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2011
R. F. Sun, Zhu, Y. S., Feng, J. L., Tian, Z., Kuang, W. J., Liu, Y., Zhang, H. B., and Li, S. B., Polymorphisms of three new microsatellite sites of the dystrophin gene, vol. 10, pp. 744-751, 2011.
Ambrosio CE, Fadel L, Gaiad TP, Martins DS, et al. (2009). Identification of three distinguishable phenotypes in Golden Retriever muscular dystrophy. Genet. Mol. Res. 8: 389-396. doi:10.4238/vol8-2gmr581 Banks GB and Chamberlain JS (2008). The value of mammalian models for Duchenne muscular dystrophy in developing therapeutic strategies. Curr. Top. Dev. Biol. 84: 431-453. doi:10.1016/S0070-2153(08)00609-1 Basak J, Dasgupta UB, Banerjee TK, Senapati AK, et al. (2006). Analysis of dystrophin gene deletions by multiplex PCR in eastern India. Neurol. India 54: 310-311. doi:10.4103/0028-3886.27164 Davies KE (1997). Challenges in Duchenne muscular dystrophy. Neuromuscul. Disord. 7: 482-486. doi:10.1016/S0960-8966(97)00107-7 Den Dunnen JT, Grootscholten PM, Bakker E, Blonden LA, et al. (1989). Topography of the Duchenne muscular dystrophy (DMD) gene: FIGE and cDNA analysis of 194 cases reveals 115 deletions and 13 duplications. Am. J. Hum. Genet. 45: 835-847. Dubowitz V (2006). Enigmatic conflict of clinical and molecular diagnosis in Duchenne/Becker muscular dystrophy. Neuromuscul. Disord. 16: 865-866. doi:10.1016/j.nmd.2006.09.003 Gao Y and Li SB (2008). Effects of sample size on the observed number of allele of 9 STR loci with various genetic data. Yi Chuan 30: 313-320. doi:10.3724/SP.J.1005.2008.00313 Giliberto F, Ferreiro V, Dalamon V, Surace E, et al. (2003). Direct deletion analysis in two Duchenne muscular dystrophy symptomatic females using polymorphic dinucleotide (CA)n loci within the dystrophin gene. J. Biochem. Mol. Biol. 36: 179-184. doi:10.5483/BMBRep.2003.36.2.179 Kimmel M and Chakraborty R (1996). Measures of variation at DNA repeat loci under a general stepwise mutation model. Theor. Popul. Biol. 50: 345-367. doi:10.1006/tpbi.1996.0035 Koenig M, Hoffman EP, Bertelson CJ, Monaco AP, et al. (1987). Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. Cell 50: 509-517. doi:10.1016/0092-8674(87)90504-6 Lai KK, Lo IF, Tong TM, Cheng LY, et al. (2006). Detecting exon deletions and duplications of the DMD gene using multiplex ligation-dependent probe amplification (MLPA). Clin. Biochem. 39: 367-372. doi:10.1016/j.clinbiochem.2005.11.019 Lai PS, Takeshima Y, Adachi K, Van Tran K, et al. (2002). Comparative study on deletions of the dystrophin gene in three Asian populations. J. Hum. Genet. 47: 552-555. doi:10.1007/s100380200084 Li Q and Wan JM (2005). SSRHunter: development of a local searching software for SSR sites. Yi Chuan 27: 808-810. Melis MA, Cau M, Muntoni F, Mateddu A, et al. (1998). Elevation of serum creatine kinase as the only manifestation of an intragenic deletion of the dystrophin gene in three unrelated families. Eur. J. Paediatr. Neurol. 2: 255-261. doi:10.1016/S1090-3798(98)80039-1 Mendell JR, Buzin CH, Feng J, Yan J, et al. (2001). Diagnosis of Duchenne dystrophy by enhanced detection of small mutations. Neurology 57: 645-650. Ribeiro Rodrigues EM, Leite FP, Hutz MH, Palha TJ, et al. (2008). A multiplex PCR for 11 X chromosome STR markers and population data from a Brazilian Amazon Region. Forensic Sci. Int. Genet. 2: 154-158. doi:10.1016/j.fsigen.2007.10.179 Roberts RG, Gardner RJ and Bobrow M (1994). Searching for the 1 in 2,400,000: a review of dystrophin gene point mutations. Hum. Mutat. 4: 1-11. doi:10.1002/humu.1380040102 Sewry CA (2010). Muscular dystrophies: an update on pathology and diagnosis. Acta Neuropathol. 120: 343-358. doi:10.1007/s00401-010-0727-5 Sifringer M, Uhlenberg B, Lammel S, Hanke R, et al. (2004). Identification of transcripts from a subtraction library which might be responsible for the mild phenotype in an intrafamilially variable course of Duchenne muscular dystrophy. Hum. Genet. 114: 149-156. doi:10.1007/s00439-003-1041-2 Suminaga R, Takeshima Y, Adachi K, Yagi M, et al. (2002). A novel cryptic exon in intron 3 of the dystrophin gene was incorporated into dystrophin mRNA with a single nucleotide deletion in exon 5. J. Hum. Genet. 47: 196-201. doi:10.1007/s100380200023 Walmsley GL, Arechavala-Gomeza V, Fernandez-Fuente M, Burke MM, et al. (2010). A Duchenne muscular dystrophy gene hot spot mutation in dystrophin-deficient Cavalier King Charles Spaniels is amenable to exon 51 skipping. PLoS One 5: e8647. doi:10.1371/journal.pone.0008647 Yan J and Hou YP (2004). Exploring Novel STR Loci on Human Chromosome 21 for Forensic and Medical Genetics. Doctoral thesis, Sichuan University, Chengdu.
