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Volumn 61, Issue 5, 1999, Pages 1184-1197

FSP95, a testis-specific 95-kilodalton fibrous sheath antigen that undergoes tyrosine phosphorylation in capacitated human spermatozoa

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; MONOCLONAL ANTIBODY; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN; SPERM ANTIGEN;

EID: 0032696027     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod61.5.1184     Document Type: Article
Times cited : (156)

References (67)
  • 1
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill JD (eds.), New York: Raven Press
    • Yanagimachi R. Mammalian fertilization. In: Knobil E, Neill JD (eds.), The Physiology of Reproduction. New York: Raven Press; 1994: 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 2
    • 0024845616 scopus 로고
    • Calcium requirement and increased association with bovine sperm during capacitation by heparin
    • Handrow RR, First NL, Parrish JJ. Calcium requirement and increased association with bovine sperm during capacitation by heparin. J Exp Zool 1989; 252:174-182.
    • (1989) J Exp Zool , vol.252 , pp. 174-182
    • Handrow, R.R.1    First, N.L.2    Parrish, J.J.3
  • 3
    • 0025943491 scopus 로고
    • Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa
    • Baldi E, Casana R, Falsetti C, Krausz C, Maggi M, Forti G. Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa. J Androl 1991; 12:323-330.
    • (1991) J Androl , vol.12 , pp. 323-330
    • Baldi, E.1    Casana, R.2    Falsetti, C.3    Krausz, C.4    Maggi, M.5    Forti, G.6
  • 4
    • 0029969294 scopus 로고    scopus 로고
    • ++-dependent 3′,5′-cyclic adenosine monophosphate increase in human sperm
    • ++-dependent 3′,5′-cyclic adenosine monophosphate increase in human sperm. J Clin Endrocrinol Metab 1996; 81:1357-1360.
    • (1996) J Clin Endrocrinol Metab , vol.81 , pp. 1357-1360
    • Parinaud, J.1    Milhet, P.2
  • 5
    • 0028061888 scopus 로고
    • Differences in the role of cyclic adenosine 3′,5′-monophosphate during capacitation of bovine sperm by heparin or oviduct fluid
    • Parrish JJ, Susko-Parrish JL, Uguz C, First NL. Differences in the role of cyclic adenosine 3′,5′-monophosphate during capacitation of bovine sperm by heparin or oviduct fluid. Biol Reprod 1994; 51:1099-1108.
    • (1994) Biol Reprod , vol.51 , pp. 1099-1108
    • Parrish, J.J.1    Susko-Parrish, J.L.2    Uguz, C.3    First, N.L.4
  • 6
    • 0028935169 scopus 로고
    • Intracellular pH of bovine sperm increases during capacitation
    • Vredenburgh-Wilberg WL, Parrish JJ. Intracellular pH of bovine sperm increases during capacitation. Mol Reprod Dev 1995; 40:490-502.
    • (1995) Mol Reprod Dev , vol.40 , pp. 490-502
    • Vredenburgh-Wilberg, W.L.1    Parrish, J.J.2
  • 7
    • 0031778295 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation during sperm capacitation
    • Visconti PE, Kopf GS. Regulation of protein phosphorylation during sperm capacitation. Biol Reprod 1998; 59:1-6.
    • (1998) Biol Reprod , vol.59 , pp. 1-6
    • Visconti, P.E.1    Kopf, G.S.2
  • 8
    • 0028957362 scopus 로고
    • Capacitation in mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore JD, Pan D, Olds-Clarke P, Kopf GS. Capacitation in mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 1995; 121:1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, J.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 9
    • 0031049037 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′,5′-monophosphate dependent pathway
    • Galantino-Homer HL, Visconti PE, Kopf GS. Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′,5′-monophosphate dependent pathway. Biol Reprod 1997; 56:707-719.
    • (1997) Biol Reprod , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 10
    • 0030602027 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: Identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation
    • Carrera A, Moss J, Ning XP, Gerton GL, Tesarik J, Kopf GS, Moss SB. Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation. Dev Biol 1996; 180:284-296.
    • (1996) Dev Biol , vol.180 , pp. 284-296
    • Carrera, A.1    Moss, J.2    Ning, X.P.3    Gerton, G.L.4    Tesarik, J.5    Kopf, G.S.6    Moss, S.B.7
  • 11
    • 0029789196 scopus 로고    scopus 로고
    • Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa
    • Luconi M, Krausz C, Forti G, Baldi E. Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa. Biol Reprod 1996; 55:207-216.
