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1 of a highly conserved amino acid residue in beta-tropomyosin.
2 t found to regulate mRNA splicing in chicken beta-tropomyosin.
3 und that Rad interacted with skeletal muscle beta-tropomyosin.
4 ical contexts not previously associated with beta-tropomyosin.
5 tion identified in the extreme N-terminus of beta-tropomyosin.
6 e N-terminus of the alpha-helices of dimeric beta-tropomyosin, a change predicted to alter protein-pr
8 ted to alter protein-protein binding between beta-tropomyosin and other molecules and to disturb head
9 al phenotypes not previously associated with beta-tropomyosin and pathogenic data from the first anim
10 lude that Rad interacts with skeletal muscle beta-tropomyosin and the cytoskeleton in a guanine nucle
13 eins troponin T (TnT), troponin I (TnI), and beta-tropomyosin (beta-TM) have been shown to cause auto
19 g INS), an exonic splicing silencer from the beta-tropomyosin gene, and an intronic splicing regulato
21 zed a transgenic mouse system to overexpress beta-tropomyosin in the heart to address the functional
23 study, we have rescued these high expression beta-tropomyosin mice by turning off the alpha-myosin he
24 athies through the identification of a novel beta-tropomyosin mutation in two clinical contexts not p
25 nical phenotype is core-rod myopathy, with a beta-tropomyosin mutation uncovered by whole exome seque
27 yosin regulate actin-myosin interactions and beta-tropomyosin mutations have been associated with nem
28 at the mutation interferes with head-to-tail beta-tropomyosin polymerization and with overall sarcome
29 his study, we expand the allelic spectrum of beta-tropomyosin-related myopathies through the identifi
31 Interestingly, when a high percentage of beta-tropomyosin replaces alpha-tropomyosin in the heart
32 family binds the WA1, instability (INS), and beta-tropomyosin substrates, and the core-binding site f
33 onic sequence, an (A/U)GGG repeat in chicken beta-tropomyosin that is a binding site for a protein re
34 nt charge differences between the alpha- and beta-tropomyosin (TM) isoforms are the exchange of a ser
37 ein phenotype that expresses both alpha- and beta-tropomyosin, very low levels of SERCA2a, and very l
38 expressed in striated muscle are alpha- and beta-tropomyosin, which exhibit an 86% amino acid identi
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