The byssal-producing glands and proteins of the silverlip pearl oyster Pinctada maxima (Jameson, 1901)

References

• Andrews S. 2010. FastQC: a quality control tool for high throughput sequence data. Available online at: http://www.bioinformatics.babraham.ac.uk/projects/fastqc.
   Google Scholar
• Bar I, Cummins S, Elizur A. 2016. Transcriptome analysis reveals differentially expressed genes associated with germ cell and gonad development in the southern bluefin tuna (Thunnus maccoyii). BMC Genomics. 17:217. doi:https://doi.org/10.1186/s12864-016-2397-8
   PubMed Web of Science ®Google Scholar
• Beitz E. 2000. TeXshade: shading and labeling of multiple sequence alignments using LATEX2 epsilon. Bioinformatics. 16:135–139. doi:https://doi.org/10.1093/bioinformatics/16.2.135
   PubMed Web of Science ®Google Scholar
• Berland S, Marie A, Duplat D, Milet C, Sire JY, Bedouet L. 2011. Coupling proteomics and transcriptomics for the identification of novel and variant forms of mollusk shell proteins: a study with P. margaritifera. Chembiochem. 12:950–961. doi:https://doi.org/10.1002/cbic.201000667
   PubMed Web of Science ®Google Scholar
• Björk P, Wieslander L. 2015. The Balbiani ring story: synthesis, assembly, processing, and transport of specific messenger RNA-Protein complexes. Annu Rev Biochem. 84:65–92. doi:https://doi.org/10.1146/annurev-biochem-060614-034150
   PubMed Web of Science ®Google Scholar
• Blank S, Arnoldi M, Khoshnavaz S, Treccani L, Kuntz M, Mann K, Grathwohl G, Fritz M. 2003. The nacre protein perlucin nucleates growth of calcium carbonate crystals. J Microsc. 212:280–291. doi:https://doi.org/10.1111/j.1365-2818.2003.01263.x
   PubMed Web of Science ®Google Scholar
• Bouhlel Z, Genard B, Ibrahim N, Carrington E, Babarro JMF, Lok A, Flores AAV, Pellerin C, Tremblay R, Marcotte I. 2017. Interspecies comparison of the mechanical properties and biochemical composition of byssal threads. J Exp Biol. 220:984–994.
   PubMed Web of Science ®Google Scholar
• Chambers MC, Maclean B, Burke R, Amodei D, Ruderman DL, Neumann S, Gatto L, Fischer B, Pratt B, Egertson J, et al. 2012. A cross-platform toolkit for mass spectrometry and proteomics. Nat Biotechnol. 30:918–920. doi:https://doi.org/10.1038/nbt.2377
   PubMed Web of Science ®Google Scholar
• Chieu HD, Turner L, Smith MK, Wang T, Nocillado J, Palma P, Suwansa-Ard S, Elizur A, Cummins SF. 2019. Aquaculture breeding enhancement: maturation and spawning in sea cucumbers using a recombinant relaxin-like gonad-stimulating peptide. Front Genet. 10:77. doi:https://doi.org/10.3389/fgene.2019.00077
   PubMed Web of Science ®Google Scholar
• Conesa A, Gotz S, Garcia-Gomez JM, Terol J, Talon M, Robles M. 2005. Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research. Bioinformatics. 21:3674–3676. doi:https://doi.org/10.1093/bioinformatics/bti610
   PubMed Web of Science ®Google Scholar
• Coyne KJ, Qin XX, Waite JH. 1997. Extensible collagen in mussel byssus: a natural block copolymer. Science. 277:1830–1832. doi:https://doi.org/10.1126/science.277.5333.1830
   PubMed Web of Science ®Google Scholar
• Cranfield HJ. 1973a. A study of the morphology, ultrastructure, and histochemistry of the foot of the pediveliger of Ostrea edulis. Mar Biol. 22:187–202. doi:https://doi.org/10.1007/BF00389173
