The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Docking interactions in the mitogen-activated protein kinase cascades
Abstract
Regulation of cellular functions and responses utilizes a number of the signal transduction pathways. Each pathway should transduce signals with high efficiency and fidelity to avoid unnecessary crosstalks. The mitogen-activated protein kinase (MAPK) cascades regulate a wide variety of cellular functions, including cell proliferation, differentiation, and stress responses. MAPK is activated by MAPK kinase; phosphorylates various targets, including transcription factors and MAPK-activated protein kinases; and is inactivated by several phosphatases. Recent studies have provided a cue to understand the molecular mechanism underlying the signal transduction through the MAPK cascades. In the MAPK cascades, docking interactions, which are achieved through a site outside the catalytic domain of MAPKs, regulate the efficiency and specificity of the enzymatic reactions. The docking interaction is different from a transient enzyme-substrate interaction through the active center. It has been shown that activators, substrates, and inactivators of MAPKs utilize a common site on MAPKs in the docking interaction. Then, the docking interaction may regulate not only the efficiency and specificity of the cascades, but also the ordered and integrated signaling.
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In the citing paper
“Mitogen activated protein kinases (MAPKs) have a docking groove that interacts with linear motifs in binding partners.”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [6]
In the citing paper
“Mitogen activated protein kinases (MAPKs) regulate diverse aspects of cellular life such as cell division, differentiation or apoptosis and interact with proteins through linear binding motifs (5-6).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [6]
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Computational modelling of the receptor-tyrosine-kinase-activated MAPK pathway
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Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125
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Metadata
- Authors
- Tanoue, T., & Nishida, E.
- Affiliations
- Kyoto University (JP)
- Corresponding author
- Nishida, Eisuke
- ORCID
- Nishida, Eisuke
- Venue
- Pharmacology & Therapeutics
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 93
- Issue
- 2-3
- Pages
- 193-202
- ISSN
- 0163-7258 (ISSN-L)
- OpenAlex
- W1992023215
- Cited by
- 134
- References
- 57
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 4 · 2023: 8 · 2022: 7 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 1 · 2016: 7 · 2015: 4 · 2014: 8 · 2013: 5 · 2012: 5
- FWCI
- 0.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Pharmacology & Therapeutics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- mitogen-activated protein kinase, MAPK signaling, MAPK kinase, signal transduction, enzyme regulation, signaling specificity, signaling crosstalk, MAPK phosphorylation
- MeSH terms
- Animals, Humans, Membrane Proteins, Molecular Biology, Phosphorylation, Signal Transduction, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System
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