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Volumn 7, Issue 9, 2012, Pages

Evolution of Genes Involved in Gamete Interaction: Evidence for Positive Selection, Duplications and Losses in Vertebrates

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Indexed keywords

AMINO ACID;

EID: 84866037420     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044548     Document Type: Article
Times cited : (43)

References (115)
  • 1
    • 85047700164 scopus 로고    scopus 로고
    • The rapid evolution of reproductive proteins
    • Swanson WJ, Vacquier VD, (2002) The rapid evolution of reproductive proteins. Nat Rev Genet 3: 137-144.
    • (2002) Nat Rev Genet , vol.3 , pp. 137-144
    • Swanson, W.J.1    Vacquier, V.D.2
  • 2
    • 0034688140 scopus 로고    scopus 로고
    • Rapid evolution of male reproductive genes in the descent of man
    • Wyckoff GJ, Wang W, Wu CI, (2000) Rapid evolution of male reproductive genes in the descent of man. Nature 403: 304-309.
    • (2000) Nature , vol.403 , pp. 304-309
    • Wyckoff, G.J.1    Wang, W.2    Wu, C.I.3
  • 3
    • 0037230001 scopus 로고    scopus 로고
    • Pervasive adaptive evolution in mammalian fertilization proteins
    • Swanson WJ, Nielsen R, Yang Q, (2003) Pervasive adaptive evolution in mammalian fertilization proteins. Mol Biol Evol 20: 18-20.
    • (2003) Mol Biol Evol , vol.20 , pp. 18-20
    • Swanson, W.J.1    Nielsen, R.2    Yang, Q.3
  • 4
    • 0035957018 scopus 로고    scopus 로고
    • Positive Darwinian selection drives the evolution of several female reproductive proteins in mammals
    • Swanson WJ, Yang Z, Wolfner MF, Aquadro CF, (2001) Positive Darwinian selection drives the evolution of several female reproductive proteins in mammals. Proc Natl Acad Sci U S A 98: 2509-2514.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2509-2514
    • Swanson, W.J.1    Yang, Z.2    Wolfner, M.F.3    Aquadro, C.F.4
  • 5
    • 85082784971 scopus 로고
    • Columbia University Press
    • Dobzhansky T (1964) Columbia University Press.
    • (1964)
    • Dobzhansky, T.1
  • 6
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill JD, editors. New York: Raven Press
    • Yanagimachi R (1994) Mammalian fertilization. In: Knobil E, Neill JD, editors. The physiology of reproduction. New York: Raven Press. 189-317.
    • (1994) The physiology of reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 7
    • 0027948083 scopus 로고
    • Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization
    • Baba T, Azuma S, Kashiwabara S, Toyoda Y, (1994) Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J Biol Chem 269: 31845-31849.
    • (1994) J Biol Chem , vol.269 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.3    Toyoda, Y.4
  • 8
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly
    • Lu Q, Shur BD, (1997) Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly. Development 124: 4121-4131.
    • (1997) Development , vol.124 , pp. 4121-4131
    • Lu, Q.1    Shur, B.D.2
  • 9
    • 43249100861 scopus 로고    scopus 로고
    • Phylogenetic analysis and identification of pseudogenes reveal a progressive loss of zona pellucida genes during evolution of vertebrates
    • Goudet G, Mugnier S, Callebaut I, Monget P, (2008) Phylogenetic analysis and identification of pseudogenes reveal a progressive loss of zona pellucida genes during evolution of vertebrates. Biol Reprod 78: 796-806.
    • (2008) Biol Reprod , vol.78 , pp. 796-806
    • Goudet, G.1    Mugnier, S.2    Callebaut, I.3    Monget, P.4
  • 10
    • 35548959474 scopus 로고    scopus 로고
    • A novel function for CRISP1 in rodent fertilization: involvement in sperm-zona pellucida interaction-Evidence for the involvement of testicular protein CRISP2 in mouse sperm-egg fusion
    • Busso D, Cohen DJ, Maldera JA, Dematteis A, Cuasnicu PS, et al. (2007) A novel function for CRISP1 in rodent fertilization: involvement in sperm-zona pellucida interaction-Evidence for the involvement of testicular protein CRISP2 in mouse sperm-egg fusion. Biol Reprod 77: 848-854.
    • (2007) Biol Reprod , vol.77 , pp. 848-854
    • Busso, D.1    Cohen, D.J.2    Maldera, J.A.3    Dematteis, A.4    Cuasnicu, P.S.5
  • 11
    • 54249121343 scopus 로고    scopus 로고
    • Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction
    • Cohen DJ, Busso D, Da Ros V, Ellerman DA, Maldera JA, et al. (2008) Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction. Int J Dev Biol 52: 737-742.
    • (2008) Int J Dev Biol , vol.52 , pp. 737-742
    • Cohen, D.J.1    Busso, D.2    Da Ros, V.3    Ellerman, D.A.4    Maldera, J.A.5
  • 12
    • 48949115341 scopus 로고    scopus 로고
    • Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
    • Da Ros VG, Maldera JA, Willis WD, Cohen DJ, Goulding EH, et al. (2008) Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1). Dev Biol 320: 12-18.
    • (2008) Dev Biol , vol.320 , pp. 12-18
    • Da Ros, V.G.1    Maldera, J.A.2    Willis, W.D.3    Cohen, D.J.4    Goulding, E.H.5
  • 13
    • 7244259101 scopus 로고    scopus 로고
    • Genome duplication in the teleost fish Tetraodon nigroviridis reveals the early vertebrate proto-karyotype
    • Jaillon O, Aury JM, Brunet F, Petit JL, Stange-Thomann N, et al. (2004) Genome duplication in the teleost fish Tetraodon nigroviridis reveals the early vertebrate proto-karyotype. Nature 431: 946-957.
    • (2004) Nature , vol.431 , pp. 946-957
    • Jaillon, O.1    Aury, J.M.2    Brunet, F.3    Petit, J.L.4    Stange-Thomann, N.5
  • 14
    • 77951766330 scopus 로고    scopus 로고
    • Teleost fish with specific genome duplication as unique models of vertebrate evolution
    • Sato Y, Nishida M, (2010) Teleost fish with specific genome duplication as unique models of vertebrate evolution. Environmental Biology of Fishes 88: 169-188.
    • (2010) Environmental Biology of Fishes , vol.88 , pp. 169-188
    • Sato, Y.1    Nishida, M.2
  • 15
    • 79959960522 scopus 로고    scopus 로고
    • PhyleasProg: a user-oriented web server for wide evolutionary analyses
    • Busset J, Cabau C, Meslin C, Pascal G, (2011) PhyleasProg: a user-oriented web server for wide evolutionary analyses. Nucleic Acids Res 39: W479-485.