    • (1996) Biol Reprod , vol.55 , pp. 207-216
    • Luconi, M.1    Krausz, C.2    Forti, G.3    Baldi, E.4
  • 12
    • 0031595786 scopus 로고    scopus 로고
    • ++, cyclic 3′,5′-adenosine monophosphate, the superoxide anion, and tyrosine phosphorylation pathways in the regulation of human sperm capacitation
    • ++, cyclic 3′,5′-adenosine monophosphate, the superoxide anion, and tyrosine phosphorylation pathways in the regulation of human sperm capacitation. J Androl 1998; 19:434-443.
    • (1998) J Androl , vol.19 , pp. 434-443
    • Leclerc, P.1    Lamirande, E.D.2    Gagnon, C.3
  • 13
    • 0033610895 scopus 로고    scopus 로고
    • An X-linked gene encodes a major human sperm fibrous sheath protein, hAKAP82. Genomic organization, protein kinase A-RII binding, and distribution of the precursor in the sperm tail
    • Turner RMO, Johnson LR, Haig-Ladewig L, Gerton GL, Moss SB. An X-linked gene encodes a major human sperm fibrous sheath protein, hAKAP82. Genomic organization, protein kinase A-RII binding, and distribution of the precursor in the sperm tail. J Biol Chem 1998; 273:32135-32141.
    • (1998) J Biol Chem , vol.273 , pp. 32135-32141
    • Turner, R.M.O.1    Johnson, L.R.2    Haig-Ladewig, L.3    Gerton, G.L.4    Moss, S.B.5
  • 15
    • 0029980440 scopus 로고    scopus 로고
    • Molecular glue: Kinase anchoring and scaffold proteins
    • Faux MC, Scott JD. Molecular glue: kinase anchoring and scaffold proteins. Cell 1996; 85:9-12.
    • (1996) Cell , vol.85 , pp. 9-12
    • Faux, M.C.1    Scott, J.D.2
  • 16
    • 0029887701 scopus 로고    scopus 로고
    • Coordination of three signalling enzymes by AKAP79, a mammalian scaffold protein
    • Klauck TM, Faux MC, Labudda K, Langeberg LK, Jaken S, Scott JD. Coordination of three signalling enzymes by AKAP79, a mammalian scaffold protein. Science 1996; 271:1589-1592.
    • (1996) Science , vol.271 , pp. 1589-1592
    • Klauck, T.M.1    Faux, M.C.2    Labudda, K.3    Langeberg, L.K.4    Jaken, S.5    Scott, J.D.6
  • 17
    • 0020623097 scopus 로고
    • Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility
    • Tash JS, Means AR. Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility. Biol Reprod 1983; 28:75-104.
    • (1983) Biol Reprod , vol.28 , pp. 75-104
    • Tash, J.S.1    Means, A.R.2
  • 18
    • 0028230419 scopus 로고
    • Role of cAMP in the reactivation of demembranated ram spermatozoa
    • San Augustin JT, Witman GB. Role of cAMP in the reactivation of demembranated ram spermatozoa. Cell Motil Cytoskeleton 1994; 27: 206-218.
    • (1994) Cell Motil Cytoskeleton , vol.27 , pp. 206-218
    • San Augustin, J.T.1    Witman, G.B.2
  • 19
    • 0024329482 scopus 로고
    • Protein phosphorylation: The second messenger signal transducer of flagellar motility
    • Tash JS. Protein phosphorylation: the second messenger signal transducer of flagellar motility. Cell Motil Cytoskeleton 1989; 14:332-339.
    • (1989) Cell Motil Cytoskeleton , vol.14 , pp. 332-339
    • Tash, J.S.1
  • 20
    • 0028605927 scopus 로고
    • Regulation of sperm motility: Emerging evidence for a major role for protein phosphatases
    • Tash JS, Bracho GE. Regulation of sperm motility: emerging evidence for a major role for protein phosphatases. J Androl 1994; 15:505-509.
    • (1994) J Androl , vol.15 , pp. 505-509
    • Tash, J.S.1    Bracho, G.E.2
  • 21
    • 0023815181 scopus 로고
    • Fully effective contraception in male and female guinea pigs immunized with the sperm protein PH-20
    • Primakoff P, Lathrop W, Woolman L, Cowan A, Myles D. Fully effective contraception in male and female guinea pigs immunized with the sperm protein PH-20. Nature 1988; 335:543-546.
