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Volumn 15, Issue 1, 2014, Pages

A comprehensive proteomic approach to identifying capacitation related proteins in boar spermatozoa

Author keywords

2DE; Boar; Capacitation; Proteomics; Spermatozoa

Indexed keywords

ACROSIN; APOLIPOPROTEIN A1; PEPTIDES AND PROTEINS; PEROXIREDOXIN 5; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE E1 SUBUNIT BETA; RAB PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE 1 BETA SUBCOMPLEX 6; ROPPORIN 1A; SPERMADHESIN AWN; SUCCINATE COENZYME A LIGASE; SUCCINATE COENZYME A LIGASE BETA; UNCLASSIFIED DRUG;

EID: 84964315197     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-15-897     Document Type: Article
Times cited : (118)

References (68)
  • 2
    • 0026786016 scopus 로고
    • Ca2+-related changes in the mouse sperm capacitation state: a possible role for Ca2+-ATPase
    • Fraser LR, McDermott A: Ca2+-related changes in the mouse sperm capacitation state: a possible role for Ca2+-ATPase. J Reprod Fertil 1992, 96:363-377.
    • (1992) J Reprod Fertil , vol.96 , pp. 363-377
    • Fraser, L.R.1    McDermott, A.2
  • 3
    • 0029789196 scopus 로고    scopus 로고
    • Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa
    • Luconi M, Krausz C, Forti G, Baldi E: Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa. Biol Reprod 1996, 55:207-216.
    • (1996) Biol Reprod , vol.55 , pp. 207-216
    • Luconi, M.1    Krausz, C.2    Forti, G.3    Baldi, E.4
  • 4
    • 29844448212 scopus 로고    scopus 로고
    • Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel
    • Kirichok Y, Navarro B, Clapham DE: Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel. Nature 2006, 439:737-740.
    • (2006) Nature , vol.439 , pp. 737-740
    • Kirichok, Y.1    Navarro, B.2    Clapham, D.E.3
  • 5
    • 34547231222 scopus 로고    scopus 로고
    • A sperm specific Na+/H+ exchanger (sNHE) is critical for expression and in vivo bicarbonate regulation of the soluble adenylyl cyclase (sAC)
    • Wang D, Hu J, Bobulescu IA, Quill TA, McLeroy P, Moe OW, Garbers DL: A sperm specific Na+/H+ exchanger (sNHE) is critical for expression and in vivo bicarbonate regulation of the soluble adenylyl cyclase (sAC). Proc Natl Acad Sci U S A 2007, 104:9325-9330.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9325-9330
    • Wang, D.1    Hu, J.2    Bobulescu, I.A.3    Quill, T.A.4    McLeroy, P.5    Moe, O.W.6    Garbers, D.L.7
  • 6
    • 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, 52:463-472.
    • (2008) Int J Dev Biol , vol.52 , pp. 463-472
    • Arcelay, E.1    Salicioni, A.M.2    Wertheimer, E.3    Visconti, P.E.4
  • 7
    • 42949094171 scopus 로고    scopus 로고
    • Bicarbonate induced phosphorylation of p270 protein in mouse sperm by cAMP-dependent protein kinase
    • Kaneto M, Krisfalusi M, Eddy EM, O'Brien DA, Miki K: Bicarbonate induced phosphorylation of p270 protein in mouse sperm by cAMP-dependent protein kinase. Mol Reprod Dev 2008, 75:1045-1053.
    • (2008) Mol Reprod Dev , vol.75 , pp. 1045-1053
    • Kaneto, M.1    Krisfalusi, M.2    Eddy, E.M.3    O'Brien, D.A.4    Miki, K.5
  • 8
    • 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 U S A 2009, 106:667-668.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 667-668
    • Visconti, P.E.1
  • 10
    • 84873287245 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are a key factor of male fertility
    • Kwon WS, Park YJ, El SA M, Pang MG: Voltage-dependent anion channels are a key factor of male fertility. Fertil Steril 2013, 99:354-361.
    • (2013) Fertil Steril , vol.99 , pp. 354-361
    • Kwon, W.S.1    Park, Y.J.2    El Sa, M.3    Pang, M.G.4
  • 11
    • 36949091315 scopus 로고
    • Fertilizing capacity of spermatozoa deposited into the fallopian tubes
    • Chang MC: Fertilizing capacity of spermatozoa deposited into the fallopian tubes. Nature 1951, 168:697-698.
    • (1951) Nature , vol.168 , pp. 697-698
    • Chang, M.C.1
  • 12
    • 76949114656 scopus 로고
    • Observations on the penetration of the sperm in the mammalian egg
    • Austin CR: Observations on the penetration of the sperm in the mammalian egg. Aust J Sci Res B 1951, 4:581-596.
