N-terminal amino acid sequences of three functionally different troponin T isoforms from rabbit fast skeletal muscle
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference26 articles.
1. Molecular basis of cooperativity in vertebrate muscle thin filaments
2. Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle
3. Intricate combinatorial patterns of exon splicing generate multiple regulated troponin T isoforms from a single gene
4. Heterogeneity of contractile proteins. Purification and characterization of two species of troponin T from rabbit fast skeletal muscle.
5. The extent of amino-terminal heterogeneity in rabbit fast skeletal muscle troponin T
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1. Troponin Variants as Markers of Skeletal Muscle Health and Diseases;Frontiers in Physiology;2021-09-27
2. Kardiales Troponin T zur Diagnostik und Verlaufsbeurteilung bei klinischem Verdacht auf Myokarditis;DMW - Deutsche Medizinische Wochenschrift;2008-03-25
3. Troponin T isoform expression is modulated during Atlantic Halibut metamorphosis;BMC Developmental Biology;2007-06-18
4. Regulation of troponin T expression during muscle development in sea breamSparus auratusLinnaeus: the potential role of thyroid hormones;Journal of Experimental Biology;2006-12-01
5. N-terminal amino acid sequences of troponin T fragments, including 30 kDa one, produced during postmortem aging of bovine longissimus muscle;Meat Science;2004-05
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