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The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

How MAP Kinases Are Regulated

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Cobb, Melanie H., Goldsmith, Elizabeth J.·1995·Journal of Biological Chemistry

Abstract

The closely related MAP kinases,1(1) extracellular signal-regulated protein kinases 1 and 2 (ERK1 and ERK2), are ubiquitous components of signal transduction pathways. ERK1 and ERK2 are activated by diverse extracellular stimuli and by protooncogene products that induce proliferation or enhance differentiation (reviewed in Refs. 1 and 2). MAP kinase phosphorylations have an impact on processes in the cytoplasm, the nucleus, the cytoskeleton, and the membrane. The variety of signals that conscript the MAP kinase pathway demonstrates that this cascade serves a myriad of purposes, and the consequences of its activation will depend on cellular context.

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Metadata

Authors
Cobb, M. H., & Goldsmith, E. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1995-06
Volume
270
Issue
25
Pages
14843-14846
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2068502127
Cited by
1,719
References
2
FWCI
41.92
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: How MAP Kinases Are Regulated. https://app.cochat.ai/papers/10.1074/jbc.270.25.14843
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Cobb, M. H., & Goldsmith, E. J. (1995). How MAP Kinases Are Regulated. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.25.14843

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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