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Study of functional significance of cooh terminal isoforms of fast skeletal troponin t using genetically expressed tnt fragments


Study of functional significance of cooh terminal isoforms of fast skeletal troponin t using genetically expressed tnt fragments



Biophysical Journal 61(2 Part 2): A279



ISSN/ISBN: 0006-3495


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(PDF emailed within 1 workday: $29.90)

Accession: 033552317

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Related references

Study of functional significance of carboxyl terminal isoforms of fast skeletal troponin t using genetically expressed tnt fragments. FASEB Journal 6(1): A279, 1992

Two genetically expressed troponin T fragments representing a and b isoforms exhibit functional differences. The Journal of Biological Chemistry 267: 052-6, 1992

Two genetically expressed troponin T fragments representing α and β isoforms exhibit functional differences. The Journal of Biological Chemistry 267(32): 23052-23056, 1992

Two genetically expressed troponin T fragments representing alpha and beta isoforms exhibit functional differences. Journal of Biological Chemistry 267(32): 23052-23056, 1992

Developmentally regulated muscle type-specific alternative splicing of the COOH-terminal variable region of fast skeletal muscle troponin T and an aberrant splicing pathway to encode a mutant COOH-terminus. Biochemical and Biophysical Research Communications 242(3): 540-544, 1998

N-terminal amino acid sequences of three functionally different troponin T isoforms from rabbit fast skeletal muscle. Journal of Molecular Biology 206(1): 245-249, 1989

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Study on functional differences among fast skeletal muscle troponin T isoforms. Zoological Science 15(Suppl ): 93, 1998

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Amino terminal amino acid sequences of three functionally different troponin t isoforms from rabbit fast skeletal muscle. Journal of Molecular Biology 206(1): 245-250, 1989

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Transitions from fetal to fast troponin T isoforms are coordinated with changes in tropomyosin and a-actinin isoforms in developing rabbit skeletal muscle. Developmental Biology 140: 3-60, 1990

Transitions from fetal to fast troponin T isoforms are coordinated with changes in tropomyosin and alpha-actinin isoforms in developing rabbit skeletal muscle. Developmental Biology 140(2): 253-260, 1990