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Volumn 9, Issue 10, 2012, Pages 550-560

Testicular and epididymal ADAMs: Expression and function during fertilization

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; ADAM1 PROTEIN; ADAM10 ENDOPEPTIDASE; ADAM11 PROTEIN; ADAM12 PROTEIN; ADAM15 PROTEIN; ADAM17 PROTEIN; ADAM18 PROTEIN; ADAM19 PROTEIN; ADAM1B PROTEIN; ADAM2 PROTEIN; ADAM20 PROTEIN; ADAM21 PROTEIN; ADAM22 PROTEIN; ADAM23 PROTEIN; ADAM24 PROTEIN; ADAM25 PROTEIN; ADAM26 PROTEIN; ADAM29 PROTEIN; ADAM3 PROTEIN; ADAM30 PROTEIN; ADAM32 PROTEIN; ADAM33 PROTEIN; ADAM34 PROTEIN; ADAM4 PROTEIN; ADAM5 PROTEIN; ADAM6 PROTEIN; ADAM7 PROTEIN; ADAM8 PROTEIN; ADAM9 PROTEIN; UNCLASSIFIED DRUG;

EID: 84867572642     PISSN: 17594812     EISSN: 17594820     Source Type: Journal    
DOI: 10.1038/nrurol.2012.167     Document Type: Review
Times cited : (74)

References (110)
  • 1
    • 33645051605 scopus 로고    scopus 로고
    • (ed. Hooper, N. M. & Lendeckel, U.), Springer, Dordrecht
    • Cho, C. in The ADAM family of proteases (ed. Hooper, N. M. & Lendeckel, U.) 239-259 (Springer, Dordrecht, 2005).
    • (2005) The ADAM Family of Proteases , pp. 239-259
    • Cho, C.1
  • 3
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • DOI 10.1016/S0168-9525(99)01926-5, PII S0168952599019265
    • Primakoff, P. & Myls, D. G. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 16, 83-87 (2000). (Pubitemid 30084721)
    • (2000) Trends in Genetics , vol.16 , Issue.2 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 4
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: Modulators of cell-cell and cell-matrix interactions
    • DOI 10.1016/j.ceb.2003.08.001
    • White, J. M. ADAMs: modulators of cell-cell and cell-matrix interactions. Curr. Opin. Cell Biol. 15, 598-606 (2003). (Pubitemid 37176969)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.5 , pp. 598-606
    • White, J.M.1
  • 5
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • DOI 10.1101/gad.1039703
    • Seals, D. F. & Courtneidge, S. A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17, 7-30 (2003). (Pubitemid 36062504)
    • (2003) Genes and Development , vol.17 , Issue.1 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 6
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in egfr signalling and development
    • DOI 10.1038/nrm1548
    • Blobel, C. P. ADAMs: key components in EGFR signalling and development. Nat. Rev. Mol. Cell Biol. 6, 32-43 (2005). (Pubitemid 40064897)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 32-43
    • Blobel, C.P.1
  • 7
    • 79951519159 scopus 로고    scopus 로고
    • Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: Biological function and structure
    • Klein, T. & Bischoff, R. Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: biological function and structure. J. Proteome Res. 10, 17-33 (2011).
    • (2011) J. Proteome Res. , vol.10 , pp. 17-33
    • Klein, T.1    Bischoff, R.2
  • 8
    • 0032838908 scopus 로고    scopus 로고
    • The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries
    • DOI 10.1016/S0378-1119(99)00302-9, PII S0378111999003029
    • Poindexter, K., Nelson, N., DuBose, R. F., Black, R. A. & Cerretti, D. P. The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries. Gene 237, 61-70 (1999). (Pubitemid 29406198)
    • (1999) Gene , vol.237 , Issue.1 , pp. 61-70
    • Poindexter, K.1    Nelson, N.2    Dubose, R.F.3    Black, R.A.4    Cerretti, D.P.5
  • 9
    • 1542719063 scopus 로고    scopus 로고
    • Characterization and comparative genomic analysis of intronless Adams with testicular gene expression
    • DOI 10.1016/j.ygeno.2003.10.001, PII S0888754303003173
    • Choi, I. et al. Characterization and comparative genomic analysis of intronless Adams with testicular gene expression. Genomics 83, 636-646 (2004). (Pubitemid 38340805)
    • (2004) Genomics , vol.83 , Issue.4 , pp. 636-646
    • Choi, I.1    Oh, J.2    Cho, B.-N.3    Ahnn, J.4    Jung, Y.-K.5    Kim, D.H.6    Cho, C.7
  • 10
    • 77950019812 scopus 로고    scopus 로고
    • Expression analysis of the Adam21 gene in mouse testis
    • Yi, C. et al. Expression analysis of the Adam21 gene in mouse testis. Gene Expr. Patterns 10, 152-158 (2010).
