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Article

Characterization of phospho-(tyrosine)-mimetic calmodulin mutants.

PloS one - 1 Jan 2015

Stateva Silviya R, Salas Valentina, Benaim Gustavo, Menéndez Margarita, Solís Dolores, Villalobo Antonio

Abstract excerpt

Calmodulin (CaM) phosphorylated at different serine/threonine and tyrosine residues is known to exert differential regulatory effects on a variety of CaM-binding enzymes as compared to non-phosphorylated CaM. In this report we describe the preparation and characterization of a series of phospho-(Y)-mimetic CaM mutants in which either one or the two tyrosine residues present in CaM (Y99 and Y138) were substituted...

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Identifiers

PMID: 25830911
DOI: 10.1371/journal.pone.0120798
PMCID: PMC4382182

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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