메뉴 건너뛰기




Volumn 14, Issue 6, 2012, Pages 816-821

Mechanism of sperm capacitation and the acrosome reaction: Role of protein kinases

Author keywords

acrosome reaction; AR; gelsolin; PI3K; PIP2; PKA; PKC ; sperm capacitation

Indexed keywords

ACTIN; ADENYLATE CYCLASE; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; F ACTIN; GELSOLIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE; PROTEIN KINASE; PROTEIN KINASE C ALPHA; PROTEIN KINASE P60;

EID: 84869043390     PISSN: 1008682X     EISSN: 17457262     Source Type: Journal    
DOI: 10.1038/aja.2012.81     Document Type: Review
Times cited : (198)

References (104)
  • 1
    • 84884102082 scopus 로고    scopus 로고
    • Dertilization in mammals
    • Neill JD, editor. San Diego, CA Elsevier
    • Florman HM, Ducibella T. Dertilization in mammals. In: Neill JD, editor. Physiology of Reproduction. San Diego, CA: Elsevier; 2006. p55-112.
    • (2006) Physiology of Reproduction , pp. 55-112
    • Florman, H.M.1    Ducibella, T.2
  • 2
    • 84926965205 scopus 로고    scopus 로고
    • Regulation of capacitation
    • de Jonge CJ, Barratt C, editors. Cambridge: Cambridge University Press
    • Gadella BM, Visconti A. Regulation of capacitation. In: de Jonge CJ, Barratt C, editors. The Sperm Cell. Cambridge: Cambridge University Press; 2006. p134-69.
    • (2006) The Sperm Cell , pp. 134-169
    • Gadella, B.M.1    Visconti, A.2
  • 3
    • 76949114656 scopus 로고
    • Observations on the penetration of the sperm into the mammalian egg
    • Austin CR. Observations on the penetration of the sperm into the mammalian egg. Aust J Sci Res B 1951; 4: 581-96.
    • (1951) Aust J Sci Res B , vol.4 , pp. 581-596
    • Austin, C.R.1
  • 4
    • 36949091315 scopus 로고
    • Fertilization capacity of spermatozoa deposited in fallopian tubes
    • Chang MC. Fertilization capacity of spermatozoa deposited in fallopian tubes. Nature 1951; 168: 697-8.
    • (1951) Nature , vol.168 , pp. 697-698
    • Chang, M.C.1
  • 5
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neil JD, editors, New York: Raven Press
    • Yanagimachi R. Mammalian fertilization. In: Knobil E, Neil JD, editors. The Physiology of Reproduction. New York: Raven Press; 1994. p189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 6
    • 34249816501 scopus 로고    scopus 로고
    • Sperm phospholipases and acrosomal exocytosis
    • DOI 10.2741/2050
    • Roldan ER, Shi QX. Sperm phospholipases and acrosomal exocytosis. Front Biosci 2007; 12: 89-104. (Pubitemid 46852829)
    • (2007) Frontiers in Bioscience , vol.12 , Issue.1 , pp. 89-104
    • Roldan, E.R.S.1    Shi, Q.X.2
  • 8
    • 1542542704 scopus 로고    scopus 로고
    • Signaling pathways in sperm capacitation and acrosome reaction
    • Breitbart H. Signaling pathways in sperm capacitation and acrosome reaction. Cell Mol Biol 2003; 49: 321-7.
    • (2003) Cell Mol Biol , vol.49 , pp. 321-327
    • Breitbart, H.1
  • 10
    • 54249087642 scopus 로고    scopus 로고
    • Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation
    • Arcelay E, Salicioni AM, Wertheimer E, Visconti PE. Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation. Int J Dev Biol 2008; 52: 463-72.
    • (2008) Int J Dev Biol , vol.52 , pp. 463-472
    • Arcelay, E.1    Salicioni, A.M.2    Wertheimer, E.3    Visconti, P.E.4
  • 11
    • 58849163274 scopus 로고    scopus 로고
    • Understanding the molecular basis of sperm capacitation through kinase design
    • Visconti PE. Understanding the molecular basis of sperm capacitation through kinase design. Proc Natl Acad Sci USA 2009; 106: 667-8.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 667-668
    • Visconti, P.E.1
  • 12
    • 0034321639 scopus 로고    scopus 로고
    • Intracellular events and signaling pathways involved in sperm acquisition of fertilizing capacity and acrosome reaction
    • Baldi E, Luconi M, Bonaccorsi L, Muratori M, Forti G. Intracellular events and signaling pathways involved in sperm acquisition of fertilizing capacity and acrosome reaction. Front Biosci 2000; 5: E110-23.
    • (2000) Front Biosci , vol.5
    • Baldi, E.1    Luconi, M.2    Bonaccorsi, L.3    Muratori, M.4    Forti, G.5
  • 14
    • 0034614490 scopus 로고    scopus 로고
    • Signaling -2000 and beyond
    • Hunter T. Signaling - 2000 and beyond. Cell 2000; 100: 113-27.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 15
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • DOI 10.1016/S0092-8674(03)01077-8
    • Pawson T. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 2004; 116: 191-203. (Pubitemid 38167312)
    • (2004) Cell , vol.116 , Issue.2 , pp. 191-203
    • Pawson, T.1
  • 17
    • 38049009064 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of a 38-kDa capacitation-associated buffalo (Bubalus bubalis) sperm protein is induced by L-arginine and regulated through a cAMP/PKA-independent pathway
    • Roy SC, Atreja SK. Tyrosine phosphorylation of a 38-kDa capacitation-associated buffalo (Bubalus bubalis) sperm protein is induced by L-arginine and regulated through a cAMP/PKA-independent pathway. Int J Androl 2008; 31: 12-24.
