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Volumn 11, Issue 2 P.1199-1590, 2006, Pages 1433-1447

Pathophysiology of sperm motility

Author keywords

Asthenozoospermia; Kinases; Review; Sperm Motility

Indexed keywords

MAMMALIA;

EID: 32844475537     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1894     Document Type: Review
Times cited : (53)

References (137)
  • 1
    • 1542542683 scopus 로고    scopus 로고
    • How do sperm swim? Molecular mechanisms underlying sperm motility
    • Luconi M. and E. Baldi. How do sperm swim?: molecular mechanisms underlying sperm motility: Cell Mol Biol: 49,357-369 (2003)
    • (2003) Cell Mol Biol , vol.49 , pp. 357-369
    • Luconi, M.1    Baldi, E.2
  • 4
    • 0037464465 scopus 로고    scopus 로고
    • Transient receptor potential (TRPC) channels in human sperm: Expression, cellular localization and involvement in the regulation of flagellar motility
    • Castellano L.E., C.L. Trevino, D. Rodriguez, C.J. Serrano, J. Pacheco, V. Tsutsumi, R. Felix, A. Darszon: Transient receptor potential (TRPC) channels in human sperm: expression, cellular localization and involvement in the regulation of flagellar motility. FEBS Lett 541,69-74 (2003)
    • (2003) FEBS Lett , vol.541 , pp. 69-74
    • Castellano, L.E.1    Trevino, C.L.2    Rodriguez, D.3    Serrano, C.J.4    Pacheco, J.5    Tsutsumi, V.6    Felix, R.7    Darszon, A.8
  • 6
    • 0029125139 scopus 로고
    • Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm
    • Snyder L.D. and S.H. Walensky: Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm. J Cell Biol 130,857-869 (1995)
    • (1995) J Cell Biol , vol.130 , pp. 857-869
    • Snyder, L.D.1    Walensky, S.H.2
  • 7
    • 0034766933 scopus 로고    scopus 로고
    • An inositol 1,4,5-trisphosphate receptor-gated intracellular Ca(2+) store is involved in regulating sperm hyperactivated motility
    • Ho H.C. and S.S. Suarez: An inositol 1,4,5-trisphosphate receptor-gated intracellular Ca(2+) store is involved in regulating sperm hyperactivated motility. Biol Reprod 65,1606-1615 (2001a)
    • (2001) Biol Reprod , vol.65 , pp. 1606-1615
    • Ho, H.C.1    Suarez, S.S.2
  • 8
    • 0023258569 scopus 로고
    • Calmodulin-mediated adenylate cyclase from mammalian sperm
    • Gross R.A., R.L. Macdonald, T. Ryan-Jastrow: Calmodulin-mediated adenylate cyclase from mammalian sperm. J Biol Chem 262,8672-8676 (1987)
    • (1987) J Biol Chem , vol.262 , pp. 8672-8676
    • Gross, R.A.1    Macdonald, R.L.2    Ryan-Jastrow, T.3
  • 9
    • 0141703301 scopus 로고    scopus 로고
    • Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa
    • Jaiswal B.S. and M. Conti: Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa. Proc Natl Acad Sci U S A. 100,10676-10681 (2003)
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10676-10681
    • Jaiswal, B.S.1    Conti, M.2
  • 10
    • 19444363673 scopus 로고    scopus 로고
    • Evidence of the presence of calcium/calmodulin-dependent protein kinase IV in human sperm and its involvement in motility regulation
    • Marin-Briggiler C.I., K.N. Jha, O. Chertihin, M.G. Buffone, J.C. Herr, M.H. Vazquez-Levin, P.E. Visconti: Evidence of the presence of calcium/calmodulin-dependent protein kinase IV in human sperm and its involvement in motility regulation. J Cell Sci 118,2013-2022 (2005)
    • (2005) J Cell Sci , vol.118 , pp. 2013-2022
    • Marin-Briggiler, C.I.1    Jha, K.N.2    Chertihin, O.3    Buffone, M.G.4    Herr, J.C.5    Vazquez-Levin, M.H.6    Visconti, P.E.7
  • 11
    • 23844550274 scopus 로고    scopus 로고
    • Calcium/calmodulin and calmodulin kinase II stimulate hyperactivation in demembranated bovine sperm
    • Ignotz G.G. and S.S. Suarez: Calcium/Calmodulin and Calmodulin Kinase II Stimulate Hyperactivation in Demembranated Bovine Sperm. Biol Reprod 73,519-526 (2005)
    • (2005) Biol Reprod , vol.73 , pp. 519-526
    • Ignotz, G.G.1    Suarez, S.S.2
  • 12
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak F. and P. Mertz: Calcineurin: form and function. Physiol Rev 80,1483-1521 (2000)
    • (2000) Physiol Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 13
    • 0021347846 scopus 로고
    • Function of calmodulin in mammalian sperm: Presence of a calmodulin-dependent cyclic nucleotide phosphodiesterase associated with demembranated rat caudal epididymal sperm
    • Wasco W.M., G.A. Orr: Function of calmodulin in mammalian sperm: presence of a calmodulin-dependent cyclic nucleotide phosphodiesterase associated with demembranated rat caudal epididymal sperm. Biochem Biophys Res Commun 118,636-642 (1984)
    • (1984) Biochem Biophys Res Commun , vol.118 , pp. 636-642
    • Wasco, W.M.1    Orr, G.A.2
  • 14
    • 0026326540 scopus 로고
    • The calcium-induced curvature reversal of rat sperm is potentiated by cAMP and inhibited by anti-calmodulin
    • Lindemann C.B., T.K. Gardner, E. Westbrook, K.S. Kanous: The calcium-induced curvature reversal of rat sperm is potentiated by cAMP and inhibited by anti-calmodulin. Cell Motil Cytoskeleton 20,316-324 (1991)
    • (1991) Cell Motil Cytoskeleton , vol.20 , pp. 316-324
    • Lindemann, C.B.1    Gardner, T.K.2    Westbrook, E.3    Kanous, K.S.4
  • 15
    • 0023194187 scopus 로고
    • Concentrations of calmodulin in sperm in relation to their motility in fertile euspermic and infertile asthenozoospermic men
    • Reyes R. Martinez, M. Luna, M.E. Chavarria:Concentrations of calmodulin in sperm in relation to their motility in fertile euspermic and infertile asthenozoospermic men. Int J Androl 10, 507-515 (1987)
    • (1987) Int J Androl , vol.10 , pp. 507-515
    • Martinez, R.R.1    Luna, M.2    Chavarria, M.E.3
  • 16
    • 0024149836 scopus 로고
    • Analysis of calmodulin acceptor proteins and the influence of calmodulin antagonists on human spermatozoa
    • Aitken R.J., J.S. Clarkson, M.J. Hulme, C.J. Henderson: Analysis of calmodulin acceptor proteins and the influence of calmodulin antagonists on human spermatozoa. Gamete Res. 21,93-111 (1988)
    • (1988) Gamete Res , vol.21 , pp. 93-111
    • Aitken, R.J.1    Clarkson, J.S.2    Hulme, M.J.3    Henderson, C.J.4
  • 17
    • 0029789196 scopus 로고    scopus 로고
    • Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa
    • Luconi M., C. Krausz, G. Forti, E. Baldi: Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa. Biol Reprod 55,207-216 (1996)
    • (1996) Biol Reprod , vol.55 , pp. 207-216
    • Luconi, M.1    Krausz, C.2    Forti, G.3    Baldi, E.4
  • 18
    • 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., J. Moos, X.P. Ning, G.L. Gerton, J. Tesarik, G.S. Kopf, S.B. Moss. 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 180,284-296 (1996)
    • (1996) Dev Biol , vol.180 , pp. 284-296
    • Carrera, A.1    Moos, J.2    Ning, X.P.3    Gerton, G.L.4    Tesarik, J.5    Kopf, G.S.6    Moss, S.B.7
  • 19
    • 0035027048 scopus 로고    scopus 로고
    • Impact of epididymal maturation on the tyrosine phosphorylation patterns exhibited by rat spermatozoa
    • Lewis A., R.J. Aitken: Impact of epididymal maturation on the tyrosine phosphorylation patterns exhibited by rat spermatozoa. Biol Reprod 64,1545-1556 (2001)
    • (2001) Biol Reprod , vol.64 , pp. 1545-1556
    • Lewis, A.1    Aitken, R.J.2
  • 20
    • 0025217162 scopus 로고
    • Changes in the mitochondrial calcium influx and efflux properties are responsible for the decline in sperm calcium during epididymal maturation
    • Vijayaraghavan S. and D.D. Hoskins: Changes in the mitochondrial calcium influx and efflux properties are responsible for the decline in sperm calcium during epididymal maturation. Mol Reprod Dev 25,186-194 (1990)
    • (1990) Mol Reprod Dev , vol.25 , pp. 186-194
    • Vijayaraghavan, S.1    Hoskins, D.D.2
  • 21
    • 0034922245 scopus 로고    scopus 로고
    • The motility of demembranated human spermatozoa is inhibited by free calcium ion activities of 500 nmol/L or more
    • Williams K.M. and W.C. Ford: The motility of demembranated human spermatozoa is inhibited by free calcium ion activities of 500 nmol/L or more. Int J Androl 24,216-224 (2001)
    • (2001) Int J Androl , vol.24 , pp. 216-224
    • Williams, K.M.1    Ford, W.C.2
  • 22
    • 0028326010 scopus 로고
    • Effects of cryopreservation on the intracellular calcium concentration of human spermatozoa and its response to progesterone
    • McLaughlin E.A. and W.C. Ford: Effects of cryopreservation on the intracellular calcium concentration of human spermatozoa and its response to progesterone. Mol Reprod Dev 37,241-246 (1994)
    • (1994) Mol Reprod Dev , vol.37 , pp. 241-246
    • McLaughlin, E.A.1    Ford, W.C.2
  • 24
    • 0023952125 scopus 로고
    • Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm
    • Tash J.S., M. Krinks, J. Patel, R.L. Means, C.B. Klee and A.R. Means: Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm. J Cell Biol 106,1625-1633 (1988)
    • (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
  • 25
    • 1642462435 scopus 로고    scopus 로고
    • Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation
    • Baker M.A., L. Hetherington, H. Ecroyd, S.D Roman, R.J. Aitken: Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation. J Cell Sci 117,211-222 (2004)
    • (2004) J Cell Sci , vol.117 , pp. 211-222
    • Baker, M.A.1    Hetherington, L.2    Ecroyd, H.3    Roman, S.D.4    Aitken, R.J.5
  • 26
    • 0030923852 scopus 로고    scopus 로고
    • A tyrosine-phosphorylated 55-kilodalton motility-associated bovine sperm protein is regulated by cyclic adenosine 3′,5′-monophosphates and calcium
    • Vijayaraghavan S., K.D. Trautman, S.A. Goueli and D.W. Carr: A tyrosine-phosphorylated 55-kilodalton motility-associated bovine sperm protein is regulated by cyclic adenosine 3′,5′-monophosphates and calcium. Biol Reprod 56, 1450-1457 (1997)
    • (1997) Biol Reprod , vol.56 , pp. 1450-1457
    • Vijayaraghavan, S.1    Trautman, K.D.2    Goueli, S.A.3    Carr, D.W.4
  • 27
    • 0042025019 scopus 로고    scopus 로고
    • Involvement of tyrosine kinase and cAMP-dependent kinase cross-talk in the regulation of human sperm motility
    • Bajpai M. and G.F. Doncel: Involvement of tyrosine kinase and cAMP-dependent kinase cross-talk in the regulation of human sperm motility. Reprod 126, 183-195 (2003)
    • (2003) Reprod , vol.126 , pp. 183-195
    • Bajpai, M.1    Doncel, G.F.2
  • 30
    • 0141695189 scopus 로고    scopus 로고
    • Specific order in the appearance of protein tyrosine phosphorylation patterns is functionally coordinated with dog sperm hyperactivation and capacitation
    • Petrunkina A.M., J. Friedrich, W. Drommer, G. Bicker, D. Waberski, E. Topfer-Petersen: Specific order in the appearance of protein tyrosine phosphorylation patterns is functionally coordinated with dog sperm hyperactivation and capacitation. J Androl 24,423-437 (2003)
    • (2003) J Androl , vol.24 , pp. 423-437
    • Petrunkina, A.M.1    Friedrich, J.2    Drommer, W.3    Bicker, G.4    Waberski, D.5    Topfer-Petersen, E.6
  • 31
    • 0038802713 scopus 로고    scopus 로고
    • Incidence of sperm-tail tyrosine phosphorylation and hyperactivated motility in normozoospermic and asthenozoospermic human sperm samples
    • Yunes R., G.F. Doncel, A.A. Acosta: Incidence of sperm-tail tyrosine phosphorylation and hyperactivated motility in normozoospermic and asthenozoospermic human sperm samples. Biocell 27,29-36 (2003)
    • (2003) Biocell , vol.27 , pp. 29-36
    • Yunes, R.1    Doncel, G.F.2    Acosta, A.A.3
  • 32
    • 21044434065 scopus 로고    scopus 로고
    • Capacitation-associated protein tyrosine phosphorylation and membrane fluidity changes are impaired in the spermatozoa of asthenozoospermic patients
    • Buffone M.G., J.C. Calamera, S.V. Verstraeten, G.F. Doncel: Capacitation-associated protein tyrosine phosphorylation and membrane fluidity changes are impaired in the spermatozoa of asthenozoospermic patients. Reproduction 129,697-705 (2005)
    • (2005) Reproduction , vol.129 , pp. 697-705
    • Buffone, M.G.1    Calamera, J.C.2    Verstraeten, S.V.3    Doncel, G.F.4
  • 33
    • 0347316380 scopus 로고    scopus 로고
    • Human sperm subpopulations: Relationship between functional quality and protein tyrosine phosphorylation
    • Buffone M.G., G.F. Doncel, C.I. Marin Briggiler, M.H. Vazquez-Levin, J.C. Calamera. Human sperm subpopulations: relationship between functional quality and protein tyrosine phosphorylation. Hum Reprod. 19,139-146 (2004)
