메뉴 건너뛰기




Volumn 116, Issue 10, 2003, Pages 1981-1989

Calmodulin antagonists differentially affect capacitation-associated protein tyrosine phosphorylation of mouse sperm components

Author keywords

Calmodulin; Calmodulin antagonists; Mammalian spermatozoa; Protein tyrosine phosphorylation; Sperm capacitation; Sperm mobility

Indexed keywords

CALMIDAZOLIUM; CALMODULIN; CALMODULIN INHIBITOR; COMPOUND 48-80; N (4 AMINOBUTYL) 5 CHLORO 2 NAPSYLAMIDE; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; OPHIOBOLIN A; PROPIDIUM IODIDE; PROTEIN INHIBITOR; TYROSINE; UNCLASSIFIED DRUG;

EID: 0038106212     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00396     Document Type: Article
Times cited : (32)

References (51)
  • 1
    • 0034661419 scopus 로고    scopus 로고
    • Mammalian sperm acrosome: Formation, content, and function
    • Abou-Haila, A. and Tulsiani, D. R. P. (2000). Mammalian sperm acrosome: formation, content, and function. Arch. Biochem. Biophys. 379, 173-182.
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 173-182
    • Abou-Haila, A.1    Tulsiani, D.R.P.2
  • 2
    • 0037509718 scopus 로고    scopus 로고
    • Acrosomal glycohydrolases as markers to assess membrane priming that occurs during capacitation of mouse spermatozoa
    • Abst. #178
    • Abou-Haila, A. and Tulsiani, D. R. P. (2002). Acrosomal glycohydrolases as markers to assess membrane priming that occurs during capacitation of mouse spermatozoa. Biol. Reprod. 66 Suppl., Abst. #178.
    • (2002) Biol. Reprod. , vol.66 , Issue.SUPPL.
    • Abou-Haila, A.1    Tulsiani, D.R.P.2
  • 3
    • 76949114656 scopus 로고
    • Observation on the penetration of the sperm into the mammalian ovum
    • Austin, C. R. (1951). Observation on the penetration of the sperm into the mammalian ovum. Aust. J. Sci. Res. 4, 581-596.
    • (1951) Aust. J. Sci. Res. , vol.4 , pp. 581-596
    • Austin, C.R.1
  • 4
    • 0035370448 scopus 로고    scopus 로고
    • Calmodulin signals capacitation and triggers the agonist-induced acrosome reaction in mouse spermatozoa
    • Bendahmane, M., Lynch, C. and Tulsiani, D. R. P. (2001). Calmodulin signals capacitation and triggers the agonist-induced acrosome reaction in mouse spermatozoa. Arch. Biochem. Biophys. 390, 1-8.
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 1-8
    • Bendahmane, M.1    Lynch, C.2    Tulsiani, D.R.P.3
  • 5
    • 0036683808 scopus 로고    scopus 로고
    • Assessment of acrosomal status in rat spermatozoa: Studies on carbohydrate and non-carbohydrate agonists
    • Bendahmane, M., Zeng, H.-T. and Tulsiani, D. R. P. (2002). Assessment of acrosomal status in rat spermatozoa: studies on carbohydrate and non-carbohydrate agonists. Arch. Biochem. Biophys. 404, 38-47.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 38-47
    • Bendahmane, M.1    Zeng, H.-T.2    Tulsiani, D.R.P.3
  • 6
    • 36949091315 scopus 로고
    • Fertilizing capacity of spermatozoa deposited into the fallopian tubes
    • Chang, M. C. (1951). Fertilizing capacity of spermatozoa deposited into the fallopian tubes. Nature 168, 697-698.
    • (1951) Nature , vol.168 , pp. 697-698
    • Chang, M.C.1
  • 7
    • 0023759785 scopus 로고
    • An extracellular role for calmodulin-like activity in cell proliferation
    • Crocker, G., Dawson, R. A., Barton, C. H. and MacNeil, S. (1988). An extracellular role for calmodulin-like activity in cell proliferation. Biochem. J. 253, 877-884.
    • (1988) Biochem. J. , vol.253 , pp. 877-884
    • Crocker, G.1    Dawson, R.A.2    Barton, C.H.3    MacNeil, S.4
  • 8
    • 0031776647 scopus 로고    scopus 로고
    • Role of cholesterol in sperm capacitation
    • Cross, N. L. (1998). Role of cholesterol in sperm capacitation. Biol. Reprod. 59, 7-11.