   Web of Science ®Google Scholar
• Cranfield HJ. 1973b. Observations on the function of the glands of the foot of the pediveliger of Ostrea edulis during settlement. Mar Biol. 22:211–223. doi:https://doi.org/10.1007/BF00389175
   Web of Science ®Google Scholar
• Deng Y, Fu S, Liang F, Du X, Xie S. 2013. Growth and survival of pearl oyster Pinctada maxima spat reared under different environmental conditions. J Shellfish Res. 32:675–679. doi:https://doi.org/10.2983/035.032.0308
   Web of Science ®Google Scholar
• Deng Y, Fu S, Liang F, Xie S. 2013. Effects of stocking density, diet, and water exchange on growth and survival of pearl oyster Pinctada maxima larvae. Aquacult Int. 21:1185–1194. doi:https://doi.org/10.1007/s10499-013-9622-0
   Web of Science ®Google Scholar
• Deng Y, Lei Q, Tian Q, Xie S, Du X, Li J, Wang L, Xiong Y. 2014. De novo assembly, gene annotation, and simple sequence repeat marker development using Illumina paired-end transcriptome sequences in the pearl oyster Pinctada maxima. Biosci Biotechnol Biochem. 78:1685–1692. doi:https://doi.org/10.1080/09168451.2014.936351
   PubMed Web of Science ®Google Scholar
• Du X, Fan G, Jiao Y, Zhang H, Guo X, Huang R, Zheng Z, Bian C, Deng Y, Wang Q, et al. 2017. The pearl oyster Pinctada fucata martensii genome and multi-omic analyses provide insights into biomineralization. Gigascience. 6:1–12. doi:https://doi.org/10.1093/gigascience/gix059
   Web of Science ®Google Scholar
• Fischer AH, Jacobson KA, Rose J, Zeller R. 2008. Hematoxylin and eosin staining of tissue and cell sections. Cold Spring Harb Protoc. 2008:pdb.prot4986. doi:https://doi.org/10.1101/pdb.prot4986
   Google Scholar
• Foulon V, Boudry P, Artigaud S, Guerard F, Hellio C. 2019. In silico analysis of pacific oyster (Crassostrea gigas) transcriptome over developmental stages reveals candidate genes for larval settlement. Int J Mol Sci. 20:1–16.
   Web of Science ®Google Scholar
• Giraldes BW, Leitao A, Smyth D. 2019. The benthic sea-silk-thread displacement of a sessile bivalve, Pinctada imbricata radiata (Leach, 1819) in the Arabian-Persian Gulf. PLoS One. 14:e0215865. doi:https://doi.org/10.1371/journal.pone.0215865
   PubMed Web of Science ®Google Scholar
• Hajishengallis G, Russell MW. 2015. Chapter 15 - Innate Humoral Defense Factors. In: Mestecky J, Strober W, Russell MW et al., editors. Mucosal Immunology (Fourth Edition). Boston: Academic Press; p. 251–270.
   Google Scholar
• Harrington MJ, Jehle F, Priemel T. 2018. Mussel byssus structure-function and fabrication as inspiration for biotechnological production of advanced materials. Biotechnol J. 13:1800133. doi:https://doi.org/10.1002/biot.201800133
   PubMed Web of Science ®Google Scholar
• Harrington MJ, Waite JH. 2007. Holdfast heroics: comparing the molecular and mechanical properties of Mytilus californianus byssal threads. J Exp Biol. 210:4307–4318. doi:https://doi.org/10.1242/jeb.009753
   PubMed Web of Science ®Google Scholar
• Hine PM, Thorne T. 1998. Haplosporidium sp. (Haplosporidia) in hatchery-reared pearl oysters, Pinctada maxima (Jameson, 1901), in north Western Australia. J Invertebr Pathol. 71:48–52.