    • (2004) Hum Reprod , vol.19 , pp. 139-146
    • Buffone, M.G.1    Doncel, G.F.2    Marin Briggiler, C.I.3    Vazquez-Levin, M.H.4    Calamera, J.C.5
  • 34
    • 0029792629 scopus 로고    scopus 로고
    • Cyclic adenosine 3′,5′monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility
    • Leclerc P., E. de Lamirande, C. Gagnon: Cyclic adenosine 3′,5′monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol Reprod 55,684-692 (1996)
    • (1996) Biol Reprod , vol.55 , pp. 684-692
    • Leclerc, P.1    De Lamirande, E.2    Gagnon, C.3
  • 35
    • 0036230744 scopus 로고    scopus 로고
    • Reactivation of motility of demembranated hamster spermatozoa: Role of protein tyrosine kinase and protein phosphatases
    • Patil S.B., J. Kulanand, P. Padma and S. Shivaji: Reactivation of motility of demembranated hamster spermatozoa: role of protein tyrosine kinase and protein phosphatases. Andrologia 34, 74-86 (2002)
    • (2002) Andrologia , vol.34 , pp. 74-86
    • Patil, S.B.1    Kulanand, J.2    Padma, P.3    Shivaji, S.4
  • 36
    • 0033024113 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation
    • Si Y. and M. Okuno: Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation. Biol Reprod 61,240-246 (1999)
    • (1999) Biol Reprod , vol.61 , pp. 240-246
    • Si, Y.1    Okuno, M.2
  • 37
    • 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 H.L., P.E. Visconti, G.S. Kopf: Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway. Biol Reprod 56,707-719 (1997)
    • (1997) Biol Reprod , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 38
    • 0036085646 scopus 로고    scopus 로고
    • Regulation of the human sperm tyrosine kinase c-yes. Activation by cyclic adenosine 3′,5′-monophosphate and inhibition by Ca(2+)
    • Leclerc P. and S. Goupil. Regulation of the human sperm tyrosine kinase c-yes. Activation by cyclic adenosine 3′,5′-monophosphate and inhibition by Ca(2+). Biol Reprod 67, 301-307 (2002)
    • (2002) Biol Reprod , vol.67 , pp. 301-307
    • Leclerc, P.1    Goupil, S.2
  • 39
    • 1842583980 scopus 로고    scopus 로고
    • Increased phosphorylation of AKAP by inhibition of phosphatidylinositol 3-kinase enhances human sperm motility through tail recruitment of protein kinase A
    • Luconi M., V. Carloni, F. Marra, P. Ferruzzi, G. Forti, E. Baldi: Increased phosphorylation of AKAP by inhibition of phosphatidylinositol 3-kinase enhances human sperm motility through tail recruitment of protein kinase A. J Cell Sci 117,1235-1246 (2004)
    • (2004) J Cell Sci , vol.117 , pp. 1235-1246
    • Luconi, M.1    Carloni, V.2    Marra, F.3    Ferruzzi, P.4    Forti, G.5    Baldi, E.6
  • 40
    • 10944221735 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the a kinase anchoring protein 3 (AKAP3) and soluble adenylate cyclase are involved in the increase of human sperm motility by bicarbonate
    • Luconi M., I. Porazzi, P. Ferruzzi, S. Marchiani, G. Forti, E. Baldi: Tyrosine phosphorylation of the a kinase anchoring protein 3 (AKAP3) and soluble adenylate cyclase are involved in the increase of human sperm motility by bicarbonate. Biol Reprod 72,22-32 (2005)
    • (2005) Biol Reprod , vol.72 , pp. 22-32
    • Luconi, M.1    Porazzi, I.2    Ferruzzi, P.3    Marchiani, S.4    Forti, G.5    Baldi, E.6
  • 41
    • 0031573950 scopus 로고    scopus 로고
    • Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation
    • Visconti P.E., L.R. Johnson, M. Oyaski, M. Fornes, S.B. Moss, G.L. Gerton, G.S. Kopf: Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation. Dev Biol 192,351-363 (1997)
    • (1997) Dev Biol , vol.192 , pp. 351-363
    • Visconti, P.E.1    Johnson, L.R.2    Oyaski, M.3    Fornes, M.4    Moss, S.B.5    Gerton, G.L.6    Kopf, G.S.7
  • 42
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti P.E., G.D. Moore, J.L. Bailey, P. Leclerc, S.A. Connors, D. Pan, P. Olds-Clarke, G.S. Kopf: Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121,1139-1150 (1995)
    • (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
  • 43
    • 2642516261 scopus 로고    scopus 로고
    • Phosphoiylation of the Arginine-X-X-(Serine/Threonine) motif in human sperm proteins during capacitation: Modulation and protein kinase A dependency
    • O'Flaherty C., E. de Lamirande, C. Gagnon: Phosphoiylation of the Arginine-X-X-(Serine/Threonine) motif in human sperm proteins during capacitation: modulation and protein kinase A dependency. Mol Hum Reprod 10,355-363 (2004)
    • (2004) Mol Hum Reprod , vol.10 , pp. 355-363
    • O'Flaherty, C.1    De Lamirande, E.2    Gagnon, C.3
  • 44
    • 0036041264 scopus 로고    scopus 로고
    • Targeted disruption of the Akap4 gene causes defects in sperm flagellum and motility
    • Miki K., W.D. Willis, P.R. Brown, E.H. Goulding, K.D. Fulcher, E.M. Eddy: Targeted disruption of the Akap4 gene causes defects in sperm flagellum and motility. Dev Biol 248,331-342(2002)
    • (2002) Dev Biol , vol.248 , pp. 331-342
    • Miki, K.1    Willis, W.D.2    Brown, P.R.3    Goulding, E.H.4    Fulcher, K.D.5    Eddy, E.M.6
  • 45
    • 0035110573 scopus 로고    scopus 로고
    • Molecular genetic analysis of two human sperm fibrous sheath proteins, AKAP4 and AKAP3, in men with dysplasia of the fibrous sheath
    • Turner R.M., M.P. Musse, A. Mandal, K. Klotz, F.C. Jayes, J.C. Herr, G.L. Gerton, S.B. Moss, H.E. Chemes: Molecular genetic analysis of two human sperm fibrous sheath proteins, AKAP4 and AKAP3, in men with dysplasia of the fibrous sheath. J Androl 22,302-315 (2001)
    • (2001) J Androl , vol.22 , pp. 302-315
    • Turner, R.M.1    Musse, M.P.2    Mandal, A.3    Klotz, K.4    Jayes, F.C.5    Herr, J.C.6    Gerton, G.L.7    Moss, S.B.8    Chemes, H.E.9
  • 46
    • 27144544743 scopus 로고    scopus 로고
    • Gene deletions in an infertile man with sperm fibrous sheath displasia
    • Jun 24; [Epub ahead of print]
    • Baccetti B., G. Collodel, M. Estenoz, D. Manca, E. Moretti and P. Piomboni: Gene deletions in an infertile man with sperm fibrous sheath displasia. Hum Reprod 2005 Jun 24; [Epub ahead of print]
    • (2005) Hum Reprod
    • Baccetti, B.1    Collodel, G.2    Estenoz, M.3    Manca, D.4    Moretti, E.5    Piomboni, P.6
  • 47
