Publications
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“Identification and expression analysis of the MSP130-related-2 gene from Hyriopsis cumingii”, vol. 14, pp. 4903-4913, 2015.
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“Association of bovine Toll-like receptor 4 with tick infestation rates and blood histamine concentration”, vol. 12, pp. 2783-2793, 2013.
, “Two chitin metabolic enzyme genes from Hyriopsis cumingii: cloning, characterization, and potential functions”, vol. 11, pp. 4539-4551, 2012.
, Badariotti F, Thuau R, Lelong C, Dubos MP, et al. (2007). Characterization of an atypical family 18 chitinase from the oyster Crassostrea gigas: evidence for a role in early development and immunity. Dev. Comp. Immunol. 31: 559-570.
http://dx.doi.org/10.1016/j.dci.2006.09.002
PMid:17056114
Badariotti F, Lelong C, Dubos MP and Favrel P (2011). Identification of three singular glycosyl hydrolase family 18 members from the oyster Crassostrea gigas: Structural characterization, phylogenetic analysis and gene expression. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 158: 56-63.
http://dx.doi.org/10.1016/j.cbpb.2010.09.009
PMid:20868765
Bai ZY, Yin YX, Hu SN, Wang GL, et al. (2010). Identification of genes potentially involved in pearl formation by expressed sequence tag analysis of mantle from freshwater pearl mussel (Hyriopsis cumingii lea). J. Shellfish Res. 29: 527-534.
http://dx.doi.org/10.2983/035.029.0232
Bendtsen JD, Nielsen H, von HG and Brunak S (2004). Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340: 783-795.
http://dx.doi.org/10.1016/j.jmb.2004.05.028
PMid:15223320
Cheng TC (1996). Hemocytes: Forms and Functions. In: The Eastern Oyster Crassostrea virginica (Kennedy VS, Newell RIE and Eble AF, eds.). Maryland Sea Grant Book, College Park, Maryland, 299-333.
PMid:8682321
Dixit R, Arakane Y, Specht CA, Richard C, et al. (2008). Domain organization and phylogenetic analysis of proteins from the chitin deacetylase gene family of Tribolium castaneum and three other species of insects. Insect Biochem. Mol. Biol. 38: 440-451.
http://dx.doi.org/10.1016/j.ibmb.2007.12.002
PMid:18342249
Falini G, Weiner S and Addadi L (2003). Chitin-silk fibroin interactions: relevance to calcium carbonate formation in invertebrates. Calcif. Tissue Int. 72: 548-554.
http://dx.doi.org/10.1007/s00223-002-1055-0
PMid:12724827
Furuhashi T, Schwarzinger C, Miksik I, Smrz M, et al. (2009). Molluscan shell evolution with review of shell calcification hypothesis. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 154: 351-371.
http://dx.doi.org/10.1016/j.cbpb.2009.07.011
PMid:19665573
Huang QS, Yan JH, Tang JY, Tao YM, et al. (2010). Cloning and tissue expressions of seven chitinase family genes in Litopenaeus vannamei. Fish Shellfish Immunol. 29: 75-81.
http://dx.doi.org/10.1016/j.fsi.2010.02.014
PMid:20202477
Jeanmougin F, Thompson JD, Gouy M, Higgins DG, et al. (1998). Multiple sequence alignment with Clustal X. Trends Biochem. Sci. 23: 403-405.
http://dx.doi.org/10.1016/S0968-0004(98)01285-7
Kumirska J, Czerwicka M, Kaczynski Z, Bychowska A, et al. (2010). Application of spectroscopic methods for structural analysis of chitin and chitosan. Mar. Drugs 8: 1567-1636.
http://dx.doi.org/10.3390/md8051567
PMid:20559489 PMCid:2885081
Lelong C, Badariotti F, Le Quéré H, Rodet F, et al. (2007). Cg-TGF-beta, a TGF-beta/activin homologue in the Pacific Oyster Crassostrea gigas, is involved in immunity against Gram-negative microbial infection. Dev. Comp. Immunol. 31: 30-38.
http://dx.doi.org/10.1016/j.dci.2006.05.005
PMid:16820208
Li JL, Qian RH, Bao BL, Wang GL, et al. (2005). RAPD analysis on genetic diversity among the stocks of Hyriopsis cumingii from the five large lakes of China. J. Shanghai Fish. Univ. 14: 1-5.