   PubMed Web of Science ®Google Scholar
• Hong S, Lee H, Lee H. 2014. Controlling mechanical properties of bio-inspired hydrogels by modulating nano-scale, inter-polymeric junctions. Beilstein J Nanotechnol. 5:887–894. doi:https://doi.org/10.3762/bjnano.5.101
   PubMed Web of Science ®Google Scholar
• Hopwood MJ, Rapp I, Schlosser C, Achterberg EP. 2017. Hydrogen peroxide in deep waters from the Mediterranean Sea, South Atlantic and South Pacific Oceans. Sci Rep. 7:43436. doi:https://doi.org/10.1038/srep43436
   PubMed Web of Science ®Google Scholar
• Huang Y, Niu B, Gao Y, Fu L, Li W. 2010. CD-HIT Suite: a web server for clustering and comparing biological sequences. Bioinformatics. 26:680–682. doi:https://doi.org/10.1093/bioinformatics/btq003
   PubMed Web of Science ®Google Scholar
• Huang XD, Zhao M, Liu WG, Guan YY, Shi Y, Wang Q, Wu SZ, He MX. 2013. Gigabase-scale transcriptome analysis on four species of pearl oysters. Mar Biotechnol (NY). 15:253–264. doi:https://doi.org/10.1007/s10126-012-9484-x
   PubMed Web of Science ®Google Scholar
• Humphrey JD, Norton JH. 2005. The pearl oyster Pinctada maxima (Jameson, 1901): an atlas of functional anatomy, pathology and histopathology. Darwin, N.T: Northern Territory Dept. of Primary Industry, Fisheries and Mines.
   Google Scholar
• Inoue K, Takeuchi Y, Miki D, Odo S. 1995. Mussel adhesive plaque protein gene is a novel member of epidermal growth factor-like gene family. J Biol Chem. 270:6698–6701. doi:https://doi.org/10.1074/jbc.270.12.6698
   PubMed Web of Science ®Google Scholar
• Jones DB, Jerry DR, Forêt S, Konovalov DA, Zenger KR. 2013. Genome-wide SNP validation and mantle tissue transcriptome analysis in the silver-lipped pearl oyster, Pinctada maxima. Mar Biotechnol (NY)). 15:647–658. doi:https://doi.org/10.1007/s10126-013-9514-3
   PubMed Web of Science ®Google Scholar
• Knight SD, Presto J, Linse S, Johansson J. 2013. The BRICHOS domain, amyloid fibril formation, and their relationship. Biochemistry. 52:7523–7531. doi:https://doi.org/10.1021/bi400908x
   PubMed Web of Science ®Google Scholar
• Kohn JM, Riedel J, Horsch J, Stephanowitz H, Borner HG. 2020. Mussel-inspired polymerization of peptides: the chemical activation route as key to broaden the sequential space of artificial mussel-glue proteins. Macromol Rapid Commun. 41:e1900431. doi:https://doi.org/10.1002/marc.201900431
   PubMed Web of Science ®Google Scholar
• Lal MM, Southgate PC, Jerry DR, Zenger KR. 2018. Genome-wide comparisons reveal evidence for a species complex in the black-lip pearl oyster Pinctada margaritifera (Bivalvia: Pteriidae). Sci Rep. 8:doi:https://doi.org/10.1038/s41598-017-18602-5
   Google Scholar
• Li S, Xia Z, Chen Y, Gao Y, Zhan A. 2018. Byssus structure and protein composition in the highly invasive fouling mussel Limnoperna fortunei. Front Physiol. 9:418–418. doi:https://doi.org/10.3389/fphys.2018.00418
   PubMed Web of Science ®Google Scholar
• Liu C, Li S, Huang J, Liu Y, Jia G, Xie L, Zhang R. 2015. Extensible byssus of Pinctada fucata: Ca 2+ -stabilized nanocavities and a thrombospondin-1 protein. Sci Rep. 5. doi:https://doi.org/10.1038/srep15018
   Google Scholar
• Liu C, Xie L, Zhang R. 2016. Ca2+ mediates the self-assembly of the foot proteins of Pinctada fucata from the nanoscale to the microscale. Biomacromolecules. 17:3347–3355. doi:https://doi.org/10.1021/acs.biomac.6b01125