    • (1951) Aust J Sci Res B , vol.4 , pp. 581-596
    • Austin, C.R.1
  • 14
    • 76649131265 scopus 로고    scopus 로고
    • Analysis of proteomic changes associated with sperm capacitation through the combined use of IPG-strip pre-fractionation followed by RP chromatography LC-MS/MS analysis
    • Baker MA, Reeves G, Hetherington L, Aitken RJ: Analysis of proteomic changes associated with sperm capacitation through the combined use of IPG-strip pre-fractionation followed by RP chromatography LC-MS/MS analysis. Proteomics 2010, 10:482-495.
    • (2010) Proteomics , vol.10 , pp. 482-495
    • Baker, M.A.1    Reeves, G.2    Hetherington, L.3    Aitken, R.J.4
  • 15
    • 65349100504 scopus 로고    scopus 로고
    • Tyrosine phosphoproteome of hamster spermatozoa: role of glycerol-3-phosphate dehydrogenase 2 in sperm capacitation
    • Kota V, Dhople VM, Shivaji S: Tyrosine phosphoproteome of hamster spermatozoa: role of glycerol-3-phosphate dehydrogenase 2 in sperm capacitation. Proteomics 2009, 9:1809-1826.
    • (2009) Proteomics , vol.9 , pp. 1809-1826
    • Kota, V.1    Dhople, V.M.2    Shivaji, S.3
  • 17
    • 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, 123:40-47.
    • (2011) Anim Reprod Sci , vol.123 , pp. 40-47
    • Jagan Mohanarao, G.1    Atreja, S.K.2
  • 18
    • 33750202016 scopus 로고    scopus 로고
    • Towards a better understanding of RNA carriage by ejaculate spermatozoa
    • Miller D, Ostermeier GC: Towards a better understanding of RNA carriage by ejaculate spermatozoa. Hum Reprod Update 2006, 12:757-767.
    • (2006) Hum Reprod Update , vol.12 , pp. 757-767
    • Miller, D.1    Ostermeier, G.C.2
  • 19
    • 39149143310 scopus 로고    scopus 로고
    • Protein synthesis in sperm: dialog between mitochondria and cytoplasm
    • Gur Y, Breitbart H: Protein synthesis in sperm: dialog between mitochondria and cytoplasm. Mol Cell Endocrinol 2008, 282:45-55.
    • (2008) Mol Cell Endocrinol , vol.282 , pp. 45-55
    • Gur, Y.1    Breitbart, H.2
  • 21
    • 84892886192 scopus 로고    scopus 로고
    • Protein degradation and phosphorylation after freeze thawing result in spermatozoon dysfunction
    • Yuan J: Protein degradation and phosphorylation after freeze thawing result in spermatozoon dysfunction. Proteomics 2014, 14:155-156.
    • (2014) Proteomics , vol.14 , pp. 155-156
    • Yuan, J.1
  • 24
    • 58149196450 scopus 로고    scopus 로고
    • Breeding soundness evaluation and semen analysis for predicting bull fertility
    • Kastelic JP, Thundathil JC: Breeding soundness evaluation and semen analysis for predicting bull fertility. Reprod Domest Anim 2008, 43:368-373.
    • (2008) Reprod Domest Anim , vol.43 , pp. 368-373
    • Kastelic, J.P.1    Thundathil, J.C.2
  • 25
    • 0023760807 scopus 로고
    • Relationships between computerized measurements of motion of frozen-thawed bull spermatozoa and fertility
    • Budworth PR, Amann RP, Chapman PL: Relationships between computerized measurements of motion of frozen-thawed bull spermatozoa and fertility. J Androl 1988, 9:41-54.
    • (1988) J Androl , vol.9 , pp. 41-54
    • Budworth, P.R.1    Amann, R.P.2    Chapman, P.L.3
  • 26
    • 0025471846 scopus 로고
    • Determination of the relationship between sperm morphologic classifications and fertility in stallions: 66 cases (1987-1988)
    • Jasko DJ, Lein DH, Foote RH: Determination of the relationship between sperm morphologic classifications and fertility in stallions: 66 cases (1987-1988). J Am Vet Med Assoc 1990, 197:389-394.
    • (1990) J Am Vet Med Assoc , vol.197 , pp. 389-394
    • Jasko, D.J.1    Lein, D.H.2    Foote, R.H.3
  • 27
    • 0345189505 scopus 로고    scopus 로고
    • Fertility and its relationship to motility characteristics of spermatozoa in ewes after cervical, transcervical, and intrauterine insemination with frozen-thawed ram semen
    • Sánchez-Partida LG, Windsor DP, Eppleston J, Setchell BP, Maxwell WM: Fertility and its relationship to motility characteristics of spermatozoa in ewes after cervical, transcervical, and intrauterine insemination with frozen-thawed ram semen. J Androl 1999, 20:280-288.
    • (1999) J Androl , vol.20 , pp. 280-288
    • Sánchez-Partida, L.G.1    Windsor, D.P.2    Eppleston, J.3    Setchell, B.P.4    Maxwell, W.M.5