    • (1998) Biol. Reprod. , vol.59 , pp. 7-11
    • Cross, N.L.1
  • 9
    • 0030947943 scopus 로고    scopus 로고
    • Control of human sperm intracellular pH by cholesterol and its relationship to the response of the acrosome to progesterone
    • Cross, N. L. and Razy-Faulkner, P. (1997). Control of human sperm intracellular pH by cholesterol and its relationship to the response of the acrosome to progesterone. Biol. Reprod. 56, 1169-1174.
    • (1997) Biol. Reprod. , vol.56 , pp. 1169-1174
    • Cross, N.L.1    Razy-Faulkner, P.2
  • 10
    • 0024383609 scopus 로고
    • Direct contact is required between serum albumin and hamster spermatozoa for capacitation in vitro
    • Dow, M. P. and Bavister, B. D. (1989). Direct contact is required between serum albumin and hamster spermatozoa for capacitation in vitro. Gamete Res. 23, 171-180.
    • (1989) Gamete Res. , vol.23 , pp. 171-180
    • Dow, M.P.1    Bavister, B.D.2
  • 11
    • 0021709251 scopus 로고
    • Mouse sperm capacitation in vitro involves loss of a surface-associated inhibitory component
    • Fraser, L. R. (1984). Mouse sperm capacitation in vitro involves loss of a surface-associated inhibitory component. J. Reprod. Fertil. 72, 373-384.
    • (1984) J. Reprod. Fertil. , vol.72 , pp. 373-384
    • Fraser, L.R.1
  • 12
    • 0028847426 scopus 로고
    • Cellular biology of capacitation and acrosome reaction
    • Fraser, L. R. (1995). Cellular biology of capacitation and acrosome reaction. Human Reprod. 10 Suppl. 1, 22-30.
    • (1995) Human Reprod. , vol.10 , Issue.SUPPL. 1 , pp. 22-30
    • Fraser, L.R.1
  • 13
    • 0027455026 scopus 로고
    • Calyculin A, a protein phosphatase inhibitor, enhances capacitation of human sperm
    • Furuya, S., Endo, Y., Osumi, K., Oba, M., Nozawa, S. and Suzuki, S. (1993). Calyculin A, a protein phosphatase inhibitor, enhances capacitation of human sperm. Fertil. Steril. 59, 216-222.
    • (1993) Fertil. Steril. , vol.59 , pp. 216-222
    • Furuya, S.1    Endo, Y.2    Osumi, K.3    Oba, M.4    Nozawa, S.5    Suzuki, S.6
  • 14
    • 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., Visconti, P. E. and Kopf, G. S. (1997). Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′, 5′ monophosphate-dependent pathway. Biol. Reprod. 56, 707-719.
    • (1997) Biol. Reprod. , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 15
    • 0029150135 scopus 로고
    • Viability assessment of mammalian sperm using SYBR-14 and propidium iodine
    • Garner, D. L. and Johnson, L. A. (1995). Viability assessment of mammalian sperm using SYBR-14 and propidium iodine. Biol. Reprod. 53, 276-284.