    • (2010) Gene Expr. Patterns , vol.10 , pp. 152-158
    • Yi, C.1
  • 11
    • 0030793567 scopus 로고    scopus 로고
    • Genomic organization of the mouse fertilin β gene that encodes an ADAM family protein active in sperm-egg fusion
    • DOI 10.1002/(SICI)1520-6408(1997)20:4<320::AID-DVG3>3.0.CO;2-9
    • Cho, C., Turner, L., Primakoff, P. & Myles, D. G. Genomic organization of the mouse fertilin beta gene that encodes an ADAM family protein active in sperm-egg fusion. Dev. Genet. 20, 320-328 (1997). (Pubitemid 27337978)
    • (1997) Developmental Genetics , vol.20 , Issue.4 , pp. 320-328
    • Cho, C.1    Turner, L.2    Primakoff, P.3    Myles, D.G.4
  • 12
    • 0037472673 scopus 로고    scopus 로고
    • Identification and characterization of ADAM32 with testis-predominant gene expression
    • DOI 10.1016/S0378-1119(02)01202-7
    • Choi, I. et al. Identification and characterization of ADAM32 with testis-predominant gene expression. Gene 304, 151-162 (2003). (Pubitemid 36142064)
    • (2003) Gene , vol.304 , Issue.1-2 , pp. 151-162
    • Choi, I.1    Woo, J.-M.2    Hong, S.3    Jung, Y.-K.4    Kim, D.H.5    Cho, C.6
  • 14
    • 0030585736 scopus 로고    scopus 로고
    • Chromosomal assignment of four testis-expressed mouse genes from a new family of transmembrane proteins (ADAMs) involved in cell-cell adhesion and fusion
    • DOI 10.1006/geno.1996.0305
    • Cho, C., Primakoff, P., White, J. M. & Myles, D. G. Chromosomal assignment of four testis-expressed mouse genes from a new family of transmembrane proteins (ADAMs) involved in cell-cell adhesion and fusion. Genomics 34, 413-417 (1996). (Pubitemid 26234739)
    • (1996) Genomics , vol.34 , Issue.3 , pp. 413-417
    • Cho, C.1    Primakoff, P.2    White, J.M.3    Myles, D.G.4
  • 15
    • 0037193685 scopus 로고    scopus 로고
    • The ADAM1a and ADAM1b genes, instead of the ADAM1 (fertilin α) gene, are localized on mouse chromosome 5
    • DOI 10.1016/S0378-1119(02)00540-1, PII S0378111902005401
    • Nishimura, H. et al. The ADAM1a and ADAM1b genes, instead of the ADAM1 (fertilin alpha) gene, are localized on mouse chromosome 5. Gene 291, 67-76 (2002). (Pubitemid 34722378)
    • (2002) Gene , vol.291 , Issue.1-2 , pp. 67-76
    • Nishimura, H.1    Kim, E.2    Fujimori, T.3    Kashiwabara, S.-I.4    Kuroiwa, A.5    Matsuda, Y.6    Baba, T.7
  • 16
    • 0037401749 scopus 로고    scopus 로고
    • ADAM family genes testase 2α and 2β are chromosomally linked and simultaneously expressed in male germ cells
    • DOI 10.1002/mrd.10256
    • Bolcun, E., Rzymski, T., Nayernia, K. & Engel, W. ADAM family genes testase 2alpha and 2beta are chromosomally linked and simultaneously expressed in male germ cells. Mol. Reprod. Dev. 65, 19-22 (2003). (Pubitemid 36373957)
    • (2003) Molecular Reproduction and Development , vol.65 , Issue.1 , pp. 19-22
    • Bolcun, E.1    Rzymski, T.2    Nayernia, K.3    Engel, W.4
  • 17
    • 0031890388 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal localization, and expression analysis of CYRN1 and CYRN2, two human genes coding for cyritestin, a sperm protein involved in gamete interaction
    • Adham, I. M. et al. Molecular cloning, chromosomal localization, and expression analysis of CYRN1 and CYRN2, two human genes coding for cyritestin, a sperm protein involved in gamete interaction. DNA Cell Biol. 17, 161-168 (1998). (Pubitemid 28113864)
    • (1998) DNA and Cell Biology , vol.17 , Issue.2 , pp. 161-168
    • Adham, I.M.1
  • 18
    • 0031059822 scopus 로고    scopus 로고
    • The human fertilin α gene is non-functional: Implications for its proposed role in fertilization
    • Jury, J. A., Frayne, J. & Hall, L. The human fertilin alpha gene is non-functional: implications for its proposed role in fertilization. Biochem. J. 321, 577-581 (1997). (Pubitemid 27084861)
    • (1997) Biochemical Journal , vol.321 , Issue.3 , pp. 577-581
    • Jury, J.A.1    Frayne, J.2    Hall, L.3
  • 19
    • 0031877099 scopus 로고    scopus 로고
    • Sequence analysis of a variety of primate fertilin α genes: Evidence for non-functional genes in the gorilla and man
    • DOI 10.1002/(SICI)1098-2795(199809)51:1<92::AID-MRD11>3.0.CO;2-W
    • Jury, J. A., Frayne, J. & Hall, L. Sequence analysis of a variety of primate fertilin alpha genes: evidence for non-functional genes in the gorilla and man. Mol. Reprod. Dev. 51, 92-97 (1998). (Pubitemid 28372962)
    • (1998) Molecular Reproduction and Development , vol.51 , Issue.1 , pp. 92-97
    • Jury, J.A.1    Frayne, J.2    Hall, L.3
  • 21
    • 0032528978 scopus 로고    scopus 로고
    • The gene for the human tMDC I sperm surface protein is non-functional: Implications for its proposed role in mammalian sperm-egg recognition
    • Frayne, J. & Hall, L. The gene for the human tMDC I sperm surface protein is non-functional: implications for its proposed role in mammalian sperm-egg recognition. Biochem. J. 334, 171-176 (1998). (Pubitemid 28420986)
    • (1998) Biochemical Journal , vol.334 , Issue.1 , pp. 171-176
    • Frayne, J.1    Hall, L.2
  • 23
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C. P. et al. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356, 248-252 (1992).
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1
  • 25
    • 0029021536 scopus 로고
    • Cloning and analysis of monkey fertilin reveals novel alpha subunit isoforms
    • Perry, A. C., Gichuhi, P. M., Jones, R. & Hall, L. Cloning and analysis of monkey fertilin reveals novel alpha subunit isoforms. Biochem. J. 307, 843-850 (1995).
    • (1995) Biochem. J. , vol.307 , pp. 843-850
    • Perry, A.C.1    Gichuhi, P.M.2    Jones, R.3    Hall, L.4
  • 26
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg, T. G. et al. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev. Biol. 169, 378-383 (1995).