    • (2011) Nucleic Acids Res , vol.39
    • Busset, J.1    Cabau, C.2    Meslin, C.3    Pascal, G.4
  • 16
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: phylogenetic analysis by maximum likelihood
    • Yang Z, (2007) PAML 4: phylogenetic analysis by maximum likelihood. Mol Biol Evol 24: 1586-1591.
    • (2007) Mol Biol Evol , vol.24 , pp. 1586-1591
    • Yang, Z.1
  • 17
    • 50649104620 scopus 로고    scopus 로고
    • Pervasive positive selection on duplicated and nonduplicated vertebrate protein coding genes
    • Studer RA, Penel S, Duret L, Robinson-Rechavi M, (2008) Pervasive positive selection on duplicated and nonduplicated vertebrate protein coding genes. Genome Res 18: 1393-1402.
    • (2008) Genome Res , vol.18 , pp. 1393-1402
    • Studer, R.A.1    Penel, S.2    Duret, L.3    Robinson-Rechavi, M.4
  • 18
    • 72649091351 scopus 로고    scopus 로고
    • ZP domain proteins in the abalone egg coat include a paralog of VERL under positive selection that binds lysin and 18-kDa sperm proteins
    • Aagaard JE, Vacquier VD, MacCoss MJ, Swanson WJ, (2010) ZP domain proteins in the abalone egg coat include a paralog of VERL under positive selection that binds lysin and 18-kDa sperm proteins. Mol Biol Evol 27: 193-203.
    • (2010) Mol Biol Evol , vol.27 , pp. 193-203
    • Aagaard, J.E.1    Vacquier, V.D.2    MacCoss, M.J.3    Swanson, W.J.4
  • 19
    • 1842557435 scopus 로고    scopus 로고
    • Adaptive Evolution of Sperm Bindin Tracks Egg Incompatibility in Neotropical Sea Urchins of the Genus Echinometra
    • McCartney MA, Lessios HA, (2004) Adaptive Evolution of Sperm Bindin Tracks Egg Incompatibility in Neotropical Sea Urchins of the Genus Echinometra. Molecular Biology and Evolution 21: 732-745.
    • (2004) Molecular Biology and Evolution , vol.21 , pp. 732-745
    • McCartney, M.A.1    Lessios, H.A.2
  • 20
    • 0037326867 scopus 로고    scopus 로고
    • Positive selection on an acrosomal sperm protein, M7 lysin, in three species of the mussel genus Mytilus
    • Riginos C, McDonald JH, (2003) Positive selection on an acrosomal sperm protein, M7 lysin, in three species of the mussel genus Mytilus. Mol Biol Evol 20: 200-207.
    • (2003) Mol Biol Evol , vol.20 , pp. 200-207
    • Riginos, C.1    McDonald, J.H.2
  • 21
    • 0031037939 scopus 로고    scopus 로고
    • Positive Darwinian selection on two homologous fertilization proteins: what is the selective pressure driving their divergence
    • Vacquier VD, Swanson WJ, Lee YH, (1997) Positive Darwinian selection on two homologous fertilization proteins: what is the selective pressure driving their divergence? J Mol Evol 44 (Suppl 1):: S15-22.
    • (1997) J Mol Evol , vol.44 , Issue.SUPPL. 1
    • Vacquier, V.D.1    Swanson, W.J.2    Lee, Y.H.3
  • 22
    • 28744452463 scopus 로고    scopus 로고
    • Testing for adaptive evolution of the female reproductive protein ZPC in mammals, birds and fishes reveals problems with the M7-M8 likelihood ratio test
    • Berlin S, Smith NG, (2005) Testing for adaptive evolution of the female reproductive protein ZPC in mammals, birds and fishes reveals problems with the M7-M8 likelihood ratio test. BMC Evol Biol 5: 65.
    • (2005) BMC Evol Biol , vol.5 , pp. 65
    • Berlin, S.1    Smith, N.G.2
  • 24
    • 80955159863 scopus 로고    scopus 로고
    • A Structural View of Egg-Coat Architecture and Function in Fertilization
    • Monne M, Jovine L (2011) A Structural View of Egg-Coat Architecture and Function in Fertilization. Biol Reprod.
    • (2011) Biol Reprod.
    • Monne, M.1    Jovine, L.2
  • 25
    • 14544281087 scopus 로고    scopus 로고
    • Positive selection of primate TRIM5alpha identifies a critical species-specific retroviral restriction domain
    • Sawyer SL, Wu LI, Emerman M, Malik HS, (2005) Positive selection of primate TRIM5alpha identifies a critical species-specific retroviral restriction domain. Proc Natl Acad Sci U S A 102: 2832-2837.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2832-2837
    • Sawyer, S.L.1    Wu, L.I.2    Emerman, M.3    Malik, H.S.4
  • 26
    • 85082786455 scopus 로고    scopus 로고
    • Positions under positive selection - key for selectivity and potency of scorpion {alpha}-toxins
    • Weinberger H, Moran Y, Gordon D, Turkov M, Kahn R, et al. (2009) Positions under positive selection- key for selectivity and potency of scorpion {alpha}-toxins. Mol Biol Evol 17: 17.
    • (2009) Mol Biol Evol , vol.17 , pp. 17
    • Weinberger, H.1    Moran, Y.2    Gordon, D.3    Turkov, M.4    Kahn, R.5
  • 27
    • 65249090252 scopus 로고    scopus 로고
    • Gene birth, death, and divergence: the different scenarios of reproduction-related gene evolution
    • Tian X, Pascal G, Fouchecourt S, Pontarotti P, Monget P, (2009) Gene birth, death, and divergence: the different scenarios of reproduction-related gene evolution. Biol Reprod 80: 616-621.
    • (2009) Biol Reprod , vol.80 , pp. 616-621
    • Tian, X.1    Pascal, G.2    Fouchecourt, S.3    Pontarotti, P.4    Monget, P.5
  • 28
    • 0042424602 scopus 로고    scopus 로고
    • Statistical significance for genomewide studies
    • Storey JD, Tibshirani R, (2003) Statistical significance for genomewide studies. Proc Natl Acad Sci U S A 100: 9440-9445.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9440-9445
    • Storey, J.D.1    Tibshirani, R.2
  • 30
    • 0026499429 scopus 로고
    • Conservation evaluation and phylogenetic diversity
    • Faith DP, (1992) Conservation evaluation and phylogenetic diversity. Biological Conservation 61: 1-10.
    • (1992) Biological Conservation , vol.61 , pp. 1-10
    • Faith, D.P.1
  • 31
    • 84960578999 scopus 로고
    • Squared-change parsimony reconstructions of ancestral states for continuous-valued characters on a phylogenetic tree
    • Maddison WP, (1991) Squared-change parsimony reconstructions of ancestral states for continuous-valued characters on a phylogenetic tree. Systematic Zoology 40: 304-314.