    • (1988) Nature , vol.335 , pp. 543-546
    • Primakoff, P.1    Lathrop, W.2    Woolman, L.3    Cowan, A.4    Myles, D.5
  • 22
    • 0029549903 scopus 로고
    • Infertility due to antisperm antibodies
    • Ohl DA, Naz RK. Infertility due to antisperm antibodies. Urology 1995; 46:591-602.
    • (1995) Urology , vol.46 , pp. 591-602
    • Ohl, D.A.1    Naz, R.K.2
  • 23
    • 0027489584 scopus 로고
    • Complications of vasectomy
    • Raspa RF. Complications of vasectomy. Am Family Physician 1993; 48:1264-1268.
    • (1993) Am Family Physician , vol.48 , pp. 1264-1268
    • Raspa, R.F.1
  • 24
    • 0025666482 scopus 로고
    • Correlation between quantitative antibody titers of sperm immobilizing antibodies and pregnancy rates by treatments
    • Kobayashi S, Bessho T, Shigata M, Koyama K, Isojima S. Correlation between quantitative antibody titers of sperm immobilizing antibodies and pregnancy rates by treatments. Fertil Steril 1990; 54:1107-1113.
    • (1990) Fertil Steril , vol.54 , pp. 1107-1113
    • Kobayashi, S.1    Bessho, T.2    Shigata, M.3    Koyama, K.4    Isojima, S.5
  • 25
    • 0031044330 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoretic analysis of vectorially labelled surface proteins of human spermatozoa
    • Naaby-Hansen S, Flickinger CJ, Herr JC. Two-dimensional gel electrophoretic analysis of vectorially labelled surface proteins of human spermatozoa. Biol Reprod 1997; 56:771-787.
    • (1997) Biol Reprod , vol.56 , pp. 771-787
    • Naaby-Hansen, S.1    Flickinger, C.J.2    Herr, J.C.3
  • 27
    • 0027385186 scopus 로고
    • Induction by EGF and interferon-g of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei
    • Ruff-Jamisson S, Chen K, Cohen S. Induction by EGF and interferon-g of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei. Science 1993; 261:1733-1736.
    • (1993) Science , vol.261 , pp. 1733-1736
    • Ruff-Jamisson, S.1    Chen, K.2    Cohen, S.3
  • 28
    • 0029042753 scopus 로고
    • Interaction of a tyrosine kinase from human sperm with the zona pellucida at fertilization
    • Burks DJ, Carballada R, Moore HDM, Saling PM. Interaction of a tyrosine kinase from human sperm with the zona pellucida at fertilization. Science 1995; 269:83-86.
    • (1995) Science , vol.269 , pp. 83-86
    • Burks, D.J.1    Carballada, R.2    Moore, H.D.M.3    Saling, P.M.4
  • 30
    • 84907130179 scopus 로고
    • Techniques for sperm immobilization test
    • Isojima S, Koyama K. Techniques for sperm immobilization test. Arch Androl 1989; 23:185-199.
    • (1989) Arch Androl , vol.23 , pp. 185-199
    • Isojima, S.1    Koyama, K.2
  • 31
    • 0031905269 scopus 로고    scopus 로고
    • Complement regulatory proteins on the sperm surface: Relevance to sperm motility
    • Jiang H, Pillai S. Complement regulatory proteins on the sperm surface: relevance to sperm motility. Am J Reprod Immunol 1998; 39: 243-248.
    • (1998) Am J Reprod Immunol , vol.39 , pp. 243-248
    • Jiang, H.1    Pillai, S.2
  • 32
    • 0030729271 scopus 로고    scopus 로고
    • Biochemical characterization of sperm agglutination antigen-1, a human sperm surface antigen implicated in gamete interactions
    • Diekman AB, Westbrook-Case VA, Naaby-Hansen S, Klotz KL, Flickinger CJ, Herr JC. Biochemical characterization of sperm agglutination antigen-1, a human sperm surface antigen implicated in gamete interactions. Biol Reprod 1997; 57:1136-1144.
    • (1997) Biol Reprod , vol.57 , pp. 1136-1144
    • Diekman, A.B.1    Westbrook-Case, V.A.2    Naaby-Hansen, S.3    Klotz, K.L.4    Flickinger, C.J.5    Herr, J.C.6
  • 34
    • 0025093417 scopus 로고
    • An enhanced method for post-embedding immunocytochemistry staining which preserves cell membranes
    • Berryman MA, Rodewald RD. An enhanced method for post-embedding immunocytochemistry staining which preserves cell membranes. J Histochem Cytochem 1990; 38:159-170.