    • (2008) Int J Androl , vol.31 , pp. 12-24
    • Roy, S.C.1    Atreja, S.K.2
  • 18
    • 43849094777 scopus 로고    scopus 로고
    • Effect of reactive oxygen species on capacitation and associated protein tyrosine phosphorylation in buffalo (Bubalus bubalis) spermatozoa
    • DOI 10.1016/j.anireprosci.2007.06.024, PII S0378432007002370
    • Roy SC, Atreja SK. Effect of reactive oxygen species on capacitation and associated protein tyrosine phosphorylation in buffalo (Bubalus bubalis) spermatozoa. Anim Reprod Sci 2008; 107: 68-84. (Pubitemid 351698078)
    • (2008) Animal Reproduction Science , vol.107 , Issue.1-2 , pp. 68-84
    • Roy, S.C.1    Atreja, S.K.2
  • 19
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P et al. Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 1995; 121: 1129-37.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5
  • 20
    • 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 et al. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 1995; 121: 1139-50.
    • (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
  • 21
    • 84863838423 scopus 로고    scopus 로고
    • Kinases phosphatases and proteases during sperm capacitation
    • E-pub Ahead Of Print 20 March, doi:10. 007/ s00441-012-1370-3
    • Signorelli J, Diaz ES, Morales P. Kinases, phosphatases and proteases during sperm capacitation. Cell Tissue Res; e-pub ahead of print 20 March 2012; doi:10. 007/ s00441-012-1370-3.
    • (2012) Cell Tissue Res
    • Signorelli, J.1    Diaz, E.S.2    Morales, P.3
  • 22
    • 78751702598 scopus 로고    scopus 로고
    • Identification of capacitation associated tyrosine phosphoproteins in buffalo (Bubalus bubalis) and cattle spermatozoa
    • Jagan Mohanarao G, Atreja SK. Identification of capacitation associated tyrosine phosphoproteins in buffalo (Bubalus bubalis) and cattle spermatozoa. Anim Reprod Sci 2011; 123: 40-7.
    • (2011) Anim Reprod Sci , vol.123 , pp. 40-47
    • Jagan Mohanarao, G.1    Atreja, S.K.2
  • 25
    • 0031942980 scopus 로고    scopus 로고
    • Progesterone stimulates p42 extracellular signal-regulated kinase (p42(erk)) in human spermatozoa
    • DOI 10.1093/molehr/4.3.251
    • Luconi M, Krausz C, Barni T, Vannelli GB, Forti G et al. Progesterone stimulates p42 extracellular signal-regulated kinase (p42erk) in human spermatozoa. Mol Hum Reprod 1998; 4: 251-8. (Pubitemid 28172591)
    • (1998) Molecular Human Reproduction , vol.4 , Issue.3 , pp. 251-258
    • Luconi, M.1    Krausz, C.2    Barni, T.3    Vannelli, G.B.4    Forti, G.5    Baldi, E.6
  • 28
    • 0034083188 scopus 로고    scopus 로고
    • The capacitating agent bicarbonate induces protein kinase A-dependent changes in phospholipid transbilayer behavior in the sperm plasma membrane
    • Gadella BM, Harrison RA. The capacitating agent bicarbonate induces protein kinase A-dependent changes in phospholipid transbilayer behavior in the sperm plasma membrane. Development 2000; 127: 2407-20. (Pubitemid 30386579)
    • (2000) Development , vol.127 , Issue.11 , pp. 2407-2420
    • Gadella, B.M.1    Harrison, R.A.P.2
  • 29
    • 0037383776 scopus 로고    scopus 로고
    • 2+-channel responses: Initial events in sperm activation
    • DOI 10.1242/dev.00353
    • Wennemuth G, Carlson AE, Harper AJ, Babcock DF. Bicarbonate actions on flagellar and Ca21-channel responses: initial events in sperm activation. Development 2003; 130: 1317-26. (Pubitemid 36410780)
    • (2003) Development , vol.130 , Issue.7 , pp. 1317-1326
    • Wennemuth, G.1    Carlson, A.E.2    Harper, A.J.3    Babcock, D.F.4
  • 30
    • 0022257352 scopus 로고
    • Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase
    • Okamura N, Tajima Y, Soejima A, Masuda H, Sugita Y. Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase. J Biol Chem 1985; 260: 9699-705. (Pubitemid 15013027)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.17 , pp. 9699-9705
    • Okamura, N.1    Tajima, Y.2    Soejima, A.3
  • 31
    • 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 WV, Harrison RA. 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 2002; 23: 557-65. (Pubitemid 34655090)
    • (2002) Journal of Andrology , vol.23 , Issue.4 , pp. 557-565
    • Holt, W.V.1    Harrison, R.A.P.2
  • 32
    • 0042025019 scopus 로고    scopus 로고
    • Involvement of tyrosine kinase and cAMP-dependent kinase cross-talk in the regulation of human sperm motility
    • Bajpai M, Doncel GF. Involvement of tyrosine kinase and cAMP-dependent kinase cross-talk in the regulation of human sperm motility. Reproduction 2003; 126: 183-95. (Pubitemid 36987164)
    • (2003) Reproduction , vol.126 , Issue.2 , pp. 183-195
    • Bajpai, M.1    Doncel, G.F.2
  • 33
    • 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
    • DOI 10.1095/biolreprod.104.032490
    • Luconi M, Porazzi I, Ferruzzi P, Marchiani S, Forti G et al. 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 2005; 72: 22- 32. (Pubitemid 40013750)
    • (2005) Biology of Reproduction , vol.72 , Issue.1 , pp. 22-32
    • Luconi, M.1    Porazzi, I.2    Ferruzzi, P.3    Marchiani, S.4    Forti, G.5    Baldi, E.6
  • 35
    • 56749175434 scopus 로고    scopus 로고
    • Src activation triggers capacitation and acrosome reaction but not motility in human spermatozoa
    • Varano G, Lombardi A, Cantini G, Forti G, Baldi E et al. Src activation triggers capacitation and acrosome reaction but not motility in human spermatozoa. Hum Reprod 2008; 23: 2652-62.