    • (1995) Dev. Biol. , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1
  • 27
    • 0029850171 scopus 로고    scopus 로고
    • Cloning and expression of recombinant rabbit fertilin
    • DOI 10.1002/(SICI)1098-2795(199610)45:2<107::AID-MRD1>3.0.CO;2-X
    • Hardy, C. M. & Holland, M. K. Cloning and expression of recombinant rabbit fertilin. Mol. Reprod. Dev. 45, 107-116 (1996). (Pubitemid 26382482)
    • (1996) Molecular Reproduction and Development , vol.45 , Issue.2 , pp. 107-116
    • Hardy, C.M.1    Holland, M.K.2
  • 29
    • 0030940446 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of bovine fertilin α and β (ADAM 1 and ADAM 2): A candidate sperm-egg binding/fusion complex
    • Waters, S. I. & White, J. M. Biochemical and molecular characterization of bovine fertilin alpha and beta (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion complex. Biol. Reprod. 56, 1245-1254 (1997). (Pubitemid 27184510)
    • (1997) Biology of Reproduction , vol.56 , Issue.5 , pp. 1245-1254
    • Waters, S.I.1    White, J.M.2
  • 30
    • 0030767188 scopus 로고    scopus 로고
    • Rat MDC family of proteins: Sequence analysis, tissue distribution, and expression in prepubertal and adult rat testis
    • DOI 10.1002/(SICI)1098-2795(199710)48:2<159::AID-MRD3>3.0.CO;2-R
    • Frayne, J., Jury, J. A., Barker, H. L. & Hall, L. Rat MDC family of proteins: sequence analysis, tissue distribution, and expression in prepubertal and adult rat testis. Mol. Reprod. Dev. 48, 159-167 (1997). (Pubitemid 27396216)
    • (1997) Molecular Reproduction and Development , vol.48 , Issue.2 , pp. 159-167
    • Frayne, J.1    Jury, J.A.2    Barker, H.L.3    Hall, L.4
  • 31
    • 0032509768 scopus 로고    scopus 로고
    • ADAM 20 and 21; Two novel human testis-specific membrane metalloproteases with similarity to fertilin-α
    • DOI 10.1016/S0378-1119(97)00597-0, PII S0378111997005970
    • Hooft van Huijsduijnen, R. ADAM 20 and 21; two novel human testis-specific membrane metalloproteases with similarity to fertilin-alpha. Gene 206, 273-282 (1998). (Pubitemid 28083284)
    • (1998) Gene , vol.206 , Issue.2 , pp. 273-282
    • Hooft Van Huijsduijnen, R.1
  • 32
    • 0033527442 scopus 로고    scopus 로고
    • Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression
    • DOI 10.1006/bbrc.1999.1322
    • Cerretti, D. P., DuBose, R. F., Black, R. A. & Nelson, N. Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression. Biochem. Biophys. Res. Commun. 263, 810-815 (1999). (Pubitemid 29490709)
    • (1999) Biochemical and Biophysical Research Communications , vol.263 , Issue.3 , pp. 810-815
    • Cerretti, D.P.1    Dubose, R.F.2    Black, R.A.3    Nelson, N.4
  • 33
    • 0037123373 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of a novel member of the Disintegrin and Metalloprotease-Domain (ADAM) family
    • DOI 10.1016/S0378-1119(02)00508-5, PII S0378111902005085
    • Brachvogel, B. et al. Molecular cloning and expression analysis of a novel member of the Disintegrin and Metalloprotease-Domain (ADAM) family. Gene 288, 203-210 (2002). (Pubitemid 34595378)
    • (2002) Gene , vol.288 , Issue.1-2 , pp. 203-210
    • Brachvogel, B.1    Reichenberg, D.2    Beyer, S.3    Jehn, B.4    Von Der Mark, K.5    Bielke, W.6
  • 34
    • 0032988577 scopus 로고    scopus 로고
    • Identification of four novel ADAMs with potential roles in spermatogenesis and fertilization
    • DOI 10.1016/S0378-1119(99)00208-5, PII S0378111999002085
    • Zhu, G. Z., Lin, Y., Myles, D. G. & Primakoff, P. Identification of four novel ADAMs with potential roles in spermatogenesis and fertilization. Gene 234, 227-237 (1999). (Pubitemid 29296897)
    • (1999) Gene , vol.234 , Issue.2 , pp. 227-237
    • Zhu, G.-Z.1    Lin, Y.2    Myles, D.G.3    Primakoff, P.4
  • 35
    • 0034457254 scopus 로고    scopus 로고
    • Identification of ADAM 31: A protein expressed in Leydig cells and specialized epithelia
    • DOI 10.1210/en.141.6.2033
    • Liu, L. & Smith, J. W. Identification of ADAM 31: a protein expressed in Leydig cells and specialized epithelia. Endocrinology 141, 2033-2042 (2000). (Pubitemid 32274353)
    • (2000) Endocrinology , vol.141 , Issue.6 , pp. 2033-2042
    • Liu, L.1    Smith, J.W.2
  • 36
    • 0141595198 scopus 로고    scopus 로고
    • Chromosomal mapping, sequence and transcription analysis of the porcine fertilin beta gene (ADAM2)
    • DOI 10.1046/j.1365-2052.2003.01029.x
    • Day, A. E., Quilter, C. R., Sargent, C. A. & Mileham, A. J. Chromosomal mapping, sequence and transcription analysis of the porcine fertilin beta gene (ADAM2). Anim. Genet. 34, 375-378 (2003). (Pubitemid 37211992)
    • (2003) Animal Genetics , vol.34 , Issue.5 , pp. 375-378
    • Day, A.E.1    Quilter, C.R.2    Sargent, C.A.3    Mileham, A.J.4
  • 39
    • 0031568911 scopus 로고    scopus 로고
    • Mapping, sequence, and expression analysis of the human fertilin β gene (FTNB)
    • DOI 10.1006/geno.1996.4531
    • Burkin, H. R., Burkin, D. J., Davey, P. M., Griffin, D. K. & Affara, N. A. Mapping, sequence, and expression analysis of the human fertilin beta gene (FTNB). Genomics 40, 190-192 (1997). (Pubitemid 27108269)
    • (1997) Genomics , vol.40 , Issue.1 , pp. 190-192
    • Burkin, H.R.1    Burkin, D.J.2    Davey, P.M.3    Griffin, D.K.4    Affara, N.A.5
  • 40
    • 0026774863 scopus 로고
    • A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptides
    • Perry, A. C., Jones, R., Barker, P. J. & Hall, L. A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptides. Biochem. J. 286, 671-675 (1992).