    • (1990) J Histochem Cytochem , vol.38 , pp. 159-170
    • Berryman, M.A.1    Rodewald, R.D.2
  • 35
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak M. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J Biol Chem 1991; 266:19867-19870.
    • (1991) J Biol Chem , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 36
    • 0025866021 scopus 로고
    • Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins
    • Juretic N, Theus M. Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins. FEBS Lett 1991; 290:4-8.
    • (1991) FEBS Lett , vol.290 , pp. 4-8
    • Juretic, N.1    Theus, M.2
  • 37
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997; 10:1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 39
    • 0030860232 scopus 로고    scopus 로고
    • O-GLYCOBASE version 2.0: A revised database of O-glycosylated proteins
    • Hansen JE, Lund O, Rapacki K, Brunak S. O-GLYCOBASE version 2.0: a revised database of O-glycosylated proteins. Nucleic Acids Res 1997; 25:278-282.
    • (1997) Nucleic Acids Res , vol.25 , pp. 278-282
    • Hansen, J.E.1    Lund, O.2    Rapacki, K.3    Brunak, S.4
  • 41
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson WR, Lipman DJ. Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988; 85:2444-2448.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 42
    • 0028023326 scopus 로고
    • The major fibrous sheath polypeptide of mouse sperm: Structural and functional similarities to the A-kinase anchoring proteins
    • Carrera A, Gerton GL, Moss SB. The major fibrous sheath polypeptide of mouse sperm: structural and functional similarities to the A-kinase anchoring proteins. Dev Biol 1994; 165:272-284.
    • (1994) Dev Biol , vol.165 , pp. 272-284
    • Carrera, A.1    Gerton, G.L.2    Moss, S.B.3
  • 43
    • 0026603594 scopus 로고
    • Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain
    • Van Dyke MW, Sirito M, Sawadogo M. Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain. Gene 1992; 111:99-104.
    • (1992) Gene , vol.111 , pp. 99-104
    • Van Dyke, M.W.1    Sirito, M.2    Sawadogo, M.3
  • 44
    • 0030794404 scopus 로고    scopus 로고
    • On-line derivatization of peptides for improved sequence analysis by micro-column liquid chromatography coupled with electrospray ionization-tandem mass spectrometry
    • Cardenas MS, van der Heeft E, de Jong AP. On-line derivatization of peptides for improved sequence analysis by micro-column liquid chromatography coupled with electrospray ionization-tandem mass spectrometry. Rapid Commun Mass Spectrom 1997; 11:1271-1278.
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1271-1278
    • Cardenas, M.S.1    Van Der Heeft, E.2    De Jong, A.P.3
  • 45
    • 0028966773 scopus 로고
    • Stimulation of protein tyrosine phosphorylation by platelet-activating factor and progesterone in human spermatozoa
    • Luconi M, Bonaccorsi L, Krausz C, Gervasi G, Forti G, Baldi E. Stimulation of protein tyrosine phosphorylation by platelet-activating factor and progesterone in human spermatozoa. Mol Cell Endocrinol 1995; 108:35-42.
    • (1995) Mol Cell Endocrinol , vol.108 , pp. 35-42
    • Luconi, M.1    Bonaccorsi, L.2    Krausz, C.3    Gervasi, G.4    Forti, G.5    Baldi, E.6
  • 46
    • 0029920932 scopus 로고    scopus 로고
    • sp42, the boar sperm tyrosine kinase, is a male germ cell-specific product with a highly conserved tissue expression extending to other mammalian species
    • Berruti G, Borgonovo B. sp42, the boar sperm tyrosine kinase, is a male germ cell-specific product with a highly conserved tissue expression extending to other mammalian species. J Cell Sci 1996; 109:851-858.
    • (1996) J Cell Sci , vol.109 , pp. 851-858
    • Berruti, G.1    Borgonovo, B.2
  • 47
    • 0023952125 scopus 로고
    • Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm
    • Tash JS, Krinks M, Patel J, Means RL, Klee CB, Means AR. Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm. J Cell Biol 1988; 106:1625-1633.
    • (1988) J Cell Biol , vol.106 , pp. 1625-1633
    • Tash, J.S.1    Krinks, M.2    Patel, J.3    Means, R.L.4    Klee, C.B.5    Means, A.R.6
  • 48
    • 0027194031 scopus 로고
    • Characterization of distinct tethering and intracellular targeting domains in AKAP75, a protein that links cAMP-dependent protein kinase lib to the cytoskeleton
    • Glantz SB, Li Y, Rubin CS. Characterization of distinct tethering and intracellular targeting domains in AKAP75, a protein that links cAMP-dependent protein kinase lib to the cytoskeleton. J Biol Chem 1993; 268:12796-12804.