    • (1991) Systematic Zoology , vol.40 , pp. 304-314
    • Maddison, W.P.1
  • 33
    • 0022203256 scopus 로고
    • Phylogenies and the comparative method
    • Felsenstein J, (1985) Phylogenies and the comparative method. American Naturalist 125: 1-15.
    • (1985) American Naturalist , vol.125 , pp. 1-15
    • Felsenstein, J.1
  • 35
    • 60849092277 scopus 로고    scopus 로고
    • Evolution of ossification sequences in salamanders and urodele origins assessed through event-pairing and new methods
    • Germain D, Laurin M, (2009) Evolution of ossification sequences in salamanders and urodele origins assessed through event-pairing and new methods. Evol Dev 11: 170-190.
    • (2009) Evol Dev , vol.11 , pp. 170-190
    • Germain, D.1    Laurin, M.2
  • 36
    • 0346195665 scopus 로고    scopus 로고
    • Crystal structure of the human angiotensin-converting enzyme-lisinopril complex
    • Natesh R, Schwager SL, Sturrock ED, Acharya KR, (2003) Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421: 551-554.
    • (2003) Nature , vol.421 , pp. 551-554
    • Natesh, R.1    Schwager, S.L.2    Sturrock, E.D.3    Acharya, K.R.4
  • 37
    • 0000110931 scopus 로고
    • Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning
    • Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, et al. (1988) Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci U S A 85: 9386-9390.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 9386-9390
    • Soubrier, F.1    Alhenc-Gelas, F.2    Hubert, C.3    Allegrini, J.4    John, M.5
  • 38
    • 0027970068 scopus 로고
    • Identification of two active site residues in human angiotensin I-converting enzyme
    • Williams TA, Corvol P, Soubrier F, (1994) Identification of two active site residues in human angiotensin I-converting enzyme. J Biol Chem 269: 29430-29434.
    • (1994) J Biol Chem , vol.269 , pp. 29430-29434
    • Williams, T.A.1    Corvol, P.2    Soubrier, F.3
  • 39
    • 0029925360 scopus 로고    scopus 로고
    • Mice lacking angiotensin-converting enzyme have low blood pressure, renal pathology, and reduced male fertility
    • Esther CR Jr, Howard TE, Marino EM, Goddard JM, Capecchi MR, et al. (1996) Mice lacking angiotensin-converting enzyme have low blood pressure, renal pathology, and reduced male fertility. Lab Invest 74: 953-965.
    • (1996) Lab Invest , vol.74 , pp. 953-965
    • Esther Jr., C.R.1    Howard, T.E.2    Marino, E.M.3    Goddard, J.M.4    Capecchi, M.R.5
  • 41
    • 0029060861 scopus 로고
    • Male-female differences in fertility and blood pressure in ACE-deficient mice
    • Krege JH, John SW, Langenbach LL, Hodgin JB, Hagaman JR, et al. (1995) Male-female differences in fertility and blood pressure in ACE-deficient mice. Nature 375: 146-148.
    • (1995) Nature , vol.375 , pp. 146-148
    • Krege, J.H.1    John, S.W.2    Langenbach, L.L.3    Hodgin, J.B.4    Hagaman, J.R.5
  • 42
    • 0034815743 scopus 로고    scopus 로고
    • Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
    • Cohen DJ, Ellerman DA, Busso D, Morgenfeld MM, Piazza AD, et al. (2001) Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg. Biol Reprod 65: 1000-1005.
    • (2001) Biol Reprod , vol.65 , pp. 1000-1005
    • Cohen, D.J.1    Ellerman, D.A.2    Busso, D.3    Morgenfeld, M.M.4    Piazza, A.D.5
  • 43
    • 55549122993 scopus 로고    scopus 로고
    • Effects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa
    • Chiu PC, Wong BS, Chung MK, Lam KK, Pang RT, et al. (2008) Effects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa. Biol Reprod 79: 869-877.
    • (2008) Biol Reprod , vol.79 , pp. 869-877
    • Chiu, P.C.1    Wong, B.S.2    Chung, M.K.3    Lam, K.K.4    Pang, R.T.5
  • 44
    • 77954600245 scopus 로고    scopus 로고
    • Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein
    • Gahlay G, Gauthier L, Baibakov B, Epifano O, Dean J, (2010) Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein. Science 329: 216-219.
    • (2010) Science , vol.329 , pp. 216-219
    • Gahlay, G.1    Gauthier, L.2    Baibakov, B.3    Epifano, O.4    Dean, J.5
  • 45
    • 11244280891 scopus 로고    scopus 로고
    • Isolation and mapping the chicken zona pellucida genes: an insight into the evolution of orthologous genes in different species
    • Smith J, Paton IR, Hughes DC, Burt DW, (2005) Isolation and mapping the chicken zona pellucida genes: an insight into the evolution of orthologous genes in different species. Mol Reprod Dev 70: 133-145.
    • (2005) Mol Reprod Dev , vol.70 , pp. 133-145
    • Smith, J.1    Paton, I.R.2    Hughes, D.C.3    Burt, D.W.4
  • 46
    • 35548935984 scopus 로고    scopus 로고
    • Dipeptidase-inactivated tACE action in vivo: selective inhibition of sperm-zona pellucida binding in the mouse
    • Deguchi E, Tani T, Watanabe H, Yamada S, Kondoh G, (2007) Dipeptidase-inactivated tACE action in vivo: selective inhibition of sperm-zona pellucida binding in the mouse. Biol Reprod 77: 794-802.
    • (2007) Biol Reprod , vol.77 , pp. 794-802
    • Deguchi, E.1    Tani, T.2    Watanabe, H.3    Yamada, S.4    Kondoh, G.5
  • 47
    • 0043029287 scopus 로고    scopus 로고
    • Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding
    • Ensslin MA, Shur BD, (2003) Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding. Cell 114: 405-417.
    • (2003) Cell , vol.114 , pp. 405-417
    • Ensslin, M.A.1    Shur, B.D.2
  • 48
    • 0037296759 scopus 로고    scopus 로고
    • Sperm surface hyaluronan binding protein (HABP1) interacts with zona pellucida of water buffalo (Bubalus bubalis) through its clustered mannose residues
    • Ghosh I, Datta K, (2003) Sperm surface hyaluronan binding protein (HABP1) interacts with zona pellucida of water buffalo (Bubalus bubalis) through its clustered mannose residues. Mol Reprod Dev 64: 235-244.
    • (2003) Mol Reprod Dev , vol.64 , pp. 235-244
    • Ghosh, I.1    Datta, K.2
  • 49
    • 0036119370 scopus 로고    scopus 로고
    • Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice
    • Saxena DK, Oh-Oka T, Kadomatsu K, Muramatsu T, Toshimori K, (2002) Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice. Reproduction 123: 435-444.
