Publications
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“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.
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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.
“A potential indicator of denervated muscle atrophy: the ratio of myostatin to follistatin in peripheral blood”, vol. 10, pp. 3914-3923, 2011.
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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
“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
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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
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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.
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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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