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Updated: Aug 13, 2026

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Related proteins are phosphorylated at tyrosine in response to mitogenic stimuli and at meiosis
1Fred Hutchinson Cancer Research Center, Seattle, Washington 98104.
Molecular and Cellular Biology
|July 1, 1989
Abstract:
Forty-two-kilodalton proteins that contain phosphotyrosine in metaphase-arrested Xenopus laevis eggs are closely related to p42, a protein that is phosphorylated at tyrosine when somatic cells are exposed to mitogenic stimuli.
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