    • (2002) Reproduction , vol.123 , pp. 435-444
    • Saxena, D.K.1    Oh-Oka, T.2    Kadomatsu, K.3    Muramatsu, T.4    Toshimori, K.5
  • 50
    • 0028909347 scopus 로고
    • Expression of the rabbit sperm protein Sp17 in COS cells and interaction of recombinant Sp17 with the rabbit zona pellucida
    • Yamasaki N, Richardson RT, O'Rand MG, (1995) Expression of the rabbit sperm protein Sp17 in COS cells and interaction of recombinant Sp17 with the rabbit zona pellucida. Mol Reprod Dev 40: 48-55.
    • (1995) Mol Reprod Dev , vol.40 , pp. 48-55
    • Yamasaki, N.1    Richardson, R.T.2    O'Rand, M.G.3
  • 51
    • 20444459926 scopus 로고    scopus 로고
    • Binding of recombinant human proacrosin/acrosin to zona pellucida (ZP) glycoproteins. I. Studies with recombinant human ZPA, ZPB, and ZPC
    • Furlong LI, Harris JD, Vazquez-Levin MH, (2005) Binding of recombinant human proacrosin/acrosin to zona pellucida (ZP) glycoproteins. I. Studies with recombinant human ZPA, ZPB, and ZPC. Fertil Steril 83: 1780-1790.
    • (2005) Fertil Steril , vol.83 , pp. 1780-1790
    • Furlong, L.I.1    Harris, J.D.2    Vazquez-Levin, M.H.3
  • 52
    • 0025801542 scopus 로고
    • Inhibition of the mouse sperm surface alpha-D-mannosidase inhibits sperm-egg binding in vitro
    • Cornwall GA, Tulsiani DR, Orgebin-Crist MC, (1991) Inhibition of the mouse sperm surface alpha-D-mannosidase inhibits sperm-egg binding in vitro. Biol Reprod 44: 913-921.
    • (1991) Biol Reprod , vol.44 , pp. 913-921
    • Cornwall, G.A.1    Tulsiani, D.R.2    Orgebin-Crist, M.C.3
  • 53
    • 34748822250 scopus 로고    scopus 로고
    • Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis
    • Lin YN, Roy A, Yan W, Burns KH, Matzuk MM, (2007) Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol Cell Biol 27: 6794-6805.
    • (2007) Mol Cell Biol , vol.27 , pp. 6794-6805
    • Lin, Y.N.1    Roy, A.2    Yan, W.3    Burns, K.H.4    Matzuk, M.M.5
  • 54
    • 0034746758 scopus 로고    scopus 로고
    • Subcellular localization of beta1,4-galactosyltransferase on bull sperm and its function during sperm-egg interactions
    • Tengowski MW, Wassler MJ, Shur BD, Schatten G, (2001) Subcellular localization of beta1,4-galactosyltransferase on bull sperm and its function during sperm-egg interactions. Mol Reprod Dev 58: 236-244.
    • (2001) Mol Reprod Dev , vol.58 , pp. 236-244
    • Tengowski, M.W.1    Wassler, M.J.2    Shur, B.D.3    Schatten, G.4
  • 55
    • 0035578387 scopus 로고    scopus 로고
    • Calmegin is required for fertilin alpha/beta heterodimerization and sperm fertility
    • Ikawa M, Nakanishi T, Yamada S, Wada I, Kominami K, et al. (2001) Calmegin is required for fertilin alpha/beta heterodimerization and sperm fertility. Dev Biol 240: 254-261.
    • (2001) Dev Biol , vol.240 , pp. 254-261
    • Ikawa, M.1    Nakanishi, T.2    Yamada, S.3    Wada, I.4    Kominami, K.5
  • 56
    • 0028108577 scopus 로고
    • Human sperm-zona pellucida interaction is inhibited by an antiserum against a hamster sperm protein
    • Boue F, Berube B, De Lamirande E, Gagnon C, Sullivan R, (1994) Human sperm-zona pellucida interaction is inhibited by an antiserum against a hamster sperm protein. Biol Reprod 51: 577-587.
    • (1994) Biol Reprod , vol.51 , pp. 577-587
    • Boue, F.1    Berube, B.2    De Lamirande, E.3    Gagnon, C.4    Sullivan, R.5
  • 57
    • 44349152970 scopus 로고    scopus 로고
    • Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse
    • Walsh A, Whelan D, Bielanowicz A, Skinner B, Aitken RJ, et al. (2008) Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse. Biol Reprod 78: 983-993.
    • (2008) Biol Reprod , vol.78 , pp. 983-993
    • Walsh, A.1    Whelan, D.2    Bielanowicz, A.3    Skinner, B.4    Aitken, R.J.5
  • 58
    • 30544449581 scopus 로고    scopus 로고
    • The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38)
    • Yu Y, Xu W, Yi YJ, Sutovsky P, Oko R, (2006) The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38). Dev Biol 290: 32-43.
    • (2006) Dev Biol , vol.290 , pp. 32-43
    • Yu, Y.1    Xu, W.2    Yi, Y.J.3    Sutovsky, P.4    Oko, R.5
  • 59
    • 0142231558 scopus 로고    scopus 로고
    • Processing, localization and binding activity of zonadhesin suggest a function in sperm adhesion to the zona pellucida during exocytosis of the acrosome
    • Bi M, Hickox JR, Winfrey VP, Olson GE, Hardy DM, (2003) Processing, localization and binding activity of zonadhesin suggest a function in sperm adhesion to the zona pellucida during exocytosis of the acrosome. Biochem J 375: 477-488.
    • (2003) Biochem J , vol.375 , pp. 477-488
    • Bi, M.1    Hickox, J.R.2    Winfrey, V.P.3    Olson, G.E.4    Hardy, D.M.5
  • 60
    • 4544250782 scopus 로고    scopus 로고
    • Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface
    • Nishimura H, Kim E, Nakanishi T, Baba T, (2004) Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface. J Biol Chem 279: 34957-34962.
    • (2004) J Biol Chem , vol.279 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 61
    • 33750845874 scopus 로고    scopus 로고
    • Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice
    • Yamaguchi R, Yamagata K, Ikawa M, Moss SB, Okabe M, (2006) Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice. Biol Reprod 75: 760-766.
    • (2006) Biol Reprod , vol.75 , pp. 760-766
    • Yamaguchi, R.1    Yamagata, K.2    Ikawa, M.3    Moss, S.B.4    Okabe, M.5
  • 62
    • 0345466592 scopus 로고    scopus 로고
    • Characterization of boar spermadhesins by monoclonal and polyclonal antibodies and their role in binding to oocytes
    • Veselsky L, Peknicova J, Cechova D, Kraus M, Geussova G, et al. (1999) Characterization of boar spermadhesins by monoclonal and polyclonal antibodies and their role in binding to oocytes. Am J Reprod Immunol 42: 187-197.
    • (1999) Am J Reprod Immunol , vol.42 , pp. 187-197
    • Veselsky, L.1    Peknicova, J.2    Cechova, D.3    Kraus, M.4    Geussova, G.5
  • 63
    • 77956116290 scopus 로고    scopus 로고
    • Infertility with impaired zona pellucida adhesion of spermatozoa from mice lacking TauCstF-64
    • Tardif S, Akrofi AS, Dass B, Hardy DM, MacDonald CC, (2010) Infertility with impaired zona pellucida adhesion of spermatozoa from mice lacking TauCstF-64. Biol Reprod 83: 464-472.
    • (2010) Biol Reprod , vol.83 , pp. 464-472
    • Tardif, S.1    Akrofi, A.S.2    Dass, B.3    Hardy, D.M.4    MacDonald, C.C.5
  • 64
    • 9444249289 scopus 로고    scopus 로고
    • A newly identified zona pellucida glycoprotein, ZPD, and dimeric ZP1 of chicken egg envelope are involved in sperm activation on sperm-egg interaction
    • Okumura H, Kohno Y, Iwata Y, Mori H, Aoki N, et al. (2004) A newly identified zona pellucida glycoprotein, ZPD, and dimeric ZP1 of chicken egg envelope are involved in sperm activation on sperm-egg interaction. Biochem J 384: 191-199.
    • (2004) Biochem J , vol.384 , pp. 191-199
    • Okumura, H.1    Kohno, Y.2    Iwata, Y.3    Mori, H.4    Aoki, N.5
  • 65
    • 34547125812 scopus 로고    scopus 로고
    • Identification of an ADAM2-ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm
    • Nishimura H, Myles DG, Primakoff P, (2007) Identification of an ADAM2-ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm. J Biol Chem 282: 17900-17907.
    • (2007) J Biol Chem , vol.282 , pp. 17900-17907
    • Nishimura, H.1    Myles, D.G.2    Primakoff, P.3
  • 66
    • 33846828527 scopus 로고    scopus 로고
    • Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding
    • Chiu PC, Chung MK, Koistinen R, Koistinen H, Seppala M, et al. (2007) Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding. J Cell Sci 120: 33-44.
    • (2007) J Cell Sci , vol.120 , pp. 33-44
    • Chiu, P.C.1    Chung, M.K.2    Koistinen, R.3    Koistinen, H.4    Seppala, M.5
  • 67
    • 77953174328 scopus 로고    scopus 로고
    • Glioma pathogenesis-related 1-like 1 is testis enriched, dynamically modified, and redistributed during male germ cell maturation and has a potential role in sperm-oocyte binding
    • Gibbs GM, Lo JC, Nixon B, Jamsai D, O'Connor AE, et al. (2010) Glioma pathogenesis-related 1-like 1 is testis enriched, dynamically modified, and redistributed during male germ cell maturation and has a potential role in sperm-oocyte binding. Endocrinology 151: 2331-2342.
    • (2010) Endocrinology , vol.151 , pp. 2331-2342
    • Gibbs, G.M.1    Lo, J.C.2    Nixon, B.3    Jamsai, D.4    O'Connor, A.E.5
  • 68
    • 41549100909 scopus 로고    scopus 로고
    • Pre-treatment of cattle sperm and/or oocyte with antibody to lipocalin type prostaglandin D synthase inhibits in vitro fertilization and increases sperm-oocyte binding
    • Goncalves RF, Barnabe VH, Killian GJ, (2008) Pre-treatment of cattle sperm and/or oocyte with antibody to lipocalin type prostaglandin D synthase inhibits in vitro fertilization and increases sperm-oocyte binding. Anim Reprod Sci 106: 188-193.
    • (2008) Anim Reprod Sci , vol.106 , pp. 188-193
    • Goncalves, R.F.1    Barnabe, V.H.2    Killian, G.J.3
  • 69
    • 33845980589 scopus 로고    scopus 로고
    • Inhibition of mouse acrosome reaction and sperm-zona pellucida binding by anti-human sperm membrane protein 1 antibody
    • Cheng GY, Shi JL, Wang M, Hu YQ, Liu CM, et al. (2007) Inhibition of mouse acrosome reaction and sperm-zona pellucida binding by anti-human sperm membrane protein 1 antibody. Asian J Androl 9: 23-29.
    • (2007) Asian J Androl , vol.9 , pp. 23-29
    • Cheng, G.Y.1    Shi, J.L.2    Wang, M.3    Hu, Y.Q.4    Liu, C.M.5
  • 70
    • 45549097542 scopus 로고    scopus 로고
    • Recombinant mouse sperm ZP3-binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro
    • Buffone MG, Zhuang T, Ord TS, Hui L, Moss SB, et al. (2008) Recombinant mouse sperm ZP3-binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro. J Biol Chem 283: 12438-12445.
    • (2008) J Biol Chem , vol.283 , pp. 12438-12445
    • Buffone, M.G.1    Zhuang, T.2    Ord, T.S.3    Hui, L.4    Moss, S.B.5
  • 72
    • 33750402872 scopus 로고    scopus 로고
    • Sperm N-acetylglucosaminidase is involved in primary binding to the zona pellucida
    • Zitta K, Wertheimer EV, Miranda PV, (2006) Sperm N-acetylglucosaminidase is involved in primary binding to the zona pellucida. Mol Hum Reprod 12: 557-563.
    • (2006) Mol Hum Reprod , vol.12 , pp. 557-563
    • Zitta, K.1    Wertheimer, E.V.2    Miranda, P.V.3
  • 73
    • 1942521152 scopus 로고    scopus 로고
    • Spatio-temporal organization of Vam6P and SNAP on mouse spermatozoa and their involvement in sperm-zona pellucida interactions
    • Brahmaraju M, Shoeb M, Laloraya M, Kumar PG, (2004) Spatio-temporal organization of Vam6P and SNAP on mouse spermatozoa and their involvement in sperm-zona pellucida interactions. Biochem Biophys Res Commun 318: 148-155.
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 148-155
    • Brahmaraju, M.1    Shoeb, M.2    Laloraya, M.3    Kumar, P.G.4
  • 74
    • 77951836649 scopus 로고    scopus 로고
    • Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice
    • Escoffier J, Jemel I, Tanemoto A, Taketomi Y, Payre C, et al. (2010) Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice. J Clin Invest 120: 1415-1428.
