z-logo
open-access-imgOpen Access
Molecular and Functional Characterization of a Novel Cardiac-Specific Human Tropomyosin Isoform
Author(s) -
Sudarsan Rajan,
Ganapathy Jagatheesan,
Chehade N. Karam,
Marco Stephan LofranoAlves,
Ilona Bódi,
Arnold Schwartz,
Christian F. Bulcao,
Karen M. D’Souza,
Shahab A. Akhter,
Greg P. Boivin,
Dipak K. Dube,
Natalia Petrashevskaya,
Andrew B. Herr,
Roger Hullin,
Stephen B. Liggett,
Beata M. Wolska,
R. John Solaro,
David F. Wieczorek
Publication year - 2010
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/circulationaha.109.889725
Subject(s) - myofilament , gene isoform , tropomyosin , myofibril , dilated cardiomyopathy , heart failure , medicine , cardiomyopathy , cardiac muscle , actin , genetically modified mouse , endocrinology , microbiology and biotechnology , transgene , myocyte , biology , biochemistry , gene
Tropomyosin (TM), an essential actin-binding protein, is central to the control of calcium-regulated striated muscle contraction. Although TPM1alpha (also called alpha-TM) is the predominant TM isoform in human hearts, the precise TM isoform composition remains unclear.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom