메뉴 건너뛰기




Volumn 35, Issue 4, 2009, Pages 567-581

Sperm proteins in teleostean and chondrostean (sturgeon) fishes

Author keywords

Cryopreservation; Fertilisation; Motility; Protein; Seminal plasma; Spermatozoa

Indexed keywords

PROTEIN;

EID: 70349504870     PISSN: 09201742     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10695-008-9261-y     Document Type: Article
Times cited : (56)

References (156)
  • 1
    • 0018141544 scopus 로고
    • Fine structure of the garfish spermatozoa
    • doi: 10.1016/S0022-5320(78)90039-4
    • Afzelius BA (1978) Fine structure of the garfish spermatozoa. J Ultrastruct Res 64:309-314. doi: 10.1016/S0022-5320(78)90039-4
    • (1978) J Ultrastruct Res , vol.64 , pp. 309-314
    • Afzelius, B.A.1
  • 2
    • 70349506944 scopus 로고
    • MIR publications, Moscow doi: 10.1002/mmnd.4800040102
    • Alberts B, Bray D, Lewis J et al (1987) Molecular biology of the cell, vol 4. MIR publications, Moscow, pp 1-200. doi: 10.1002/mmnd.4800040102
    • (1987) Molecular Biology of the Cell , vol.4 , pp. 1-200
    • Alberts, B.1    Bray, D.2    Lewis, J.3
  • 3
    • 0001011098 scopus 로고    scopus 로고
    • Cryopreservation of the milt of the northern pike
    • doi: 10.1111/j.1095-8649.1995.tb01604.x
    • Babiak I, Glogowski J, Luczynski MJ et al (1997) Cryopreservation of the milt of the northern pike. J Fish Biol 46:819-828. doi: 10.1111/ j.1095-8649.1995.tb01604.x
    • (1997) J Fish Biol , vol.46 , pp. 819-828
    • Babiak, I.1    Glogowski, J.2    Luczynski, M.J.3
  • 4
    • 0035397843 scopus 로고    scopus 로고
    • Effect of extender composition and equilibration time on fertilization ability and enzymatic activity of rainbow trout cryopreserved spermatozoa
    • doi: 10.1016/S0093-691X(01)00553-2
    • Babiak I, Glogowski J, Goryczko K et al (2001) Effect of extender composition and equilibration time on fertilization ability and enzymatic activity of rainbow trout cryopreserved spermatozoa. Theriogenology 56:177-192. doi: 10.1016/S0093-691X(01)00553-2
    • (2001) Theriogenology , vol.56 , pp. 177-192
    • Babiak, I.1    Glogowski, J.2    Goryczko, K.3
  • 5
    • 0016436459 scopus 로고
    • Localization and catalytic properties of lactate dehydrogenase in different sperm models
    • doi: 10.1016/0014-4827(75)90372-9
    • Baccetti B, Pallini A, Burrini AG (1975) Localization and catalytic properties of lactate dehydrogenase in different sperm models. Exp Cell Res 90:183-190. doi: 10.1016/0014-4827(75)90372-9
    • (1975) Exp Cell Res , vol.90 , pp. 183-190
    • Baccetti, B.1    Pallini, A.2    Burrini, A.G.3
  • 6
    • 0024654381 scopus 로고
    • Localization of acrosomal enzymes in Arthropoda, Echinodermata, Vertebrata
    • Baccetti B, Burrini AG, Collodel G et al (1989) Localization of acrosomal enzymes in Arthropoda, Echinodermata, Vertebrata. J Submicrosc Cytol Pathol 21:385-389
    • (1989) J Submicrosc Cytol Pathol , vol.21 , pp. 385-389
    • Baccetti, B.1    Burrini, A.G.2    Collodel, G.3
  • 7
    • 0034106642 scopus 로고    scopus 로고
    • Calcium regulation of microtubule sliding in reactivated sea urchin sperm flagella
    • Bannai H, Yoshimura M, Takahashi K et al (2000) Calcium regulation of microtubule sliding in reactivated sea urchin sperm flagella. J Cell Sci 113:831-839
    • (2000) J Cell Sci , vol.113 , pp. 831-839
    • Bannai, H.1    Yoshimura, M.2    Takahashi, K.3
  • 8
    • 84998233781 scopus 로고
    • Resorption of spermatozoa in the sperm duct of rainbow trout during the post-spawning period
    • Billard R, Takashima F (1983) Resorption of spermatozoa in the sperm duct of rainbow trout during the post-spawning period. Bull Jpn Soc Sci Fish 49:387-392
    • (1983) Bull Jpn Soc Sci Fish , vol.49 , pp. 387-392
    • Billard, R.1    Takashima, F.2
  • 9
    • 84987521675 scopus 로고
    • Some problems related to the assessment of sperm motility in freshwater fish
    • doi: 10.1002/jez.1402610203
    • Billard R, Cosson MP (1992) Some problems related to the assessment of sperm motility in freshwater fish. J Exp Zool 261:122-131. doi: 10.1002/ jez.1402610203
    • (1992) J Exp Zool , vol.261 , pp. 122-131
    • Billard, R.1    Cosson, M.P.2
  • 10
    • 84988990251 scopus 로고
    • Motility of fresh and aged halibut sperm
    • doi: 10.1051/alr:1993008
    • Billard R, Cosson J, Crim LW (1993) Motility of fresh and aged halibut sperm. Aquat Living Resour 6:67-75. doi: 10.1051/alr:1993008
    • (1993) Aquat Living Resour , vol.6 , pp. 67-75
    • Billard, R.1    Cosson, J.2    Crim, L.W.3
  • 12
    • 0001405848 scopus 로고    scopus 로고
    • Motility of Silurus glanis spermatozoa in the testicles and in the milt
    • Billard R, Linhart O, Fierville F et al (1997) Motility of Silurus glanis spermatozoa in the testicles and in the milt. Pol Arch Hydrobiol 44:115-122
    • (1997) Pol Arch Hydrobiol , vol.44 , pp. 115-122
    • Billard, R.1    Linhart, O.2    Fierville, F.3
  • 13
    • 0026065024 scopus 로고
    • Membrane hyperpolarization activates trout sperm without an increase in intracellular pH
    • Boitano S, Omoto CK (1991) Membrane hyperpolarization activates trout sperm without an increase in intracellular pH. J Cell Sci 98:343-349
    • (1991) J Cell Sci , vol.98 , pp. 343-349
    • Boitano, S.1    Omoto, C.K.2
  • 15
    • 0033213244 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility
    • doi: 10.1016/S0093-691X(99)00178-8
    • Brandon CI, Heusner GL, Caudle AB et al (1999) Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility. Theriogenology 52:863-873. doi: 10.1016/S0093-691X(99)00178-8
    • (1999) Theriogenology , vol.52 , pp. 863-873
    • Brandon, C.I.1    Heusner, G.L.2    Caudle, A.B.3
  • 16
    • 0016401513 scopus 로고
    • Mise en évidence de quelques enzymes dans le sperme de la carpe Cyprinus carpio L et de la truite Salmo gairdneri Richardson et dans le liquide coelomatique de la truite
    • Breton B, Menezo Y, Billard R et al (1974) Mise en évidence de quelques enzymes dans le sperme de la carpe Cyprinus carpio L et de la truite Salmo gairdneri Richardson et dans le liquide coelomatique de la truite. C R Acad Sci Paris D 278:1285-1288
    • (1974) C R Acad Sci Paris D , vol.278 , pp. 1285-1288
    • Breton, B.1    Menezo, Y.2    Billard, R.3
  • 17
    • 0018584031 scopus 로고
    • Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella
    • doi: 10.1083/jcb.82.2.401
    • Brokaw CJ (1979) Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella. J Cell Biol 82:401-411. doi: 10.1083/jcb.82.2.401
    • (1979) J Cell Biol , vol.82 , pp. 401-411
    • Brokaw, C.J.1
  • 18
    • 12344275508 scopus 로고    scopus 로고
    • Motility, ATP levels and metabolic enzyme activity of sperm from bluegill (Lepomis macrochirus)
    • Burness G, Moyes CD, Montgomerie R (2005) Motility, ATP levels and metabolic enzyme activity of sperm from bluegill (Lepomis macrochirus). Comp Biochem Physiol Mol Integr Physiol 140:11-17
    • (2005) Comp Biochem Physiol Mol Integr Physiol , vol.140 , pp. 11-17
    • Burness, G.1    Moyes, C.D.2    Montgomerie, R.3
  • 19
    • 0035447599 scopus 로고    scopus 로고
    • Effect of external cryoprotectants as membrane stabilizers on cryopreserved rainbow trout sperm
    • doi: 10.1016/S0093-691X(01)00594-5
    • Cabrita E, Anel L, Herraéz MP (2001) Effect of external cryoprotectants as membrane stabilizers on cryopreserved rainbow trout sperm. Theriogenology 56:623-635. doi: 10.1016/S0093-691X(01)00594-5
    • (2001) Theriogenology , vol.56 , pp. 623-635
    • Cabrita, E.1    Anel, L.2    Herraéz, M.P.3
  • 20
    • 0029033920 scopus 로고
    • Aminopeptidase-B in the rat testes: Isolation, functional properties and cellular localization in the seminiferous tubules
    • doi: 10.1016/0303-7207(95)03529-G
    • Cadel S, Pierotti AR, Foulon T et al (1995) Aminopeptidase-B in the rat testes: Isolation, functional properties and cellular localization in the seminiferous tubules. Mol Cell Endocrinol 110:149-160. doi: 10.1016/ 0303-7207(95)03529-G
    • (1995) Mol Cell Endocrinol , vol.110 , pp. 149-160
    • Cadel, S.1    Pierotti, A.R.2    Foulon, T.3
  • 21
    • 0039552056 scopus 로고
    • Carbohydrate-binding proteins involved in gamete interaction in the pig
    • In: Nieschlag E, Habenicht UF (eds) Springer, Berlin
    • Calvete JJ, Sanz L, Topfer-Petersen E (1992) Carbohydrate-binding proteins involved in gamete interaction in the pig. In: Nieschlag E, Habenicht UF (eds) Spermatogenesis-fertilization-contraception. Springer, Berlin, pp 395-417
    • (1992) Spermatogenesis-fertilization-contraception , pp. 395-417
    • Calvete, J.J.1    Sanz, L.2    Topfer-Petersen, E.3
  • 22
    • 0037359387 scopus 로고    scopus 로고
    • Cryopreservation-induced decrease in heat-shock protein 90 in human spermatozoa and its mechanism
    • Cao WL, Wang YX, Xiang ZQ et al (2003) Cryopreservation-induced decrease in heat-shock protein 90 in human spermatozoa and its mechanism. Asian J Androl 5:43-46
    • (2003) Asian J Androl , vol.5 , pp. 43-46
    • Cao, W.L.1    Wang, Y.X.2    Xiang, Z.Q.3
  • 23
    • 70349501560 scopus 로고    scopus 로고
    • The mechanism of heat-induced hyperactivation of human sperm and the relationship to pregnancy
    • doi: 10.1016/S0015-0282(97)90755-X
    • Chan PJ, Corselli JU, Patton WC et al (1997) The mechanism of heat-induced hyperactivation of human sperm and the relationship to pregnancy. Fertil Steril 68[Suppl 1]:S61-S62. doi: 10.1016/ S0015-0282(97)90755-X
    • (1997) Fertil Steril , vol.68 , Issue.SUPPL. 1
    • Chan, P.J.1    Corselli, J.U.2    Patton, W.C.3
  • 24
    • 34249761575 scopus 로고
    • Sperm motility in turbot, Scophthalmus maximus: Initiation of movement and changes with time of spawning characteristics
    • doi: 10.1007/BF00001167
    • Chauvaud L, Cosson J, Suquet M et al (1995) Sperm motility in turbot, Scophthalmus maximus: Initiation of movement and changes with time of spawning characteristics. Environ Biol Fishes 43:341-349. doi: 10.1007/ BF00001167
    • (1995) Environ Biol Fishes , vol.43 , pp. 341-349
    • Chauvaud, L.1    Cosson, J.2    Suquet, M.3
  • 25
    • 84985855295 scopus 로고
    • Fine-structure of the envelope and micropyles in the eggs of the white sturgeon, Acipenser transmontanus Richardson
    • doi: 10.1111/j.1440-169X.1982.00341.x
    • Cherr GN, Clark WH (1982) Fine-structure of the envelope and micropyles in the eggs of the white sturgeon, Acipenser transmontanus Richardson. Dev Growth Differ 24:341-352. doi: 10.1111/j.1440-169X.1982.00341.x
    • (1982) Dev Growth Differ , vol.24 , pp. 341-352
    • Cherr, G.N.1    Clark, W.H.2
  • 26
    • 51249178900 scopus 로고
    • Gamete interaction in the white sturgeon Acipenser transmontanus: A morphological and physiological review
    • doi: 10.1007/BF00001572
    • Cherr GN, Clark WN (1985) Gamete interaction in the white sturgeon Acipenser transmontanus: A morphological and physiological review. Environ Biol Fishes 14:11-22. doi: 10.1007/BF00001572
    • (1985) Environ Biol Fishes , vol.14 , pp. 11-22
    • Cherr, G.N.1    Clark, W.N.2
  • 28
    • 0023643126 scopus 로고
    • Trout sperm motility. The transient movement of trout sperm motility is related to changes in concentrations of ATP following the activation of flagellar movement
    • doi: 10.1111/j.1432-1033.1987.tb13565.x
    • Christen R, Gatti JL, Billard R (1987) Trout sperm motility. The transient movement of trout sperm motility is related to changes in concentrations of ATP following the activation of flagellar movement. Eur J Biochem 166:667-671. doi: 10.1111/j.1432-1033.1987.tb13565.x
    • (1987) Eur J Biochem , vol.166 , pp. 667-671
    • Christen, R.1    Gatti, J.L.2    Billard, R.3
  • 29
    • 41949085337 scopus 로고    scopus 로고
    • Chemical composition of seminal plasma and its physiological relationship with sperm motility, fertilizing capacity and cryopreservation success in fish
    • In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Alpha Science Int, Oxford
    • Cierezko A (2008) Chemical composition of seminal plasma and its physiological relationship with sperm motility, fertilizing capacity and cryopreservation success in fish. In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Fish spermatology. Alpha Science Int, Oxford, pp 215-240
    • (2008) Fish Spermatology , pp. 215-240
    • Cierezko, A.1
  • 30
    • 51249163085 scopus 로고
    • Relationship between biochemical constituents of fish semen and fertility: The effect of short-term storage
    • doi: 10.1007/BF00004300
    • Ciereszko A, Dabrowski K (1994) Relationship between biochemical constituents of fish semen and fertility: The effect of short-term storage. Fish Physiol Biochem 12:357-369. doi: 10.1007/BF00004300
    • (1994) Fish Physiol Biochem , vol.12 , pp. 357-369
    • Ciereszko, A.1    Dabrowski, K.2
  • 31
    • 0026975569 scopus 로고
    • The covalent oscillator - A paradigm accounting for the sliding bending mechanism and wave-propagation in cilia and flagella
    • Cosson J (1992) The covalent oscillator - a paradigm accounting for the sliding bending mechanism and wave-propagation in cilia and flagella. Biocell 76:319-327
    • (1992) Biocell , vol.76 , pp. 319-327
    • Cosson, J.1
  • 32
    • 48249129432 scopus 로고    scopus 로고
    • The motility apparatus of fish spermatozoa
    • In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Alpha Science Int, Oxford
    • Cosson J (2008) The motility apparatus of fish spermatozoa. In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Fish spermatology. Alpha Science Int, Oxford, pp 281-316
    • (2008) Fish Spermatology , pp. 281-316
    • Cosson, J.1
  • 33
    • 0023694662 scopus 로고
    • Protease inhibitor and substrates block motility and microtubule sliding of sea urchin and carp spermatozoa
    • doi: 10.1002/cm.970100408
    • Cosson M-P, Gagnon C (1988) Protease inhibitor and substrates block motility and microtubule sliding of sea urchin and carp spermatozoa. Cell Motil Cytoskeleton 10:518-527. doi: 10.1002/cm.970100408
    • (1988) Cell Motil Cytoskeleton , vol.10 , pp. 518-527
    • Cosson, M.-P.1    Gagnon, C.2
  • 34
    • 0021438677 scopus 로고
    • Sperm chemotaxis in siphonophores II. Calcium-dependent asymmetrical movement of spermatozoa induced by attractant
    • Cosson M-P, Carré D, Cosson J (1984) Sperm chemotaxis in siphonophores II. Calcium-dependent asymmetrical movement of spermatozoa induced by attractant. J Cell Sci 68:163-181
    • (1984) J Cell Sci , vol.68 , pp. 163-181
    • Cosson, M.-P.1    Carré, D.2    Cosson, J.3
  • 35
    • 12444335086 scopus 로고
    • CAMP/ATP relationship in the activation of trout sperm motility: Their interaction in membrane-deprived models and in live spermatozoa
    • Cosson M-P, Cosson J, André F, Billard R (1995) CAMP/ATP relationship in the activation of trout sperm motility: Their interaction in membrane-deprived models and in live spermatozoa. Cell Motil Physiol 143:546-554
    • (1995) Cell Motil Physiol , vol.143 , pp. 546-554
    • Cosson, M.-P.1    Cosson, J.2    André, F.3    Billard, R.4
  • 36
    • 0001508217 scopus 로고    scopus 로고
    • Regulation of axonemal wave parameters of fish spermatozoa by ionic factors
    • In: Gagnon C (ed) Cache River Press, Montreal
    • Cosson J, Dreanno C, Billard R et al (1999) Regulation of axonemal wave parameters of fish spermatozoa by ionic factors. In: Gagnon C (ed) The male gamete: From basic knowledge to clinical applications. Cache River Press, Montreal, pp 161-186
    • (1999) The Male Gamete: From Basic Knowledge to Clinical Applications , pp. 161-186
    • Cosson, J.1    Dreanno, C.2    Billard, R.3
  • 37
    • 0033852653 scopus 로고    scopus 로고
    • Analysis of motility parameters from paddlefish and shovelnose sturgeon spermatozoa
    • doi: 10.1111/j.1095-8649.2000.tb02148.x
    • Cosson J, Linhart O, Mims SD et al (2000) Analysis of motility parameters from paddlefish and shovelnose sturgeon spermatozoa. J Fish Biol 56:1348-1367. doi: 10.1111/j.1095-8649.2000.tb02148.x
    • (2000) J Fish Biol , vol.56 , pp. 1348-1367
    • Cosson, J.1    Linhart, O.2    Mims, S.D.3
  • 38
    • 48249156205 scopus 로고    scopus 로고
    • Studying sperm motility in marine fish: An overview on the state of the art
    • doi: 10.1111/j.1439-0426.2008.01151.x
    • Cosson J, Groison AL, Suquet M et al (2008) Studying sperm motility in marine fish: An overview on the state of the art. J Appl Ichtyol 24:460-486. doi: 10.1111/j.1439-0426.2008.01151.x
    • (2000) J Appl Ichtyol , vol.24 , pp. 460-486
    • Cosson, J.1    Groison, A.L.2    Suquet, M.3
  • 39
    • 0028224982 scopus 로고
    • L-carnitine in idiopathic asthenozoospermia: A multicenter study Italian study group on carnitine and male infertility
    • Costa M, Canale D, Filicori M et al (1994) L-carnitine in idiopathic asthenozoospermia: A multicenter study Italian study group on carnitine and male infertility. Andrologia 26:155-159
    • (1994) Andrologia , vol.26 , pp. 155-159
    • Costa, M.1    Canale, D.2    Filicori, M.3