    • (2010) J Clin Invest , vol.120 , pp. 1415-1428
    • Escoffier, J.1    Jemel, I.2    Tanemoto, A.3    Taketomi, Y.4    Payre, C.5
  • 75
    • 77954594769 scopus 로고    scopus 로고
    • Analysis of CAPZA3 localization reveals temporally discrete events during the acrosome reaction
    • Sosnik J, Buffone MG, Visconti PE, (2010) Analysis of CAPZA3 localization reveals temporally discrete events during the acrosome reaction. J Cell Physiol 224: 575-580.
    • (2010) J Cell Physiol , vol.224 , pp. 575-580
    • Sosnik, J.1    Buffone, M.G.2    Visconti, P.E.3
  • 76
    • 53749103998 scopus 로고    scopus 로고
    • Complexin-I-deficient sperm are subfertile due to a defect in zona pellucida penetration
    • Zhao L, Reim K, Miller DJ, (2008) Complexin-I-deficient sperm are subfertile due to a defect in zona pellucida penetration. Reproduction 136: 323-334.
    • (2008) Reproduction , vol.136 , pp. 323-334
    • Zhao, L.1    Reim, K.2    Miller, D.J.3
  • 77
    • 34247098353 scopus 로고    scopus 로고
    • Effect of monosaccharide L-fucose and polysaccharide fucoidan on sperm alpha-L-fucosidase activity and relation to sperm-oocyte interaction in pig
    • Song XX, Park CK, Piao YJ, Niwa K, (2007) Effect of monosaccharide L-fucose and polysaccharide fucoidan on sperm alpha-L-fucosidase activity and relation to sperm-oocyte interaction in pig. Asian-Australasian Journal of Animal Sciences 20: 351-358.
    • (2007) Asian-Australasian Journal of Animal Sciences , vol.20 , pp. 351-358
    • Song, X.X.1    Park, C.K.2    Piao, Y.J.3    Niwa, K.4
  • 78
    • 35548979382 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization
    • Yi YJ, Manandhar G, Sutovsky M, Li R, Jonakova V, et al. (2007) Ubiquitin C-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization. Biol Reprod 77: 780-793.
    • (2007) Biol Reprod , vol.77 , pp. 780-793
    • Yi, Y.J.1    Manandhar, G.2    Sutovsky, M.3    Li, R.4    Jonakova, V.5
  • 79
    • 77955907224 scopus 로고    scopus 로고
    • In humans, zona pellucida glycoprotein-1 binds to spermatozoa and induces acrosomal exocytosis
    • Ganguly A, Bukovsky A, Sharma RK, Bansal P, Bhandari B, et al. (2010) In humans, zona pellucida glycoprotein-1 binds to spermatozoa and induces acrosomal exocytosis. Hum Reprod 25: 1643-1656.
    • (2010) Hum Reprod , vol.25 , pp. 1643-1656
    • Ganguly, A.1    Bukovsky, A.2    Sharma, R.K.3    Bansal, P.4    Bhandari, B.5
  • 80
    • 77949269062 scopus 로고    scopus 로고
    • The acrosomal protein Dickkopf-like 1 (DKKL1) facilitates sperm penetration of the zona pellucida
    • Kohn MJ, Sztein J, Yagi R, DePamphilis ML, Kaneko KJ, (2010) The acrosomal protein Dickkopf-like 1 (DKKL1) facilitates sperm penetration of the zona pellucida. Fertil Steril 93: 1533-1537.
    • (2010) Fertil Steril , vol.93 , pp. 1533-1537
    • Kohn, M.J.1    Sztein, J.2    Yagi, R.3    DePamphilis, M.L.4    Kaneko, K.J.5
  • 81
    • 56049087354 scopus 로고    scopus 로고
    • Reduced fertility of mouse epididymal sperm lacking Prss21/Tesp5 is rescued by sperm exposure to uterine microenvironment
    • Yamashita M, Honda A, Ogura A, Kashiwabara S, Fukami K, et al. (2008) Reduced fertility of mouse epididymal sperm lacking Prss21/Tesp5 is rescued by sperm exposure to uterine microenvironment. Genes Cells 13: 1001-1013.
    • (2008) Genes Cells , vol.13 , pp. 1001-1013
    • Yamashita, M.1    Honda, A.2    Ogura, A.3    Kashiwabara, S.4    Fukami, K.5
  • 82
    • 63049113417 scopus 로고    scopus 로고
    • A sperm GPI-anchored protein elicits sperm-cumulus cross-talk leading to the acrosome reaction
    • Yin L, Chung CM, Huo R, Liu H, Zhou C, et al. (2009) A sperm GPI-anchored protein elicits sperm-cumulus cross-talk leading to the acrosome reaction. Cell Mol Life Sci 66: 900-908.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 900-908
    • Yin, L.1    Chung, C.M.2    Huo, R.3    Liu, H.4    Zhou, C.5
  • 83
    • 70449397213 scopus 로고    scopus 로고
    • Expression and putative function of fibronectin and its receptor (integrin alpha(5)beta(1)) in male and female gametes during bovine fertilization in vitro
    • Thys M, Nauwynck H, Maes D, Hoogewijs M, Vercauteren D, et al. (2009) Expression and putative function of fibronectin and its receptor (integrin alpha(5)beta(1)) in male and female gametes during bovine fertilization in vitro. Reproduction 138: 471-482.
    • (2009) Reproduction , vol.138 , pp. 471-482
    • Thys, M.1    Nauwynck, H.2    Maes, D.3    Hoogewijs, M.4    Vercauteren, D.5
  • 84
    • 33644977667 scopus 로고    scopus 로고
    • CD9 controls the formation of clusters that contain tetraspanins and the integrin alpha 6 beta 1, which are involved in human and mouse gamete fusion
    • Ziyyat A, Rubinstein E, Monier-Gavelle F, Barraud V, Kulski O, et al. (2006) CD9 controls the formation of clusters that contain tetraspanins and the integrin alpha 6 beta 1, which are involved in human and mouse gamete fusion. J Cell Sci 119: 416-424.
    • (2006) J Cell Sci , vol.119 , pp. 416-424
    • Ziyyat, A.1    Rubinstein, E.2    Monier-Gavelle, F.3    Barraud, V.4    Kulski, O.5
  • 85
    • 0035163797 scopus 로고    scopus 로고
    • Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of beta1 integrin-associated proteins CD9, CD81, and CD98
    • Takahashi Y, Bigler D, Ito Y, White JM, (2001) Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of beta1 integrin-associated proteins CD9, CD81, and CD98. Mol Biol Cell 12: 809-820.
    • (2001) Mol Biol Cell , vol.12 , pp. 809-820
    • Takahashi, Y.1    Bigler, D.2    Ito, Y.3    White, J.M.4
  • 87
    • 28544442231 scopus 로고    scopus 로고
    • Cyclic FEE peptide increases human gamete fusion and potentiates its RGD-induced inhibition
    • Ziyyat A, Naud-Barriant N, Barraud-Lange V, Chevalier F, Kulski O, et al. (2005) Cyclic FEE peptide increases human gamete fusion and potentiates its RGD-induced inhibition. Hum Reprod 20: 3452-3458.
    • (2005) Hum Reprod , vol.20 , pp. 3452-3458
    • Ziyyat, A.1    Naud-Barriant, N.2    Barraud-Lange, V.3    Chevalier, F.4    Kulski, O.5
  • 89
    • 33646882179 scopus 로고    scopus 로고
    • A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57
    • Ellerman DA, Myles DG, Primakoff P, (2006) A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev Cell 10: 831-837.
    • (2006) Dev Cell , vol.10 , pp. 831-837
    • Ellerman, D.A.1    Myles, D.G.2    Primakoff, P.3
  • 90
    • 0028276817 scopus 로고
    • Inhibition of human spermatozoon-oocyte interaction in vitro by monoclonal antibodies to CD46 (membrane cofactor protein)
    • Taylor CT, Biljan MM, Kingsland CR, Johnson PM, (1994) Inhibition of human spermatozoon-oocyte interaction in vitro by monoclonal antibodies to CD46 (membrane cofactor protein). Hum Reprod 9: 907-911.
    • (1994) Hum Reprod , vol.9 , pp. 907-911
    • Taylor, C.T.1    Biljan, M.M.2    Kingsland, C.R.3    Johnson, P.M.4
  • 91
    • 26144481268 scopus 로고    scopus 로고
    • Immunogenicity and contraceptive potential of recombinant human sperm associated antigen (SPAG9)
    • Jagadish N, Rana R, Mishra D, Garg M, Chaurasiya D, et al. (2005) Immunogenicity and contraceptive potential of recombinant human sperm associated antigen (SPAG9). J Reprod Immunol 67: 69-76.
    • (2005) J Reprod Immunol , vol.67 , pp. 69-76
    • Jagadish, N.1    Rana, R.2    Mishra, D.3    Garg, M.4    Chaurasiya, D.5
  • 92
    • 0033623350 scopus 로고    scopus 로고
    • Potential role of alphav and beta1 integrins as oocyte adhesion molecules during fertilization in pigs
    • Linfor J, Berger T, (2000) Potential role of alphav and beta1 integrins as oocyte adhesion molecules during fertilization in pigs. J Reprod Fertil 120: 65-72.
    • (2000) J Reprod Fertil , vol.120 , pp. 65-72
    • Linfor, J.1    Berger, T.2
  • 93
    • 59849083832 scopus 로고    scopus 로고
    • Immunoglobulin superfamily member IgSF8 (EWI-2) and CD9 in fertilisation: evidence of distinct functions for CD9 and a CD9-associated protein in mammalian sperm-egg interaction
    • Glazar AI, Evans JP, (2009) Immunoglobulin superfamily member IgSF8 (EWI-2) and CD9 in fertilisation: evidence of distinct functions for CD9 and a CD9-associated protein in mammalian sperm-egg interaction. Reprod Fertil Dev 21: 293-303.
    • (2009) Reprod Fertil Dev , vol.21 , pp. 293-303
    • Glazar, A.I.1    Evans, J.P.2
  • 94
    • 65249141091 scopus 로고    scopus 로고
    • Reduction of mouse egg surface integrin alpha9 subunit (ITGA9) reduces the egg's ability to support sperm-egg binding and fusion
    • Vjugina U, Zhu X, Oh E, Bracero NJ, Evans JP, (2009) Reduction of mouse egg surface integrin alpha9 subunit (ITGA9) reduces the egg's ability to support sperm-egg binding and fusion. Biol Reprod 80: 833-841.
    • (2009) Biol Reprod , vol.80 , pp. 833-841
    • Vjugina, U.1    Zhu, X.2    Oh, E.3    Bracero, N.J.4    Evans, J.P.5
  • 95
    • 58249095066 scopus 로고    scopus 로고
    • Expression of epithelial cadherin in the human male reproductive tract and gametes and evidence of its participation in fertilization
    • Marin-Briggiler CI, Veiga MF, Matos ML, Echeverria MF, Furlong LI, et al. (2008) Expression of epithelial cadherin in the human male reproductive tract and gametes and evidence of its participation in fertilization. Mol Hum Reprod 14: 561-571.
    • (2008) Mol Hum Reprod , vol.14 , pp. 561-571
    • Marin-Briggiler, C.I.1    Veiga, M.F.2    Matos, M.L.3    Echeverria, M.F.4    Furlong, L.I.5
  • 96
    • 34547525018 scopus 로고    scopus 로고
    • Localization of ubiquitin C-terminal hydrolase L1 in mouse ova and its function in the plasma membrane to block polyspermy
    • Sekiguchi S, Kwon J, Yoshida E, Hamasaki H, Ichinose S, et al. (2006) Localization of ubiquitin C-terminal hydrolase L1 in mouse ova and its function in the plasma membrane to block polyspermy. Am J Pathol 169: 1722-1729.
    • (2006) Am J Pathol , vol.169 , pp. 1722-1729
    • Sekiguchi, S.1    Kwon, J.2    Yoshida, E.3    Hamasaki, H.4    Ichinose, S.5
  • 97
    • 47249089617 scopus 로고    scopus 로고
    • Presence, processing, and localization of mouse ADAM15 during sperm maturation and the role of its disintegrin domain during sperm-egg binding
    • Pasten-Hidalgo K, Hernandez-Rivas R, Roa-Espitia AL, Sanchez-Gutierrez M, Martinez-Perez F, et al. (2008) Presence, processing, and localization of mouse ADAM15 during sperm maturation and the role of its disintegrin domain during sperm-egg binding. Reproduction 136: 41-51.
    • (2008) Reproduction , vol.136 , pp. 41-51
    • Pasten-Hidalgo, K.1    Hernandez-Rivas, R.2    Roa-Espitia, A.L.3    Sanchez-Gutierrez, M.4    Martinez-Perez, F.5
  • 98
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • Inoue N, Ikawa M, Isotani A, Okabe M, (2005) The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434: 234-238.
    • (2005) Nature , vol.434 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 99
    • 0036019170 scopus 로고    scopus 로고
    • Cadherins expression during gamete maturation and fertilization in the rat
    • Ziv S, Rufas O, Shalgi R, (2002) Cadherins expression during gamete maturation and fertilization in the rat. Mol Reprod Dev 62: 547-556.