    • (1995) Biol. Reprod. , vol.53 , pp. 276-284
    • Garner, D.L.1    Johnson, L.A.2
  • 16
    • 0023258569 scopus 로고
    • Calmodulin-mediated adenylate cyclase from mammalian sperm
    • Gross, M. K., Toscano, D. G. and Toscano, W. A. (1987). Calmodulin-mediated adenylate cyclase from mammalian sperm. J. Biol. Chem. 262, 8672-8676.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8672-8676
    • Gross, M.K.1    Toscano, D.G.2    Toscano, W.A.3
  • 17
    • 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. V. and Harrison, R. A. P. (2002). 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) J. Androl. , vol.23 , pp. 557-565
    • Holt, W.V.1    Harrison, R.A.P.2
  • 18
    • 0030977015 scopus 로고    scopus 로고
    • Endothelial cells and extracellular calmodulin inhibit monocyte tumor necrosis factor release and augment neutrophil elastase release
    • Houston, D. S., Carson, C. W. and Esmon, C. T. (1997). Endothelial cells and extracellular calmodulin inhibit monocyte tumor necrosis factor release and augment neutrophil elastase release. J. Biol. Chem. 272, 11778-11785.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11778-11785
    • Houston, D.S.1    Carson, C.W.2    Esmon, C.T.3
  • 19
    • 0024517280 scopus 로고
    • Calyculin A and okadaic acid: Inhibitors of protein phosphatase activities
    • Ishihara, H., Martin, B. L. and Brautigan, D. L. (1989). Calyculin A and okadaic acid: inhibitors of protein phosphatase activities. Biochem. Biophys. Res. Commun. 159, 871-877.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 871-877
    • Ishihara, H.1    Martin, B.L.2    Brautigan, D.L.3
  • 20
    • 0028111490 scopus 로고
    • p95. the major phosphotyrosine containing protein in mouse spermatozoa is a hexokinase with unique properties
    • Kalab, P., Visconti, P., Leclerc, P. and Kopf, G. S. (1994). p95, the major phosphotyrosine containing protein in mouse spermatozoa is a hexokinase with unique properties. J. Biol. Chem. 269, 3810-3817.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3810-3817
    • Kalab, P.1    Visconti, P.2    Leclerc, P.3    Kopf, G.S.4
  • 21
    • 0000060856 scopus 로고
    • Analysis and interpretation of the forces generated by spermatozoa
    • (ed. B. Bavister, J. Cummins and E. R. S. Roldan) Norwell, MA: Serona Symposium
    • Katz, D. and Drobnis, E. (1990). Analysis and interpretation of the forces generated by spermatozoa. In Fertilization in Mammals (ed. B. Bavister, J. Cummins and E. R. S. Roldan), pp. 125-137. Norwell, MA: Serona Symposium.
    • (1990) Fertilization in Mammals , pp. 125-137
    • Katz, D.1    Drobnis, E.2
  • 22
    • 0021251345 scopus 로고
    • Characterization of a calmodulin stimulated adenylate cyclase from abalone spermatozoa
    • Kopf, G. S. and Vacquier, V. D. (1984). Characterization of a calmodulin stimulated adenylate cyclase from abalone spermatozoa. J. Biol. Chem. 259, 7590-7596.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7590-7596
    • Kopf, G.S.1    Vacquier, V.D.2
  • 24
    • 0033061672 scopus 로고    scopus 로고
    • Simple histochemical stain for acrosomes on sperm from several species
    • Larson, J. L. and Miller, D. J. (1999). Simple histochemical stain for acrosomes on sperm from several species. Mol. Reprod. Dev. 52, 445-449.
    • (1999) Mol. Reprod. Dev. , vol.52 , pp. 445-449
    • Larson, J.L.1    Miller, D.J.2
  • 25
    • 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., De-Lamirande, E. and Gagnon, C. (1996). 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) Biol. Reprod. , vol.55 , pp. 684-692
    • Leclerc, P.1    De-Lamirande, E.2    Gagnon, C.3
  • 26
    • 0023236655 scopus 로고
    • An investigation using lectins for glycocomponents of mouse spermatozoa during capacitation and spermzona binding
    • Lee, S. H. and Ahuja, K. K. (1987). An investigation using lectins for glycocomponents of mouse spermatozoa during capacitation and spermzona binding. J. Reprod. Fertil. 80, 65-74.
    • (1987) J. Reprod. Fertil. , vol.80 , pp. 65-74
    • Lee, S.H.1    Ahuja, K.K.2
  • 27
    • 0024356430 scopus 로고
    • 95 kDa sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding
    • Leyton, L. and Saling, P. (1989). 95 kDa sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding. Cell 57, 1123-1130.
    • (1989) Cell , vol.57 , pp. 1123-1130
    • Leyton, L.1    Saling, P.2
  • 28
    • 0032941207 scopus 로고    scopus 로고
    • The role of carbohydrates in the induction of the acrosome reaction in mouse spermatozoa
    • Loeser, C. R. and Tulsiani, D. R. P. (1999). The role of carbohydrates in the induction of the acrosome reaction in mouse spermatozoa. Biol. Reprod. 60, 94-101.
    • (1999) Biol. Reprod. , vol.60 , pp. 94-101
    • Loeser, C.R.1    Tulsiani, D.R.P.2
  • 29
    • 0032773060 scopus 로고    scopus 로고
    • Characterization of pharmacological-sensitivity profile of neoglycoprotein-induced acrosome reaction in mouse spermatozoa
    • Loeser, C. R., Lynch, C. and Tulsiani, D. R. P. (1999). Characterization of pharmacological-sensitivity profile of neoglycoprotein-induced acrosome reaction in mouse spermatozoa. Biol. Reprod. 61, 629-634.
