ReviewCurrent biology : CB2013
ERK as a model for systems biology of enzyme kinetics in cells.
Review in Current biology : CB, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed.
- Systems-level consequences of low RAF abundance for EGFR-ERK signaling.Biophysical journal · 2026Article
- Phosphorylation of POU3F3 Mediated Nuclear Translocation Promotes Proliferation in Non-Small Cell Lung Cancer through Accelerating ATP5PF Transcription and ATP Production.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- ERK synchronizes embryonic cleavages in Drosophila.Developmental cell · 2024Article
- Determining the ERK-regulated phosphoproteome driving KRAS-mutant cancer.Science (New York, N.Y.) · 2024Article
- An Affordable Topography-Based Protocol for Assigning a Residue's Character on a Hydropathy (PARCH) Scale.Journal of chemical theory and computation · 2024Article
- Stochastic phenotypes in RAS-dependent developmental diseases.Current biology : CB · 2023Article
- Topological descriptors of the parameter region of multistationarity: Deciding upon connectivity.PLoS computational biology · 2023Article
- hucMSC-Ex Alleviates IBD-Associated Intestinal Fibrosis by Inhibiting ERK Phosphorylation in Intestinal Fibroblasts.Stem cells international · 2023Article
- ERK2 MAP kinase regulates SUFU binding by multisite phosphorylation of GLI1.Life science alliance · 2022Article
- Molecular mechanisms underlying cellular effects of human MEK1 mutations.Molecular biology of the cell · 2021Article
- Dynamics of ERK regulation in the processive limit.Journal of mathematical biology · 2021Article
- Identifying hydrophobic protein patches to inform protein interaction interfaces.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Inference of Multisite Phosphorylation Rate Constants and Their Modulation by Pathogenic Mutations.Current biology : CB · 2020Article
- Activation-induced substrate engagement in ERK signaling.Molecular biology of the cell · 2020Article
- Oscillations and bistability in a model of ERK regulation.Journal of mathematical biology · 2019Article
- Raman micro-spectroscopy monitors acquired resistance to targeted cancer therapy at the cellular level.Scientific reports · 2018Article
- When More Is Less: Dual Phosphorylation Protects Signaling Off State against Overexpression.Biophysical journal · 2018Article
- A quantitative model of developmental RTK signaling.Developmental biology · 2018Review
- [The role of extracellular signal regulated kinase 1/2 in mediating osteodifferentiation of human periodontal ligament cells induced by cyclic stretch].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2017Article
- Two faces of competition: target-mediated reverse signalling in microRNA and mitogen-activated protein kinase regulatory networks.IET systems biology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
A key step towards a chemical picture of enzyme catalysis was taken in 1913, when Leonor Michaelis and Maud Menten published their studies of sucrose hydrolysis by invertase. Based on a novel experimental design and a mathematical model, their work offered a quantitative view of biochemical kinetics well before the protein nature of enzymes was established and complexes with substrates could be detected. Michaelis-Menten kinetics provides a solid framework for enzyme kinetics in vitro, but what about kinetics in cells, where enzymes can be highly regulated and participate in a multitude of interactions? We discuss this question using the Extracellular Signal Regulated Kinase (ERK), which controls a myriad functions in cells, as a model of an important enzyme for which we have crystal structures, quantitative in vitro assays, and a vast list of binding partners. Despite great progress, we still cannot quantitatively predict how the rates of ERK-dependent reactions respond to genetic and pharmacological perturbations. Achieving this goal, which is important from both fundamental and practical standpoints, requires measuring the rates of enzyme reactions in their native environment and interpreting these measurements using simple but realistic mathematical models--the two elements which served as the cornerstones for Michaelis' and Menten's seminal 1913 paper.
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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.