    • (2002) Mol Reprod Dev , vol.62 , pp. 547-556
    • Ziv, S.1    Rufas, O.2    Shalgi, R.3
  • 100
    • 77950103889 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein 29 (ERp29), a protein related to sperm maturation is involved in sperm-oocyte fusion in mouse
    • Ying X, Liu Y, Guo Q, Qu F, Guo W, et al. (2010) Endoplasmic reticulum protein 29 (ERp29), a protein related to sperm maturation is involved in sperm-oocyte fusion in mouse. Reprod Biol Endocrinol 8: 10.
    • (2010) Reprod Biol Endocrinol , vol.8 , pp. 10
    • Ying, X.1    Liu, Y.2    Guo, Q.3    Qu, F.4    Guo, W.5
  • 101
    • 23244434065 scopus 로고    scopus 로고
    • Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization
    • Herrero MB, Mandal A, Digilio LC, Coonrod SA, Maier B, et al. (2005) Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization. Dev Biol 284: 126-142.
    • (2005) Dev Biol , vol.284 , pp. 126-142
    • Herrero, M.B.1    Mandal, A.2    Digilio, L.C.3    Coonrod, S.A.4    Maier, B.5
  • 102
    • 33947494440 scopus 로고    scopus 로고
    • Evidence for the involvement of testicular protein CRISP2 in mouse sperm-egg fusion
    • Busso D, Goldweic NM, Hayashi M, Kasahara M, Cuasnicu PS, (2007) Evidence for the involvement of testicular protein CRISP2 in mouse sperm-egg fusion. Biol Reprod 76: 701-708.
    • (2007) Biol Reprod , vol.76 , pp. 701-708
    • Busso, D.1    Goldweic, N.M.2    Hayashi, M.3    Kasahara, M.4    Cuasnicu, P.S.5
  • 103
    • 85082785579 scopus 로고    scopus 로고
    • Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in mouse
    • Fujihara Y, Murakami M, Inoue N, Satouh Y, Kaseda K, et al. (2010) Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in mouse. J Cell Sci 2010: 7.
    • (2010) J Cell Sci , vol.2010 , pp. 7
    • Fujihara, Y.1    Murakami, M.2    Inoue, N.3    Satouh, Y.4    Kaseda, K.5
  • 104
    • 0041732182 scopus 로고    scopus 로고
    • SAMP14, a novel, acrosomal membrane-associated, glycosylphosphatidylinositol-anchored member of the Ly-6/urokinase-type plasminogen activator receptor superfamily with a role in sperm-egg interaction
    • Shetty J, Wolkowicz MJ, Digilio LC, Klotz KL, Jayes FL, et al. (2003) SAMP14, a novel, acrosomal membrane-associated, glycosylphosphatidylinositol-anchored member of the Ly-6/urokinase-type plasminogen activator receptor superfamily with a role in sperm-egg interaction. J Biol Chem 278: 30506-30515.
    • (2003) J Biol Chem , vol.278 , pp. 30506-30515
    • Shetty, J.1    Wolkowicz, M.J.2    Digilio, L.C.3    Klotz, K.L.4    Jayes, F.L.5
  • 105
    • 12444270132 scopus 로고    scopus 로고
    • Crystal structure of a covalent intermediate of endogenous human arylsulfatase A
    • Chruszcz M, Laidler P, Monkiewicz M, Ortlund E, Lebioda L, et al. (2003) Crystal structure of a covalent intermediate of endogenous human arylsulfatase A. J Inorg Biochem. 96: 386-392.
    • (2003) J Inorg Biochem , vol.96 , pp. 386-392
    • Chruszcz, M.1    Laidler, P.2    Monkiewicz, M.3    Ortlund, E.4    Lebioda, L.5
  • 106
    • 0033616764 scopus 로고    scopus 로고
    • Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein
    • Jiang J, Zhang Y, Krainer AR, Xu RM, (1999) Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein. Proc Natl Acad Sci U S A 96: 3572-3577.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3572-3577
    • Jiang, J.1    Zhang, Y.2    Krainer, A.R.3    Xu, R.M.4
  • 107
    • 0028317007 scopus 로고
    • Evidence for presence of hyaluronan binding protein on spermatozoa and its possible involvement in sperm function
    • Ranganathan S, Ganguly AK, Datta K, (1994) Evidence for presence of hyaluronan binding protein on spermatozoa and its possible involvement in sperm function. Mol Reprod Dev 38: 69-76.
    • (1994) Mol Reprod Dev , vol.38 , pp. 69-76
    • Ranganathan, S.1    Ganguly, A.K.2    Datta, K.3
  • 108
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, et al. (2002) Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science 296: 151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5
  • 109
    • 33845895236 scopus 로고    scopus 로고
    • Influence of arginine-glycine-aspartic acid (RGD), integrins (alphaV and alpha5) and osteopontin on bovine sperm-egg binding, and fertilization in vitro
    • Goncalves RF, Wolinetz CD, Killian GJ, (2007) Influence of arginine-glycine-aspartic acid (RGD), integrins (alphaV and alpha5) and osteopontin on bovine sperm-egg binding, and fertilization in vitro. Theriogenology 67: 468-474.
    • (2007) Theriogenology , vol.67 , pp. 468-474
    • Goncalves, R.F.1    Wolinetz, C.D.2    Killian, G.J.3
  • 110
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM, (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 30: 21-32.
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 111
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution
    • Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP, (1997) Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. Embo J 16: 3787-3796.
    • (1997) Embo J , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 112
    • 33645772189 scopus 로고    scopus 로고
    • The mitochondrial genome of spotted green pufferfish Tetraodon nigroviridis (Teleostei: Tetraodontiformes) and divergence time estimation among model organisms in fishes
    • Yamanoue Y, Miya M, Inoue JG, Matsuura K, Nishida M, (2006) The mitochondrial genome of spotted green pufferfish Tetraodon nigroviridis (Teleostei: Tetraodontiformes) and divergence time estimation among model organisms in fishes. Genes Genet Syst 81: 29-39.
    • (2006) Genes Genet Syst , vol.81 , pp. 29-39
    • Yamanoue, Y.1    Miya, M.2    Inoue, J.G.3    Matsuura, K.4    Nishida, M.5
  • 114
    • 70349298549 scopus 로고    scopus 로고
    • S. BH, S. K, editors. New York: Oxford University Press
    • van Tuinen M (2009) The Timetree of Life; S. BH, S. K, editors. New York: Oxford University Press.
    • (2009) The Timetree of Life
    • van Tuinen, M.1
  • 115
    • 34249739745 scopus 로고    scopus 로고
    • Fossils, molecules, divergence times, and the origin of lissamphibians
    • Marjanovic D, Laurin M, (2007) Fossils, molecules, divergence times, and the origin of lissamphibians. Syst Biol 56: 369-388.
    • (2007) Syst Biol , vol.56 , pp. 369-388
    • Marjanovic, D.1    Laurin, M.2


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