    • (1993) J Biol Chem , vol.268 , pp. 12796-12804
    • Glantz, S.B.1    Li, Y.2    Rubin, C.S.3
  • 49
    • 0026795614 scopus 로고
    • Localization of the cAMP-dependent protein kinase to post-synthetic densities by A-kinase anchoring proteins: Characterization of AKAP79
    • Carr DW, Stofko-Hahn RE, Fraser ID, Cone RD, Scott JD. Localization of the cAMP-dependent protein kinase to post-synthetic densities by A-kinase anchoring proteins: characterization of AKAP79. J Biol Chem 1992; 267:16816-16823.
    • (1992) J Biol Chem , vol.267 , pp. 16816-16823
    • Carr, D.W.1    Stofko-Hahn, R.E.2    Fraser, I.D.3    Cone, R.D.4    Scott, J.D.5
  • 50
    • 0026348474 scopus 로고
    • Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif
    • Carr DW, Stofko-Hahn RE, Fraser IDC, Bishop SM, Acott TS, Brennan RG, Scott JD. Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif. J Biol Chem 1991; 266:14188-14192.
    • (1991) J Biol Chem , vol.266 , pp. 14188-14192
    • Carr, D.W.1    Stofko-Hahn, R.E.2    Fraser, I.D.C.3    Bishop, S.M.4    Acott, T.S.5    Brennan, R.G.6    Scott, J.D.7
  • 51
    • 0031040893 scopus 로고    scopus 로고
    • Protein kinase A-anchoring inhibitor peptides arrest mammalian sperm motility
    • Vijayaraghavan S, Goueli SA, Michael PD, Carr DW. Protein kinase A-anchoring inhibitor peptides arrest mammalian sperm motility. J Biol Chem 1997; 272:4747-4752.
    • (1997) J Biol Chem , vol.272 , pp. 4747-4752
    • Vijayaraghavan, S.1    Goueli, S.A.2    Michael, P.D.3    Carr, D.W.4
  • 52
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Bailey JL, Leclerc P, Connors SA, Pan D, Olds-Clarke P, Kopf GS. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 1995; 121:1139-1150.
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 53
    • 0002711979 scopus 로고
    • Sperm and testicular autoimmunity
    • Rose NR, Mackay IR (eds.), New York: Academic Press
    • Tung KSK, Menge AC. Sperm and testicular autoimmunity. In: Rose NR, Mackay IR (eds.), The Autoimmune Diseases. New York: Academic Press; 1985: 537-590.
    • (1985) The Autoimmune Diseases , pp. 537-590
    • Tung, K.S.K.1    Menge, A.C.2
  • 55
    • 0021195984 scopus 로고
    • Morphological evidence for a blood-epididymis barrier and the effects of gossypol on its integrity
    • Hoffer AP, Hinton BT. Morphological evidence for a blood-epididymis barrier and the effects of gossypol on its integrity. Biol Reprod 1984; 30:991-1004.
    • (1984) Biol Reprod , vol.30 , pp. 991-1004
    • Hoffer, A.P.1    Hinton, B.T.2
  • 56
    • 0031834895 scopus 로고    scopus 로고
    • Expression of the human antigen SPAG2 in the testis and localization to the outer dense fibers in spermatozoa
    • Diekman AB, Olson G, Goldberg E. Expression of the human antigen SPAG2 in the testis and localization to the outer dense fibers in spermatozoa. Mol Reprod Dev 1998; 50:284-293.
    • (1998) Mol Reprod Dev , vol.50 , pp. 284-293
    • Diekman, A.B.1    Olson, G.2    Goldberg, E.3
  • 57
    • 0031026505 scopus 로고    scopus 로고
    • Autoimmunogenicity of the human sperm protein SP17 in vasectomized men and identification of linear B cell epitopes
    • Lea IA, Adoyo P, O'Rand MG. Autoimmunogenicity of the human sperm protein SP17 in vasectomized men and identification of linear B cell epitopes. Fertil Steril 1997; 67:355-361.