    • (1992) Biochem. J. , vol.286 , pp. 671-675
    • Perry, A.C.1    Jones, R.2    Barker, P.J.3    Hall, L.4
  • 41
    • 0030886989 scopus 로고    scopus 로고
    • ADAM7, a member of the ADAM (a disintegrin and metalloprotease) gene family is specifically expressed in the mouse anterior pituitary and epididymis
    • DOI 10.1210/en.138.10.4262
    • Cornwall, G. A. & Hsia, N. ADAM7, a member of the ADAM (a disintegrin and metalloprotease) gene family is specifically expressed in the mouse anterior pituitary and epididymis. Endocrinology 138, 4262-4272 (1997). (Pubitemid 27408470)
    • (1997) Endocrinology , vol.138 , Issue.10 , pp. 4262-4272
    • Cornwall, G.A.1    Hsia, N.2
  • 42
    • 0034889346 scopus 로고    scopus 로고
    • Cloning and characterization of a complementary DNA encoding a human epididymis-associated disintegrin and metalloprotease 7 protein
    • Lin, Y. C., Sun, G. H., Lee, Y. M., Guo, Y. W. & Liu, H. W. Cloning and characterization of a complementary DNA encoding a human epididymis-associated disintegrin and metalloprotease 7 protein. Biol. Reprod. 65, 944-950 (2001).
    • (2001) Biol. Reprod. , vol.65 , pp. 944-950
    • Lin, Y.C.1    Sun, G.H.2    Lee, Y.M.3    Guo, Y.W.4    Liu, H.W.5
  • 43
    • 0032750640 scopus 로고    scopus 로고
    • Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis
    • Jury, J. A., Perry, A. C. & Hall, L. Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis. Mol. Hum. Reprod. 5, 1127-1134 (1999).
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 1127-1134
    • Jury, J.A.1    Perry, A.C.2    Hall, L.3
  • 44
    • 0034657228 scopus 로고    scopus 로고
    • Cloning and characterization of ADAM28: Evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28
    • DOI 10.1042/0264-6021:3480021
    • Howard, L., Maciewicz, R. A. & Blobel, C. P. Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. Biochem. J. 348, 21-27 (2000). (Pubitemid 30312126)
    • (2000) Biochemical Journal , vol.348 , Issue.1 , pp. 21-27
    • Howard, L.1    Maciewicz, R.A.2    Blobel, C.P.3
  • 45
    • 0037160518 scopus 로고    scopus 로고
    • An ADAM family member with expression in thymic epithelial cells and related tissues
    • DOI 10.1016/S0378-1119(01)00871-X, PII S037811190100871X
    • Haidl, I. D., Huber, G. & Eichmann, K. An ADAM family member with expression in thymic epithelial cells and related tissues. Gene 283, 163-170 (2002). (Pubitemid 34178520)
    • (2002) Gene , vol.283 , Issue.1-2 , pp. 163-170
    • Haidl, I.D.1    Huber, G.2    Eichmann, K.3
  • 46
    • 0035370612 scopus 로고    scopus 로고
    • Catalytic activity of ADAM28
    • DOI 10.1016/S0014-5793(01)02506-6, PII S0014579301025066
    • Howard, L., Zheng, Y., Horrocks, M., Maciewicz, R. A. & Blobel, C. Catalytic activity of ADAM28. FEBS Lett. 498, 82-86 (2001). (Pubitemid 32522896)
    • (2001) FEBS Letters , vol.498 , Issue.1 , pp. 82-86
    • Howard, L.1    Zheng, Y.2    Horrocks, M.3    Maciewicz, R.A.4    Blobel, C.5
  • 47
    • 0031193325 scopus 로고    scopus 로고
    • 1 integrin-mediated interaction
    • DOI 10.1006/dbio.1997.8611
    • Evans, J. P., Kopf, G. S. & Schultz, R. M. Characterization of the binding of recombinant mouse sperm fertilin beta subunit to mouse eggs: evidence for adhesive activity via an egg beta1 integrin-mediated interaction. Dev. Biol. 187, 79-93 (1997). (Pubitemid 27359427)
    • (1997) Developmental Biology , vol.187 , Issue.1 , pp. 79-93
    • Evans, J.P.1    Kopf, G.S.2    Schultz, R.M.3
  • 48
    • 0034677883 scopus 로고    scopus 로고
    • Identification of key functional amino acids of the mouse fertilin β (ADAM2) disintegrin loop for cell-cell adhesion during fertilization
    • DOI 10.1074/jbc.275.11.7677
    • Zhu, X., Bansal, N. P. & Evans, J. P. Identification of key functional amino acids of the mouse fertilin beta (ADAM2) disintegrin loop for cell-cell adhesion during fertilization. J. Biol. Chem. 275, 7677-7683 (2000). (Pubitemid 30159670)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 7677-7683
    • Zhu, X.1    Bansal, N.P.2    Evans, J.P.3
  • 50
    • 0035163797 scopus 로고    scopus 로고
    • Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: Role of β1 integrin-associated proteins CD9, CD81, and CD98
    • Takahashi, Y., Bigler, D., Ito, Y. & White, J. M. 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). (Pubitemid 33051980)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 809-820
    • Takahashi, Y.1    Bigler, D.2    Ito, Y.3    White, J.M.4
  • 52
    • 78149486376 scopus 로고    scopus 로고
    • ADAM2 interactions with mouse eggs and cell lines expressing alpha4/alpha9 (ITGA4/ITGA9) integrins: Implications for integrin-based adhesion and fertilization
    • Desiderio, U. V., Zhu, X. & Evans, J. P. ADAM2 interactions with mouse eggs and cell lines expressing alpha4/alpha9 (ITGA4/ITGA9) integrins: implications for integrin-based adhesion and fertilization. PLoS ONE 5, e13744 (2010).