Liu YY (1979). Economic Fauna of China (Freshwater mollusk). Science Press, Beijing, 83-84.
Livak KJ and Schmittgen TD (2001). Analysis of relative gene expression data using real-time quantitative PCR and the 2-DDCT Method. Methods 25: 402-408.
http://dx.doi.org/10.1006/meth.2001.1262
PMid:11846609
Minagawa T, Okamura Y, Shigemasa Y, Minami S, et al. (2007). Effects of molecular weight and deacetylation degree of chitin/chitosan on wound healing. Carbohydr. Polym. 67: 640-644.
http://dx.doi.org/10.1016/j.carbpol.2006.07.007
Montagnani C, Le Roux F, Berthe F and Escoubas JM (2001). Cg-TIMP, an inducible tissue inhibitor of metalloproteinase from the Pacific oyster Crassostrea gigas with a potential role in wound healing and defense mechanisms(1). FEBS Lett. 500: 64-70.
http://dx.doi.org/10.1016/S0014-5793(01)02559-5
Mount AS, Wheeler AP, Paradkar RP and Snider D (2004). Hemocyte-mediated shell mineralization in the eastern oyster. Science 304: 297-300.
http://dx.doi.org/10.1126/science.1090506
PMid:15073378
Proespraiwong P, Tassanakajon A and Rimphanitchayakit V (2010). Chitinases from the black tiger shrimp Penaeus monodon: phylogenetics, expression and activities. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 156: 86-96.
http://dx.doi.org/10.1016/j.cbpb.2010.02.007
PMid:20197105
Ravi Kumar MNV (2000). A review of chitin and chitosan applications. React. Funct. Polym. 46: 1-27.
http://dx.doi.org/10.1016/S1381-5148(00)00038-9
Riccardo AAM (2009). Chitosan composites with inorganics, morphogenetic proteins and stem cells, for bone regeneration. Carbohydr. Polym. 83: 1433-1445.
Suzuki M, Saruwatari K, Kagure T, Yamamoto Y, et al. (2009). An acidic matrix protein, Pif, is a key macromolecule for nacre formation. Science 325: 1388-1390.
http://dx.doi.org/10.1126/science.1173793
PMid:19679771
Wang GL, Wang JJ and Li JL (2006). Preliminary study on applicability of microsatellite primers developed from Crassostrea gigas to genomic analysis of Hyriopsis cumingii. J. Fish. China 1: 30-38.
Weiss IM, Kaufmann S, Heiland B and Tanaka M (2009). Covalent modification of chitin with silk-derivatives acts as an amphiphilic self-organizing template in nacre biomineralisation. J. Struct. Biol. 167: 68-75.
http://dx.doi.org/10.1016/j.jsb.2009.04.005
PMid:19401236
Zhang J, Zhang X, Arakane Y, Muthukrishnan S, et al. (2011). Identification and characterization of a novel chitinase-like gene cluster (AgCht5) possibly derived from tandem duplications in the African malaria mosquito, Anopheles gambiae. Insect Biochem. Mol. Biol. 41: 521-528.
http://dx.doi.org/10.1016/j.ibmb.2011.03.001
PMid:21419847
Zhou J, Gao YF, Li L, Zhai HN, et al. (2011). Identification and functional characterization of a putative 17β-hydroxysteroid dehydrogenase 12 in abalone (Haliotis diversicolor supertexta). Mol. Cell. Biochem. 354: 123-133.
http://dx.doi.org/10.1007/s11010-011-0811-8
PMid:21479786
Zhu Q, Arakane Y, Banerjee D, Beeman RW, et al. (2008). Domain organization and phylogenetic analysis of the chitinase-like family of proteins in three species of insects. Insect Biochem. Mol. Biol. 38: 452-466.
http://dx.doi.org/10.1016/j.ibmb.2007.06.010
PMid:18342250