with PC12 cells suggest that the duration of ERK activation is critical for cell signaling decisions, and the extracellular signal-regulated kinase (ERK-regulated) MAPK pathway may be sufficient for these cellular responses.
4,803 citations
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.
Abstract: Hydrolysis of inositol phospholipids by phospholipase C is initiated by either receptor stimulation or opening of Ca2+ channels. This was once thought to be the sole mechanism to produce the diacylglycerol that links extracellular signals to intracellular events through activation of protein kinase C. It is becoming clear that agonist-induced hydrolysis of other membrane phospholipids, particularly choline phospholipids, by phospholipase D and phospholipase A2 may also take part in cell signaling. The products of hydrolysis of these phospholipids may enhance and prolong the activation of protein kinase C. Such prolonged activation of protein kinase C is essential for long-term cellular responses such as cell proliferation and differentiation.
4,666 citations
TL;DR: Nonenzymatic mechanisms that impact MAP kinase functions and findings from gene disruption studies are highlighted and particular emphasis is on ERK1/2.
Abstract: Mitogen-activated protein (MAP) kinases comprise a family of ubiquitous proline-directed, protein-serine/threonine kinases, which participate in signal transduction pathways that control intracellular events including acute responses to hormones and major developmental changes in organisms. MAP kinases lie in protein kinase cascades. This review discusses the regulation and functions of mammalian MAP kinases. Nonenzymatic mechanisms that impact MAP kinase functions and findings from gene disruption studies are highlighted. Particular emphasis is on ERK1/2.
4,314 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 15 |
| 2024 | 16 |
| 2023 | 89 |
| 2022 | 61 |
| 2021 | 63 |
| 2020 | 51 |