A ribonucleoprotein of skeletal muscle and its relation to the myofibril.
نویسندگان
چکیده
Asboe-Hansen, G. (1958). Physiol. Rev. 38, 446. Budy, A. M. (1955). Arch. int. Pharmacodyn. 103, 435. Cantarow, A., Rakoff, A. E., Paschkis, K. E., Hansen, L. P. & Walkling, A. A. (1943). Proc. Soc. exp. Biol., N. Y., 52, 256. Courtice, F. C. (1943). J. Physiol. 102, 290. Dodds, E. C., Folley, S. J., Glascock, R. F. & Lawson, W. (1958). Biochem. J. 68, 161. Dodds, E. C., Golberg, L., Grunfeld, E. I., Lawson, W., Saffer, C. M., jun. & Robinson, R. (1944). Proc. Roy. Soc. B, 132, 83. Dodgson, K. S., Garton, G. A., Stubbs, A. L. & Williams, R. T. (1948). Biochem. J. 42, 357. Emmens, C. W. (1940-41). J. End,ocrin. 2, 448. Folley, S. J. (1956). The Physiology and Biochemistry of Lactation. Edinburgh and London: Oliver and Boyd. Glascock, R. F. (1954a). Radioisotope Conference, vol. 1, p. 262. Ed. Johnston, J. E., Faires, R. A. & Millett, R. J. London: Butterworths Scientific Publications. Glascock, R. F. (1954b). Isotopic Gas Analysis for Biochemists. New York: Academic Press Inc. Glascock, R. F. (1956). Proc. Int. Conf. Peaceful Uses of Atomic Energy, 12, 397. New York: United Nations. Glascock, R. F. & Hoekstra, W. G. (1958). Proc. 2nd Int. Conf. Peaceful Uses of Atomic Energy, (in the Press). New York: United Nations. Green, S. (1954). Proc. Soc. exp. Biol., N. Y., 86, 653. Hanahan, D. J., Daskalakis, E. G., Edwards, T. & Dauben, H. J., jun. (1953). Endocrinology, 53, 163. Joseph, N. R., Engel, M. B. & Catchpole, H. R. (1954). Arch. Path. 58, 40. Kalman, S. M. (1955). J. Pharmacol. 115, 442. McCorquodale, D. J. & Mueller, G. C. (1958). J. biol. Chem. 232, 31. Rapp, G. W. & Richardson, G. C. (1952). Science, 115, 265. Robinson, T. J., Moore, N. W. & Binet, F. E. (1956). J. Endocrin. 14, 1. Sandberg, A. A. & Slaunwhite, W. R., jun. (1957). J. clin. Invest. 36, 1266. Smith, A. E. W. & Williams, P. C. (1948). Biochem. J. 42, 253. Szego, C. M. (1957). In Physiological Triggers, p. 152. Ed. by Bullock, T. H. Washington, D.C.: American Physiological Society. Turner, C. W. (1956). J. Anim. Sci. 15, 13. Twombly, G. H. (1951). Acta Un. int. Cancr. 7, 882. Twombly, G. H. & Schoenewaldt, E. F. (1951). Cancer, 4, 296. Wiberg, G. S. & Stephenson, N. R. (1957). Canad. J. Biochem. Physiol. 35, 1107.
منابع مشابه
تاثیر یک دوره تمرین مقاومتی بر بیان اینترلوکین-6 و RCAN-1 در عضله اسکلتی موشهای صحرایی دیابتی شده با استروپتوزوسین
Background: Myokines released from skeletal muscle have multiple metabolic and hypertrophic effects. On the other hand, one of proposed pathways for effects of exercise training on metabolic diseases is calcineurin signaling pathway. With considering to relation between interleukin-6 (IL-6) and calcineurin, the purpose of this study was to investigate whether the resistance training has an effe...
متن کاملExpression and Functional Characterization of Smyd1a in Myofibril Organization of Skeletal Muscles
BACKGROUND Smyd1, the founding member of the Smyd family including Smyd-1, 2, 3, 4 and 5, is a SET and MYND domain containing protein that plays a key role in myofibril assembly in skeletal and cardiac muscles. Bioinformatic analysis revealed that zebrafish genome contains two highly related smyd1 genes, smyd1a and smyd1b. Although Smyd1b function is well characterized in skeletal and cardiac m...
متن کاملEvaluation of Canonical Correlations between Masticatory Muscle Orientation and Craniodentofacial Morphology in 10-17 Year_Olds
Objectives: Different theories have been suggested to define factors involved in skeletal and craniofacial morphology. Many of these theories explain that the bone morphology is the result of the bone tissue capability to adapt in response to biomechanical forces exerted during growth. Also, it seems logical to hypothesize that there is a relationship between biomechanical connections of muscle...
متن کاملSmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos.
Histone modification has emerged as a fundamental mechanism for control of gene expression and cell differentiation. Recent studies suggest that SmyD1, a novo SET domain-containing protein, may play a critical role in cardiac muscle differentiation. However, its role in skeletal muscle development and its mechanism of actions remains elusive. Here we report that SmyD1a and SmyD1b, generated by ...
متن کاملNeuregulins Response to Exercise: a Mini Review
The Neuregulin is a member of the epidermal growth factors (EGF) family of receptor kinases, was originally identified as the product of the transforming gene derived from chemically induced rat neuroblastoms. A variety of different protein isoforms are produced from single Neuregulin gene. Four distinct vertebrate gene encode Neuregulin, prosaically named NRG1, NRG2, NRG3, and NRG4. Most of bi...
متن کاملTC10 controls human myofibril organization and is activated by the sarcomeric RhoGEF obscurin.
The contractile activity of striated muscle depends on myofibrils that are highly ordered macromolecular complexes. The protein components of myofibrils are well characterized, but it remains largely unclear how signaling at the molecular level within the sarcomere and the control of assembly are coordinated. We show that the Rho GTPase TC10 appears during differentiation of human primary skele...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Biochemical journal
دوره 72 شماره
صفحات -
تاریخ انتشار 1959