    • (2008) Hum Reprod , vol.23 , pp. 2652-2662
    • Varano, G.1    Lombardi, A.2    Cantini, G.3    Forti, G.4    Baldi, E.5
  • 36
    • 53349143708 scopus 로고    scopus 로고
    • Increased activity of the human sperm tyrosine kinase SRC by the cAMP-dependent pathway in the presence of calcium
    • Lawson C, Goupil S, Leclerc P. Increased activity of the human sperm tyrosine kinase SRC by the cAMP-dependent pathway in the presence of calcium.Biol Reprod 2008; 79: 657-66.
    • (2008) Biol Reprod , vol.79 , pp. 657-666
    • Lawson, C.1    Goupil, S.2    Leclerc, P.3
  • 37
    • 43049102422 scopus 로고    scopus 로고
    • Investigation of the role of SRC in capacitation-associated tyrosine phosphorylation of human spermatozoa
    • DOI 10.1093/molehr/gan007
    • Mitchell LA, Nixon B, Baker MA, Aitken RJ. Investigation of the role of SRC in capacitation-associated tyrosine phosphorylation of human spermatozoa. Mol Hum Reprod 2008; 14: 235-43. (Pubitemid 351627293)
    • (2008) Molecular Human Reproduction , vol.14 , Issue.4 , pp. 235-243
    • Mitchel, L.A.1    Nixon, B.2    Baker, M.A.3    Aitken, R.J.4
  • 38
    • 34547445125 scopus 로고    scopus 로고
    • Role of PI3-kinase and PI4-kinase in actin polymerization during bovine sperm capacitation
    • DOI 10.1095/biolreprod.106.056705
    • Etkovitz N, Rubinstein S, Daniel L, Breitbart H. Role of PI3-kinase and PI4-kinase in actin polymerization during bovine sperm capacitation.Biol Reprod 2007; 77: 263- 73. (Pubitemid 47173608)
    • (2007) Biology of Reproduction , vol.77 , Issue.2 , pp. 263-273
    • Etkovitz, N.1    Rubinstein, S.2    Daniel, L.3    Breitbart, H.4
  • 39
    • 0028023078 scopus 로고
    • Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain
    • Becker W, Kentrup H, Klumpp S, Schultz JE, Joost HG. Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain. J Biol Chem 1994; 269: 22586-92. (Pubitemid 24273364)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.36 , pp. 22586-22592
    • Becker, W.1    Kentrup, H.2    Klumpp, S.3    Schultz, J.E.4    Joost, H.G.5
  • 40
    • 33748374699 scopus 로고    scopus 로고
    • Identification of the proteins present in the bull sperm cytosolic fraction enriched in tyrosine kinase activity: A proteomic approach
    • DOI 10.1002/pmic.200500578
    • Lalancette C, Faure RL, Leclerc P. Identification of the proteins present in the bull sperm cytosolic fraction enriched in tyrosine kinase activity: a proteomic approach. Proteomics 2006; 6: 4523-40. (Pubitemid 44336969)
    • (2006) Proteomics , vol.6 , Issue.16 , pp. 4523-4540
    • Lalancette, C.1    Faure, R.L.2    Leclerc, P.3
  • 41
    • 33748316506 scopus 로고    scopus 로고
    • Identification of SRC as a key PKA-stimulated tyrosine kinase involved in the capacitation-associated hyperactivation of murine spermatozoa
    • DOI 10.1242/jcs.03055
    • Baker MA, Hetherington L, Aitken RJ. Identification of SRC as a key PKA-stimulated tyrosine kinase involved in the capacitation-associated hyperactivation of murine spermatozoa. J Cell Sci 2006; 119: 3182-92. (Pubitemid 44322132)
    • (2006) Journal of Cell Science , vol.119 , Issue.15 , pp. 3182-3192
    • Baker, M.A.1    Hetherington, L.2    Aitken, R.J.3
  • 42
    • 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, Gagnon C. Cyclic adenosine 39,59monophosphatedependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol Reprod 1996; 55: 684-92. (Pubitemid 26295070)
    • (1996) Biology of Reproduction , vol.55 , Issue.3 , pp. 684-692
    • Leclerc, P.1    De Lamirande, E.2    Gagnon, C.3
  • 43
    • 33645300734 scopus 로고    scopus 로고
    • Tyrosine phosphorylation on capacitated human sperm tail detected by immunofluorescence correlates strongly with sperm-zona pellucida (ZP) binding but not with the ZP-induced acrosome reaction
    • Liu DY, Clarke GN, Baker HW. Tyrosine phosphorylation on capacitated human sperm tail detected by immunofluorescence correlates strongly with sperm-zona pellucida (ZP) binding but not with the ZP-induced acrosome reaction. Hum Reprod 2006; 21: 1002-8.
    • (2006) Hum Reprod , vol.21 , pp. 1002-1008
    • Liu, D.Y.1    Clarke, G.N.2    Baker, H.W.3
  • 44
    • 70349479565 scopus 로고    scopus 로고
    • High cholesterol content and decreased membrane fluidity in human spermatozoa are associated with protein tyrosine phosphorylation and functional deficiencies
    • Buffone MG, Verstraeten SV, Calamera JC, Doncel GF. High cholesterol content and decreased membrane fluidity in human spermatozoa are associated with protein tyrosine phosphorylation and functional deficiencies. J Androl 2009; 30: 552-8.
    • (2009) J Androl , vol.30 , pp. 552-558
    • Buffone, M.G.1    Verstraeten, S.V.2    Calamera, J.C.3    Doncel, G.F.4
  • 48
    • 36549022192 scopus 로고    scopus 로고
    • 2+ acts upstream of adenylyl cyclase SACY in the bicarbonate signaled activation of sperm motility
    • DOI 10.1016/j.ydbio.2007.09.017, PII S0012160607013528
    • Carlson AE, Hille B, Babcock DF. External Ca21 acts upstream of adenylyl cyclase SACY in the bicarbonate signaled activation of sperm motility. Dev Biol 2007; 312: 183-92. (Pubitemid 350180751)
    • (2007) Developmental Biology , vol.312 , Issue.1 , pp. 183-192
    • Carlson, A.E.1    Hille, B.2    Babcock, D.F.3
  • 49
    • 80051942437 scopus 로고    scopus 로고
    • Light-mediated activation reveals a key role for protein kinase A and sarcoma protein kinase in the development of sperm hyper-activated motility
    • Shahar S, Wiser A, Ickowicz D, Lubart R, Shulman A et al. Light-mediated activation reveals a key role for protein kinase A and sarcoma protein kinase in the development of sperm hyper-activated motility. Hum Reprod 2011; 26: 2274-82.
    • (2011) Hum Reprod , vol.26 , pp. 2274-2282
    • Shahar, S.1    Wiser, A.2    Ickowicz, D.3    Lubart, R.4    Shulman, A.5
  • 50
    • 0027164363 scopus 로고
    • Human sperm hyperactivation in whole semen and its association with low superoxide scavenging capacity in seminal plasma
    • de Lamirande E, Gagnon C. Human sperm hyperactivation in whole semen and its association with low superoxide scavenging capacity in seminal plasma. Fertil Steril 1993; 59: 1291-5. (Pubitemid 23163207)
    • (1993) Fertility and Sterility , vol.59 , Issue.6 , pp. 1291-1295
    • De Lamirande, E.1    Gagnon, C.2
  • 51
    • 79958214547 scopus 로고    scopus 로고
    • Classification of mouse sperm motility patterns using an automated multiclass support vector machines model
    • Goodson SG, Zhang Z, Tsuruta JK, Wang W, O'Brien DA. Classification of mouse sperm motility patterns using an automated multiclass support vector machines model. Biol Reprod 2011; 84: 1207-15.
    • (2011) Biol Reprod , vol.84 , pp. 1207-1215
    • Goodson, S.G.1    Zhang, Z.2    Tsuruta, J.K.3    Wang, W.4    O'Brien, D.A.5
  • 52
    • 0025325129 scopus 로고
    • Kinematics of human spermatozoa incubated under capacitating conditions
    • Mortimer ST, Mortimer D. Kinematics of human spermatozoa incubated under capacitating conditions. J Androl 1990; 11: 195-203. (Pubitemid 20186273)
    • (1990) Journal of Andrology , vol.11 , Issue.3 , pp. 195-203
    • Mortimer, S.T.1    Mortimer, D.2
  • 53
    • 0026603162 scopus 로고
    • Hyperactivated sperm progress in the mouse oviduct
    • Demott RP, Suarez SS. Hyperactivated sperm progress in the mouse oviduct. Biol Reprod 1992; 46: 779-85.
    • (1992) Biol Reprod , vol.46 , pp. 779-785
    • Demott, R.P.1    Suarez, S.S.2
  • 54
    • 0018850738 scopus 로고
    • Movement characteristics of hamster spermatozoa within the oviduct
    • DOI 10.1095/biolreprod22.4.759
    • Katz DF, Yanagimachi R. Movement characteristics of hamster spermatozoa within the oviduct. Biol Reprod 1980; 22: 759-64. (Pubitemid 10055072)
    • (1980) Biology of Reproduction , vol.22 , Issue.4 , pp. 759-764
    • Katz, D.F.1    Yanagimachi, R.2
  • 55
    • 0023440624 scopus 로고
    • Hyperactivated motility induced in mouse sperm by calcium ionophore A23187 is reversible
    • Suarez SS, Vincenti L, Ceglia MW. Hyperactivated motility induced in mouse sperm by calcium ionophore A23187 is reversible. J Exp Zool 1987; 244: 331-6.
    • (1987) J Exp Zool , vol.244 , pp. 331-336
    • Suarez, S.S.1    Vincenti, L.2    Ceglia, M.W.3
  • 56
    • 0034769287 scopus 로고    scopus 로고
    • Hyperactivation of mammalian spermatozoa: Function and regulation
    • Ho HC, Suarez SS. Hyperactivation of mammalian spermatozoa: function and regulation. Reproduction 2001; 122: 519-26. (Pubitemid 32975958)
    • (2001) Reproduction , vol.122 , Issue.4 , pp. 519-526
    • Ho, H.-C.1    Suarez, S.S.2
  • 57
    • 0028852115 scopus 로고
    • Sperm motility hyperactivation facilitates penetration of the hamster zona pellucida
    • Stauss CR, Votta TJ, Suarez SS. Sperm motility hyperactivation facilitates penetration of the hamster zona pellucida. Biol Reprod 1995; 53: 1280-5.
    • (1995) Biol Reprod , vol.53 , pp. 1280-1285
    • Stauss, C.R.1    Votta, T.J.2    Suarez, S.S.3
  • 59
    • 0025144748 scopus 로고
    • Protein kinase C is present in human sperm: Possible role in flagellar motility
    • Rotem R, Paz GF, Homonnai ZT, Kalina M, Naor Z. Protein kinase C is present in human sperm: possible role in flagellar motility. Proc Natl Acad Sci USA 1990; 87: 7305-8.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7305-7308
    • Rotem, R.1    Paz, G.F.2    Homonnai, Z.T.3    Kalina, M.4    Naor, Z.5
  • 60
    • 0023694768 scopus 로고
    • Absence of active protein kinase C in ram spermatozoa
    • Roldan ERS, Harrison RAP. Absence of active protein kinase C in ram spermatozoa. Biochem Biophys Res Commun 1988; 155: 901-6.
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 901-906
    • Ers, R.1    Harrison, R.A.P.2
  • 61
    • 0026583924 scopus 로고
    • Role of protein kinase C in the acrosome reaction of mammalian spermatozoa
    • Breitbart H, Lax Y, Rotem R, Naor Z. Role of protein kinase C in the acrosome reaction of mammalian spermatozoa. Biochem J 1992; 281: 473-6.
    • (1992) Biochem J , vol.281 , pp. 473-476
    • Breitbart, H.1    Lax, Y.2    Rotem, R.3    Naor, Z.4
  • 62
    • 0031453259 scopus 로고    scopus 로고
    • Protein kinase C and mammalian spermatozoa acrosome reaction
    • Naor Z, Breitbart H. Protein kinase C and mammalian spermatozoa acrosome reaction. TEM 1997; 8: 337-42.
    • (1997) TEM , vol.8 , pp. 337-342
    • Naor, Z.1    Breitbart, H.2
  • 63
    • 73249141210 scopus 로고    scopus 로고
    • Involvement of the PKC family in regulation of early development
    • Kalive M, Faust JJ, Koeneman BA, Capco DG. Involvement of the PKC family in regulation of early development. Mol Reprod Dev 2010; 77: 95-104.
    • (2010) Mol Reprod Dev , vol.77 , pp. 95-104
    • Kalive, M.1    Faust, J.J.2    Koeneman, B.A.3    Capco, D.G.4
  • 64
    • 33750330749 scopus 로고    scopus 로고
    • Inhibition of protein kinase C ζ blocks the attachment of stable microtubules to kinetochores leading to abnormal chromosome alignment
    • DOI 10.1016/j.cellsig.2006.05.017, PII S0898656806001185
    • Liu XF, Xie X, Miki T. Inhibition of protein kinase C zeta blocks the attachment of stable microtubules to kinetochores leading to abnormal chromosome alignment. Cell Signal 2006; 18: 2314-23. (Pubitemid 44636172)
    • (2006) Cellular Signalling , vol.18 , Issue.12 , pp. 2314-2323
    • Liu, X.F.1    Xie, X.2    Miki, T.3
  • 65
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function and regulation
    • Newton AC. Protein kinase C: structure, function and regulation. J Biol Chem 1995; 270: 28495-8.
    • (1995) J Biol Chem , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 66
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992; 258: 607-14.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 67
    • 0016132946 scopus 로고
    • Calcium dependence of the acrosome reaction and activation of the guinea pig spermatozoa
    • Yanagimachi R, Usui N. Calcium dependence of the acrosome reaction and activation of the guinea pig spermatozoa. Exp Cell Res 1974; 89: 161-74.
    • (1974) Exp Cell Res , vol.89 , pp. 161-174
    • Yanagimachi, R.1    Usui, N.2
  • 68
    • 0024366051 scopus 로고
    • An adhesion-associated agonist from the zona pellucida activates G protein-promoted elevations of internal Ca21 and pH that mediate mammalian sperm acrosomal exocytosis
    • Florman HM, Tombes RM, First NL, Babcock DF. An adhesion-associated agonist from the zona pellucida activates G protein-promoted elevations of internal Ca21 and pH that mediate mammalian sperm acrosomal exocytosis. Dev Biol 1989; 35: 133-49.
    • (1989) Dev Biol , vol.35 , pp. 133-149
    • Florman, H.M.1    Tombes, R.M.2    First, N.L.3    Babcock, D.F.4
  • 69
    • 0026481998 scopus 로고
    • Ca21-independent induction of acrosome reaction by protein kinase C in human sperm
    • Rotem R, Paz GF, Homonnai ZT, Kalina M, Lax Y et al. Ca21-independent induction of acrosome reaction by protein kinase C in human sperm. Endocrinology 1992; 131: 2235-43.
    • (1992) Endocrinology , vol.131 , pp. 2235-2243
    • Rotem, R.1    Paz, G.F.2    Homonnai, Z.T.3    Kalina, M.4    Lax, Y.5
  • 70
    • 78650039249 scopus 로고    scopus 로고
    • Role and regulation of sperm gelsolin prior to fertilization
    • Finkelstein M, Etkovitz N, Breitbart H. Role and regulation of sperm gelsolin prior to fertilization. J Biol Chem 2010; 285: 39702-9.
