ReviewBiophysical journal2014
MAP kinase modules: the excursion model and the steps that count.
Review in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- Cellular stress response to extremely low-frequency electromagnetic fields (ELF-EMF): An explanation for controversial effects of ELF-EMF on apoptosis.Cell proliferation · 2021Review
- Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- It's about time: Analysing simplifying assumptions for modelling multi-step pathways in systems biology.PLoS computational biology · 2020Article
- Inference of Multisite Phosphorylation Rate Constants and Their Modulation by Pathogenic Mutations.Current biology : CB · 2020Article
- Optimizing photoswitchable MEK.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- How activating mutations affect MEK1 regulation and function.The Journal of biological chemistry · 2017Article
- Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Long-term dynamics of multisite phosphorylation.Molecular biology of the cell · 2016Article
- Robustness of MEK-ERK Dynamics and Origins of Cell-to-Cell Variability in MAPK Signaling.Cell reports · 2016Article
- Signal inhibition by a dynamically regulated pool of monophosphorylated MAPK.Molecular biology of the cell · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
MAP kinase modules propagate diverse extracellular signals to downstream effectors. The two dual phosphorylation reactions catalyzed by the modules are thought to control the switch behavior of the pathway. Here we review recent approaches to understand these pathways through signal-to-response studies in cells and in vitro. These data are reconciled with physical models as well as predictions made on mathematical and theoretical grounds. Biochemical analysis has shown recently that the dual phosphorylation reactions catalyzed by MAP kinase modules are sequential at both levels of the cascade. The observed order of phosphorylation events suggests an excursion from the Ser/Thr kinase activity of the MAP3K into Tyr kinase activity of the central dual specificity MAP2K. How the order of events might be encoded in the structures and interactions is discussed. The ordered mechanism confirms predictions that reactions should be sequential to generate the steep signal-to-response curves and delayed responses observed in cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.