    • (2010) PLoS ONE , vol.5
    • Desiderio, U.V.1    Zhu, X.2    Evans, J.P.3
  • 53
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • DOI 10.1083/jcb.104.1.141
    • Primakoff, P., Hyatt, H. & Tredick-Kline, J. Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104, 141-149 (1987). (Pubitemid 17018665)
    • (1987) Journal of Cell Biology , vol.104 , Issue.1 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 54
    • 0025371355 scopus 로고
    • Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence
    • Blobel, C. P., Myles, D. G., Primakoff, P. & White, J. M. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J. Cell Biol. 111, 69-78 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 69-78
    • Blobel, C.P.1    Myles, D.G.2    Primakoff, P.3    White, J.M.4
  • 55
    • 0031282021 scopus 로고    scopus 로고
    • Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin
    • Lum, L. & Blobel, C. P. Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin. Dev. Biol. 191, 131-145 (1997). (Pubitemid 27519710)
    • (1997) Developmental Biology , vol.191 , Issue.1 , pp. 131-145
    • Lum, L.1    Blobel, C.P.2
  • 56
    • 0025151870 scopus 로고
    • Evidence that proteolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains
    • Phelps, B. M., Koppel, D. E., Primakoff, P. & Myles, D. G. Evidence that proteolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains. J. Cell Biol. 111, 1839-1847 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 1839-1847
    • Phelps, B.M.1    Koppel, D.E.2    Primakoff, P.3    Myles, D.G.4
  • 57
    • 0031282203 scopus 로고    scopus 로고
    • Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis
    • Hunnicutt, G. R., Koppel, D. E. & Myles, D. G. Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis. Dev. Biol. 191, 146-159 (1997). (Pubitemid 27519711)
    • (1997) Developmental Biology , vol.191 , Issue.1 , pp. 146-159
    • Hunnicutt, G.R.1    Koppel, D.E.2    Myles, D.G.3
  • 58
    • 55549115327 scopus 로고    scopus 로고
    • Cyclic 3', 5'-AMP causes ADAM1/ADAM2 to rapidly diffuse within the plasma membrane of guinea pig sperm
    • Hunnicutt, G. R., Koppel, D. E., Kwitny, S. & Cowan, A. E. Cyclic 3', 5'-AMP causes ADAM1/ADAM2 to rapidly diffuse within the plasma membrane of guinea pig sperm. Biol. Reprod. 79, 999-1007 (2008).
    • (2008) Biol. Reprod , vol.79 , pp. 999-1007
    • Hunnicutt, G.R.1    Koppel, D.E.2    Kwitny, S.3    Cowan, A.E.4
  • 59
    • 0031800745 scopus 로고    scopus 로고
    • Macaque MDC family of proteins: Sequence analysis, tissue distribution and processing in the male reproductive tract
    • DOI 10.1093/molehr/4.5.429
    • Frayne, J. et al. Macaque MDC family of proteins: sequence analysis, tissue distribution and processing in the male reproductive tract. Mol. Hum. Reprod. 4, 429-437 (1998). (Pubitemid 28253203)
    • (1998) Molecular Human Reproduction , vol.4 , Issue.5 , pp. 429-437
    • Frayne, J.1    Jury, J.A.2    Barker, H.L.3    Perry, A.C.F.4    Jones, R.5    Hall, L.6
  • 60
    • 0034660644 scopus 로고    scopus 로고
    • Analysis of mouse fertilin in wild-type and fertilin β(-/-) sperm: Evidence for C-terminal modification, α/β dimerization, and lack of essential role of fertilin α in sperm-egg fusion
    • DOI 10.1006/dbio.2000.9703
    • Cho, C., Ge, H., Branciforte, D., Primakoff, P. & Myles, D. G. Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion. Dev. Biol. 222, 289-295 (2000). (Pubitemid 30416367)
    • (2000) Developmental Biology , vol.222 , Issue.2 , pp. 289-295
    • Cho, C.1    Ge, H.2    Branciforte, D.3    Primakoff, P.4    Myles, D.G.5
  • 61
    • 0037414440 scopus 로고    scopus 로고
    • Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm
    • DOI 10.1016/S0006-291X(03)00588-6
    • Kim, E., Nishimura, H. & Baba, T. Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm. Biochem. Biophys. Res. Commun. 304, 313-319 (2003). (Pubitemid 36444571)
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.2 , pp. 313-319
    • Kim, E.1    Nishimura, H.2    Baba, T.3
  • 62
    • 70449527811 scopus 로고    scopus 로고
    • Processing and subcellular localization of ADAM2 in the Macaca fascicularis testis and sperm
    • Kim, E. et al. Processing and subcellular localization of ADAM2 in the Macaca fascicularis testis and sperm. Anim. Reprod. Sci. 117, 155-159 (2010).
    • (2010) Anim. Reprod. Sci. , vol.117 , pp. 155-159
    • Kim, E.1
  • 63
    • 0035005450 scopus 로고    scopus 로고
    • Testase 1 (ADAM 24) a plasma membrane-anchored sperm protease implicated in sperm function during epididymal maturation or fertilization
    • Zhu, G. Z., Myles, D. G. & Primakoff, P. Testase 1 (ADAM 24) a plasma membrane-anchored sperm protease implicated in sperm function during epididymal maturation or fertilization. J. Cell. Sci. 114, 1787-1794 (2001). (Pubitemid 32454676)
    • (2001) Journal of Cell Science , vol.114 , Issue.9 , pp. 1787-1794
    • Zhu, G.-Z.1    Myles, D.G.2    Primakoff, P.3
  • 64
    • 65749101619 scopus 로고    scopus 로고
    • Comprehensive analysis of reproductive ADAMs: Relationship of ADAM4 and ADAM6 with an ADAM complex required for fertilization in mice
    • Han, C. et al. Comprehensive analysis of reproductive ADAMs: relationship of ADAM4 and ADAM6 with an ADAM complex required for fertilization in mice. Biol. Reprod. 80, 1001-1008 (2009).
