Publications

Found 2 results
Filters: Author is J.G. de Almeida  [Clear All Filters]
2015
L. B. Minasi, Pinto, I. P., de Almeida, J. G., de Melo, A. V., Cunha, D. M. C., Ribeiro, C. L., Silva, G. P., Brasil, M. G., Silva, D. M., da Silva, C. C., and da Cruz, A. D., “Postnatal diagnosis of constitutive ring chromosome 13 using both conventional and molecular cytogenetic approaches”, vol. 14, pp. 1692-1699, 2015.
2011
L. B. Minasi, Costa, E. O. A., Silva, D. M., Melo, C. O. A., de Almeida, J. G., Vieira, T. C., Júnior, R. L. Silva, Ribeiro, C. L., da Silva, C. C., and da Cruz, A. D., “Cytogenetic damage in the buccal epithelium of Brazilian aviators occupationally exposed to agrochemicals”, vol. 10. pp. 3924-3929, 2011.
Amthor H, Nicholas G, McKinnell I, Kemp CF, et al. (2004). Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis. Dev. Biol. 270: 19-30. http://dx.doi.org/10.1016/j.ydbio.2004.01.046 PMid:15136138   Diel P, Schiffer T, Geisler S, Hertrampf T, et al. (2010). Analysis of the effects of androgens and training on myostatin propeptide and follistatin concentrations in blood and skeletal muscle using highly sensitive immuno PCR. Mol. Cell Endocrinol. 330: 1-9. http://dx.doi.org/10.1016/j.mce.2010.08.015 PMid:20801187   Dinh P, Hazel A, Palispis W, Suryadevara S, et al. (2009). Functional assessment after sciatic nerve injury in a rat model. Microsurgery 29: 644-649. http://dx.doi.org/10.1002/micr.20685 PMid:19653327   Gilson H, Schakman O, Kalista S, Lause P, et al. (2009). Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin. Am. J. Physiol. Endocrinol. Metab. 297: E157-E164. http://dx.doi.org/10.1152/ajpendo.00193.2009 PMid:19435857   Hill JJ, Davies MV, Pearson AA, Wang JH, et al. (2002). The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J. Biol. Chem. 277: 40735-40741. http://dx.doi.org/10.1074/jbc.M206379200 PMid:12194980   Lakshman KM, Bhasin S, Corcoran C, Collins-Racie LA, et al. (2009). Measurement of myostatin concentrations in human serum: Circulating concentrations in young and older men and effects of testosterone administration. Mol. Cell Endocrinol. 302: 26-32. http://dx.doi.org/10.1016/j.mce.2008.12.019 PMid:19356623   Lee SJ (2010). Extracellular regulation of myostatin: A molecular rheostat for muscle mass. Immunol. Endocr. Metab. Agents Med. Chem. 10: 183-194. http://dx.doi.org/10.2174/187152210793663748 PMid:21423813 PMCid:3060380   Lee SJ and McPherron AC (2001). Regulation of myostatin activity and muscle growth. Proc. Natl. Acad. Sci. U. S. A. 98: 9306-9311. http://dx.doi.org/10.1073/pnas.151270098 PMid:11459935 PMCid:55416   Lee SJ, Lee YS, Zimmers TA, Soleimani A, et al. (2010). Regulation of muscle mass by follistatin and activins. Mol. Endocrinol. 24: 1998-2008. http://dx.doi.org/10.1210/me.2010-0127 PMid:20810712 PMCid:2954636   Liu M, Zhang D, Shao C, Liu J, et al. (2007). Expression pattern of myostatin in gastrocnemius muscle of rats after sciatic nerve crush injury. Muscle Nerve 35: 649-656. http://dx.doi.org/10.1002/mus.20749 PMid:17326119   Matzuk MM, Lu N, Vogel H, Sellheyer K, et al. (1995). Multiple defects and perinatal death in mice deficient in follistatin. Nature 374: 360-363. http://dx.doi.org/10.1038/374360a0 PMid:7885475   McPherron AC, Lawler AM and Lee SJ (1997). Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 387: 83-90. http://dx.doi.org/10.1038/387083a0 PMid:9139826   Rodino-Klapac LR, Haidet AM, Kota J, Handy C, et al. (2009). Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease. Muscle Nerve 39: 283-296. http://dx.doi.org/10.1002/mus.21244 PMid:19208403 PMCid:2717722   Thies RS, Chen T, Davies MV, Tomkinson KN, et al. (2001). GDF-8 propeptide binds to GDF-8 and antagonizes biological activity by inhibiting GDF-8 receptor binding. Growth Factors 18: 251-259. http://dx.doi.org/10.3109/08977190109029114 PMid:11519824   Thompson TB, Lerch TF, Cook RW, Woodruff TK, et al. (2005). The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding. Dev. Cell 9: 535-543. http://dx.doi.org/10.1016/j.devcel.2005.09.008 PMid:16198295   Ueno N, Ling N, Ying SY, Esch F, et al. (1987). Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone. Proc. Natl. Acad. Sci. U. S. A. 84: 8282-8286. http://dx.doi.org/10.1073/pnas.84.23.8282 PMid:3120188 PMCid:299526   Wallimann T, Wyss M, Brdiczka D, Nicolay K, et al. (1992). Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis. Biochem. J. 281: 21-40. PMid:1731757 PMCid:1130636   Whittemore LA, Song K, Li X, Aghajanian J, et al. (2003). Inhibition of myostatin in adult mice increases skeletal muscle mass and strength. Biochem. Biophys. Res. Commun. 300: 965-971. http://dx.doi.org/10.1016/S0006-291X(02)02953-4   Wolfman NM, McPherron AC, Pappano WN, Davies MV, et al. (2003). Activation of latent myostatin by the BMP-1/ tolloid family of metalloproteinases. Proc. Natl. Acad. Sci. U. S. A. 100: 15842-15846. http://dx.doi.org/10.1073/pnas.2534946100 PMid:14671324 PMCid:307655   Zhang D, Liu M, Ding F and Gu X (2006). Expression of myostatin RNA transcript and protein in gastrocnemius muscle of rats after sciatic nerve resection. J. Muscle Res. Cell Motil. 27: 37-44. http://dx.doi.org/10.1007/s10974-005-9050-5 PMid:16450055