  • 40
    • 0038706027 scopus 로고    scopus 로고
    • Teleost fish spermatozoa contain a cytosolic protein factor that induces calcium release in sea urchin egg homogenates and triggers calcium oscillations when injected into mouse oocytes
    • doi: 10.1016/S0006-291X(03)00753-8
    • Coward K, Campos-Mendoza A, Larman M et al (2003) Teleost fish spermatozoa contain a cytosolic protein factor that induces calcium release in sea urchin egg homogenates and triggers calcium oscillations when injected into mouse oocytes. Biochem Biophys Res Commun 305:299-304. doi: 10.1016/S0006-291X(03)00753-8
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 299-304
    • Coward, K.1    Campos-Mendoza, A.2    Larman, M.3
  • 41
    • 0001438589 scopus 로고
    • Fertilization in the medusan, Spirocodon saltatrix
    • doi: 10.2307/1538471
    • Dan JC (1950) Fertilization in the medusan, Spirocodon saltatrix. Biol Bull 99:412-415. doi: 10.2307/1538471
    • (1950) Biol Bull , vol.99 , pp. 412-415
    • Dan, J.C.1
  • 42
    • 0035581246 scopus 로고    scopus 로고
    • Ion transport in sperm signaling
    • doi: 10.1006/dbio.2001.0387
    • Darszon A, Beltrán C, Felix R et al (2001) Ion transport in sperm signaling. Dev Biol 240:1-14. doi: 10.1006/dbio.2001.0387
    • (2001) Dev Biol , vol.240 , pp. 1-14
    • Darszon, A.1    Beltrán, C.2    Felix, R.3
  • 43
    • 0024414632 scopus 로고
    • The neuroendocrine prostate: Characterization and quantitation of calcitonin in the human gland
    • Davis NS, DiSant'Agnese PA, Ewing JF, Mooney RA et al (1989) The neuroendocrine prostate: Characterization and quantitation of calcitonin in the human gland. J Urol 142:884-888
    • (1989) J Urol , vol.142 , pp. 884-888
    • Davis, N.S.1    DiSant'Agnese, P.A.2    Ewing, J.F.3    Mooney, R.A.4
  • 44
    • 0027551111 scopus 로고
    • Effect of various cryoprotectants agents and membrane-stabilizing compounds on bull sperm membrane integrity after cooling and freezing
    • doi: 10.1006/cryo.1993.1005
    • De Leeuw FE, De Leeuw AM, Den Daas JHG et al (1993) Effect of various cryoprotectants agents and membrane-stabilizing compounds on bull sperm membrane integrity after cooling and freezing. Cryobiology 30:32-44. doi: 10.1006/cryo.1993.1005
    • (1993) Cryobiology , vol.30 , pp. 32-44
    • De Leeuw, F.E.1    De Leeuw, A.M.2    Den Daas, J.H.G.3
  • 45
    • 33744520562 scopus 로고    scopus 로고
    • Membranous and structural damage that occur during cryopreservation of human sperm may be time-related events
    • doi: 10.1016/j.fertnstert.2005.11.046
    • Desrosiers P, Légaré C, Leclerc P et al (2006) Membranous and structural damage that occur during cryopreservation of human sperm may be time-related events. Fertil Steril 85:1744-1752. doi: 10.1016/ j.fertnstert.2005.11.046
    • (2006) Fertil Steril , vol.85 , pp. 1744-1752
    • Desrosiers, P.1    Légaré, C.2    Leclerc, P.3
  • 46
    • 0032104859 scopus 로고    scopus 로고
    • Role of ions and ion channels in the regulation of Atlantic croaker sperm motility
    • doi:10.1002/(SICI)1097-010X(19980601)281:2<139::AID-JEZ8>3.0.CO;2-P
    • Detweiler C, Thomas P (1998) Role of ions and ion channels in the regulation of Atlantic croaker sperm motility. J Exp Zool 281:139-148. doi:10.1002/(SICI)1097-010X(19980601)281:2<139::AID-JEZ8>3.0.CO;2-P
    • (1998) J Exp Zool , vol.281 , pp. 139-148
    • Detweiler, C.1    Thomas, P.2
  • 47
    • 0034082149 scopus 로고    scopus 로고
    • Sperm-cell ultrastructure of North American sturgeon I. The Atlantic sturgeon (Acipenser oxyrhynchus)
    • doi: 10.1139/cjz-78-3-438
    • DiLauro MN, Kaboord WS, Walsh RA (2000) Sperm-cell ultrastructure of North American sturgeon I. The Atlantic sturgeon (Acipenser oxyrhynchus). Can J Zool 78:438-447. doi: 10.1139/cjz-78-3-438
    • (2000) Can J Zool , vol.78 , pp. 438-447
    • DiLauro, M.N.1    Kaboord, W.S.2    Walsh, R.A.3
  • 48
    • 0032968648 scopus 로고    scopus 로고
    • Effects of osmolality, morphology perturbations and intracellular nucleotide content during the movement of sea bass (Dicentrarchus labrax) spermatozoa
    • doi: 10.1530/jrf.0.1160113
    • Dréanno C, Cosson J, Suquet M et al (1999) Effects of osmolality, morphology perturbations and intracellular nucleotide content during the movement of sea bass (Dicentrarchus labrax) spermatozoa. J Reprod Fertil 116:113-125. doi: 10.1530/jrf.0.1160113
    • (1999) J Reprod Fertil , vol.116 , pp. 113-125
    • Dréanno, C.1    Cosson, J.2    Suquet, M.3
  • 49
    • 0031880170 scopus 로고    scopus 로고
    • Molecular mechanisms of sperm-egg interactions and egg activation
    • Evans JP, Kopf GS (1998) Molecular mechanisms of sperm-egg interactions and egg activation. Andrologia 30:297-307
    • (1998) Andrologia , vol.30 , pp. 297-307
    • Evans, J.P.1    Kopf, G.S.2
  • 50
    • 0017785396 scopus 로고
    • Water transport and cell survival in cryobiological procedures
    • doi: 10.1098/rstb.1977.0037
    • Farrant J (1977) Water transport and cell survival in cryobiological procedures. Philos Trans R Soc Lond Biol Sci 278:191-205. doi: 10.1098/ rstb.1977.0037
    • (1977) Philos Trans R Soc Lond Biol Sci , vol.278 , pp. 191-205
    • Farrant, J.1
  • 51
    • 3042805170 scopus 로고    scopus 로고
    • Decrease in glutathione content in boar sperm after cryopreservation - Effect of the addition of reduced glutathione to the freezing and thawing extenders
    • doi: 10.1016/j.theriogenology.2003.11.013
    • Gadea J, Selles E, Marco MA et al (2004) Decrease in glutathione content in boar sperm after cryopreservation - effect of the addition of reduced glutathione to the freezing and thawing extenders. Theriogenology 62:690-701. doi: 10.1016/j.theriogenology.2003.11.013
    • (2004) Theriogenology , vol.62 , pp. 690-701
    • Gadea, J.1    Selles, E.2    Marco, M.A.3
  • 52
    • 29244473553 scopus 로고    scopus 로고
    • Mammalian membrane block to polyspermy: New insights into how mammalian eggs prevent fertilization by multiple sperm
    • doi: 10.1071/RD05122
    • Gardner AJ, Evans JP (2006) Mammalian membrane block to polyspermy: New insights into how mammalian eggs prevent fertilization by multiple sperm. Reprod Fertil Dev 18:53-61. doi: 10.1071/RD05122
    • (2006) Reprod Fertil Dev , vol.18 , pp. 53-61
    • Gardner, A.J.1    Evans, J.P.2
  • 53
    • 0025365861 scopus 로고
    • Ionic regulation of the plasma membrane potential of rainbow trout, Salmo gairdneril, spermatozoa: Role in the initiation of sperm motility
    • doi: 10.1002/jcp.1041430320
    • Gatti JL, Billard R, Christen R (1990) Ionic regulation of the plasma membrane potential of rainbow trout, Salmo gairdneril, spermatozoa: Role in the initiation of sperm motility. J Cell Physiol 143:546-554. doi: 10.1002/jcp.1041430320
    • (1990) J Cell Physiol , vol.143 , pp. 546-554
    • Gatti, J.L.1    Billard, R.2    Christen, R.3
  • 54
    • 0010646209 scopus 로고
    • Binding characteristics of 20β-S to Atlantic croaker sperm membrane receptor
    • In: University of Texas, Austin
    • Ghosh S, Thomas P (1995) Binding characteristics of 20β-S to Atlantic croaker sperm membrane receptor. In: Proc 5th Int Symp Reprod Physiol Fish. University of Texas, Austin, pp 239-245
    • (1995) Proc 5th Int Symp Reprod Physiol Fish , pp. 239-245
    • Ghosh, S.1    Thomas, P.2
  • 55
    • 0021779571 scopus 로고
    • Motility of the 9 + 2 flagellum of Anguilla sperm
    • doi: 10.1002/cm.970050406
    • Gibbons BH, Baccetti B, Gibbons IR (1985) Motility of the 9 + 2 flagellum of Anguilla sperm. Cell Motil 5:333-350. doi: 10.1002/ cm.970050406
    • (1985) Cell Motil , vol.5 , pp. 333-350
    • Gibbons, B.H.1    Baccetti, B.2    Gibbons, I.R.3
  • 56
    • 0001554827 scopus 로고
    • Mechanisms of fertilization in fishes
    • Gilkey JC (1981) Mechanisms of fertilization in fishes. Am Zool 21:359-375
    • (1981) Am Zool , vol.21 , pp. 359-375
    • Gilkey, J.C.1
  • 58
    • 0030469441 scopus 로고    scopus 로고
    • Activity of aspartate aminotransferase and acid phosphatase in cryopreserved trout sperm
    • doi: 10.1071/RD9961179
    • Glogowski J, Babiak I, Goryczko K et al (1996) Activity of aspartate aminotransferase and acid phosphatase in cryopreserved trout sperm. Reprod Fertil Dev 8:1179-1184. doi: 10.1071/RD9961179
    • (1996) Reprod Fertil Dev , vol.8 , pp. 1179-1184
    • Glogowski, J.1    Babiak, I.2    Goryczko, K.3
  • 59
    • 0037333267 scopus 로고    scopus 로고
    • Enzyme activities in fish spermatozoa with focus on lactate dehydrogenase isoenzymes from herring Clupea harengus