    • 0032830668 scopus 로고    scopus 로고
    • Infertile spermatozoa of c-ros tyrosine kinase receptor knockout mice show flagellar angulation and maturational defects in cell volume regulatory mechanisms
    • Yeung C.H., E. Sonnenberg-Riethmacher and T.G. Cooper: Infertile spermatozoa of c-ros tyrosine kinase receptor knockout mice show flagellar angulation and maturational defects in cell volume regulatory mechanisms. Biol Reprod 61,1062-1069 (1999)
    • (1999) Biol Reprod , vol.61 , pp. 1062-1069
    • Yeung, C.H.1    Sonnenberg-Riethmacher, E.2    Cooper, T.G.3
  • 48
    • 0033873778 scopus 로고    scopus 로고
    • The cause of infertility of male c-ros tyrosine kinase receptor knockout mice
    • Yeung C.H., A. Wagenfeld, E. Nieschlag, T.G. Cooper: The cause of infertility of male c-ros tyrosine kinase receptor knockout mice. Biol Reprod 63,612-618 (2000)
    • (2000) Biol Reprod , vol.63 , pp. 612-618
    • Yeung, C.H.1    Wagenfeld, A.2    Nieschlag, E.3    Cooper, T.G.4
  • 49
    • 0036082477 scopus 로고    scopus 로고
    • Sperm volume regulation: Maturational changes in fertile and infertile transgenic mice and association with kinematics and tail angulation
    • Yeung C.H., M. Anapolski, P. Sipila, A. Wagenfeld, M. Poutanen, I. Huhtaniemi, E. Nieschlag, T.G. Cooper Sperm volume regulation: maturational changes in fertile and infertile transgenic mice and association with kinematics and tail angulation. Biol Reprod 67,269-275 (2002)
    • (2002) Biol Reprod , vol.67 , pp. 269-275
    • Yeung, C.H.1    Anapolski, M.2    Sipila, P.3    Wagenfeld, A.4    Poutanen, M.5    Huhtaniemi, I.6    Nieschlag, E.7    Cooper, T.G.8
  • 51
    • 0030321545 scopus 로고    scopus 로고
    • Involvement of osmo-sensitive calcium influx in human sperm activation
    • Rossato M., F. Di Virgilio, C. Foresta: Involvement of osmo-sensitive calcium influx in human sperm activation. Mol Hum Reprod 2,903-909 (1996)
    • (1996) Mol Hum Reprod , vol.2 , pp. 903-909
    • Rossato, M.1    Di Virgilio, F.2    Foresta, C.3
  • 54
    • 21044435869 scopus 로고    scopus 로고
    • Aquaporin-1 and -9 are differentially regulated by oestrogen in the efferent ductule epithelium and initial segment of the epididymis
    • Oliveira C.A., K. Carnes, L.R. Franca, L. Hermo, R.A. Hess: Aquaporin-1 and -9 are differentially regulated by oestrogen in the efferent ductule epithelium and initial segment of the epididymis. Biol Cell 97,385-395 (2005)
    • (2005) Biol Cell , vol.97 , pp. 385-395
    • Oliveira, C.A.1    Carnes, K.2    Franca, L.R.3    Hermo, L.4    Hess, R.A.5
  • 55
    • 5444242067 scopus 로고    scopus 로고
    • Localization of aquaporin-7 in human testis and ejaculated sperm: Possible involvement in maintenance of sperm quality
    • Saito K., Y. Kageyama, Y. Okada, S. Kawakami, K. Kihara, K. Ishibashi, S. Sasaki: Localization of aquaporin-7 in human testis and ejaculated sperm: possible involvement in maintenance of sperm quality. J Urol 172,2073-2076 (2004)
    • (2004) J Urol , vol.172 , pp. 2073-2076
    • Saito, K.1    Kageyama, Y.2    Okada, Y.3    Kawakami, S.4    Kihara, K.5    Ishibashi, K.6    Sasaki, S.7
  • 56
    • 0037309210 scopus 로고    scopus 로고
    • Use of carnitine therapy in selected cases of male factor infertility: A double-blind crossover trial
    • Lenzi A., F. Lombardo, P. Sgro, P. Salacone, L. Caponecchia, F. Dondero, L. Gandini: Use of carnitine therapy in selected cases of male factor infertility: a double-blind crossover trial. Fertil Steril 79,292-300 (2003)
    • (2003) Fertil Steril , vol.79 , pp. 292-300
    • Lenzi, A.1    Lombardo, F.2    Sgro, P.3    Salacone, P.4    Caponecchia, L.5    Dondero, F.6    Gandini, L.7
  • 57
    • 13544258840 scopus 로고    scopus 로고
    • Oral carnitine supplementation increases sperm motility in asthenozoospermic men with normal sperm phospholipid hydroperoxide glutathione peroxidase levels
    • Garolla A., M. Maiorino, A. Roverato, A. Roveri, F. Ursini, C. Foresta: Oral carnitine supplementation increases sperm motility in asthenozoospermic men with normal sperm phospholipid hydroperoxide glutathione peroxidase levels. Fertil Steril 83,355-361 (2005)
    • (2005) Fertil Steril , vol.83 , pp. 355-361
    • Garolla, A.1    Maiorino, M.2    Roverato, A.3    Roveri, A.4    Ursini, F.5    Foresta, C.6
  • 58
    • 0031890532 scopus 로고    scopus 로고
    • A novel signal transduction cascade in capacitating human spermatozoa characterized by redox-regulated, c-AMP-mediated induction of tyrosine phosphorylation
    • Aitken R.J., D. Harkiss, W. Knox, M. Paterson, D.S. Irvine: A novel signal transduction cascade in capacitating human spermatozoa characterized by redox-regulated, c-AMP-mediated induction of tyrosine phosphorylation. J Cell Science 111,645-656 (1998)
    • (1998) J Cell Science , vol.111 , pp. 645-656
    • Aitken, R.J.1    Harkiss, D.2    Knox, W.3    Paterson, M.4    Irvine, D.S.5
  • 59
    • 0038269094 scopus 로고    scopus 로고
    • The human spermatozoon-not waving but drowning
    • Aitken R.J., D. Sawyer: The human spermatozoon-not waving but drowning. Adv Exp Med Biol 518,85-98 (2003)
    • (2003) Adv Exp Med Biol , vol.518 , pp. 85-98
    • Aitken, R.J.1    Sawyer, D.2
  • 60
    • 4544223127 scopus 로고    scopus 로고
    • Regulation of sperm function by reactive oxygen species
    • Ford W.C. Regulation of sperm function by reactive oxygen species. Hum Reprod Update 10,387-399 (2004)
    • (2004) Hum Reprod Update , vol.10 , pp. 387-399
    • Ford, W.C.1
  • 61
    • 17044432580 scopus 로고    scopus 로고
    • Relationship between reactive oxygen species production and lipid peroxidation in human sperm suspensions and their association with sperm function
    • Williams A.C. and W.C. Ford. Relationship between reactive oxygen species production and lipid peroxidation in human sperm suspensions and their association with sperm function. Fertil Steril 83:929-936 (2005)
    • (2005) Fertil Steril , vol.83 , pp. 929-936
    • Williams, A.C.1    Ford, W.C.2
  • 62
    • 0031751339 scopus 로고    scopus 로고
    • Is antioxidant therapy a promising strategy to improve human reproduction? Are anti-oxidants useful in the treatment of male infertility?