   PubMed Web of Science ®Google Scholar
• Liu L-L, Wu C-H, Qian P-Y. 2021. Identification of novel adhesive proteins in pearl oyster by proteomic and bioinformatic analysis. Biofouling.: 1–10. doi:https://doi.org/10.1080/08927014.2021.1901890
   Google Scholar
• Liu C, Zhang R. 2021. Identification of novel adhesive proteins in pearl oyster by proteomic and bioinformatic analysis. Biofouling. 37(3):299–308. https://doi.org/10.1080/08927014.2021.1901890
   PubMed Web of Science ®Google Scholar
• Marie B, Joubert C, Tayalé A, Zanella-Cléon I, Belliard C, Piquemal D, Cochennec-Laureau N, Marin F, Gueguen Y, Montagnani C. 2012. Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell. Proc Natl Acad Sci U S A. 109:20986–20991. doi:https://doi.org/10.1073/pnas.1210552109
   PubMed Web of Science ®Google Scholar
• Martinez Rodriguez NR, Das S, Kaufman Y, Israelachvili JN, Waite JH. 2015. Interfacial pH during mussel adhesive plaque formation. Biofouling. 31:221–227. doi:https://doi.org/10.1080/08927014.2015.1026337
   PubMed Web of Science ®Google Scholar
• McDougall C, Moase P, Degnan BM. 2016. Host and donor influence on pearls produced by the silver-lip pearl oyster, Pinctada maxima. Aquaculture. 450:313–320. doi:https://doi.org/10.1016/j.aquaculture.2015.08.008
   Web of Science ®Google Scholar
• McDougall C, Woodcroft BJ, Degnan BM. 2016. The widespread prevalence and functional significance of silk-like structural proteins in metazoan biological materials. PLoS One. 11:e0159128. doi:https://doi.org/10.1371/journal.pone.0159128
   PubMed Web of Science ®Google Scholar
• Miao Y, Zhang L, Sun Y, Jiao W, Li Y, Sun J, Wang Y, Wang S, Bao Z, Liu W. 2015. Integration of transcriptomic and proteomic approaches provides a core set of genes for understanding of scallop attachment. Mar Biotechnol (NY). 17:523–532. doi:https://doi.org/10.1007/s10126-015-9635-y
   PubMed Web of Science ®Google Scholar
• Ni G, Liang D, Cummins SF, Walton SF, Chen S, Wang Y, Mounsey K, Wei MQ, Yuan J, Pan X, et al. 2018. Comparative proteomic study of the antiproliferative activity of frog host-defence peptide caerin 1.9 and its additive effect with caerin 1.1 on TC-1 Cells transformed with HPV16 E6 and E7. Biomed Res Int. 2018:7382351. doi:https://doi.org/10.1155/2018/7382351
   PubMed Web of Science ®Google Scholar
• Nicklisch SC, Spahn JE, Zhou H, Gruian CM, Waite JH. 2016. Redox capacity of an extracellular matrix protein associated with adhesion in Mytilus californianus. Biochemistry. 55:2022–2030. doi:https://doi.org/10.1021/acs.biochem.6b00044
   PubMed Web of Science ®Google Scholar
• Partlow BP, Applegate MB, Omenetto FG, Kaplan DL. 2016. Dityrosine cross-linking in designing biomaterials. ACS Biomater Sci Eng. 2:2108–2121. doi:https://doi.org/10.1021/acsbiomaterials.6b00454
   PubMed Web of Science ®Google Scholar
• Pasche D, Horbelt N, Marin F, Motreuil S, Macías-Sánchez E, Falini G, Hwang DS, Fratzl P, Harrington MJ. 2018. A new twist on sea silk: the peculiar protein ultrastructure of fan shell and pearl oyster byssus. Soft Matter. 14:5654–5664. doi:https://doi.org/10.1039/c8sm00821c
   PubMed Web of Science ®Google Scholar