    • doi: 10.1016/S1096-4959(02)00192-6
    • Gronczewska J, Zietara MS, Biegniewska A et al (2003) Enzyme activities in fish spermatozoa with focus on lactate dehydrogenase isoenzymes from herring Clupea harengus. Comp Biochem Physiol B 134:399-406. doi: 10.1016/S1096-4959(02)00192-6
    • (2003) Comp Biochem Physiol B , vol.134 , pp. 399-406
    • Gronczewska, J.1    Zietara, M.S.2    Biegniewska, A.3
  • 60
    • 0037313798 scopus 로고    scopus 로고
    • Quantitative determination of creatine kinase release from herring (Clupea harengus) spermatozoa induced by tributyltin
    • Grzyb K, Rychowski M, Biegniewska A et al (2003) Quantitative determination of creatine kinase release from herring (Clupea harengus) spermatozoa induced by tributyltin. Comp Biochem Physiol C 134:207-213
    • (2003) Comp Biochem Physiol C , vol.134 , pp. 207-213
    • Grzyb, K.1    Rychowski, M.2    Biegniewska, A.3
  • 61
    • 0023646056 scopus 로고
    • Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa
    • Hayashi H, Yamamoto K, Richmond J et al (1987) Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa. J Biol Chem 262:16692-16698
    • (1987) J Biol Chem , vol.262 , pp. 16692-16698
    • Hayashi, H.1    Yamamoto, K.2    Richmond, J.3
  • 62
    • 0028915737 scopus 로고
    • A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: I Protein purification and characterization
    • Huang CJ, Chen CC, Chen HJ et al (1995a) A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: I Protein purification and characterization. J Neurochem 64:1715-1720
    • (1995) J Neurochem , vol.64 , pp. 1715-1720
    • Huang, C.J.1    Chen, C.C.2    Chen, H.J.3
  • 63
    • 0028915738 scopus 로고
    • A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression
    • Huang CJ, Lee MS, Huang FL et al (1995b) A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J Neurochem 64:1721-1727
    • (1995) J Neurochem , vol.64 , pp. 1721-1727
    • Huang, C.J.1    Lee, M.S.2    Huang, F.L.3
  • 64
    • 0033118926 scopus 로고    scopus 로고
    • Substantial decrease of heat-shock protein precedes the decline of sperm motility during cooling of boar spermatozoa
    • doi: 10.1016/S0093-691X(99)00046-1
    • Huang SY, Kuo YH, Lee WC et al (1999) Substantial decrease of heat-shock protein precedes the decline of sperm motility during cooling of boar spermatozoa. Theriogenology 51:1007-1016. doi: 10.1016/ S0093-691X(99)00046-1
    • (1999) Theriogenology , vol.51 , pp. 1007-1016
    • Huang, S.Y.1    Kuo, Y.H.2    Lee, W.C.3
  • 65
    • 0347604867 scopus 로고    scopus 로고
    • Molecular architecture of sperm flagella: Molecules for motility and signaling
    • doi: 10.2108/zsj.20.1043
    • Inaba K (2003) Molecular architecture of sperm flagella: Molecules for motility and signaling. Zool Sci 20:1043-1056. doi: 10.2108/zsj.20.1043
    • (2003) Zool Sci , vol.20 , pp. 1043-1056
    • Inaba, K.1
  • 66
    • 48249152780 scopus 로고    scopus 로고
    • Molecular mechanisms of the activation of flagellar motility in sperm
    • In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Alpha Science Int, Oxford
    • Inaba K (2008) Molecular mechanisms of the activation of flagellar motility in sperm. In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Fish spermatology. Alpha Science Int, Oxford, pp 267-280
    • (2008) Fish Spermatology , pp. 267-280
    • Inaba, K.1
  • 67
    • 0026349092 scopus 로고
    • A chymotrypsin-like proteinase involved in motility of sperm in salmonid fish
    • Inaba K, Morisawa M (1991) A chymotrypsin-like proteinase involved in motility of sperm in salmonid fish. Biomed Res 12:435-437
    • (1991) Biomed Res , vol.12 , pp. 435-437
    • Inaba, K.1    Morisawa, M.2
  • 68
    • 0033525743 scopus 로고    scopus 로고
    • Tctex2-related outer arm dynein light chain is phosphorylated at activation of sperm motility
    • doi: 10.1006/bbrc.1999.0309
    • Inaba K, Kagami O, Ogawa K (1999) Tctex2-related outer arm dynein light chain is phosphorylated at activation of sperm motility. Biochem Biophys Res Commun 256:177-183. doi: 10.1006/bbrc.1999.0309
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 177-183
    • Inaba, K.1    Kagami, O.2    Ogawa, K.3
  • 69
    • 0346233291 scopus 로고    scopus 로고
    • Isolation of an inner arm dynein intermediate chain IC116 from Ciona intestinalis and its roles in flagellar motility
    • Inaba K, Padma P, Hozumi A (2002) Isolation of an inner arm dynein intermediate chain IC116 from Ciona intestinalis and its roles in flagellar motility. Zool Sci 19:1435
    • (2002) Zool Sci , vol.19 , pp. 1435
    • Inaba, K.1    Padma, P.2    Hozumi, A.3
  • 71
    • 0037566889 scopus 로고    scopus 로고
    • Characterization of cAMP-dependent protein kinase catalytic subunit from rainbow trout sperm
    • doi: 10.1016/S0006-291X(03)00840-4
    • Itoh A, Inaba K, Ohtake H et al (2003) Characterization of cAMP-dependent protein kinase catalytic subunit from rainbow trout sperm. Biochem Biophys Res Commun 305:855-861. doi: 10.1016/ S0006-291X(03)00840-4
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 855-861
    • Itoh, A.1    Inaba, K.2    Ohtake, H.3
  • 72
    • 0025582545 scopus 로고
    • First messengers at fertilization
    • Jaffe LA (1990) First messengers at fertilization. J Reprod Fertil Suppl 42:107-116
    • (1990) J Reprod Fertil Suppl , vol.42 , pp. 107-116
    • Jaffe, L.A.1
  • 74
    • 0347657532 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of bovine seminal plasma proteins and their relation with semen freezability
    • doi: 10.1016/S0093-691X(03)00230-9
    • Jobim MIM, Oberst ER, Salbego CG et al (2004) Two-dimensional polyacrylamide gel electrophoresis of bovine seminal plasma proteins and their relation with semen freezability. Theriogenology 61:255-266. doi: 10.1016/S0093-691X(03)00230-9
    • (2004) Theriogenology , vol.61 , pp. 255-266
    • Jobim, M.I.M.1    Oberst, E.R.2    Salbego, C.G.3
  • 75
    • 0025619642 scopus 로고
    • Identification and functions of mammalian egg recognition molecules during fertilization
    • Jones R (1990) Identification and functions of mammalian egg recognition molecules during fertilization. J Reprod Fertil Suppl 42:89-105
    • (1990) J Reprod Fertil Suppl , vol.42 , pp. 89-105
    • Jones, R.1
  • 76
    • 0035995284 scopus 로고    scopus 로고
    • Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants
    • doi: 10.1016/S0074-7696(02)19012-7
    • Kamiya R (2002) Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants. Int Rev Cytol 219:115-155. doi: 10.1016/ S0074-7696(02)19012-7
    • (2002) Int Rev Cytol , vol.219 , pp. 115-155
    • Kamiya, R.1
  • 77
    • 0030879134 scopus 로고    scopus 로고
    • Miltpain, new cysteine proteinase from the milt of chum salmon, (Oncorhynchus keta)
    • doi: 10.1016/S0305-0491(97)00142-9
    • Kawabata C, Ichishima E (1997) Miltpain, new cysteine proteinase from the milt of chum salmon, (Oncorhynchus keta). Comp Biochem Physiol B 117:445-452. doi: 10.1016/S0305-0491(97)00142-9
    • (1997) Comp Biochem Physiol B , vol.117 , pp. 445-452
    • Kawabata, C.1    Ichishima, E.2
  • 78
    • 13144254225 scopus 로고    scopus 로고
    • Effect of cryopreservation on mitochondrial DNA of zebrafish (Danio rerio) blastomere cells
    • doi: 10.1016/j.mrfmmm.2004.09.007
    • Kopeika EF, Zhang T, Rawson DM et al (2005) Effect of cryopreservation on mitochondrial DNA of zebrafish (Danio rerio) blastomere cells. Mutat Res 570:49-61. doi: 10.1016/j.mrfmmm.2004.09.007
    • (2005) Mutat Res , vol.570 , pp. 49-61
    • Kopeika, E.F.1    Zhang, T.2    Rawson, D.M.3
  • 79
    • 1542364070 scopus 로고    scopus 로고
    • Proteolytic activity and electrophoretic profiles of proteases from seminal plasma of teleosts
    • doi: 10.1046/j.1095-8649.2003.00224.x
    • Kowalski R, Glogowski J, Kucharczyk D et al (2003) Proteolytic activity and electrophoretic profiles of proteases from seminal plasma of teleosts. J Fish Biol 63:1008-1019. doi: 10.1046/j.1095-8649.2003.00224.x
    • (2003) J Fish Biol , vol.63 , pp. 1008-1019
    • Kowalski, R.1    Glogowski, J.2    Kucharczyk, D.3
  • 80
    • 0034049202 scopus 로고    scopus 로고
    • 2+ influx and subsequent initiation of sperm motility in the common carp
    • doi: 10.1073/pnas.040558097
    • 2+ influx and subsequent initiation of sperm motility in the common carp. Proc Natl Acad Sci USA 97:2052-2057. doi: 10.1073/pnas.040558097
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2052-2057