    • Martin-Du Pan R.C. and D. Sakkas: Is antioxidant therapy a promising strategy to improve human reproduction? Are anti-oxidants useful in the treatment of male infertility? Hum Reprod 13,2984-2985 (1998)
    • (1998) Hum Reprod , vol.13 , pp. 2984-2985
    • Martin-Du Pan, R.C.1    Sakkas, D.2
  • 63
    • 0031862054 scopus 로고    scopus 로고
    • Rationale for glutathione therapy
    • Lenzi A., L. Gandini, M.A. Picaro: Rationale for glutathione therapy. Hum Reprod 13,1419-1422 (1998)
    • (1998) Hum Reprod , vol.13 , pp. 1419-1422
    • Lenzi, A.1    Gandini, L.2    Picaro, M.A.3
  • 64
    • 1642482673 scopus 로고    scopus 로고
    • Native specific activity of glutathione peroxidase (GPx-1), phospholipid hydroperoxide glutathione peroxidase (PHGPx) and glutathione reductase (GR) does not differ between normo- and hypomotile human sperm samples
    • Tramer F., L. Caponecchia, P. Sgro, M. Martinelli, G. Sandri, E. Panfili, A. Lenzi, L. Gandini: Native specific activity of glutathione peroxidase (GPx-1), phospholipid hydroperoxide glutathione peroxidase (PHGPx) and glutathione reductase (GR) does not differ between normo- and hypomotile human sperm samples. Int J Androl 27,88-93 (2004)
    • (2004) Int J Androl , vol.27 , pp. 88-93
    • Tramer, F.1    Caponecchia, L.2    Sgro, P.3    Martinelli, M.4    Sandri, G.5    Panfili, E.6    Lenzi, A.7    Gandini, L.8
  • 65
    • 7044264971 scopus 로고    scopus 로고
    • Sperm motility in men with spinal cord injuries is enhanced by inactivating cytokines in the seminal plasma
    • Cohen D.R., S. Basu, J.M. Randall, T.C. Aballa, C.M. Lynne, N.L. Brackett: Sperm motility in men with spinal cord injuries is enhanced by inactivating cytokines in the seminal plasma. J Androl 25,922-925 (2004)
    • (2004) J Androl , vol.25 , pp. 922-925
    • Cohen, D.R.1    Basu, S.2    Randall, J.M.3    Aballa, T.C.4    Lynne, C.M.5    Brackett, N.L.6
  • 66
    • 0016691976 scopus 로고
    • The mammalian spermatozoon
    • Fawcett D.W.: The mammalian spermatozoon. Dev Biol 44,394-436 (1975)
    • (1975) Dev Biol , vol.44 , pp. 394-436
    • Fawcett, D.W.1
  • 67
    • 0025040520 scopus 로고
    • Dense fibers protect mammalian sperm against damage
    • Baltz J.M., P.O. Williams, R.A. Cone: Dense fibers protect mammalian sperm against damage. Biol Reprod 43,485-491 (1990)
    • (1990) Biol Reprod , vol.43 , pp. 485-491
    • Baltz, J.M.1    Williams, P.O.2    Cone, R.A.3
  • 68
    • 10044246306 scopus 로고    scopus 로고
    • Basal sliding and the mechanics of oscillation in a mammalian sperm flagellum
    • Vernon G.G. and D.M. Woolley: Basal sliding and the mechanics of oscillation in a mammalian sperm flagellum. Biophys J 87,3934-3944 (2004)
    • (2004) Biophys J , vol.87 , pp. 3934-3944
    • Vernon, G.G.1    Woolley, D.M.2
  • 69
    • 19944412178 scopus 로고    scopus 로고
    • Further studies on knockout mice lacking a functional dynein heavy chain (MDHC7). 2. A developmental explanation for the asthenozoospermia
    • Woolley D.M., J. Neesen, G.G. Vernon: Further studies on knockout mice lacking a functional dynein heavy chain (MDHC7). 2. A developmental explanation for the asthenozoospermia. Cell Motil Cytoskeleton 61,74-82 (2005)
    • (2005) Cell Motil Cytoskeleton , vol.61 , pp. 74-82
    • Woolley, D.M.1    Neesen, J.2    Vernon, G.G.3
  • 70
    • 0036314771 scopus 로고    scopus 로고
    • Testis-specific cytochrome c-null mice produce functional sperm but undergo early testicular atrophy
    • Narisawa S., N.B. Hecht, E. Goldberg, K.M. Boatright, J.C. Reed, J.L. Millan: Testis-specific cytochrome c-null mice produce functional sperm but undergo early testicular atrophy. Mol Cell Biol 22,5554-5562 (2002)
    • (2002) Mol Cell Biol , vol.22 , pp. 5554-5562
    • Narisawa, S.1    Hecht, N.B.2    Goldberg, E.3    Boatright, K.M.4    Reed, J.C.5    Millan, J.L.6
  • 74
    • 1842504015 scopus 로고    scopus 로고
    • Genetic regulation of cilia assembly and the relationship to human disease
    • Brody S.L.: Genetic regulation of cilia assembly and the relationship to human disease. Am J Respir Cell Mol Biol 30,435-437 (2004)
    • (2004) Am J Respir Cell Mol Biol , vol.30 , pp. 435-437
    • Brody, S.L.1
  • 75
    • 1342329609 scopus 로고    scopus 로고
    • Cilia, primary ciliary dyskinesia and molecular genetics
    • Chodhari R., H.M. Mitchison, M. Meeks: Cilia, primary ciliary dyskinesia and molecular genetics. Paediatr Respir Rev 5,69-76 (2004)
    • (2004) Paediatr Respir Rev , vol.5 , pp. 69-76
    • Chodhari, R.1    Mitchison, H.M.2    Meeks, M.3
  • 76
    • 3543070992 scopus 로고    scopus 로고
    • Ultrastructural pathology of the sperm flagellum: Association between flagellar pathology and fertility prognosis in severely asthenozoospermic men
    • Chemes H.E., S.B. Olmedo, C. Carrere, R. Oses, C. Carizza, M. Leisner, J. Blaquier: Ultrastructural pathology of the sperm flagellum: association between flagellar pathology and fertility prognosis in severely asthenozoospermic men. Hum Reprod 13,252l-2526 (1998)
    • (1998) Hum Reprod , vol.13
    • Chemes, H.E.1    Olmedo, S.B.2    Carrere, C.3    Oses, R.4    Carizza, C.5    Leisner, M.6    Blaquier, J.7
  • 77
    • 0028347862 scopus 로고
    • Effect of platelet-activating factor on motility and acrosome reaction of human spermatozoa
    • Krausz C., G. Gervasi, G. Forti, E. Baldi: Effect of platelet-activating factor on motility and acrosome reaction of human spermatozoa. Hum Reprod 9,471 -476 (1994)
    • (1994) Hum Reprod , vol.9 , pp. 471-476
    • Krausz, C.1    Gervasi, G.2    Forti, G.3    Baldi, E.4
  • 78
    • 0027375526 scopus 로고
    • Pentoxifylline actions and applications in assisted reproduction
    • Yovich L.: Pentoxifylline actions and applications in assisted reproduction. Hum Reprod 8,1786-1791 (1993)
    • (1993) Hum Reprod , vol.8 , pp. 1786-1791
    • Yovich, L.1
  • 79
    • 0028832886 scopus 로고