• Paulsson G, Lendahl U, Galli J, Ericsson C, Wieslander L. 1990. The Balbiani ring 3 gene in Chironomus tentans has a diverged repetitive structure split by many introns. J Mol Biol. 211:331–349. doi:https://doi.org/10.1016/0022-2836(90)90355-P
   PubMed Web of Science ®Google Scholar
• Pearce T, LaBarbera M. 2009. A comparative study of the mechanical properties of mytilid byssal threads. J Exp Biol. 212:1442–1448. doi:https://doi.org/10.1242/jeb.025544
   PubMed Web of Science ®Google Scholar
• Priemel T, Degtyar E, Dean MN, Harrington MJ. 2017. Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication. Nat Commun. 8:14539. doi:https://doi.org/10.1038/ncomms14539
   PubMed Web of Science ®Google Scholar
• Pujol JP. 1967. Formation of the byssus in the common mussel (Mytilus edulis L.) [47] [Letter]. Nature. 214:204–205. doi:https://doi.org/10.1038/214204a0
   Web of Science ®Google Scholar
• Pujol JP, Rolland M, Larsy S, Vinet S. 1970. Comparative study of the amino acid composition of the byssus in some common bivalve molluscs. Comp Biochem Physiol. 34:193–201. doi:https://doi.org/10.1016/0010-406X(70)90066-6
   Google Scholar
• Qin XX, Coyne KJ, Waite JH. 1997. Tough tendons. Mussel byssus has collagen with silk-like domains. J Biol Chem. 272:32623–32627. doi:https://doi.org/10.1074/jbc.272.51.32623
   PubMed Web of Science ®Google Scholar
• Qin CL, Pan QD, Qi Q, Fan MH, Sun JJ, Li NN, Liao Z. 2016. In-depth proteomic analysis of the byssus from marine mussel Mytilus coruscus. J Proteomics. 144:87–98. doi:https://doi.org/10.1016/j.jprot.2016.06.014
   PubMed Web of Science ®Google Scholar
• Qin X, Waite JH. 1995. Exotic collagen gradients in the byssus of the mussel Mytilus edulis. J Exp Biol. 198:633–644. doi:https://doi.org/10.1242/jeb.198.3.633
   PubMed Web of Science ®Google Scholar
• Qin XX, Waite JH. 1998. A potential mediator of collagenous block copolymer gradients in mussel byssal threads. Proc Natl Acad Sci U S A. 95:10517–10522. doi:https://doi.org/10.1073/pnas.95.18.10517
   PubMed Web of Science ®Google Scholar
• Robinson MD, Oshlack A. 2010. A scaling normalization method for differential expression analysis of RNA-seq data. Genome Biol. 11:R25. doi:https://doi.org/10.1186/gb-2010-11-3-r25
   PubMed Web of Science ®Google Scholar
• Robinson NE, Robinson AB. 2001. Prediction of protein deamidation rates from primary and three-dimensional structure. Proc Natl Acad Sci U S A. 98:4367–4372. doi:https://doi.org/10.1073/pnas.071066498
   PubMed Web of Science ®Google Scholar
• Rodríguez F, Morán L, González G, Troncoso E, Zúñiga RN. 2017. Collagen extraction from mussel byssus: a new marine collagen source with physicochemical properties of industrial interest. J Food Sci Technol. 54:1228–1238. doi:https://doi.org/10.1007/s13197-017-2566-z
   PubMed Web of Science ®Google Scholar
• Rosini S, Pugh N, Bonna AM, Hulmes DJS, Farndale RW, Adams JC. 2018. Thrombospondin-1 promotes matrix homeostasis by interacting with collagen and lysyl oxidase precursors and collagen cross-linking sites. Sci Signaling. 11:eaar2566.
   PubMed Web of Science ®Google Scholar
• Sagert J, Sun C, Waite JH. 2006. Chemical subtleties of mussel and polychaete holdfasts. In Smith AM, Callow JA, editors. Biological adhesives. Berlin, Heidelberg: Springer Berlin Heidelberg; p. 125–143.