    • Krasznai, Z.1    Marian, T.2    Izumi, H.3
  • 81
    • 84985748351 scopus 로고
    • Response to sperm penetration of the cortex of eggs of the fish, Plecoglossus altivelis
    • doi: 10.1111/j.1440-169X.1983.00163.x
    • Kudo S (1983) Response to sperm penetration of the cortex of eggs of the fish, Plecoglossus altivelis. Dev Growth Differ 25:163-170. doi: 10.1111/ j.1440-169X.1983.00163.x
    • (1983) Dev Growth Differ , vol.25 , pp. 163-170
    • Kudo, S.1
  • 82
    • 0032529734 scopus 로고    scopus 로고
    • Role of sperm head syndecan at fertilization in fish
    • doi:10.1002/ (SICI)1097-010X(19980815)281:6<620::AID-JEZ10>3.0.CO;2-6
    • Kudo S (1998) Role of sperm head syndecan at fertilization in fish. J Exp Zool 281:620-625. doi:10.1002/ (SICI)1097-010X(19980815)281:6<620::AID-JEZ10>3.0.CO;2-6
    • (1998) J Exp Zool , vol.281 , pp. 620-625
    • Kudo, S.1
  • 83
    • 33646774332 scopus 로고    scopus 로고
    • Effect of oviductal proteins on sperm functions and lipid peroxidation levels during cryopreservation in buffaloes
    • doi: 10.1016/j.anireprosci.2005.06.030
    • Kumaresan A, Ansari MR, Garg A et al (2006) Effect of oviductal proteins on sperm functions and lipid peroxidation levels during cryopreservation in buffaloes. Anim Reprod Sci 93:246-257. doi: 10.1016/ j.anireprosci.2005.06.030
    • (2006) Anim Reprod Sci , vol.93 , pp. 246-257
    • Kumaresan, A.1    Ansari, M.R.2    Garg, A.3
  • 84
    • 0011990121 scopus 로고
    • Plasma membrane of trout spermatozoa: I Isolation and partial characterization
    • doi: 10.1007/BF02265153
    • Labbé C, Loir M (1991) Plasma membrane of trout spermatozoa: I Isolation and partial characterization. Fish Physiol Biochem 9:325-338. doi: 10.1007/BF02265153
    • (1991) Fish Physiol Biochem , vol.9 , pp. 325-338
    • Labbé, C.1    Loir, M.2
  • 85
    • 4243602097 scopus 로고    scopus 로고
    • Cryopreservation protocols for sperm of salmonid fishes
    • In: Tiersch TR, Mazik PM (eds) World Aquaculture Society, Baton Rouge
    • Lahnsteiner F (2000) Cryopreservation protocols for sperm of salmonid fishes. In: Tiersch TR, Mazik PM (eds) Cryopreservation in aquatic species. World Aquaculture Society, Baton Rouge, pp 91-100
    • (2000) Cryopreservation in Aquatic Species , pp. 91-100
    • Lahnsteiner, F.1
  • 86
    • 0141920790 scopus 로고    scopus 로고
    • Morphology, fine structure, biochemistry, and function of the spermatic ducts in marine fish
    • doi: 10.1016/S0040-8166(03)00057-0
    • Lahnsteiner F (2003) Morphology, fine structure, biochemistry, and function of the spermatic ducts in marine fish. Tissue Cell 35:363-373. doi: 10.1016/S0040-8166(03)00057-0
    • (2003) Tissue Cell , vol.35 , pp. 363-373
    • Lahnsteiner, F.1
  • 87
    • 33750699350 scopus 로고    scopus 로고
    • Characterization of seminal plasma proteins stabilizing the sperm viability in rainbow trout (Oncorhynchus mykiss)
    • doi: 10.1016/j.anireprosci.2006.01.003
    • Lahnsteiner F (2007) Characterization of seminal plasma proteins stabilizing the sperm viability in rainbow trout (Oncorhynchus mykiss). Anim Reprod Sci 97:151-164. doi: 10.1016/j.anireprosci.2006.01.003
    • (2007) Anim Reprod Sci , vol.97 , pp. 151-164
    • Lahnsteiner, F.1
  • 88
    • 25844491002 scopus 로고
    • Monosaccharides as energy resources during motility of spermatozoa in Leuciscus cephalus (Cyprinidae, Teleostei)
    • doi: 10.1007/BF00004477
    • Lahnsteiner F, Patzner RA, Weismann T (1992) Monosaccharides as energy resources during motility of spermatozoa in Leuciscus cephalus (Cyprinidae, Teleostei). Fish Physiol Biochem 10:283-289. doi: 10.1007/ BF00004477
    • (1992) Fish Physiol Biochem , vol.10 , pp. 283-289
    • Lahnsteiner, F.1    Patzner, R.A.2    Weismann, T.3
  • 89
    • 0027143071 scopus 로고
    • Energy resources of spermatozoa of the rainbow trout (Oncorhynchus mykiss) (Pisces, Teleostei)
    • doi: 10.1051/rnd:19930404
    • Lahnsteiner F, Patzner RA, Weismann T (1993) Energy resources of spermatozoa of the rainbow trout (Oncorhynchus mykiss) (Pisces, Teleostei). Reprod Nutr Dev 33:349-360. doi: 10.1051/rnd:19930404
    • (1993) Reprod Nutr Dev , vol.33 , pp. 349-360
    • Lahnsteiner, F.1    Patzner, R.A.2    Weismann, T.3
  • 90
    • 0002848875 scopus 로고
    • Testicular main ducts and spermatic ducts in some cyprinid fishes I. Morphology, fine structure and histochemistry
    • doi: 10.1111/j.1095-8649.1994.tb01266.x
    • Lahnsteiner F, Patzner RA, Weismann T (1994) Testicular main ducts and spermatic ducts in some cyprinid fishes I. Morphology, fine structure and histochemistry. J Fish Biol 44:937-951. doi: 10.1111/ j.1095-8649.1994.tb01266.x
    • (1994) J Fish Biol , vol.44 , pp. 937-951
    • Lahnsteiner, F.1    Patzner, R.A.2    Weismann, T.3
  • 91
    • 0032052558 scopus 로고    scopus 로고
    • Determination of semen quality of the rainbow trout by sperm motility, seminal plasma parameters and spermatozoal metabolism
    • doi: 10.1016/S0044-8486(98)00243-9
    • Lahnsteiner F, Berger B, Weismann T et al (1998) Determination of semen quality of the rainbow trout by sperm motility, seminal plasma parameters and spermatozoal metabolism. Aquaculture 163:163-181. doi: 10.1016/S0044-8486(98)00243-9
    • (1998) Aquaculture , vol.163 , pp. 163-181
    • Lahnsteiner, F.1    Berger, B.2    Weismann, T.3
  • 92
    • 0033181321 scopus 로고    scopus 로고
    • Sperm metabolism of the teleost fishes Chalcalburnus chalcoides and Oncorhynchus mykiss and its relation to motility and viability
    • doi:10.1002/ (SICI)1097-010X(19990901)284:4<454::AID-JEZ12>3.0.CO;2-O
    • Lahnsteiner F, Berger B, Weismann T (1999) Sperm metabolism of the teleost fishes Chalcalburnus chalcoides and Oncorhynchus mykiss and its relation to motility and viability. J Exp Zool 284:454-465. doi:10.1002/ (SICI)1097-010X(19990901)284:4<454::AID-JEZ12>3.0.CO;2-O
    • (1999) J Exp Zool , vol.284 , pp. 454-465
    • Lahnsteiner, F.1    Berger, B.2    Weismann, T.3
  • 93
    • 2342519958 scopus 로고    scopus 로고
    • Studies on the semen biology and sperm cryopreservation in the sterlet, Acipenser ruthenus L
    • doi: 10.1111/j.1365-2109.2004.01034.x
    • Lahnsteiner F, Berger B, Horvath A et al (2004) Studies on the semen biology and sperm cryopreservation in the sterlet, Acipenser ruthenus L. Aquacult Res 35:519-528. doi: 10.1111/j.1365-2109.2004.01034.x
    • (2004) Aquacult Res , vol.35 , pp. 519-528
    • Lahnsteiner, F.1    Berger, B.2    Horvath, A.3
  • 94
    • 0033817690 scopus 로고    scopus 로고
    • Cryopreservation alters the levels of the bull sperm surface protein P25b
    • Lessard C, Parent S, Leclerc P et al (2000) Cryopreservation alters the levels of the bull sperm surface protein P25b. J Androl 21:700-707
    • (2000) J Androl , vol.21 , pp. 700-707
    • Lessard, C.1    Parent, S.2    Leclerc, P.3
  • 95
    • 40649096188 scopus 로고    scopus 로고
    • DNA integrity of Polyodon spathula cryopreserved sperm
    • doi: 10.1111/j.1439-0426.2007.01025.x
    • Li P, Wei QW, Liu L (2008) DNA integrity of Polyodon spathula cryopreserved sperm. J Appl Ichthyol 24:121-125. doi: 10.1111/ j.1439-0426.2007.01025.x
    • (2008) J Appl Ichthyol , vol.24 , pp. 121-125
    • Li, P.1    Wei, Q.W.2    Liu, L.3
  • 96
    • 0033368431 scopus 로고    scopus 로고
    • Effects of osmolality and ions on the motility of stripped and testicular of freshwater- and seawater-acclimated tilapia, Oreochromis mossambicus
    • Linhart O, Walford J, Sivaloganathan B et al (1999) Effects of osmolality and ions on the motility of stripped and testicular of freshwater- and seawater-acclimated tilapia, Oreochromis mossambicus. J Fish Biol 55:1344-1358
    • (1999) J Fish Biol , vol.55 , pp. 1344-1358
    • Linhart, O.1    Walford, J.2    Sivaloganathan, B.3
  • 97
    • 51249176891 scopus 로고
    • Proteins of seminal fluid and spermatozoa in the trout (Oncorhynchus mykiss): Partial characterization and variations
    • doi: 10.1007/BF00003405
    • Loir M, Labbé C, Maisse G et al (1990) Proteins of seminal fluid and spermatozoa in the trout (Oncorhynchus mykiss): Partial characterization and variations. Fish Physiol Biochem 8:485-495. doi: 10.1007/BF00003405
    • (1990) Fish Physiol Biochem , vol.8 , pp. 485-495
    • Loir, M.1    Labbé, C.2    Maisse, G.3
  • 98
    • 1542298273 scopus 로고    scopus 로고
    • Isolation, characterization, and cDNA sequencing of alpha-1-antiproteinase-like protein from rainbow trout seminal plasma