    • (1999) Biol. Reprod. , vol.61 , pp. 629-634
    • Loeser, C.R.1    Lynch, C.2    Tulsiani, D.R.P.3
  • 31
    • 0000467683 scopus 로고
    • Isolation, separation, and short-term culture of spermatogenic cells
    • O'Brien, D. A. (1993). Isolation, separation, and short-term culture of spermatogenic cells. Methods Toxicol. 3A, 246-264.
    • (1993) Methods Toxicol. , vol.3 A , pp. 246-264
    • O'Brien, D.A.1
  • 32
    • 0038523622 scopus 로고
    • Variation in the quality of sperm motility and its relationship to capacitation
    • (ed. B. Bavister, J. Cummins and E. R. S. Roldan), Norwell, MA: Serona Symposium
    • Olds-Clarke, P. (1990). Variation in the quality of sperm motility and its relationship to capacitation. In Fertilization in Mammals (ed. B. Bavister, J. Cummins and E. R. S. Roldan), pp. 91-99. Norwell, MA: Serona Symposium.
    • (1990) Fertilization in Mammals , pp. 91-99
    • Olds-Clarke, P.1
  • 33
    • 0020335879 scopus 로고
    • Modification of the sperm membrane during capacitation
    • O'Rand, M. G. (1982). Modification of the sperm membrane during capacitation. Ann. N. Y. Acad. Sci. 383, 392-402.
    • (1982) Ann. N. Y. Acad. Sci. , vol.383 , pp. 392-402
    • O'Rand, M.G.1
  • 34
    • 0028061888 scopus 로고
    • Differences in the role of cyclic adenosine 3′, 5′-monophosphate during capacitation of bovine sperm by haparin or oviduct fluid
    • Parish, J. J., Susko-Parish, J. L., Uguz, C. and First, N. L. (1994). Differences in the role of cyclic adenosine 3′, 5′-monophosphate during capacitation of bovine sperm by haparin or oviduct fluid. Biol. Reprod. 51, 1099-1108.
    • (1994) Biol. Reprod. , vol.51 , pp. 1099-1108
    • Parish, J.J.1    Susko-Parish, J.L.2    Uguz, C.3    First, N.L.4
  • 35
    • 0031770660 scopus 로고    scopus 로고
    • Rat sperm plasma membrane is first expressed on plasma membrane of testicular germ cells
    • Pereira, B. M. J., Abou-Haila, A. and Tulsiani, D. R. P. (1998). Rat sperm plasma membrane is first expressed on plasma membrane of testicular germ cells. Biol. Reprod. 59, 1288-1295.
    • (1998) Biol. Reprod. , vol.59 , pp. 1288-1295
    • Pereira, B.M.J.1    Abou-Haila, A.2    Tulsiani, D.R.P.3
  • 36
    • 0033024113 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation
    • Si, Y. and Okuno, M. (1999). Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation. Biol. Reprod. 61, 240-246.
    • (1999) Biol. Reprod. , vol.61 , pp. 240-246
    • Si, Y.1    Okuno, M.2
  • 37
    • 0018142579 scopus 로고
    • Increased calcium ion influx is a component of capacitation of spermatozoa
    • Singh, J. P., Babcock, D. J. and Lardy, H. L. (1978). Increased calcium ion influx is a component of capacitation of spermatozoa. Biochem. J. 172, 549-556.
    • (1978) Biochem. J. , vol.172 , pp. 549-556
    • Singh, J.P.1    Babcock, D.J.2    Lardy, H.L.3
  • 38
    • 0029819276 scopus 로고    scopus 로고
    • Hyperactivated motility in sperm
    • Suarez, S. S. (1996). Hyperactivated motility in sperm. J. Androl. 17, 331-335.
    • (1996) J. Androl. , vol.17 , pp. 331-335
    • Suarez, S.S.1
  • 39
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some application
    • Towbin, H., Staehelin, T. and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some application. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 40
    • 0035260708 scopus 로고    scopus 로고
    • Mammalian sperm molecules that are potentially important in interaction with female genital tract and egg vestments
    • Tulsiani, D. R. P. and Abou-Haila, A. (2001). Mammalian sperm molecules that are potentially important in interaction with female genital tract and egg vestments. Zygote 9, 51-69.
