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Updated: Aug 4, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

MAPキナーゼによって媒介されるc-junのリン酸化

B J Pulverer1, J M Kyriakis, J Avruch

  • 1Ludwig Institute for Cancer Research, London, UK.

Nature
|October 17, 1991
PubMed
まとめ

この研究は,ミトゲン活性化タンパク質 (MAP) キナーゼがc-junタンパク質の特定の部位をリン酸化し,その活性性を高めることを明らかにしています. このリン酸化メカニズムは,様々な成長信号がc-jun転写因子を活性化する方法を説明しています.

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Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Microtubule Associated Proteins (MAPs)

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Calmodulin-dependent Signaling

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