    • (2009) Biol. Reprod. , vol.80 , pp. 1001-1008
    • Han, C.1
  • 66
    • 33645061771 scopus 로고    scopus 로고
    • Expression and relationship of male reproductive ADAMs in mouse
    • Kim, T. et al. Expression and relationship of male reproductive ADAMs in mouse. Biol. Reprod. 74, 744-750 (2006).
    • (2006) Biol. Reprod. , vol.74 , pp. 744-750
    • Kim, T.1
  • 67
    • 0028841726 scopus 로고
    • Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome
    • Linder, B., Bammer, S. & Heinlein, U. A. Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome. Exp. Cell Res. 221, 66-72 (1995).
    • (1995) Exp. Cell Res. , vol.221 , pp. 66-72
    • Linder, B.1    Bammer, S.2    Heinlein, U.A.3
  • 68
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • DOI 10.1083/jcb.137.1.105
    • Yuan, R., Primakoff, P. & Myles, D. G. A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J. Cell Biol. 137, 105-112 (1997). (Pubitemid 27167299)
    • (1997) Journal of Cell Biology , vol.137 , Issue.1 , pp. 105-112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3
  • 69
    • 34547125812 scopus 로고    scopus 로고
    • Identification of an ADAM2-ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm
    • DOI 10.1074/jbc.M702268200
    • Nishimura, H., Myles, D. G. & Primakoff, P. 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). (Pubitemid 47100315)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17900-17907
    • Nishimura, H.1    Myles, D.G.2    Primakoff, P.3
  • 70
    • 0034014578 scopus 로고    scopus 로고
    • GP-83 and GP-39, two glycoproteins secreted by human epididymis are conjugated to spermatozoa during maturation
    • Liu, H. W., Lin, Y. C., Chao, C. F., Chang, S. Y. & Sun, G. H. GP-83 and GP-39, two glycoproteins secreted by human epididymis are conjugated to spermatozoa during maturation. Mol. Hum. Reprod. 6, 422-428 (2000).
    • (2000) Mol. Hum. Reprod. , vol.6 , pp. 422-428
    • Liu, H.W.1    Lin, Y.C.2    Chao, C.F.3    Chang, S.Y.4    Sun, G.H.5
  • 71
    • 0034015188 scopus 로고    scopus 로고
    • Purification of GP-83, a glycoprotein secreted by the human epididymis and conjugated to mature spermatozoa
    • Sun, G. H., Lin, Y. C., Guo, Y. W., Chang, S. Y. & Liu, H. W. Purification of GP-83, a glycoprotein secreted by the human epididymis and conjugated to mature spermatozoa. Mol. Hum. Reprod. 6, 429-434 (2000).
    • (2000) Mol. Hum. Reprod. , vol.6 , pp. 429-434
    • Sun, G.H.1    Lin, Y.C.2    Guo, Y.W.3    Chang, S.Y.4    Liu, H.W.5
  • 72
    • 72949087959 scopus 로고    scopus 로고
    • ADAM7 is associated with epididymosomes and integrated into sperm plasma membrane
    • Oh, J. S., Han, C. & Cho, C. ADAM7 is associated with epididymosomes and integrated into sperm plasma membrane. Mol. Cells 28, 441-446 (2009).
    • (2009) Mol. Cells , vol.28 , pp. 441-446
    • Oh, J.S.1    Han, C.2    Cho, C.3
  • 73
    • 79951799586 scopus 로고    scopus 로고
    • Identification of heat shock protein 5, calnexin and integral membrane protein 2B as Adam7-interacting membrane proteins in mouse sperm
    • Han, C. et al. Identification of heat shock protein 5, calnexin and integral membrane protein 2B as Adam7-interacting membrane proteins in mouse sperm. J. Cell. Physiol. 226, 1186-1195 (2011).
    • (2011) J. Cell. Physiol. , vol.226 , pp. 1186-1195
    • Han, C.1
  • 75
    • 0032710099 scopus 로고    scopus 로고
    • Male mice deficient for germ-cell cyritestin are infertile
    • Shamsadin, R. et al. Male mice deficient for germ-cell cyritestin are infertile. Biol. Reprod. 61, 1445-1451 (1999).
    • (1999) Biol. Reprod. , vol.61 , pp. 1445-1451
    • Shamsadin, R.1
  • 76
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β
    • DOI 10.1006/dbio.2001.0166
    • Nishimura, H., Cho, C., Branciforte, D. R., Myles, D. G. & Primakoff, P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev. Biol. 233, 204-213 (2001). (Pubitemid 32411305)
    • (2001) Developmental Biology , vol.233 , Issue.1 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 77
    • 4544250782 scopus 로고    scopus 로고
    • Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface
    • DOI 10.1074/jbc.M314249200
    • Nishimura, H., Kim, E., Nakanishi, T. & Baba, T. Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface. J. Biol. Chem. 279, 34957-34962 (2004). (Pubitemid 39318132)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 79
    • 70349266847 scopus 로고    scopus 로고
    • Testase 1 (ADAM 24) a sperm surface metalloprotease is required for normal fertility in mice
    • Zhu, G. Z., Gupta, S., Myles, D. G. & Primakoff, P. Testase 1 (ADAM 24) a sperm surface metalloprotease is required for normal fertility in mice. Mol. Reprod. Dev. 76, 1106-1114 (2009).