    • Successful use of pentoxifylline in male-factor infertility and previous failure of in vitro fertilization: A prospective randomized study
    • Rizk B., S. Fountain, S. Avery, C. Palmer, M. Blayney, M. Macnamee, C. Mills, P. Brinsden: Successful use of pentoxifylline in male-factor infertility and previous failure of in vitro fertilization: a prospective randomized study. J Assist Reprod Genet 12,710-714 (1995)
    • (1995) J Assist Reprod Genet , vol.12 , pp. 710-714
    • Rizk, B.1    Fountain, S.2    Avery, S.3    Palmer, C.4    Blayney, M.5    Macnamee, M.6    Mills, C.7    Brinsden, P.8
  • 80
    • 0029940796 scopus 로고    scopus 로고
    • The paradoxical effects of pentoxifylline on the binding of spermatozoa to the human zona pellucida
    • Paul M., J.P. Sumpter, K.S. Lindsay: The paradoxical effects of pentoxifylline on the binding of spermatozoa to the human zona pellucida. Hum Reprod 11,814-819 (1996)
    • (1996) Hum Reprod , vol.11 , pp. 814-819
    • Paul, M.1    Sumpter, J.P.2    Lindsay, K.S.3
  • 81
    • 0029030550 scopus 로고
    • Differential responses of human sperm to varying concentrations of pentoxyfylline with demonstration of toxicity
    • Centola G.M., R.J. Cartie, C. Cox: Differential responses of human sperm to varying concentrations of pentoxyfylline with demonstration of toxicity. J Androl 16,136-142 (1995)
    • (1995) J Androl , vol.16 , pp. 136-142
    • Centola, G.M.1    Cartie, R.J.2    Cox, C.3
  • 83
    • 0028564861 scopus 로고
    • Effects of pentoxifylline and progesterone on human sperm capacitation and acrosome reaction
    • Kay V.J., J.R. Coutts, L. Robertson: Effects of pentoxifylline and progesterone on human sperm capacitation and acrosome reaction. Hum Reprod 9,2318-2323 (1994)
    • (1994) Hum Reprod , vol.9 , pp. 2318-2323
    • Kay, V.J.1    Coutts, J.R.2    Robertson, L.3
  • 84
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • Wymann M.P. and L. Pirola: Structure and function of phosphoinositide 3-kinases. Biochim Biophys Acta 1436, 127-150 (1998)
    • (1998) Biochim Biophys Acta , vol.1436 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 85
    • 0842308793 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase inhibition enhances human sperm motility and sperm-zona pellucida binding
    • du Plessis S.S., D.R. Franken, E. Baldi, M. Luconi: Phosphatidylinositol 3-kinase inhibition enhances human sperm motility and sperm-zona pellucida binding. Int J Androl 27,19-26 (2004)
    • (2004) Int J Androl , vol.27 , pp. 19-26
    • Du Plessis, S.S.1    Franken, D.R.2    Baldi, E.3    Luconi, M.4
  • 88
    • 28544442352 scopus 로고    scopus 로고
    • Enhancement of sperm motility by the PI3-kinase inhibitor LY294002 does not result in toxic effect on preimplantation embryo development in the mouse
    • Luconi M., S. Torcia, D. Grillo, M.T. Fiorenza, G. Forti, F. Mangia, E. Baldi: Enhancement of sperm motility by the PI3-kinase inhibitor LY294002 does not result in toxic effect on preimplantation embryo development in the mouse. Hum Reprod (2005)
    • (2005) Hum Reprod
    • Luconi, M.1    Torcia, S.2    Grillo, D.3    Fiorenza, M.T.4    Forti, G.5    Mangia, F.6    Baldi, E.7
  • 89
    • 0036081736 scopus 로고    scopus 로고
    • Bicarbonate stimulation of boar sperm motility via a protein kinase A-dependent pathway: Between-cell and between-ejaculate differences are not due to deficiencies in protein kinase A activation
    • Holt W.W. and R.A. Harrison: Bicarbonate stimulation of boar sperm motility via a protein kinase A-dependent pathway: between-cell and between-ejaculate differences are not due to deficiencies in protein kinase A activation. J Androl 23,557-565 (2002)
    • (2002) J Androl , vol.23 , pp. 557-565
    • Holt, W.W.1    Harrison, R.A.2
  • 90
    • 0032732658 scopus 로고    scopus 로고
    • Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphoiylation
    • Osheroff J.E., P.E. Visconti, J.P. Valenzuela, A.J. Travis, J. Alvarez, G.S. Kopf: Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphoiylation. Mol Hum Reprod 5,1017-1026 (1999)
    • (1999) Mol Hum Reprod , vol.5 , pp. 1017-1026
    • Osheroff, J.E.1    Visconti, P.E.2    Valenzuela, J.P.3    Travis, A.J.4    Alvarez, J.5    Kopf, G.S.6
  • 91
    • 0034918277 scopus 로고    scopus 로고
    • Evaluation of in vitro capacitation of stallion spermatozoa
    • Rathi R., B. Colenbrander, M.M. Bevers, B.M. Gadella: Evaluation of in vitro capacitation of stallion spermatozoa. Biol Reprod 65,462-470 (2001)
    • (2001) Biol Reprod , vol.65 , pp. 462-470
    • Rathi, R.1    Colenbrander, B.2    Bevers, M.M.3    Gadella, B.M.4
  • 92
    • 0032985619 scopus 로고    scopus 로고
    • Roles of bicarbonate, cAMP, and protein tyrosine phosphorylation on capacitation and the spontaneous acrosome reaction of hamster sperm
    • Visconti P.E., J. Stewart-Savage, A. Blasco, L. Battaglia, P. Mirando, G.S. Kopf, J.G. Tezon. Roles of bicarbonate, cAMP, and protein tyrosine phosphorylation on capacitation and the spontaneous acrosome reaction of hamster sperm. Biol Reprod 61, 76-84 (1999)
    • (1999) Biol Reprod , vol.61 , pp. 76-84
    • Visconti, P.E.1    Stewart-Savage, J.2    Blasco, A.3    Battaglia, L.4    Mirando, P.5    Kopf, G.S.6    Tezon, J.G.7
  • 93
    • 0022257352 scopus 로고
    • Lowered levels of bicarbonate in seminal plasma cause the poor sperm motility in human infertile patients
    • Okamura N., Y. Tajima, A. Soejima, H. Masuda, Y. Sugita: Lowered levels of bicarbonate in seminal plasma cause the poor sperm motility in human infertile patients. J Biol Chem 260,9699-9705 (1985)
    • (1985) J Biol Chem , vol.260 , pp. 9699-9705
    • Okamura, N.1    Tajima, Y.2    Soejima, A.3    Masuda, H.4    Sugita, Y.5
  • 94
    • 0015875985 scopus 로고
    • Chemical composition of human oviduct fluid
    • David A., D.M. Serr, B. Czernobilsky: Chemical composition of human oviduct fluid Fertil Steril 24,435-439 (1973)
    • (1973) Fertil Steril , vol.24 , pp. 435-439
    • David, A.1    Serr, D.M.2    Czernobilsky, B.3