    • (2010) J Biol Chem , vol.285 , pp. 39702-39709
    • Finkelstein, M.1    Etkovitz, N.2    Breitbart, H.3
  • 71
    • 1242272860 scopus 로고    scopus 로고
    • Crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation
    • DOI 10.1016/j.ydbio.2003.10.034
    • Cohen G, Rubinstein S, Gur Y, Breitbart H. Crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation. Dev Biol 2004; 267: 230-41. (Pubitemid 38234746)
    • (2004) Developmental Biology , vol.267 , Issue.1 , pp. 230-241
    • Cohen, G.1    Rubinstein, S.2    Gur, Y.3    Breitbart, H.4
  • 72
    • 0029884493 scopus 로고    scopus 로고
    • Calcium mobilization and influx during sperm exocytosis
    • Spungin B, Breitbart H. Calcium mobilization and influx during sperm exocytosis. J Cell Sci 1996; 109: 1947-55. (Pubitemid 26248640)
    • (1996) Journal of Cell Science , vol.109 , Issue.7 , pp. 1947-1955
    • Spungin, B.1    Breitbart, H.2
  • 74
    • 0025151931 scopus 로고
    • Further studies on the involvement of protein kinase C in human sperm flagellar motility
    • Rotem R, Paz GF, Homonnai ZT, Kalina M, Naor Z. Further studies on the involvement of protein kinase C in human sperm flagellar motility. Endocrinology 1990; 127: 2571-7. (Pubitemid 20381796)
    • (1990) Endocrinology , vol.127 , Issue.5 , pp. 2571-2577
    • Rotem, R.1    Paz, G.F.2    Homonnai, Z.T.3    Kalina, M.4    Naor, Z.5
  • 75
    • 0031059387 scopus 로고    scopus 로고
    • Subcellular distribution of protein kinase Cα and βI in bovine spermatozoa, and their regulation by calcium and phorbol esters
    • DOI 10.1095/biolreprod56.2.454
    • Lax Y, Rubinstein S, Breitbart H. Subcellular distribution of protein kinase C alpha and betal in bovine spermatozoa, and their regulation by calcium and phorbol esters. Biol Reprod 1997; 56: 454-9. (Pubitemid 27081588)
    • (1997) Biology of Reproduction , vol.56 , Issue.2 , pp. 454-459
    • Lax, Y.1    Rubinstein, S.2    Breitbart, H.3
  • 76
    • 77954207945 scopus 로고    scopus 로고
    • Protein kinase A and protein kinase C(alpha)/PPP1CC2 play opposing roles in the regulation of phosphatidylinositol 3-kinase activation in bovine sperm
    • Rotman T, Etkovitz N, Spiegel A, Rubinstein S, Breitbart H. Protein kinase A and protein kinase C(alpha)/PPP1CC2 play opposing roles in the regulation of phosphatidylinositol 3-kinase activation in bovine sperm. Reproduction 2010; 140: 43-56.
    • (2010) Reproduction , vol.140 , pp. 43-56
    • Rotman, T.1    Etkovitz, N.2    Spiegel, A.3    Rubinstein, S.4    Breitbart, H.5
  • 77
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • DOI 10.1126/science.296.5573.1655
    • Cantley LC. The phosphoinositide 3-kinase pathway. Science 2002; 296: 1655-7. (Pubitemid 34579158)
    • (2002) Science , vol.296 , Issue.5573 , pp. 1655-1657
    • Cantley, L.C.1
  • 78
    • 0031691005 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase is involved in the induction of the human sperm acrosome reaction downstream of tyrosine phosphorylation
    • DOI 10.1093/molehr/4.9.849
    • Fisher HM, Brewis IA, Barratt CL, Cooke ID, Moore HD. Phosphoinositide 3-kinase is involved in the induction of the human sperm acrosome reaction downstream of tyrosine phosphorylation. Mol Hum Reprod 1998; 4: 849-55. (Pubitemid 28430647)
    • (1998) Molecular Human Reproduction , vol.4 , Issue.9 , pp. 849-855
    • Fisher, H.M.1    Brewis, I.A.2    Barratt, C.L.R.3    Cooke, I.D.4    Moore, H.D.M.5
  • 79
    • 33947173171 scopus 로고    scopus 로고
    • Phosphoinositide-dependent pathways in mouse sperm are regulated by egg ZP3 and drive the acrosome reaction
    • DOI 10.1016/j.ydbio.2006.12.023, PII S0012160606014588
    • Jungnickel MK, Sutton KA, Wang Y, Florman HM. Phosphoinositide-dependent pathways in mouse sperm are regulated by egg ZP3 and drive the acrosome reaction. Dev Biol 2007; 304: 116-26. (Pubitemid 46399677)
    • (2007) Developmental Biology , vol.304 , Issue.1 , pp. 116-126
    • Jungnickel, M.K.1    Sutton, K.A.2    Wang, Y.3    Florman, H.M.4
  • 80
    • 34250635347 scopus 로고    scopus 로고
    • Protein kinase C-mediated down-regulation of cyclin D1 involves activation of the translational repressor 4E-BP1 via a phosphoinositide 3-kinase/Akt-independent, protein phosphatase 2A-dependent mechanism in intestinal epithelial cells
    • DOI 10.1074/jbc.M610513200
    • Guan L, Song K, Pysz MA, Curry KJ, Hizli AA et al. Protein kinase C-mediated downregulation of cyclin D1 involves activation of the translational repressor 4E-BP1 via a phosphoinositide 3-kinase/Akt-independent, protein phosphatase 2A-dependent mechanism in intestinal epithelial cells. J Biol Chem 2007; 282: 14213-25. (Pubitemid 47100475)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14213-14225
    • Guan, L.1    Song, K.2    Pysz, M.A.3    Curry, K.J.4    Hizli, A.A.5    Danielpour, D.6    Black, A.R.7    Black, J.D.8
  • 81
    • 33748852206 scopus 로고    scopus 로고
    • The mammalian acrosome as a secretory lysosome: New and old evidence
    • DOI 10.1002/mrd.20581
    • Moreno RD, Alvarado CP. The mammalian acrosome as a secretory lysosome: new and old evidence. Mol Reprod Dev 2006; 73: 1430-4. (Pubitemid 44423732)
    • (2006) Molecular Reproduction and Development , vol.73 , Issue.11 , pp. 1430-1434
    • Moreno, R.D.1    Alvarado, C.P.2
  • 82
    • 65949117010 scopus 로고    scopus 로고
    • Participation of the human sperm proteasome in the capacitation process and its regulation by protein kinase A and tyrosine kinase
    • Kong M, Diaz ES, Morales P. Participation of the human sperm proteasome in the capacitation process and its regulation by protein kinase A and tyrosine kinase. Biol Reprod 2009; 80: 1026-35.