    • (2009) Mol. Reprod. Dev. , vol.76 , pp. 1106-1114
    • Zhu, G.Z.1    Gupta, S.2    Myles, D.G.3    Primakoff, P.4
  • 80
    • 27144540547 scopus 로고    scopus 로고
    • Defects in secretory pathway trafficking during sperm development in Adam2 knockout mice
    • DOI 10.1095/biolreprod.105.040972
    • Stein, K. K., Go, J. C., Primakoff, P. & Myles, D. G. Defects in secretory pathway trafficking during sperm development in Adam2 knockout mice. Biol. Reprod. 73, 1032-1038 (2005). (Pubitemid 41507509)
    • (2005) Biology of Reproduction , vol.73 , Issue.5 , pp. 1032-1038
    • Stein, K.K.1    Go, J.C.2    Primakoff, P.3    Myles, D.G.4
  • 81
    • 79953901981 scopus 로고    scopus 로고
    • Lack of tyrosylprotein sulfotransferase-2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm
    • Marcello, M. R., Jia, W., Leary, J. A., Moore, K. L. & Evans, J. P. Lack of tyrosylprotein sulfotransferase-2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm. J. Biol. Chem. 286, 13060-13070 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 13060-13070
    • Marcello, M.R.1    Jia, W.2    Leary, J.A.3    Moore, K.L.4    Evans, J.P.5
  • 82
    • 29544450106 scopus 로고    scopus 로고
    • Sperm transport in the female reproductive tract
    • DOI 10.1093/humupd/dmi047
    • Suarez, S. S. & Pacey, A. A. Sperm transport in the female reproductive tract. Hum. Reprod. Update 12, 23-37 (2006). (Pubitemid 43013744)
    • (2006) Human Reproduction Update , vol.12 , Issue.1 , pp. 23-37
    • Suarez, S.S.1    Pacey, A.A.2
  • 83
    • 67649654442 scopus 로고    scopus 로고
    • Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse
    • Yamaguchi, R. et al. Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse. Biol. Reprod. 81, 142-146 (2009).
    • (2009) Biol. Reprod. , vol.81 , pp. 142-146
    • Yamaguchi, R.1
  • 84
    • 77952111403 scopus 로고    scopus 로고
    • Impaired sperm aggregation in Adam2 and Adam3 null mice
    • Han, C. et al. Impaired sperm aggregation in Adam2 and Adam3 null mice. Fertil. Steril. 93, 2754-2756 (2010).
    • (2010) Fertil. Steril. , vol.93 , pp. 2754-2756
    • Han, C.1
  • 85
    • 84857969832 scopus 로고    scopus 로고
    • Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male infertility
    • Tokuhiro, K., Ikawa, M., Benham, A. M. & Okabe, M. Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male infertility. Proc. Natl Acad. Sci. USA 109, 3850-3855 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 3850-3855
    • Tokuhiro, K.1    Ikawa, M.2    Benham, A.M.3    Okabe, M.4
  • 86
    • 34547461129 scopus 로고    scopus 로고
    • Mouse sperm rosette: Assembling during epididymal transit, in vitro disassemble, and oligosaccharide participation in the linkage material
    • Monclus, M. A. et al. Mouse sperm rosette: assembling during epididymal transit, in vitro disassemble, and oligosaccharide participation in the linkage material. Anat. Rec. (Hoboken) 290, 814-824 (2007).
    • (2007) Anat. Rec. (Hoboken) , vol.290 , pp. 814-824
    • Monclus, M.A.1
  • 87
    • 0016915553 scopus 로고
    • The sperm acrosome reaction and fertilization in the guinea-pig: A study in vivo
    • Yanagimachi, R. & Mahi, C. A. The sperm acrosome reaction and fertilization in the guinea-pig: a study in vivo. J. Reprod. Fertil. 46, 49-54 (1976).
    • (1976) J. Reprod. Fertil. , vol.46 , pp. 49-54
    • Yanagimachi, R.1    Mahi, C.A.2
  • 88
    • 0037062937 scopus 로고    scopus 로고
    • Exceptional sperm cooperation in the wood mouse
    • DOI 10.1038/nature00832
    • Moore, H., Dvorakova, K., Jenkins, N. & Breed, W. Exceptional sperm cooperation in the wood mouse. Nature 418, 174-177 (2002). (Pubitemid 34773770)
    • (2002) Nature , vol.418 , Issue.6894 , pp. 174-177
    • Moore, H.1    Dvorakova, K.2    Jenkins, N.3    Breed, W.4
  • 89
    • 45149133837 scopus 로고    scopus 로고
    • Sperm sociality: Cooperation, altruism, and spite
    • Pizzari, T. & Foster, K. R. Sperm sociality: cooperation, altruism, and spite. PLoS Biol. 6, e130 (2008).
    • (2008) PLoS Biol , vol.6
    • Pizzari, T.1    Foster, K.R.2
  • 90
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • Muga, A., Neugebauer, W., Hirama, T. & Surewicz, W. K. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry 33, 4444-4448 (1994). (Pubitemid 24145089)
    • (1994) Biochemistry , vol.33 , Issue.15 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 91
    • 0030788927 scopus 로고    scopus 로고
    • Membrane interaction of synthetic peptides related to the putative fusogenic region of PH-30α, a protein in sperm-egg fusion
    • Niidome, T. et al. Membrane interaction of synthetic peptides related to the putative fusogenic region of PH-30 alpha, a protein in sperm-egg fusion. J. Pept. Res. 49, 563-569 (1997). (Pubitemid 27335001)
    • (1997) Journal of Peptide Research , vol.49 , Issue.6 , pp. 563-569
    • Niidome, T.1    Kimura, M.2    Chiba, T.3    Ohmori, N.4    Mihara, H.5    Aoyagi, H.6
  • 92
    • 0032387628 scopus 로고    scopus 로고
    • Structural properties of the putative fusion peptide of fertilin, a protein active in sperm-egg fusion, upon interaction with the lipid bilayer
    • DOI 10.1021/bi980909i
    • Martin, I., Epand, R. M. & Ruysschaert, J. M. Structural properties of the putative fusion peptide of fertilin, a protein active in sperm-egg fusion, upon interaction with the lipid bilayer. Biochemistry 37, 17030-17039 (1998). (Pubitemid 28566782)
    • (1998) Biochemistry , vol.37 , Issue.48 , pp. 17030-17039
    • Martin, I.1    Epand, R.M.2    Ruysschaert, J.-M.3
  • 93
    • 0032849530 scopus 로고    scopus 로고
    • Membrane interactions of the putative fusion peptide (MFαP) from fertilin-α, the mouse sperm protein complex involved in fertilization
    • DOI 10.1080/096876899294571
    • Wolfe, C. A. et al. Membrane interactions of the putative fusion peptide (MF alpha P) from fertilin-alpha, the mouse sperm protein complex involved in fertilization. Mol. Membr. Biol. 16, 257-263 (1999). (Pubitemid 29419700)
    • (1999) Molecular Membrane Biology , vol.16 , Issue.3 , pp. 257-263
    • Wolfe, C.A.1    Cladera, J.2    Ladha, S.3    Senior, S.4    Jones, R.5    O'Shea, P.6
  • 95
    • 0029047919 scopus 로고
    • Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor
    • Almeida, E. A. et al. Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor. Cell 81, 1095-1104 (1995).