R. H. Wu, Wang, P., Yang, L., Li, Y., Liu, Y., and Liu, M., A potential indicator of denervated muscle atrophy: the ratio of myostatin to follistatin in peripheral blood, vol. 10, pp. 3914-3923, 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
2010
Y. Liu, Zhou, Y. L., Qian, Y. Y., Wang, Y. J., Ding, F., Gu, X. S., and Liu, M., The noggin2 gene of Gekko japonicus (Gekkonidae) is down-regulated in the spinal cord after tail amputation, vol. 9, pp. 1606-1614, 2010.
Alibardi L (1995). Muscle differentiation and morphogenesis in the regenerating tail of lizards. J. Anat. 186: 143-151. PMid:7649809 PMCid:1167280   Aspenberg P, Jeppsson C and Economides AN (2001). The bone morphogenetic proteins antagonist noggin inhibits membranous ossification. J. Bone Miner. Res. 16: 497-500. http://dx.doi.org/10.1359/jbmr.2001.16.3.497 PMid:11277267   Bachiller D, Klingensmith J, Kemp C, Belo JA, et al. (2000). The organizer factors chordin and noggin are required for mouse forebrain development. Nature 403: 658-661. http://dx.doi.org/10.1038/35001072 PMid:10688202   Brockes JP (1997). Amphibian limb regeneration: rebuilding a complex structure. Science 276: 81-87. http://dx.doi.org/10.1126/science.276.5309.81 PMid:9082990   Chernoff EA, Stocum DL, Nye HL and Cameron JA (2003). Urodele spinal cord regeneration and related processes. Dev. Dyn. 226: 295-307. http://dx.doi.org/10.1002/dvdy.10240 PMid:12557207   Echeverri K and Tanaka EM (2002). Ectoderm to mesoderm lineage switching during axolotl tail regeneration. Science 298: 1993-1996. http://dx.doi.org/10.1126/science.1077804 PMid:12471259   Egar M, Simpson SB and Singer M (1970). The growth and differentiation of the regenerating spinal cord of the lizard, Anolis carolinensis. J. Morphol. 131: 131-151. http://dx.doi.org/10.1002/jmor.1051310202 PMid:5425076   Eroshkin FM, Ermakova GV, Bayramov AV and Zaraisky AG (2006). Multiple noggins in vertebrate genome: cloning and expression of noggin2 and noggin4 in Xenopus laevis. Gene Expr. Patterns 6: 180-186. http://dx.doi.org/10.1016/j.modgep.2005.06.007 PMid:16168719   Fletcher RB, Watson AL and Harland RM (2004). Expression of Xenopus tropicalis noggin1 and noggin2 in early development: two noggin genes in a tetrapod. Gene Expr. Patterns 5: 225-230. http://dx.doi.org/10.1016/j.modgep.2004.08.001 PMid:15567718   Fürthauer M, Thisse B and Thisse C (1999). Three different noggin genes antagonize the activity of bone morphogenetic proteins in the zebrafish embryo. Dev. Biol. 214: 181-196. http://dx.doi.org/10.1006/dbio.1999.9401 PMid:10491267   Kulessa H, Turk G and Hogan BL (2000). Inhibition of Bmp signaling affects growth and differentiation in the anagen hair follicle. EMBO J. 19: 6664-6674. http://dx.doi.org/10.1093/emboj/19.24.6664 PMid:11118201 PMCid:305899   Lamb TM, Knecht AK, Smith WC, Stachel SE, et al. (1993). Neural induction by the secreted polypeptide noggin. Science 262: 713-718. http://dx.doi.org/10.1126/science.8235591 PMid:8235591   Liu Y, Ding F, Liu M, Jiang M, et al. (2006). EST-based identification of genes expressed in brain and spinal cord of Gekko japonicus, a species demonstrating intrinsic capacity of spinal cord regeneration. J. Mol. Neurosci. 29: 21-28. http://dx.doi.org/10.1385/JMN:29:1:21   McMahon JA, Takada S, Zimmerman LB, Fan CM, et al. (1998). Noggin-mediated antagonism of BMP signaling is required for growth and patterning of the neural tube and somite. Genes Dev. 12: 1438-1452. http://dx.doi.org/10.1101/gad.12.10.1438 PMid:9585504 PMCid:316831   Reddi AH (2001). Interplay between bone morphogenetic proteins and cognate binding proteins in bone and cartilage development: noggin, chordin and DAN. Arthritis Res. 3: 1-5. http://dx.doi.org/10.1186/ar133 PMid:11178121 PMCid:128877   Simpson SB Jr (1968). Morphology of the regenerated spinal cord in the lizard, Anolis carolinensis. J. Comp. Neurol. 134: 193-210. http://dx.doi.org/10.1002/cne.901340207 PMid:5712416   Smith WC and Harland RM (1992). Expression cloning of noggin, a new dorsalizing factor localized to the Spemann organizer in Xenopus embryos. Cell 70: 829-840. http://dx.doi.org/10.1016/0092-8674(92)90316-5   Valenzuela DM, Economides AN, Rojas E, Lamb TM, et al. (1995). Identification of mammalian noggin and its expression in the adult nervous system. J. Neurosci. 15: 6077-6084. PMid:7666191   Zimmerman LB, De Jesus-Escobar JM and Harland RM (1996). The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4. Cell 86: 599-606. http://dx.doi.org/10.1016/S0092-8674(00)80133-6

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