  • 95
    • 0022257352 scopus 로고
    • Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase
    • Okamura N., Y. Tajima, H. Ishikawa, S. Yoshii, K. Koiso, Y. Sugita: Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase. J Biol Chem 260, 9699-9605 (1986)
    • (1986) J Biol Chem , vol.260 , pp. 9699-19605
    • Okamura, N.1    Tajima, Y.2    Ishikawa, H.3    Yoshii, S.4    Koiso, K.5    Sugita, Y.6
  • 98
    • 0037844844 scopus 로고    scopus 로고
    • Kinetic properties of "soluble" adenylyl cyclase. Synergism between calcium and bicarbonate
    • Litvin T.N., M. Kamenetsky, A. Zarifyan, J. Buck, L.R. Levin: Kinetic Properties of "Soluble" Adenylyl Cyclase. Synergism between calcium and bicarbonate. J Biol Chem 278,15922-15926 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 15922-15926
    • Litvin, T.N.1    Kamenetsky, M.2    Zarifyan, A.3    Buck, J.4    Levin, L.R.5
  • 99
    • 0029030462 scopus 로고
    • Mouse sperm adenylyl cyclase: General properties and regulation by the zona pellucida
    • Leclerc P. and G. Kopf: Mouse sperm adenylyl cyclase: general properties and regulation by the zona pellucida. Biol Reprod 52,1227-1233 (1995)
    • (1995) Biol Reprod , vol.52 , pp. 1227-1233
    • Leclerc, P.1    Kopf, G.2
  • 100
    • 0042856454 scopus 로고    scopus 로고
    • Evidence for multiple distinctly localized adenylyl cyclase isoforms in mammalian spermatozoa
    • Baxendale R.W., L.R. Fraser: Evidence for multiple distinctly localized adenylyl cyclase isoforms in mammalian spermatozoa. Mol Reprod Dev 66,181-189 (2003)
    • (2003) Mol Reprod Dev , vol.66 , pp. 181-189
    • Baxendale, R.W.1    Fraser, L.R.2
  • 101
    • 0037386903 scopus 로고    scopus 로고
    • Cyclic AMP signalling during mammalian sperm capacitation-still largely terra Incognita
    • Harrison R.A.P.: Cyclic AMP signalling during mammalian sperm capacitation-still largely terra Incognita. Reprod Dom Anim 38,102-110 (2003)
    • (2003) Reprod Dom Anim , vol.38 , pp. 102-110
    • Harrison, R.A.P.1
  • 104
    • 0036708433 scopus 로고    scopus 로고
    • Activation of protein kinase A during human sperm capacitation and acrosome reaction
    • Lefievre L., K.N. Jha, E. De Lamirande, P.E. Visconti and C. Gagnon: Activation of protein kinase A during human sperm capacitation and acrosome reaction. J Androl 23,709-716 (2002)
    • (2002) J Androl , vol.23 , pp. 709-716
    • Lefievre, L.1    Jha, K.N.2    De Lamirande, E.3    Visconti, P.E.4    Gagnon, C.5
  • 105
    • 0003255048 scopus 로고
    • 2+-sensitive, "Soluble" adenylate cyclase in rat testis
    • 2+-sensitive, "Soluble" adenylate cyclase in rat testis. Proc Natl Acad Sci U S A 72,1097-1101 (1975)
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 1097-1101
    • Braun, T.1    Dods, R.F.2
  • 108
    • 17644378592 scopus 로고    scopus 로고
    • Inactivation of the mouse adenylyl cyclase 3 gene disrupts male fertility and spermatozoon function
    • Livera G., F. Xie, M.A. Garcia, B. Jaiswal, J. Chen, E. Law, D.R. Storm, M. Conti: Inactivation of the mouse adenylyl cyclase 3 gene disrupts male fertility and spermatozoon function. Mol Endocrinol 19,1277-1290 (2005)
    • (2005) Mol Endocrinol , vol.19 , pp. 1277-1290
    • Livera, G.1    Xie, F.2    Garcia, M.A.3    Jaiswal, B.4    Chen, J.5    Law, E.6    Storm, D.R.7    Conti, M.8
  • 109
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Eds: Knobil E, Neill J, Raven Press, NY
    • R. Yanagimachi: Mammalian fertilization. In: Physiology of Reproduction. Eds: Knobil E, Neill J, Raven Press, NY 189-317 (1994)
    • (1994) Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 110
    • 0026605225 scopus 로고
    • Hyperactivation enhances mouse sperm capacity for penetrating viscoelastic media
    • S.S. Suarez, X.H. Dai. Hyperactivation enhances mouse sperm capacity for penetrating viscoelastic media. Biol. Reprod. 46,686-691 (1992)
    • (1992) Biol Reprod , vol.46 , pp. 686-691
    • Suarez, S.S.1    Dai, X.H.2
  • 111
    • 0034769287 scopus 로고    scopus 로고
    • Hyperactivation of mammalian spermatozoa: Function and regulation
    • Ho H.C. and S.S. Suarez: Hyperactivation of mammalian spermatozoa: function and regulation. Reproduction 122,519-526 2001
    • (2001) Reproduction , vol.122 , pp. 519-526
    • Ho, H.C.1    Suarez, S.S.2
  • 112
    • 0026603162 scopus 로고
    • Hyperactivated sperm progress in the mouse oviduct
    • DeMott R.P. and S.S. Suarez: Hyperactivated sperm progress in the mouse oviduct. Biol Reprod 49,779-785 (1992)
    • (1992) Biol Reprod , vol.49 , pp. 779-785
    • DeMott, R.P.1    Suarez, S.S.2
  • 113
    • 0037291789 scopus 로고    scopus 로고
    • Selection of highly fertilization-competent bovine spermatozoa through adhesion to the Fallopian tube epithelium in vitro
    • Gualtieri R. and R. Talevi: Selection of highly fertilization-competent bovine spermatozoa through adhesion to the Fallopian tube epithelium in vitro. Reproduction 125,251-258 (2003)
    • (2003) Reproduction , vol.125 , pp. 251-258
    • Gualtieri, R.1    Talevi, R.2
  • 114
    • 0027520977 scopus 로고
    • t haplotypes in the mouse compromise sperm flagellar function
    • Olds-Clarke P. and L.R. Johnson: t haplotypes in the mouse compromise sperm flagellar function. Dev Biol 155,14-25 (1993)
    • (1993) Dev Biol , vol.155 , pp. 14-25
    • Olds-Clarke, P.1    Johnson, L.R.2
  • 115
    • 0021984948 scopus 로고
    • Linear and nonlinear mouse sperm motility patterns. A quantitative classification
    • Tessler S. and P. Olds-Clarke: Linear and nonlinear mouse sperm motility patterns. A quantitative classification. J Androl 6, 35-44 (1985)
    • (1985) J Androl , vol.6 , pp. 35-44
    • Tessler, S.1    Olds-Clarke, P.2
  • 116
    • 0031951008 scopus 로고    scopus 로고
    • Follicular fluid and human granulosa cell cultures: Influence on sperm kinetic parameters, hyperactivation, and acrosome reaction