    • (1995) Cell , vol.81 , pp. 1095-1104
    • Almeida, E.A.1
  • 96
    • 0029162781 scopus 로고
    • Mouse sperm-egg plasma membrane interactions: Analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta
    • Evans, J. P., Schultz, R. M. & Kopf, G. S. Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta. J. Cell. Sci. 108, 3267-3278 (1995).
    • (1995) J. Cell. Sci. , vol.108 , pp. 3267-3278
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 97
    • 0031778296 scopus 로고    scopus 로고
    • Roles of the disintegrin domains of mouse fertilins α and β in fertilization
    • DOI 10.1095/biolreprod59.1.145
    • Evans, J. P., Schultz, R. M. & Kopf, G. S. Roles of the disintegrin domains of mouse fertilins alpha and beta in fertilization. Biol. Reprod. 59, 145-152 (1998). (Pubitemid 28304365)
    • (1998) Biology of Reproduction , vol.59 , Issue.1 , pp. 145-152
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 100
    • 0031011488 scopus 로고    scopus 로고
    • The putative chaperone calmegin is required for sperm fertility
    • Ikawa, M. et al. The putative chaperone calmegin is required for sperm fertility. Nature 387, 607-611 (1997).
    • (1997) Nature , vol.387 , pp. 607-611
    • Ikawa, M.1
  • 101
    • 79953135154 scopus 로고    scopus 로고
    • Calsperin is a testis-specific chaperone required for sperm fertility
    • Ikawa, M. et al. Calsperin is a testis-specific chaperone required for sperm fertility. J. Biol. Chem. 286, 5639-5646 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 5639-5646
    • Ikawa, M.1
  • 103
    • 33750845874 scopus 로고    scopus 로고
    • Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice
    • DOI 10.1095/biolreprod.106.052977
    • Yamaguchi, R., Yamagata, K., Ikawa, M., Moss, S. B. & Okabe, M. Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)-and calmegin (Clgn)-deficient mice. Biol. Reprod. 75, 760-766 (2006). (Pubitemid 44720396)
    • (2006) Biology of Reproduction , vol.75 , Issue.5 , pp. 760-766
    • Yamaguchi, R.1    Yamagata, K.2    Ikawa, M.3    Moss, S.B.4    Okabe, M.5
  • 104
    • 79960917875 scopus 로고    scopus 로고
    • Mechanisms of fertilization - A view from the study of gene-manipulated mice
    • Muro, Y. & Okabe, M. Mechanisms of fertilization - a view from the study of gene-manipulated mice. J. Androl. 32, 218-225 (2011).
    • (2011) J. Androl. , vol.32 , pp. 218-225
    • Muro, Y.1    Okabe, M.2
  • 105
    • 54249143638 scopus 로고    scopus 로고
    • Regulation of sperm storage and movement in the mammalian oviduct
    • Suarez, S. S. Regulation of sperm storage and movement in the mammalian oviduct. Int. J. Dev. Biol. 52, 455-462 (2008).
    • (2008) Int. J. Dev. Biol. , vol.52 , pp. 455-462
    • Suarez, S.S.1
  • 106
    • 77951148607 scopus 로고    scopus 로고
    • Fertilization: A sperm's journey to and interaction with the oocyte
    • Ikawa, M., Inoue, N., Benham, A. M. & Okabe, M. Fertilization: a sperm's journey to and interaction with the oocyte. J. Clin. Invest. 120, 984-994 (2010).
    • (2010) J. Clin. Invest. , vol.120 , pp. 984-994
    • Ikawa, M.1    Inoue, N.2    Benham, A.M.3    Okabe, M.4
  • 107
    • 67349115402 scopus 로고    scopus 로고
    • Cyclic QDE peptide increases fertilization rates and provides healthy pups in mouse
    • Barraud-Lange, V. et al. Cyclic QDE peptide increases fertilization rates and provides healthy pups in mouse. Fertil. Steril. 91, 2110-2115 (2009).
    • (2009) Fertil. Steril. , vol.91 , pp. 2110-2115
    • Barraud-Lange, V.1
  • 108
    • 84878052354 scopus 로고    scopus 로고
    • EMBL-EBI European Bioinformatics Institute. [online]
    • EMBL-EBI European Bioinformatics Institute. MUSCLE - Multiple Sequence Alignment [online], http://www.ebi.ac.uk/Tools/msa/muscle/ (2012).
    • (2012) MUSCLE - Multiple Sequence Alignment
  • 109
    • 84878045869 scopus 로고    scopus 로고
    • Department Of Genome Sciences And The Department Of Biology University Of Washington. [online]
    • Department of Genome Sciences and the Department of Biology, University of Washington. PHYLIP [online], http://evolution.genetics.washington.edu/phylip. html (2012).
    • (2012) PHYLIP
  • 110
    • 84878066418 scopus 로고    scopus 로고
    • [online]
    • National Center for Biotechnology Information. Gene [online], http://www.ncbi.nlm.nih.gov/gene (2012).
    • (2012) Gene


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.