    • (2009) Biol Reprod , vol.80 , pp. 1026-1035
    • Kong, M.1    Diaz, E.S.2    Morales, P.3
  • 83
    • 34547953209 scopus 로고    scopus 로고
    • Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6
    • DOI 10.1074/jbc.M702439200
    • Zhang F, Hu Y, Huang P, Toleman CA, Paterson AJ et al. Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J Biol Chem 2007; 282: 22460-71. (Pubitemid 47267329)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22460-22471
    • Zhang, F.1    Hu, Y.2    Huang, P.3    Toleman, C.A.4    Paterson, A.J.5    Kudlow, J.E.6
  • 86
    • 0037369769 scopus 로고    scopus 로고
    • Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction
    • DOI 10.1095/biolreprod.102.009233
    • Brener E, Rubinstein S, Cohen G, Shternall K, Rivlin J et al. Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction. Biol Reprod 2003; 68: 837-45. (Pubitemid 36245827)
    • (2003) Biology of Reproduction , vol.68 , Issue.3 , pp. 837-845
    • Brener, E.1    Rubinstein, S.2    Cohen, G.3    Shternall, K.4    Rivlin, J.5    Breitbart, H.6
  • 88
    • 15844363885 scopus 로고    scopus 로고
    • Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction
    • DOI 10.1530/rep.1.00269
    • Breitbart H, Cohen G, Rubinstein S. Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction. Reproduction 2005; 129: 263-8. (Pubitemid 40425636)
    • (2005) Reproduction , vol.129 , Issue.3 , pp. 263-268
    • Breitbart, H.1    Cohen, G.2    Rubinstein, S.3
  • 89
    • 0029045897 scopus 로고
    • Sperm exocytosis reconstructed in a cell-free system: Evidence for the involvement of phospholipase C and actin filaments in membrane fusion
    • Spungin B, Margalit I, Breitbart H. Sperm exocytosis reconstructed in a cell-free system: evidence for the involvement of phospholipase C and actin filaments in membrane fusion. J Cell Sci 1995; 108(Pt 6): 2525-35.
    • (1995) J Cell Sci , vol.108 , Issue.PART 6 , pp. 2525-2535
    • Spungin, B.1    Margalit, I.2    Breitbart, H.3
  • 90
    • 0028102764 scopus 로고
    • Isolation and characterization of cDNA clones specifically expressed in testicular germ cells
    • DOI 10.1016/0014-5793(94)01155-9
    • Tanaka H, Yoshimura Y, Nishina Y, Nozaki M, Nojima H et al. Isolation and characterization of cDNA clones specifically expressed in testicular germ cells. FEBS Lett 1994; 355: 4-10. (Pubitemid 24352091)
    • (1994) FEBS Letters , vol.355 , Issue.1 , pp. 4-10
    • Tanaka, H.1
  • 91
    • 0029148609 scopus 로고
    • Molecular nature of calicin, a major basic protein of the mammalian sperm head cytoskeleton
    • von Bulow M, Heid H, Hess H, Franke WW. Molecular nature of calicin, a major basic protein of the mammalian sperm head cytoskeleton. Exp Cell Res 1995; 219: 407- 13.
    • (1995) Exp Cell Res , vol.219 , pp. 407-413
    • Von Bulow, M.1    Heid, H.2    Hess, H.3    Franke, W.W.4
  • 92
    • 0031586004 scopus 로고    scopus 로고
    • CP β3, a novel isoform of an actin-binding protein, is a component of the cytoskeletal calyx of the mammalian sperm head
    • DOI 10.1006/excr.1997.3564
    • von Bulow M, Rackwitz HR, Zimbelmann R, Franke WW. CP beta3, a novel isoform of an actin-binding protein, is a component of the cytoskeletal calyx of the mammalian sperm head. Exp Cell Res 1997; 233: 216-24. (Pubitemid 27229993)
    • (1997) Experimental Cell Research , vol.233 , Issue.1 , pp. 216-224
    • Von Bulow, M.1    Rackwitz, H.-R.2    Zimbelmann, R.3    Franke, W.W.4
  • 93
    • 0023199043 scopus 로고
    • Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin
    • Janmey PA, Iida K, Yin HL, Stossel TP. Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin. J Biol Chem 1987; 262: 12228-36. (Pubitemid 17137443)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.25 , pp. 12228-12236
    • Jammey, P.A.1    Iida, K.2    Yin, H.L.3    Stossel, T.P.4
  • 94
    • 0033910826 scopus 로고    scopus 로고
    • Gelsolin as a calcium-regulated actin filament-capping protein
    • DOI 10.1046/j.1432-1327.2000.01463.x
    • Gremm D, Wegner A. Gelsolin as a calcium-regulated actin filament-capping protein. Eur J Biochem 2000; 267: 4339-45. (Pubitemid 30461065)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.14 , pp. 4339-4345
    • Gremm, D.1    Wegner, A.2
  • 95
    • 0028069472 scopus 로고
    • Epidermal growth factor induces acrosomal exocytosis in bovine sperm
    • DOI 10.1016/0014-5793(94)80422-2
    • Lax Y, Rubinstein S, Breitbart H. Epidermal growth factor induces acrosomal exocytosis in bovine sperm. FEBS Lett 1994; 339: 234-8. (Pubitemid 24063454)
    • (1994) FEBS Letters , vol.339 , Issue.3 , pp. 234-238
    • Lax, Y.1    Rubinstein, S.2    Breitbart, H.3
  • 96
    • 78650969370 scopus 로고    scopus 로고
    • Role and regulation of EGFR in actin remodeling in sperm capacitation and the acrosome reaction
    • Breitbart H, Etkovitz N. Role and regulation of EGFR in actin remodeling in sperm capacitation and the acrosome reaction. Asian J Androl 2011; 13: 106-10.
