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All intrinsically active Erk1/2 mutants autophosphorylate threonine207/188, a plausible regulator of the TEY motif phosphorylation.

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Title: All intrinsically active Erk1/2 mutants autophosphorylate threonine207/188, a plausible regulator of the TEY motif phosphorylation.
Authors: Baskin A; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel., Soudah N; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel., Gilad N; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel; Singapore-HUJ Alliance for Research and Enterprise, Mechanisms of Liver Inflammatory Diseases Program, National University of Singapore, Singapore., Halevi N; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel., Darlyuk-Saadon I; Singapore-HUJ Alliance for Research and Enterprise, Mechanisms of Liver Inflammatory Diseases Program, National University of Singapore, Singapore., Schoffman H; Stein Family Mass Spectrometry Unit, The Research Infrastructure Center, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel., Engelberg D; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel; Singapore-HUJ Alliance for Research and Enterprise, Mechanisms of Liver Inflammatory Diseases Program, National University of Singapore, Singapore; Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore. Electronic address: engelber@mail.huji.ac.il.
Source: The Journal of biological chemistry [J Biol Chem] 2025 Jun; Vol. 301 (6), pp. 108509. Date of Electronic Publication: 2025 Apr 11.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: All intrinsically active Erk1/2 mutants autophosphorylate threonine207/188, a plausible regulator of the TEY motif phosphorylation.
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  Data: <searchLink fieldCode="AU" term="%22Baskin+A%22">Baskin A</searchLink>; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel.<br /><searchLink fieldCode="AU" term="%22Soudah+N%22">Soudah N</searchLink>; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel.<br /><searchLink fieldCode="AU" term="%22Gilad+N%22">Gilad N</searchLink>; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel; Singapore-HUJ Alliance for Research and Enterprise, Mechanisms of Liver Inflammatory Diseases Program, National University of Singapore, Singapore.<br /><searchLink fieldCode="AU" term="%22Halevi+N%22">Halevi N</searchLink>; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel.<br /><searchLink fieldCode="AU" term="%22Darlyuk-Saadon+I%22">Darlyuk-Saadon I</searchLink>; Singapore-HUJ Alliance for Research and Enterprise, Mechanisms of Liver Inflammatory Diseases Program, National University of Singapore, Singapore.<br /><searchLink fieldCode="AU" term="%22Schoffman+H%22">Schoffman H</searchLink>; Stein Family Mass Spectrometry Unit, The Research Infrastructure Center, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel.<br /><searchLink fieldCode="AU" term="%22Engelberg+D%22">Engelberg D</searchLink>; Department of Biological Chemistry, The Institute of Life Science, The Hebrew University of Jerusalem, Jerusalem, Israel; Singapore-HUJ Alliance for Research and Enterprise, Mechanisms of Liver Inflammatory Diseases Program, National University of Singapore, Singapore; Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore. Electronic address: engelber@mail.huji.ac.il.
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  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2025 Jun; Vol. 301 (6), pp. 108509. <i>Date of Electronic Publication: </i>2025 Apr 11.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier+Inc%2E+on+behalf+of+American+Society+for+Biochemistry+and+Molecular+Biology%22">Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>2985121R <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1083-351X (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200219258%22">00219258 </searchLink><i>NLM ISO Abbreviation: </i>J Biol Chem <i>Subsets: </i>MEDLINE
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        Value: 10.1016/j.jbc.2025.108509
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        Text: English
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              Text: 2025 Jun
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