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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
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High impact information on Strongylocentrotus

  • To analyze the mechanism of assembly of the fertilization membrane of the sea urchin Strongylocentrotus purpuratus, we inhibited the ovoperoxidase that catalyzes dityrosine formation to isolate an uncrosslinked, soft fertilization membrane (SFM) [1].
  • A sea urchin (Strongylocentrotus purpuratus) messenger RNA encoding a protein (SpEGF2) related to epidermal growth factor (EGF) was identified [2].
  • We have begun an investigation of the molecular basis for the temporal embryonic expression of the early histone H3 gene of the sea urchin Strongylocentrotus purpuratus [3].
  • We report the unexpected observation that cis-regulatory sequences of a Strongylocentrotus purpuratus actin gene, which direct a particular, lineage-specific pattern of embryonic expression, confer a completely different spatial pattern of expression when introduced into embryos of another sea urchin species [4].
  • beta-Tubulin mRNAs associated with cilium formation in Strongylocentrotus purpurpatus sea urchin embryos are expressed selectively from a multiple gene family [5].

Biological context of Strongylocentrotus


Anatomical context of Strongylocentrotus


Associations of Strongylocentrotus with chemical compounds

  • Strongylocentrotus purpuratus eggs were treated with dithiothreitol to modify the vitelline layer and to prevent formation of a fertilization membrane [16].
  • The Strongylocentrotus purpuratus sea urchin egg receptor for sperm is a cell surface glycoprotein with a molecular mass of 350 kDa [17].
  • During the first 6 hr after fertilization of freshly obtained sea urchin eggs (Strongylocentrotus purpuratus), which are incubated in the presence of exogenous [3H]-spermidine, up to 7% of the total cell-associated spermidine appears uniquely as spermidine bound in macromolecular form [18].
  • In studies on the antiproliferative actions of coumarin compounds, we discovered that dicoumarol (a coumarin anticoagulant; 3,3'-methylenebis[4-hydroxycoumarin]) inhibits the first cleavage of Strongylocentrotus purpuratus (sea urchin) embryos in a concentration-dependent manner with 50% inhibition occurring at a concentration of 10 microM [19].
  • The ECM of three species of sea urchin, Strongylocentrotus purpuratus, Lytechinus variegatus and Lytechinus pictus, was disrupted with the lathrytic agent beta-aminopropionitrile (BAPN), which inhibits collagen deposition in the ECM and arrests gastrulation (Wessel & McClay, Devl Biol. 121: 149, 1987) [20].

Gene context of Strongylocentrotus

  • The heterotrimeric kinesin-II holoenzyme purified from sea urchin (Strongylocentrotus purpuratus) eggs is assembled from two heterodimerized kinesin-related motor subunits of known sequence, together with a third, previously uncharacterized 115-kD subunit, SpKAP115 [21].
  • Evolution of late H2A, H2B, and H4 histone genes of the sea urchin, Strongylocentrotus purpuratus [22].
  • We describe here the isolation and characterization of several cDNA clones that encode a single 30.6-kDa Strongylocentrotus purpuratus spicule matrix protein designated SM30 [23].
  • We have identified a gene in the sea urchin Strongylocentrotus purpuratus that encodes a member of the transforming growth factor beta (TGF-beta) gene superfamily [24].
  • Amino acid microsequencing of one of these proteins led to the identification of a 4.75-kb cDNA clone from a Strongylocentrotus purpuratus ovary cDNA library that encodes a 160-kDa protein called p160 [25].