    • (2011) Asian J Androl , vol.13 , pp. 106-110
    • Breitbart, H.1    Etkovitz, N.2
  • 97
    • 70349298304 scopus 로고    scopus 로고
    • Bovine sperm acrosome reaction induced by G protein-coupled receptor agonists is mediated by epidermal growth factor receptor transactivation
    • Etkovitz N, Tirosh Y, Chazan R, Jaldety Y, Daniel L et al. Bovine sperm acrosome reaction induced by G protein-coupled receptor agonists is mediated by epidermal growth factor receptor transactivation. Dev Biol 2009; 334: 447-57.
    • (2009) Dev Biol , vol.334 , pp. 447-457
    • Etkovitz, N.1    Tirosh, Y.2    Chazan, R.3    Jaldety, Y.4    Daniel, L.5
  • 98
    • 84862696408 scopus 로고    scopus 로고
    • Sperm EGFR mediates alpha7 AChR activation to promote fertilization
    • Jaldety Y, Glick Y, Orr-Urtreger A, Iscowicz D, Gerber D et al. Sperm EGFR mediates alpha7 AChR activation to promote fertilization. J Biol Chem 2012; 287: 22328-40.
    • (2012) J Biol Chem , vol.287 , pp. 22328-22340
    • Jaldety, Y.1    Glick, Y.2    Orr-Urtreger, A.3    Iscowicz, D.4    Gerber, D.5
  • 99
    • 51449103401 scopus 로고    scopus 로고
    • Localization of the epidermal growth factor (EGF) in the epididymis and accessory genital glands of the boar and functional effects on spermatozoa
    • Oliva-Hernandez J, Perez-Gutierrez JF. Localization of the epidermal growth factor (EGF) in the epididymis and accessory genital glands of the boar and functional effects on spermatozoa. Theriogenology 2008; 70: 1159-69.
    • (2008) Theriogenology , vol.70 , pp. 1159-1169
    • Oliva-Hernandez, J.1    Perez-Gutierrez, J.F.2
  • 100
    • 42049123062 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility
    • Peddinti D, Nanduri B, Kaya A, Feugang JM, Burgess SC et al. Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility. BMC Syst Biol 2008; 2: 19.
    • (2008) BMC Syst Biol , vol.2 , pp. 19
    • Peddinti, D.1    Nanduri, B.2    Kaya, A.3    Feugang, J.M.4    Burgess, S.C.5
  • 101
    • 84856078418 scopus 로고    scopus 로고
    • Hyper-activated motility in sperm capacitation is mediated by phospholipase D-dependent actin polymerization
    • Itach SB, Finklestein M, Etkovitz N, Breitbart H. Hyper-activated motility in sperm capacitation is mediated by phospholipase D-dependent actin polymerization. Dev Biol 2012; 362: 154-61.
    • (2012) Dev Biol , vol.362 , pp. 154-161
    • Itach, S.B.1    Finklestein, M.2    Etkovitz, N.3    Breitbart, H.4
  • 102
    • 0035000530 scopus 로고    scopus 로고
    • Phospholipase D activity is required for actin stress fiber formation in fibroblasts
    • DOI 10.1128/MCB.21.12.4055-4066.2001
    • Kam Y, Exton JH. Phospholipase D activity is required for actin stress fiber formation in fibroblasts. Mol Cell Biol 2001; 21: 4055-66. (Pubitemid 32476466)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.12 , pp. 4055-4066
    • Kam, Y.1    Exton, J.H.2
  • 103
    • 0037184978 scopus 로고    scopus 로고
    • Regulation of phospholipase D activity by actin: Actin exerts bidirectional modulation of mammalian phospolipase D activity in a polymerization-dependent, isoform-specific manner
    • DOI 10.1074/jbc.M209221200
    • Kusner DJ, Barton JA, Wen KK, Wang X, Rubenstein PA et al. Regulation of phospholipase D activity by actin. Actin exerts bidirectional modulation of Mammalian phospholipase D activity in a polymerization-dependent, isoformspecific manner. J Biol Chem 2002; 277: 50683-92. (Pubitemid 36042230)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.52 , pp. 50683-50692
    • Kusner, D.J.1    Barton, J.A.2    Wen, K.-K.3    Wang, X.4    Rubenstein, P.A.5    Iyer, S.S.6
  • 104
    • 0030134434 scopus 로고    scopus 로고
    • Stimulation of actin stress fibre formation mediated by activation of phospholipase D
    • Cross MJ, Roberts S, Ridley AJ, Hodgkin MN, Stewart A et al. Stimulation of actin stress fibre formation mediated by activation of phospholipase D.Curr Biol 1996; 6: 588-97.
    • (1996) Curr Biol , vol.6 , pp. 588-597
    • Cross, M.J.1    Roberts, S.2    Ridley, A.J.3    Hodgkin, M.N.4    Stewart, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.