   Google Scholar
• Sagert J, Waite JH. 2009. Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis. J Exp Biol. 212:2224–2236. doi:https://doi.org/10.1242/jeb.029686
   PubMed Web of Science ®Google Scholar
• Silverman HG, Roberto FF. 2007. Understanding marine mussel adhesion. Mar Biotechnol (NY). 9:661–681. doi:https://doi.org/10.1007/s10126-007-9053-x
   PubMed Web of Science ®Google Scholar
• Sisco Bayse G, Morrison M. 1971. The role of peroxidase in catalyzing oxidation of polyphenols. Biochim Biophys Acta Gen Subj. 244:77–84. doi:https://doi.org/10.1016/0304-4165(71)90122-X
   Google Scholar
• Stewart MJ, Favrel P, Rotgans BA, Wang T, Zhao M, Sohail M, O'Connor WA, Elizur A, Henry J, Cummins SF. 2014. Neuropeptides encoded by the genomes of the Akoya pearl oyster Pinctata fucata and Pacific oyster Crassostrea gigas: a bioinformatic and peptidomic survey. BMC Genomics. 15:840–840. doi:https://doi.org/10.1186/1471-2164-15-840
   PubMed Web of Science ®Google Scholar
• Suhre MH, Gertz M, Steegborn C, Scheibel T. 2014. Structural and functional features of a collagen-binding matrix protein from the mussel byssus. Nat Commun. 5:3392. doi:https://doi.org/10.1038/ncomms4392
   PubMed Web of Science ®Google Scholar
• Sun C, Waite JH. 2005. Mapping chemical gradients within and along a fibrous structural tissue, mussel byssal threads. J Biol Chem. 280:39332–39336. doi:https://doi.org/10.1074/jbc.M508674200
   PubMed Web of Science ®Google Scholar
• Takeuchi T, Kawashima T, Koyanagi R, Gyoja F, Tanaka M, Ikuta T, Shoguchi E, Fujiwara M, Shinzato C, Hisata K, et al. 2012. Draft genome of the pearl oyster Pinctada fucata: a platform for understanding bivalve biology. DNA Res. 19:117–130. doi:https://doi.org/10.1093/dnares/dss005
   PubMed Web of Science ®Google Scholar
• Tamarin A. 1975. An ultrastructural study of byssus stem formation in Mytilus californianus. J Morphol. 145:151–177. doi:https://doi.org/10.1002/jmor.1051450204
   PubMed Web of Science ®Google Scholar
• Tamarin A, Lewis P, Askey J. 1976. The structure and formation of the byssus attachment plaque in Mytilus. J Morphol. 149:199–221. doi:https://doi.org/10.1002/jmor.1051490205
   PubMed Web of Science ®Google Scholar
• Taylor JJ, Rose RA, Southgate PC. 1997. Byssus production in six age classes of the silver-lip Pearl oyster, Pinctada maxima (Jameson). J Shellfish Res. 16:97–101.
   Web of Science ®Google Scholar
• Waite JH. 1986. Mussel glue from Mytilus californianus Conrad: a comparative study. J Comp Physiol B. 156:491–496. doi:https://doi.org/10.1007/BF00691034
   PubMed Web of Science ®Google Scholar
• Waite JH. 1992. The formation of mussel byssus: anatomy of a natural manufacturing process. In Case ST, editor. Structure, cellular synthesis and assembly of biopolymers. Berlin, Heidelberg: Springer Berlin Heidelberg; p. 27–54.