    • Mak M, Mak P, Olczak M et al (2004) Isolation, characterization, and cDNA sequencing of alpha-1-antiproteinase-like protein from rainbow trout seminal plasma. Biochim Biophys Acta 1671:93-105
    • (2004) Biochim Biophys Acta , vol.1671 , pp. 93-105
    • Mak, M.1    Mak, P.2    Olczak, M.3
  • 99
    • 0037904209 scopus 로고    scopus 로고
    • Metabolism of intratesticular spermatozoa of a tropical teleost fish (Clarias gariepinus)
    • doi: 10.1016/S1096-4959(03)00083-6
    • Mansour N, Lahnsteiner F, Berger B (2003) Metabolism of intratesticular spermatozoa of a tropical teleost fish (Clarias gariepinus). Comp Biochem Physiol B 135:285-296. doi: 10.1016/S1096-4959(03)00083-6
    • (2003) Comp Biochem Physiol B , vol.135 , pp. 285-296
    • Mansour, N.1    Lahnsteiner, F.2    Berger, B.3
  • 100
    • 0017374323 scopus 로고
    • Freezing injury from "solution effects" and its prevention by natural or artificial cryoprotection
    • Meryman HT, Williams RJ, Douglas MS (1977) Freezing injury from "solution effects" and its prevention by natural or artificial cryoprotection. Cryobiology 14:287-302
    • (1977) Cryobiology , vol.14 , pp. 287-302
    • Meryman, H.T.1    Williams, R.J.2    Douglas, M.S.3
  • 101
    • 0000513535 scopus 로고
    • Sperm chemo-orientation in metazoa
    • In: Metz CB, Monroy A (eds) Academic Press, New York
    • Miller RL (1985) Sperm chemo-orientation in metazoa. In: Metz CB, Monroy A (eds) Biology of fertilization. Academic Press, New York
    • (1985) Biology of Fertilization
    • Miller, R.L.1
  • 102
    • 0033849936 scopus 로고    scopus 로고
    • Chlamydomaona flagella
    • Mitchell DR (2000) Chlamydomaona flagella. J Physiol 36:261-273
    • (2000) J Physiol , vol.36 , pp. 261-273
    • Mitchell, D.R.1
  • 103
    • 0032744582 scopus 로고    scopus 로고
    • A high molecular weight glycoprotein in seminal plasma is a sperm immobilizing factor in the teleost Nile tilapia, Oreochromis niloticus
    • doi: 10.1046/j.1440-169x.1999.00463.x
    • Mochida K, Kondo T, Matsubara T et al (1999) A high molecular weight glycoprotein in seminal plasma is a sperm immobilizing factor in the teleost Nile tilapia, Oreochromis niloticus. Dev Growth Differ 41:619-627. doi: 10.1046/j.1440-169x.1999.00463.x
    • (1999) Dev Growth Differ , vol.41 , pp. 619-627
    • Mochida, K.1    Kondo, T.2    Matsubara, T.3
  • 104
    • 0036202547 scopus 로고    scopus 로고
    • A novel seminal plasma glycoprotein of a teleost, the Nile tilapia (Oreochromis niloticus), contains a partial von Willebrand factor type D domain and a zona pellucida-like domain
    • doi: 10.1002/mrd.10071
    • Mochida K, Matsubara T, Kudo H et al (2002) A novel seminal plasma glycoprotein of a teleost, the Nile tilapia (Oreochromis niloticus), contains a partial von Willebrand factor type D domain and a zona pellucida-like domain. Mol Reprod Dev 62:57-68. doi: 10.1002/mrd.10071
    • (2002) Mol Reprod Dev , vol.62 , pp. 57-68
    • Mochida, K.1    Matsubara, T.2    Kudo, H.3
  • 105
    • 0028520903 scopus 로고
    • Cell signaling mechanisms for sperm motility
    • Morisawa M (1994) Cell signaling mechanisms for sperm motility. Zool Sci 11:647-662
    • (1994) Zool Sci , vol.11 , pp. 647-662
    • Morisawa, M.1
  • 106
    • 0023341424 scopus 로고
    • Short-term changes in levels of cyclic AMP, adenylate cyclase, and phosphodiesterase during the initiation of sperm motility in rainbow trout
    • doi: 10.1002/jez.1402420211
    • Morisawa M, Ishida K (1987) Short-term changes in levels of cyclic AMP, adenylate cyclase, and phosphodiesterase during the initiation of sperm motility in rainbow trout. J Exp Zool 242:199-204. doi: 10.1002/ jez.1402420211
    • (1987) J Exp Zool , vol.242 , pp. 199-204
    • Morisawa, M.1    Ishida, K.2
  • 109
    • 0004971779 scopus 로고
    • Cold shock injury - A comprehensive bibliography
    • Morris GJ, Watson PF (1984) Cold shock injury - a comprehensive bibliography. Cryo Lett 5:352-372
    • (1984) Cryo Lett , vol.5 , pp. 352-372
    • Morris, G.J.1    Watson, P.F.2
  • 110
    • 0342452287 scopus 로고    scopus 로고
    • Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles
    • doi: 10.1007/s002490050108
    • Müller P, Erlemann KR, Müller K et al (1998) Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles. Eur Biophys J 27:33-41. doi: 10.1007/ s002490050108
    • (1998) Eur Biophys J , vol.27 , pp. 33-41
    • Müller, P.1    Erlemann, K.R.2    Müller, K.3
  • 111
    • 79961155063 scopus 로고    scopus 로고
    • Effect of seminal plasma calcitonin levels on sperm motility
    • doi: 10.1080/014850101316901316
    • Mungan NA, Mungan G, Basar MM et al (2001) Effect of seminal plasma calcitonin levels on sperm motility. Arch Androl 47:113-117. doi: 10.1080/014850101316901316
    • (2001) Arch Androl , vol.47 , pp. 113-117
    • Mungan, N.A.1    Mungan, G.2    Basar, M.M.3
  • 112
    • 1542316750 scopus 로고    scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase: Expression pattern during testicular development in mouse and evolutionary conservation in spermatozoa
    • doi: 10.1002/mrd.20039
    • Nayernia K, Diaconu M, Aumüller G et al (2004) Phospholipid hydroperoxide glutathione peroxidase: Expression pattern during testicular development in mouse and evolutionary conservation in spermatozoa. Mol Reprod Dev 67:458-464. doi: 10.1002/mrd.20039
    • (2004) Mol Reprod Dev , vol.67 , pp. 458-464
    • Nayernia, K.1    Diaconu, M.2    Aumüller, G.3
  • 113
    • 0032391339 scopus 로고    scopus 로고
    • Sperm-activating proteins obtained from the herring eggs are homologous to trypsin inhibitors and synthesized in follicle cells
    • doi: 10.1006/dbio.1998.9056
    • Oda S, Igarashi Y, Manaka et al (1998) Sperm-activating proteins obtained from the herring eggs are homologous to trypsin inhibitors and synthesized in follicle cells. Dev Biol 204:55-63. doi: 10.1006/ dbio.1998.9056
    • (1998) Dev Biol , vol.204 , pp. 55-63
    • Oda, S.1    Igarashi, Y.2    Manaka3
  • 114
    • 0030730561 scopus 로고    scopus 로고
    • Purification and characterization of 26S proteasomes from sperm flagella of chum salmon and its roles in the regulation of sperm motility
    • Ohkawa K, Inaba K, Morisawa M (1997) Purification and characterization of 26S proteasomes from sperm flagella of chum salmon and its roles in the regulation of sperm motility. Biomed Res 18:353-363
    • (1997) Biomed Res , vol.18 , pp. 353-363
    • Ohkawa, K.1    Inaba, K.2    Morisawa, M.3
  • 115
    • 0032805683 scopus 로고    scopus 로고
    • Identification of ubiquitin in seminal plasma from tilapia, Oreochromis niloticus
    • Osaki A, Okida N, Ishikawa K et al (1999) Identification of ubiquitin in seminal plasma from tilapia, Oreochromis niloticus. Biomed Res 20:249-252
    • (1999) Biomed Res , vol.20 , pp. 249-252
    • Osaki, A.1    Okida, N.2    Ishikawa, K.3
  • 116
    • 0033637858 scopus 로고    scopus 로고
    • Expression and characterization of trypsinogen produced in the human male genital tract
    • Paju A, Bjartell A, Zhang WM et al (2000) Expression and characterization of trypsinogen produced in the human male genital tract. Am J Pathol 157:2011-2021
    • (2000) Am J Pathol , vol.157 , pp. 2011-2021
    • Paju, A.1    Bjartell, A.2    Zhang, W.M.3
  • 118
    • 0035188694 scopus 로고    scopus 로고
    • Detection of the mouse acrosome reaction by acid phosphatase Comparison with chlortetracycline and electron microscopy
    • Pietrobon EO, Dominguez LA, Vincenti AE et al (2001) Detection of the mouse acrosome reaction by acid phosphatase Comparison with chlortetracycline and electron microscopy. J Androl 22:96-103
    • (2001) J Androl , vol.22 , pp. 96-103
    • Pietrobon, E.O.1    Dominguez, L.A.2    Vincenti, A.E.3
  • 119
    • 0345307751 scopus 로고    scopus 로고
    • Biochemical characterization of Siberian sturgeon Acipenser baeri and sterlet, Acipenser ruthenus, milt plasma and spermatozoa
    • doi: 10.1023/A:1026280218957
    • Piros B, Glogowski J, Kolman R et al (2002) Biochemical characterization of Siberian sturgeon Acipenser baeri and sterlet, Acipenser ruthenus, milt plasma and spermatozoa. Fish Physiol Biochem 26:289-295. doi: 10.1023/A:1026280218957
    • (2002) Fish Physiol Biochem , vol.26 , pp. 289-295
    • Piros, B.1    Glogowski, J.2    Kolman, R.3
  • 120
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa J, Korzus E, Travis J (1994) The serpin superfamily of proteinase inhibitors: Structure, function, and regulation. J Biol Chem 269:15957-15960
    • (1994) J Biol Chem , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 121
