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Article

Charged residue alterations in the inner-core domain and carboxy-terminus of alpha-tropomyosin differentially affect mouse cardiac muscle contractility.

The Journal of physiology - 15 Dec 2004

Gaffin Robert D, Tong Carl W, Zawieja David C, Hewett Timothy E, Klevitsky Raisa, Robbins Jeffrey, Muthuchamy Mariappan

Abstract excerpt

Two important charge differences between the alpha- and beta-tropomyosin (TM) isoforms are the exchange of a serine residue in the inner-core region at position 229, and a histidine residue at the carboxy-terminal end at position 276, with glutamic acid and asparagine, respectively. We have recently shown that altering these two residues in alpha-TM to their beta-TM counterparts in transgenic (TG) mouse hearts...

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Identifiers

PMID: 15486021
DOI: 10.1113/jphysiol.2004.070631
PMCID: PMC1665389

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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