   Google Scholar
• Waite JH. 2002. Adhesion a la moule. Integr Comp Biol. 42:1172–1180. doi:https://doi.org/10.1093/icb/42.6.1172
   PubMed Web of Science ®Google Scholar
• Waite JH, Andersen NH, Jewhurst S, Sun C. 2005. Mussel adhesion: finding the tricks worth mimicking. J Adhes. 81:297–317. doi:https://doi.org/10.1080/00218460590944602
   Web of Science ®Google Scholar
• Waite JH, Lichtenegger HC, Stucky GD, Hansma P. 2004. Exploring molecular and mechanical gradients in structural bioscaffolds. Biochemistry. 43:7653–7662. doi:https://doi.org/10.1021/bi049380h
   PubMed Web of Science ®Google Scholar
• Waite JH, Qin XX, Coyne KJ. 1998. The peculiar collagens of mussel byssus. Matrix Biol. 17:93–106. doi:https://doi.org/10.1016/s0945-053x(98)90023-3
   PubMed Web of Science ®Google Scholar
• Waite JH, Vaccaro E, Sun C, Lucas JM. 2002. Elastomeric gradients: a hedge against stress concentration in marine holdfasts? Philos Trans R Soc Lond B Biol Sci. 357:143–153. doi:https://doi.org/10.1098/rstb.2001.1025
   PubMed Web of Science ®Google Scholar
• Wang N, Lee YH, Lee J. 2008. Recombinant perlucin nucleates the growth of calcium carbonate crystals: molecular cloning and characterization of perlucin from disk abalone, Haliotis discus discus. Comp Biochem Physiol B Biochem Mol Biol. 149:354–361. doi:https://doi.org/10.1016/j.cbpb.2007.10.007
   PubMed Web of Science ®Google Scholar
• Wang J, Scheibel T. 2018. Recombinant production of mussel byssus inspired proteins. Biotechnol J. 13:1800146. [. ]. doi:https://doi.org/10.1002/biot.201800146
   Web of Science ®Google Scholar
• Weiss IM, Kaufmann S, Mann K, Fritz M. 2000. Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata. Biochem Biophys Res Commun. 267:17–21. doi:https://doi.org/10.1006/bbrc.1999.1907
   PubMed Web of Science ®Google Scholar
• Whaite AD, Wang T, Macdonald J, Cummins SF. 2018. Major ampullate silk gland transcriptomes and fibre proteomes of the golden orb-weavers, Nephila plumipes and Nephila pilipes (Araneae: Nephilidae). PLoS One. 13:e0204243. doi:https://doi.org/10.1371/journal.pone.0204243
   PubMed Web of Science ®Google Scholar
• Wieslander L. 1994. The Balbiani ring multigene family: coding repetitive sequences and evolution of a tissue-specific cell function. Prog Nucleic Acid Res Mol Biol. 48, 275–313.
   PubMed Web of Science ®Google Scholar
• Wieslander L, Paulsson G. 1992. Sequence organization of the Balbiani ring 2.1 gene in Chironomus tentans. Proc Natl Acad Sci U S A. 89:4578–4582. doi:https://doi.org/10.1073/pnas.89.10.4578
   PubMed Web of Science ®Google Scholar
• Xu W, Faisal M. 2010. Factorial microarray analysis of zebra mussel (Dreissena polymorpha: Dreissenidae, Bivalvia) adhesion. BMC Genomics. 11:341–341. doi:https://doi.org/10.1186/1471-2164-11-341
   PubMed Web of Science ®Google Scholar
• Xu E-R, Lafita A, Bateman A, Hyvönen M. 2019. Thrombospondin module 1 domain (TSP1) of the matricellular protein CCN3 shows an atypical disulfide pattern and incomplete CWR layers. Acta crystallographica Section D, Structural biology. 76(Pt 2):124-134.
   Google Scholar
• Yap CK, Ismail A, Tan SG. 2005. Distributions of Cd, Cu, Pb and Zn in different parts of the byssus of the green-lipped mussel Perna viridis (Linnaeus) collected from contaminated and uncontaminated coastal waters. Malays Appl Biol. 34:7–13.
   Google Scholar
• Yoo HY, Iordachescu M, Huang J, Hennebert E, Kim S, Rho S, Foo M, Flammang P, Zeng H, Hwang D, et al. 2016. Sugary interfaces mitigate contact damage where stiff meets soft. Nat Commun. 7:11923. doi:https://doi.org/10.1038/ncomms11923
   PubMed Web of Science ®Google Scholar
• Yu J, Wei W, Danner E, Ashley RK, Israelachvili JN, Waite JH. 2011. Mussel protein adhesion depends on interprotein thiol-mediated redox modulation. Nat Chem Biol. 7:588–590. doi:https://doi.org/10.1038/nchembio.630
   PubMed Web of Science ®Google Scholar
• Zuccarello LV. 1980. The collagen gland of Mytilus galloprovincialis: An ultrastructural and cytochemical study on secretory granules. J Ultrastruct Res. 73:135–147. doi:https://doi.org/10.1016/S0022-5320(80)90119-7
   PubMedGoogle Scholar