    • 33846924116 scopus 로고    scopus 로고
    • Morphology and ultrastructure of Siberian sturgeon, Acipenser baerii, spermatozoa using scanning and transmission electron microscopy
    • Psenicka M, Alavi SMH, Rodina M et al (2007) Morphology and ultrastructure of Siberian sturgeon, Acipenser baerii, spermatozoa using scanning and transmission electron microscopy. Biocell 99:103-115
    • (2007) Biocell , vol.99 , pp. 103-115
    • Psenicka, M.1    Alavi, S.M.H.2    Rodina, M.3
  • 122
    • 84989607734 scopus 로고
    • Partial purification and some chemical properties of the sperm chemoattractant from the forcipulate starfish Pycnopodia helianthoides (Brandt, 1835)
    • doi: 10.1002/jez.1402620112
    • Punnett T, Miller RL, Yoo BH (1992) Partial purification and some chemical properties of the sperm chemoattractant from the forcipulate starfish Pycnopodia helianthoides (Brandt, 1835). J Exp Zool 262:87-96. doi: 10.1002/jez.1402620112
    • (1992) J Exp Zool , vol.262 , pp. 87-96
    • Punnett, T.1    Miller, R.L.2    Yoo, B.H.3
  • 123
    • 0037229257 scopus 로고    scopus 로고
    • Glutathione and gluthatione S-transferases A1-1 and P1-1 in seminal plasma may play a role in protecting against oxidative damage to spermatozoa
    • doi: 10.1016/S0015-0282(02)04404-7
    • Raijmakers MTM, Roelofs HMJ, Steegers EAP et al (2003) Glutathione and gluthatione S-transferases A1-1 and P1-1 in seminal plasma may play a role in protecting against oxidative damage to spermatozoa. Fertil Steril 79:169-172. doi: 10.1016/S0015-0282(02)04404-7
    • (2003) Fertil Steril , vol.79 , pp. 169-172
    • Raijmakers, M.T.M.1    Roelofs, H.M.J.2    Steegers, E.A.P.3
  • 124
    • 0026697198 scopus 로고
    • Loss of acid phosphatase from rat spermatozoa as a method for assessing the acrosome reaction
    • Salzberger Z, Lewin LM, Shalgi R (1992) Loss of acid phosphatase from rat spermatozoa as a method for assessing the acrosome reaction. Andrologia 24:155-159
    • (1992) Andrologia , vol.24 , pp. 155-159
    • Salzberger, Z.1    Lewin, L.M.2    Shalgi, R.3
  • 125
    • 9744221183 scopus 로고    scopus 로고
    • Characteristics of arylsulfatase present in Russian sturgeon (Acipenser gueldenstaedti Brandt) semen
    • doi: 10.1016/j.cbpc.2004.03.016
    • Sarosiek B, Ciereszko A, Kolman R et al (2004) Characteristics of arylsulfatase present in Russian sturgeon (Acipenser gueldenstaedti Brandt) semen. Comp Biochem Physiol B 139:571-579. doi: 10.1016/ j.cbpc.2004.03.016
    • (2004) Comp Biochem Physiol B , vol.139 , pp. 571-579
    • Sarosiek, B.1    Ciereszko, A.2    Kolman, R.3
  • 126
    • 34547160738 scopus 로고    scopus 로고
    • Characteristics of acid phosphatase from Russian sturgeon (Acipenser gueldenstaedii) spermatozoa
    • doi: 10.1111/j.1439-0426.2007.00989.x 10.1111/j.1439-0426.2007.00989.x
    • Sarosiek B, Wysocka J, Wysocki P et al (2006) Characteristics of acid phosphatase from Russian sturgeon (Acipenser gueldenstaedii) spermatozoa. J Appl Ichthyol 22[Suppl 1]:375-379. doi: 10.1111/ j.1439-0426.2007.00989.x 10.1111/j.1439-0426.2007.00989.x
    • (2006) J Appl Ichthyol , vol.22 , Issue.SUPPL. 1 , pp. 375-379
    • Sarosiek, B.1    Wysocka, J.2    Wysocki, P.3
  • 127
    • 34548654120 scopus 로고    scopus 로고
    • α-Tocopherol modifies tyrosine phosphorylation and capacitation-like state of cryopreserved porcine sperm
    • doi: 10.1016/j.theriogenology.2007.06.021
    • Satorre MM, Breininger E, Beconi MT et al (2007) α-Tocopherol modifies tyrosine phosphorylation and capacitation-like state of cryopreserved porcine sperm. Theriogenology 68:958-965. doi: 10.1016/ j.theriogenology.2007.06.021
    • (2007) Theriogenology , vol.68 , pp. 958-965
    • Satorre, M.M.1    Breininger, E.2    Beconi, M.T.3
  • 128
    • 0032418893 scopus 로고    scopus 로고
    • The use of phosphocreatine plus ADP as energy source for motility of membrane-deprived trout spermatozoa
    • doi:10.1002/(SICI)1097-0169(1998)41:2<91::AID-CM1>3.0.CO;2-I
    • Saudrais C, Fierville F, Loir M et al (1998) The use of phosphocreatine plus ADP as energy source for motility of membrane-deprived trout spermatozoa. Cell Motil Cytoskeleton 41:91-106 doi:10.1002/ (SICI)1097-0169(1998)41:2<91::AID-CM1>3.0.CO;2-I
    • (1998) Cell Motil Cytoskeleton , vol.41 , pp. 91-106
    • Saudrais, C.1    Fierville, F.2    Loir, M.3
  • 129
    • 0033868942 scopus 로고    scopus 로고
    • Lipid analysis of human spermatozoa and seminal plasma by MALDI-TOF mass spectrometry and NMR spectroscopy-effects of freezing and thawing
    • doi: 10.1016/S0009-3084(00)00148-1
    • Schiller J, Arnhold J, Glander HJ et al (2000) Lipid analysis of human spermatozoa and seminal plasma by MALDI-TOF mass spectrometry and NMR spectroscopy-effects of freezing and thawing. Chem Phys Lipids 106:145-156. doi: 10.1016/S0009-3084(00)00148-1
    • (2000) Chem Phys Lipids , vol.106 , pp. 145-156
    • Schiller, J.1    Arnhold, J.2    Glander, H.J.3
  • 130
    • 0000599990 scopus 로고    scopus 로고
    • Sperm viability is influenced in vitro by the bovine seminal protein a SFP: Effects on motility, mitochondrial activity and lipid peroxidation
    • doi: 10.1016/0093-691X(95)00409-2
    • Schöneck C, Braun J, Einspanier R (1996) Sperm viability is influenced in vitro by the bovine seminal protein a SFP: Effects on motility, mitochondrial activity and lipid peroxidation. Theriogenology 45:633-642. doi: 10.1016/0093-691X(95)00409-2
    • (1996) Theriogenology , vol.45 , pp. 633-642
    • Schöneck, C.1    Braun, J.2    Einspanier, R.3
  • 131
    • 0034784738 scopus 로고    scopus 로고
    • Cryopreservation of fractionated, highly motile human spermatozoa: Effect on membrane phosphatidylserine externalization and lipid peroxidation
    • doi: 10.1093/humrep/16.10.2148
    • Schuffner A, Morshedi M, Oehninger S (2001) Cryopreservation of fractionated, highly motile human spermatozoa: Effect on membrane phosphatidylserine externalization and lipid peroxidation. Hum Reprod 16:2148-2153. doi: 10.1093/humrep/16.10.2148
    • (2001) Hum Reprod , vol.16 , pp. 2148-2153
    • Schuffner, A.1    Morshedi, M.2    Oehninger, S.3
  • 132
    • 0036732941 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase
    • doi: 10.1091/mbc.E02-04-0185
    • Smith EF (2002) Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase. Mol Biol Cell 13:3303-3313. doi: 10.1091/mbc.E02-04-0185
    • (2002) Mol Biol Cell , vol.13 , pp. 3303-3313
    • Smith, E.F.1
  • 133
    • 0344110314 scopus 로고    scopus 로고
    • Long-term effects of the cryopreservation of turbot (Psetta maxima) spermatozoa
    • doi: 10.1016/S0990-7440(99)80030-8
    • Suquet M, Dreanno C, Petton B et al (1998) Long-term effects of the cryopreservation of turbot (Psetta maxima) spermatozoa. Aquat Living Resour 11:45-48. doi: 10.1016/S0990-7440(99)80030-8
    • (1998) Aquat Living Resour , vol.11 , pp. 45-48
    • Suquet, M.1    Dreanno, C.2    Petton, B.3
  • 134
    • 0034072183 scopus 로고    scopus 로고
    • Cryopreservation of sperm in marine fish
    • doi: 10.1046/j.1365-2109.2000.00445.x
    • Suquet M, Dreanno C, Fauvel C et al (2000) Cryopreservation of sperm in marine fish. Aquacult Res 31:231-243. doi: 10.1046/ j.1365-2109.2000.00445.x
    • (2000) Aquacult Res , vol.31 , pp. 231-243
    • Suquet, M.1    Dreanno, C.2    Fauvel, C.3
  • 135
    • 0033568919 scopus 로고    scopus 로고
    • 2+ release at fertilization in mammals
    • doi:10.1002/ (SICI)1097-010X(19991015)285:3<267::AID-JEZ10>3.0.CO;2-P
    • 2+ release at fertilization in mammals. J Exp Zool 285:267-275. doi:10.1002/ (SICI)1097-010X(19991015)285:3<267::AID-JEZ10>3.0.CO;2-P
    • (1999) J Exp Zool , vol.285 , pp. 267-275
    • Swann, K.1    Parrington, J.2
  • 136
    • 70349514970 scopus 로고
    • + concentration caused by external osmolality change regulates sperm motility of marine and freshwater teleosts
    • + concentration caused by external osmolality change regulates sperm motility of marine and freshwater teleosts. J Cell Biol 126:737-745
    • (1995) J Cell Biol , vol.126 , pp. 737-745
    • Takai, H.1    Morisawa, M.2
  • 137
    • 0027937829 scopus 로고
    • Implication that potassium flux and increase in intracellular calcium are necessary for the initiation of sperm motility in salmonid fishes
    • doi: 10.1002/mrd.1080390409
    • Tanimoto S, Kudo R, Nagazawa T et al (1994) Implication that potassium flux and increase in intracellular calcium are necessary for the initiation of sperm motility in salmonid fishes. Mol Reprod Dev 39:409-414. doi: 10.1002/mrd.1080390409