    • Fabbri R., E. Porcu, A. Lenzi, L. Gandini, T. Marsella, C. Flamini: Follicular fluid and human granulosa cell cultures: influence on sperm kinetic parameters, hyperactivation, and acrosome reaction. Fertil Steril 69,112-117 (1998)
    • (1998) Fertil Steril , vol.69 , pp. 112-117
    • Fabbri, R.1    Porcu, E.2    Lenzi, A.3    Gandini, L.4    Marsella, T.5    Flamini, C.6
  • 117
    • 0033977123 scopus 로고    scopus 로고
    • Human oviductal cells produce a factor(s) that maintains the motility of human spermatozoa in vitro
    • Yao Y., P. Ho, W.S. Yeung: Human oviductal cells produce a factor(s) that maintains the motility of human spermatozoa in vitro. Fertil Steril 73,479-486 (2000)
    • (2000) Fertil Steril , vol.73 , pp. 479-486
    • Yao, Y.1    Ho, P.2    Yeung, W.S.3
  • 119
    • 0023742813 scopus 로고
    • Calcium regulation of flagellar curvature and swimming pattern in triton X-100-extracted rat sperm
    • Lindemann C.B., and J.S. Goltz: Calcium regulation of flagellar curvature and swimming pattern in triton X-100-extracted rat sperm. Cell Motil Cytoskeleton 10,420-431 (1988)
    • (1988) Cell Motil Cytoskeleton , vol.10 , pp. 420-431
    • Lindemann, C.B.1    Goltz, J.S.2
  • 120
    • 0037406578 scopus 로고    scopus 로고
    • Characterization of the intracellular calcium store at the base of the sperm flagellum that regulates hyperactivated motility
    • Ho H.C. and SS Suarez: Characterization of the intracellular calcium store at the base of the sperm flagellum that regulates hyperactivated motility. Biol Reprod 68,1590-1596 (2003)
    • (2003) Biol Reprod , vol.68 , pp. 1590-1596
    • Ho, H.C.1    Suarez, S.S.2
  • 122
    • 0035940492 scopus 로고    scopus 로고
    • A voltage-gated ion channel expressed specifically in spermatozoa
    • Quill T.A., D. Ren., D.E. Clapham, D.L. Garbers: A voltage-gated ion channel expressed specifically in spermatozoa. Proc Natl Acad Sci U S A. 98,12527-12531 (2001)
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12527-12531
    • Quill, T.A.1    Ren, D.2    Clapham, D.E.3    Garbers, D.L.4
  • 124
    • 0033031174 scopus 로고    scopus 로고
    • Hyperactivation of hamster sperm motility by temperature-dependent tyrosine phosphorylation of an 80-kDa protein
    • Si Y.: Hyperactivation of hamster sperm motility by temperature-dependent tyrosine phosphorylation of an 80-kDa protein. Biol Reprod 61,247-252 (1999)
    • (1999) Biol Reprod , vol.61 , pp. 247-252
    • Si, Y.1
  • 125
    • 0033624062 scopus 로고    scopus 로고
    • CASA - Practical aspects
    • Mortimer S.T.: CASA-practical aspects. J Androl 21,515-524(2000)
    • (2000) J Androl , vol.21 , pp. 515-524
    • Mortimer, S.T.1
  • 126
    • 0031712111 scopus 로고    scopus 로고
    • Effect of seminal plasma on capacitation and hyperactivation in human spermatozoa
    • Mortimer S.T., M.A. Swan, D. Mortimer: Effect of seminal plasma on capacitation and hyperactivation in human spermatozoa. Hum Reprod 13,2139-2146 (1998)
    • (1998) Hum Reprod , vol.13 , pp. 2139-2146
    • Mortimer, S.T.1    Swan, M.A.2    Mortimer, D.3
  • 127
    • 0028049432 scopus 로고
    • Sperm chemotaxis: Egg peptides control cytosolic calcium to regulate flagellar responses
    • Cook S.P., C.J. Brokaw, C.H. Muller, D.F. Babcock: Sperm chemotaxis: egg peptides control cytosolic calcium to regulate flagellar responses. Dev Biol 165,10-19(1994)
    • (1994) Dev Biol , vol.165 , pp. 10-19
    • Cook, S.P.1    Brokaw, C.J.2    Muller, C.H.3    Babcock, D.F.4
  • 128
    • 22344450118 scopus 로고    scopus 로고
    • Real-time analysis of the role of Ca(2+) in flagellar movement and motility in single sea urchin sperm
    • Wood C.D., T. Nisihigaki, T. Furuta, S.A Baba, A. Darszon: Real-time analysis of the role of Ca(2+) in flagellar movement and motility in single sea urchin sperm. J Cell Biol 169,725-731 (2005)
    • (2005) J Cell Biol , vol.169 , pp. 725-731
    • Wood, C.D.1    Nisihigaki, T.2    Furuta, T.3    Baba, S.A.4    Darszon, A.5
  • 134
    • 4544295680 scopus 로고    scopus 로고
    • Particulate adenylate cyclase plays a key role in human sperm olfactory receptor-mediated chemotaxis
    • Spehr M., K. Schwane, J.A. Riffell, J. Barbour, R.K. Zimmer, E.M. Neuhaus, H. Hart: Particulate adenylate cyclase plays a key role in human sperm olfactory receptor-mediated chemotaxis. J Biol Chem 279,40194-40203 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 40194-40203
    • Spehr, M.1    Schwane, K.2    Riffell, J.A.3    Barbour, J.4    Zimmer, R.K.5    Neuhaus, E.M.6    Hart, H.7
  • 135
    • 15844386031 scopus 로고    scopus 로고
    • Human sperm chemotaxis: Both the oocyte and its surrounding cumulus cells secrete sperm chemoattractants
    • Sun F., A. Bahat, A. Gakamsky, E. Girsh, N. Katz, L.C. Giojalas, I. Tur-Kaspa, M. Eisenbach: Human sperm chemotaxis: both the oocyte and its surrounding cumulus cells secrete sperm chemoattractants. Hum Reprod 20,761-767 (2005).
    • (2005) Hum Reprod , vol.20 , pp. 761-767
    • Sun, F.1    Bahat, A.2    Gakamsky, A.3    Girsh, E.4    Katz, N.5    Giojalas, L.C.6    Tur-Kaspa, I.7    Eisenbach, M.8
  • 136
    • 0026728767 scopus 로고
    • Precontact mammalian sperm-egg communication and role in fertilization
    • Eisenbach M., D. Ralt: Precontact mammalian sperm-egg communication and role in fertilization. Am J Physiol 262,C1095-101 (1992)
    • (1992) Am J Physiol , vol.262
    • Eisenbach, M.1    Ralt, D.2
  • 137
    • 0028845356 scopus 로고
    • Sperm capacitation in humans is transient and correlates with chemotactic responsiveness to follicular factors
    • Cohen-Dayag A., I. Tur-Kaspa, J. Dor, S. Mashiach, M. Eisenbach: Sperm capacitation in humans is transient and correlates with chemotactic responsiveness to follicular factors. Proc Natl Acad Sci U S A 92,11039-11043 (1995)
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 11039-11043
    • Cohen-Dayag, A.1    Tur-Kaspa, I.2    Dor, J.3    Mashiach, S.4    Eisenbach, M.5


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