Analytical, diagnostic and therapeutic context of Strongylocentrotus


  1. Assembly of the fertilization membrane of the sea urchin: isolation of a divalent cation-dependent intermediate and its crosslinking in vitro. Kay, E., Eddy, E.M., Shapiro, B.M. Cell (1982) [Pubmed]
  2. Unusual pattern of accumulation of mRNA encoding EGF-related protein in sea urchin embryos. Yang, Q., Angerer, L.M., Angerer, R.C. Science (1989) [Pubmed]
  3. Developmental control of promoter-specific factors responsible for the embryonic activation and inactivation of the sea urchin early histone H3 gene. DiLiberto, M., Lai, Z.C., Fei, H., Childs, G. Genes Dev. (1989) [Pubmed]
  4. Spatially deranged though temporally correct expression of Strongylocentrotus purpuratus actin gene fusion in transgenic embryos of a different sea urchin family. Franks, R.R., Hough-Evans, B.R., Britten, R.J., Davidson, E.H. Genes Dev. (1988) [Pubmed]
  5. Coordinate and selective beta-tubulin gene expression associated with cilium formation in sea urchin embryos. Harlow, P., Nemer, M. Genes Dev. (1987) [Pubmed]
  6. SpCOUP-TF: a sea urchin member of the steroid/thyroid hormone receptor family. Chan, S.M., Xu, N., Niemeyer, C.C., Bone, J.R., Flytzanis, C.N. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  7. The Drosophila erect wing gene, which is important for both neuronal and muscle development, encodes a protein which is similar to the sea urchin P3A2 DNA binding protein. DeSimone, S.M., White, K. Mol. Cell. Biol. (1993) [Pubmed]
  8. Organization and evolution of the actin gene family in sea urchins. Johnson, P.J., Foran, D.R., Moore, G.P. Mol. Cell. Biol. (1983) [Pubmed]
  9. Negative spatial regulation of the lineage specific CyIIIa actin gene in the sea urchin embryo. Hough-Evans, B.R., Franks, R.R., Zeller, R.W., Britten, R.J., Davidson, E.H. Development (1990) [Pubmed]
  10. Tyrosine protein kinase activity during embryogenesis. Dasgupta, J.D., Garbers, D.L. J. Biol. Chem. (1983) [Pubmed]
  11. Colchicine-binding activity distinguishes sea urchin egg and outer doublet tubulins. Wilson, L., Miller, H.P., Pfeffer, T.A., Sullivan, K.F., Detrich, H.W. J. Cell Biol. (1984) [Pubmed]
  12. Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer. Ward, G.E., Brokaw, C.J., Garbers, D.L., Vacquier, V.D. J. Cell Biol. (1985) [Pubmed]
  13. Localization of tektin filaments in microtubules of sea urchin sperm flagella by immunoelectron microscopy. Linck, R.W., Amos, L.A., Amos, W.B. J. Cell Biol. (1985) [Pubmed]
  14. Sequence of mRNA coding for bindin, a species-specific sea urchin sperm protein required for fertilization. Gao, B., Klein, L.E., Britten, R.J., Davidson, E.H. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  15. Sea urchin early and late H4 histone genes bind a specific transcription factor in a stable preinitiation complex. Tung, L., Morris, G.F., Yager, L.N., Weinberg, E.S. Mol. Cell. Biol. (1989) [Pubmed]
  16. Changes in the topography of the sea urchin egg after fertilization. Eddy, E.M., Shapiro, B.M. J. Cell Biol. (1976) [Pubmed]
  17. Identification of sulfated oligosialic acid units in the O-linked glycan of the sea urchin egg receptor for sperm. Kitazume-Kawaguchi, S., Inoue, S., Inoue, Y., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  18. Spermidine is bound to a unique protein in early sea urchin embryos. Canellakis, Z.N., Bondy, P.K., Infante, A.A. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  19. Dicoumarol: a unique microtubule stabilizing natural product that is synergistic with Taxol. Madari, H., Panda, D., Wilson, L., Jacobs, R.S. Cancer Res. (2003) [Pubmed]
  20. Transcription of the Spec 1-like gene of Lytechinus is selectively inhibited in response to disruption of the extracellular matrix. Wessel, G.M., Zhang, W., Tomlinson, C.R., Lennarz, W.J., Klein, W.H. Development (1989) [Pubmed]
  21. Sequence and submolecular localization of the 115-kD accessory subunit of the heterotrimeric kinesin-II (KRP85/95) complex. Wedaman, K.P., Meyer, D.W., Rashid, D.J., Cole, D.G., Scholey, J.M. J. Cell Biol. (1996) [Pubmed]
  22. Evolution of late H2A, H2B, and H4 histone genes of the sea urchin, Strongylocentrotus purpuratus. Maxson, R., Mohun, T., Gormezano, G., Kedes, L. Nucleic Acids Res. (1987) [Pubmed]
  23. Characterization and expression of a gene encoding a 30.6-kDa Strongylocentrotus purpuratus spicule matrix protein. George, N.C., Killian, C.E., Wilt, F.H. Dev. Biol. (1991) [Pubmed]
  24. The univin gene encodes a member of the transforming growth factor-beta superfamily with restricted expression in the sea urchin embryo. Stenzel, P., Angerer, L.M., Smith, B.J., Angerer, R.C., Vale, W.W. Dev. Biol. (1994) [Pubmed]
  25. Proteolytic cleavage of the cell surface protein p160 is required for detachment of the fertilization envelope in the sea urchin. Haley, S.A., Wessel, G.M. Dev. Biol. (2004) [Pubmed]
  26. Cytoplasmic dynein-like ATPase cross-links microtubules in an ATP-sensitive manner. Hollenbeck, P.J., Suprynowicz, F., Cande, W.Z. J. Cell Biol. (1984) [Pubmed]
  27. Molecular cloning of the first metazoan beta-1,3 glucanase from eggs of the sea urchin Strongylocentrotus purpuratus. Bachman, E.S., McClay, D.R. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  28. Sea urchin FGFR muscle-specific expression: posttranscriptional regulation in embryos and adults. McCoon, P.E., Blackstone, E., Angerer, R.C., Angerer, L.M. Dev. Biol. (1998) [Pubmed]
  29. Cloning and characterization of alphaP integrin in embryos of the sea urchin Strongylocentrotus purpuratus. Susan, J.M., Just, M.L., Lennarz, W.J. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
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