    • (2001) Zygote , vol.9 , pp. 51-69
    • Tulsiani, D.R.P.1    Abou-Haila, A.2
  • 41
    • 0028900312 scopus 로고
    • Rat sperm plasma membrane mannosidase: Localization and evidence for proteolytic processing during epididymal maturation
    • Tulsiani, D. R. P., NagDas, S. K., Skudlarek, M. D. and Orgebin-Crist, M.-C. (1995). Rat sperm plasma membrane mannosidase: localization and evidence for proteolytic processing during epididymal maturation. Dev. Biol. 167, 584-595.
    • (1995) Dev. Biol. , vol.167 , pp. 584-595
    • Tulsiani, D.R.P.1    NagDas, S.K.2    Skudlarek, M.D.3    Orgebin-Crist, M.-C.4
  • 42
    • 0030872253 scopus 로고    scopus 로고
    • Mammalian fertilization: A carbohydrate-mediated event
    • Tulsiani, D. R. P., Yoshida-Komiya, H. and Araki, Y. (1997). Mammalian fertilization: A carbohydrate-mediated event. Biol. Reprod. 57, 487-494.
    • (1997) Biol. Reprod. , vol.57 , pp. 487-494
    • Tulsiani, D.R.P.1    Yoshida-Komiya, H.2    Araki, Y.3
  • 43
    • 0031826659 scopus 로고    scopus 로고
    • The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization
    • Tulsiani, D. R. P., Abou-Haila, A., Loeser, C. R. and Pereira, B. M. J. (1998). The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Exp. Cell Res. 240, 151-164.
    • (1998) Exp. Cell Res. , vol.240 , pp. 151-164
    • Tulsiani, D.R.P.1    Abou-Haila, A.2    Loeser, C.R.3    Pereira, B.M.J.4
  • 44
    • 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., Trautman, K. D., Goueli, S. A. and Carr, D. W. (1997). 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) Biol. Reprod. , vol.56 , pp. 1450-1457
    • Vijayaraghavan, S.1    Trautman, K.D.2    Goueli, S.A.3    Carr, D.W.4
  • 45
    • 0031778295 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation during capacitation
    • Visconti, P. E. and Kopf, G. S. (1998). Regulation of protein phosphorylation during capacitation. Biol. Reprod. 59, 1-6.
    • (1998) Biol. Reprod. , vol.59 , pp. 1-6
    • Visconti, P.E.1    Kopf, G.S.2
  • 46
    • 0028957362 scopus 로고
    • Capaciation of mouse spermatozoa. I. Correlation between the capacitation state and protein phosphorylation
    • Visconti, P. E., Bailey, J. L., Moore, G. D., Olds-Clarke, P. and Kopf, G. S. (1995a). Capaciation of mouse spermatozoa. I. Correlation between the capacitation state and protein phosphorylation. Development 121, 1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Olds-Clarke, P.4    Kopf, G.S.5
  • 47
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti, P. E., Moore, G. D., Bailey, J. L., Leclerc, P., Connors, S. A., Pan, D., Olds-Clarke, P. and Kopf, G. S. (1995b). Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 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
  • 49
    • 0014866677 scopus 로고
    • The movement of golden hamster spermatozoa before and after capacitation
    • Yanagimachi, R. (1970). The movement of golden hamster spermatozoa before and after capacitation. J. Reprod. Fertil. 23, 193-196.
    • (1970) J. Reprod. Fertil. , vol.23 , pp. 193-196
    • Yanagimachi, R.1
  • 50
    • 0002302562 scopus 로고
    • Mammalian Fertilization
    • (ed. E. Knobil and J. D. Neill), New York: Raven Press
    • Yanagimachi, R. (1994). Mammalian Fertilization. In The Physiology of Reproduction (ed. E. Knobil and J. D. Neill), pp. 189-317. New York: Raven Press.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 51
    • 1542677515 scopus 로고
    • Sperm ascent through the oviduct of the hamster and rabbit in relation to the time of ovulation
    • Yanagimachi, R. and Chang, M. C. (1963). Sperm ascent through the oviduct of the hamster and rabbit in relation to the time of ovulation. J. Reprod. Fertil. 6, 281-282.
    • (1963) J. Reprod. Fertil. , vol.6 , pp. 281-282
    • Yanagimachi, R.1    Chang, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.