    • (1997) Fertil Steril , vol.67 , pp. 355-361
    • Lea, I.A.1    Adoyo, P.2    O'Rand, M.G.3
  • 58
    • 0021273874 scopus 로고
    • Monoclonal antibody to a human germ cell membrane glycoprotein that inhibits fertilization
    • Naz RK, Alexander NJ, Isahakia M, Hamilton MS. Monoclonal antibody to a human germ cell membrane glycoprotein that inhibits fertilization. Science 1984; 225:342-344.
    • (1984) Science , vol.225 , pp. 342-344
    • Naz, R.K.1    Alexander, N.J.2    Isahakia, M.3    Hamilton, M.S.4
  • 59
    • 0002576729 scopus 로고    scopus 로고
    • Immunocontraceptive approaches
    • Harrison PF, Rosenfield A (eds.), Washington DC: National Academy Press
    • Herr JC. Immunocontraceptive approaches. In: Harrison PF, Rosenfield A (eds.), Contraceptive Research and Development. Washington DC: National Academy Press; 1996: 401-429.
    • (1996) Contraceptive Research and Development , pp. 401-429
    • Herr, J.C.1
  • 60
    • 0002494818 scopus 로고
    • The spermatozoon
    • Knobil E, Neill JD (eds.), New York: Raven Press
    • Eddy EM, O'Brien DA. The spermatozoon. In: Knobil E, Neill JD (eds.), The Physiology of Reproduction, Vol. I. New York: Raven Press; 1994: 29-77.
    • (1994) The Physiology of Reproduction , vol.1 , pp. 29-77
    • Eddy, E.M.1    O'Brien, D.A.2
  • 61
    • 0027199204 scopus 로고
    • The sliding of the fibrous sheath through the axoneme proximally together with microtubule extrusion
    • Si Y, Okuno M. The sliding of the fibrous sheath through the axoneme proximally together with microtubule extrusion. Exp Cell Res 1993; 208:170-174.
    • (1993) Exp Cell Res , vol.208 , pp. 170-174
    • Si, Y.1    Okuno, M.2
  • 63
    • 0032539730 scopus 로고    scopus 로고
    • Molecular cloning of human testis mRNA specifically expressed in haploid germ cells, having structural homology with the A-kinase anchoring proteins
    • Mohapatra B, Verma S, Shankar S, Suri A. Molecular cloning of human testis mRNA specifically expressed in haploid germ cells, having structural homology with the A-kinase anchoring proteins. Biochem Biophys Res Commun 1998; 244:540-545.
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 540-545
    • Mohapatra, B.1    Verma, S.2    Shankar, S.3    Suri, A.4
  • 64
    • 0030871591 scopus 로고    scopus 로고
    • Immunochemical characterization of a human sperm fibrous sheath protein, its developmental expression pattern, and morphogenetic relationships with actin
    • Escalier D, Gallo JM, Schrevel J. Immunochemical characterization of a human sperm fibrous sheath protein, its developmental expression pattern, and morphogenetic relationships with actin. J Histochem Cytochem 1997; 45:909-922.
    • (1997) J Histochem Cytochem , vol.45 , pp. 909-922
    • Escalier, D.1    Gallo, J.M.2    Schrevel, J.3
  • 65
    • 0023633025 scopus 로고
    • Dysplasia of the fibrous sheath: An ultrastructural defect of human spermatozoa associated with sperm immotility and primary sterility
    • Chemes HE, Brugo S, Zanchetti F, Carrere C, Lavieri JC. Dysplasia of the fibrous sheath: an ultrastructural defect of human spermatozoa associated with sperm immotility and primary sterility. Fertil Steril 1987; 48:664-669.
    • (1987) Fertil Steril , vol.48 , pp. 664-669
    • Chemes, H.E.1    Brugo, S.2    Zanchetti, F.3    Carrere, C.4    Lavieri, J.C.5
  • 66
    • 0022601366 scopus 로고
    • Abnormal distribution of the periaxonemal structures in a human sperm flagellar dyskinesia
    • Serres C, Feneux D, Jouannet P Abnormal distribution of the periaxonemal structures in a human sperm flagellar dyskinesia. Cell Motil Cytoskeleton 1986; 6:68-76.
    • (1986) Cell Motil Cytoskeleton , vol.6 , pp. 68-76
    • Serres, C.1    Feneux, D.2    Jouannet, P.3
  • 67
    • 0027412196 scopus 로고
    • ALSCRIPT a tool to format multiple sequence alignments
    • Barton GJ. ALSCRIPT a tool to format multiple sequence alignments. Protein Engineering 1993; 6: 37-40.
    • (1993) Protein Engineering , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.