    • (1994) Mol Reprod Dev , vol.39 , pp. 409-414
    • Tanimoto, S.1    Kudo, R.2    Nagazawa, T.3
  • 138
    • 0001011751 scopus 로고
    • The oxidative metabolism of pyruvate, acetate and glucose in isolated fish spermatozoa
    • doi: 10.1002/jcp.1030620303
    • Terner C, Korsh G (1963) The oxidative metabolism of pyruvate, acetate and glucose in isolated fish spermatozoa. J Cell Comp Physiol 62:243-249. doi: 10.1002/jcp.1030620303
    • (1963) J Cell Comp Physiol , vol.62 , pp. 243-249
    • Terner, C.1    Korsh, G.2
  • 139
    • 3643108115 scopus 로고
    • The adenosine triphosphatase activity of perch sperm flagella
    • doi: 10.1016/0006-3002(59)90517-7
    • Tibbs J (1959) The adenosine triphosphatase activity of perch sperm flagella. Biochim Biophys Acta 33:220. doi: 10.1016/0006-3002(59)90517-7
    • (1959) Biochim Biophys Acta , vol.33 , pp. 220
    • Tibbs, J.1
  • 140
    • 0001070034 scopus 로고    scopus 로고
    • Binding characteristics and regulation of the 17, 20β, 21-trihydroxy-4-pregnen-3-one (20β-S) receptor on testicular and sperm plasma membranes of spotted seatrout (Cynoscion nebulosus)
    • doi: 10.1023/A:1007781128677
    • Thomas P, Breckenridge-Miller D, Detweiler C (1997) Binding characteristics and regulation of the 17, 20β, 21-trihydroxy-4-pregnen-3-one (20β-S) receptor on testicular and sperm plasma membranes of spotted seatrout (Cynoscion nebulosus). Fish Physiol Biochem 17:109-116. doi: 10.1023/A:1007781128677
    • (1997) Fish Physiol Biochem , vol.17 , pp. 109-116
    • Thomas, P.1    Breckenridge-Miller, D.2    Detweiler, C.3
  • 141
    • 0024698510 scopus 로고
    • Energy transport and cell polarity: Relationship of phosphagen kinase activity to sperm function
    • doi: 10.1002/jez.1402510110
    • Tombes RM, Shapiro BM (1989) Energy transport and cell polarity: relationship of phosphagen kinase activity to sperm function. J Exp Zool 251:82-90. doi: 10.1002/jez.1402510110
    • (1989) J Exp Zool , vol.251 , pp. 82-90
    • Tombes, R.M.1    Shapiro, B.M.2
  • 142
    • 0030872253 scopus 로고    scopus 로고
    • Mammalian fertilization: A carbohydrate-mediated event
    • doi: 10.1095/biolreprod57.3.487
    • Tulsiani DRP, Yoshida-Komiya H, Araki Y (1997) Mammalian fertilization: a carbohydrate-mediated event. Biol Reprod 57:487-494. doi: 10.1095/ biolreprod57.3.487
    • (1997) Biol Reprod , vol.57 , pp. 487-494
    • Tulsiani, D.R.P.1    Yoshida-Komiya, H.2    Araki, Y.3
  • 143
    • 0037285863 scopus 로고    scopus 로고
    • Protein phosphorylation in mammalian spermatozoa
    • doi: 10.1530/rep.0.1250017
    • Urner F, Sakkas D (2003) Protein phosphorylation in mammalian spermatozoa. Reproduction 125:17-26. doi: 10.1530/rep.0.1250017
    • (2003) Reproduction , vol.125 , pp. 17-26
    • Urner, F.1    Sakkas, D.2
  • 144
    • 0037133349 scopus 로고    scopus 로고
    • Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange
    • doi: 10.1073/pnas.042700899
    • Vines CA, Yoshida M, Griffin FJ et al (2002) Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange. Proc Natl Acad Sci USA 99:2026-2031. doi: 10.1073/pnas.042700899
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2026-2031
    • Vines, C.A.1    Yoshida, M.2    Griffin, F.J.3
  • 145
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. 1. Correlation between the capacitation state and protein-tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD et al (1995a) Capacitation of mouse spermatozoa. 1. Correlation between the capacitation state and protein-tyrosine phosphorylation. Development 121:1129-1137
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3
  • 146
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. 2. Protein-tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Baley JL et al (1995b) Capacitation of mouse spermatozoa. 2. 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    Baley, J.L.3
  • 147
    • 0029148377 scopus 로고
    • Carnitine supplementation in human idiopathic asthenospermia: Clinical results
    • Vitali G, Parente R, Melotti C (1995) Carnitine supplementation in human idiopathic asthenospermia: Clinical results. Drugs Exp Clin Res 21:157-159
    • (1995) Drugs Exp Clin Res , vol.21 , pp. 157-159
    • Vitali, G.1    Parente, R.2    Melotti, C.3
  • 148
    • 0022372552 scopus 로고
    • Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer
    • doi: 10.1083/jcb.101.6.2324
    • Ward GE, Brokaw CJ, Garbers DL et al (1985) Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer. J Cell Biol 101:2324-2329. doi: 10.1083/jcb.101.6.2324
    • (1985) J Cell Biol , vol.101 , pp. 2324-2329
    • Ward, G.E.1    Brokaw, C.J.2    Garbers, D.L.3
  • 149
    • 0035116159 scopus 로고    scopus 로고
    • Assessment of fibronectin as a potential new clinical tool in andrology
    • doi: 10.1046/j.1439-0272.2001.00370.x
    • Wennemuth ED, Meinhardt A, Mallidis C et al (2001) Assessment of fibronectin as a potential new clinical tool in andrology. Andrologia 33:43-46. doi: 10.1046/j.1439-0272.2001.00370.x
    • (2001) Andrologia , vol.33 , pp. 43-46
    • Wennemuth, E.D.1    Meinhardt, A.2    Mallidis, C.3
  • 150
    • 18144417868 scopus 로고    scopus 로고
    • Transferrin and antiproteases are major proteins of common carp seminal plasma
    • doi: 10.1016/j.fsi.2005.01.009
    • Wojtczak M, Dietrich GJ, Ciereszko A (2005) Transferrin and antiproteases are major proteins of common carp seminal plasma. Fish Shellfish Immunol 19:387-391. doi: 10.1016/j.fsi.2005.01.009
    • (2005) Fish Shellfish Immunol , vol.19 , pp. 387-391
    • Wojtczak, M.1    Dietrich, G.J.2    Ciereszko, A.3
  • 151
    • 35548988833 scopus 로고    scopus 로고
    • Isolation and characterization of α1-proteinase inhibitor from common carp (Cyprinus carpio) seminal plasma
    • doi: 10.1016/j.cbpb.2007.06.004
    • Wojtczak M, Calka J, Glogowski J et al (2007) Isolation and characterization of α1-proteinase inhibitor from common carp (Cyprinus carpio) seminal plasma. Comp Biochem Physiol B 148:264-276. doi: 10.1016/j.cbpb.2007.06.004
    • (2007) Comp Biochem Physiol B , vol.148 , pp. 264-276
    • Wojtczak, M.1    Calka, J.2    Glogowski, J.3
  • 152
    • 0001295304 scopus 로고
    • Physiology of fertilization in fish eggs
    • doi: 10.1016/S0074-7696(08)60545-8
    • Yamamoto TO (1961) Physiology of fertilization in fish eggs. Int Rev Cytol 12:361-405. doi: 10.1016/S0074-7696(08)60545-8
    • (1961) Int Rev Cytol , vol.12 , pp. 361-405
    • Yamamoto, T.O.1
  • 153
    • 0032918229 scopus 로고    scopus 로고
    • Purification and characterization of prolyl endopeptidase from the Pacific herring, Clupea pallasi, and its role in the activation of sperm motility
    • doi: 10.1046/j.1440-169x.1999.00424.x
    • Yoshida K, Inaba K, Ohtake H et al (1999) Purification and characterization of prolyl endopeptidase from the Pacific herring, Clupea pallasi, and its role in the activation of sperm motility. Dev Growth Differ 41:217-225. doi: 10.1046/j.1440-169x.1999.00424.x
    • (1999) Dev Growth Differ , vol.41 , pp. 217-225
    • Yoshida, K.1    Inaba, K.2    Ohtake, H.3
  • 154
    • 0035874983 scopus 로고    scopus 로고
    • Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis
    • doi: 10.1006/geno.2001.6556
    • Yousef GM, Diamandis M, Jung K et al (2001) Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis. Genomics 74:385-395. doi: 10.1006/geno.2001.6556
    • (2001) Genomics , vol.74 , pp. 385-395
    • Yousef, G.M.1    Diamandis, M.2    Jung, K.3
  • 155
    • 2642571711 scopus 로고    scopus 로고
    • Adenosine triphosphate concentration and β-d-glucuronidase activity as indicators of sea bass semen quality
    • doi: 10.1095/biolreprod.103.027177
    • Zilli L, Schiavone R, Zonno V et al (2004) Adenosine triphosphate concentration and β-d-glucuronidase activity as indicators of sea bass semen quality. Biol Reprod 70:1679-1684. doi: 10.1095/ biolreprod.103.027177
    • (2004) Biol Reprod , vol.70 , pp. 1679-1684
    • Zilli, L.1    Schiavone, R.2    Zonno, V.3
  • 156
    • 17444408481 scopus 로고    scopus 로고
    • Effect of cryopreservation on sea bass sperm proteins
    • doi: 10.1095/biolreprod.104.036202
    • Zilli L, Schiavone R, Zonno V et al (2005) Effect of cryopreservation on sea bass sperm proteins. Biol Reprod 72:1262-1267. doi: 10.1095/ biolreprod.104.036202
    • (2005) Biol Reprod , vol.72 , pp. 1262-1267
    • Zilli, L.1    Schiavone, R.2    Zonno, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.