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Article

Characterisation of tyrosine-phosphorylation-defective calmodulin mutants.

Protein expression and purification - 1 Jun 2005

Salas Valentina, Sánchez-Torres Juan, Cusidó-Hita David M, García-Marchan Yael, Sojo Felipe, Benaim Gustavo, Villalobo Antonio

Abstract excerpt

Using site-directed mutagenesis, we have produced three calmodulin (CaM) mutants in which one or the two tyrosine residues of native CaM were substituted by phenylalanine. The three variants, denoted CaM(Y99F), CaM(Y138F), and CaM(Y99F/Y138F), were highly expressed in transformed Escherichia coli BL21(DE3)pLysS and purified in high yield. The three CaM mutants were able to activate the cyclic nucleotide...

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Source

Identifiers

PMID: 15866726
DOI: 10.1016/j.pep.2005.01.004

Genes

EGFR

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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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