  • 28
    • 77954456845 scopus 로고    scopus 로고
    • Capacitation status of stored boar spermatozoa is related to litter size of sows
    • Oh SA, Park YJ, You YA, Mohamed EA, Pang MG: Capacitation status of stored boar spermatozoa is related to litter size of sows. Anim Reprod Sci 2010, 121:131-138.
    • (2010) Anim Reprod Sci , vol.121 , pp. 131-138
    • Oh, S.A.1    Park, Y.J.2    You, Y.A.3    Mohamed, E.A.4    Pang, M.G.5
  • 29
    • 77954413887 scopus 로고    scopus 로고
    • The sperm penetration assay predicts the litter size in pigs
    • Oh SA, You YA, Park YJ, Pang MG: The sperm penetration assay predicts the litter size in pigs. Int J Androl 2010, 33:604-612.
    • (2010) Int J Androl , vol.33 , pp. 604-612
    • Oh, S.A.1    You, Y.A.2    Park, Y.J.3    Pang, M.G.4
  • 30
    • 34547830245 scopus 로고    scopus 로고
    • Is sperm evaluation useful in predicting human fertility?
    • Lewis SE: Is sperm evaluation useful in predicting human fertility? Reproduction 2007, 34:31-40.
    • (2007) Reproduction , vol.34 , pp. 31-40
    • Lewis, S.E.1
  • 31
    • 84864599925 scopus 로고    scopus 로고
    • Fertility-related proteomic profiling bull spermatozoa separated by percoll
    • Park YJ, Kwon WS, Oh SA, Pang MG: Fertility-related proteomic profiling bull spermatozoa separated by percoll. J Proteome Res 2012, 11:4162-4168.
    • (2012) J Proteome Res , vol.11 , pp. 4162-4168
    • Park, Y.J.1    Kwon, W.S.2    Oh, S.A.3    Pang, M.G.4
  • 32
    • 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, Memili E: 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    Memili, E.6
  • 34
    • 43249115593 scopus 로고    scopus 로고
    • The role of proteomics in understanding sperm cell biology
    • Aitken RJ, Baker MA: The role of proteomics in understanding sperm cell biology. Int J Androl 2008, 31:295-302.
    • (2008) Int J Androl , vol.31 , pp. 295-302
    • Aitken, R.J.1    Baker, M.A.2
  • 35
    • 32644435333 scopus 로고    scopus 로고
    • Mammalian sperm translate nuclear-encoded proteins by mitochondrial-type ribosomes
    • Gur Y, Breitbart H: Mammalian sperm translate nuclear-encoded proteins by mitochondrial-type ribosomes. Genes Dev 2006, 15:411-416.
    • (2006) Genes Dev , vol.15 , pp. 411-416
    • Gur, Y.1    Breitbart, H.2
  • 36
    • 48749124899 scopus 로고    scopus 로고
    • RAB2A: a major subacrosomal protein of bovine spermatozoa implicated in acrosomal biogenesis
    • Mountjoy JR, Xu W, McLeod D, Hyndman D, Oko R: RAB2A: a major subacrosomal protein of bovine spermatozoa implicated in acrosomal biogenesis. Biol Reprod 2008, 79:223-232.
    • (2008) Biol Reprod , vol.79 , pp. 223-232
    • Mountjoy, J.R.1    Xu, W.2    McLeod, D.3    Hyndman, D.4    Oko, R.5
  • 37
    • 0035798385 scopus 로고    scopus 로고
    • Evolution of the Rab family of small GTP-binding proteins
    • Pereira-Leal JB, Seabra MC: Evolution of the Rab family of small GTP-binding proteins. J Mol Biol 2001, 313:889-901.
    • (2001) J Mol Biol , vol.313 , pp. 889-901
    • Pereira-Leal, J.B.1    Seabra, M.C.2
  • 39
    • 84896738692 scopus 로고    scopus 로고
    • Fucose, mannose, and ß-N-acetylglucosamine glycopolymers initiate the mouse sperm acrosome reaction through convergent signaling pathways
    • Wu L, Sampson NS: Fucose, mannose, and ß-N-acetylglucosamine glycopolymers initiate the mouse sperm acrosome reaction through convergent signaling pathways. ACS Chem Biol 2014, 9:468-475.
    • (2014) ACS Chem Biol , vol.9 , pp. 468-475
    • Wu, L.1    Sampson, N.S.2
  • 42
    • 33644670813 scopus 로고    scopus 로고
    • Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteinerich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase
    • Maiorino M, Roveri A, Benazzi L, Bosello V, Mauri P, Toppo S, Tosatto SC, Ursini F: Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteinerich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase. J Biol Chem 2005, 280:38395-38402.
    • (2005) J Biol Chem , vol.280 , pp. 38395-38402
    • Maiorino, M.1    Roveri, A.2    Benazzi, L.3    Bosello, V.4    Mauri, P.5    Toppo, S.6    Tosatto, S.C.7    Ursini, F.8
  • 43
    • 0036720422 scopus 로고    scopus 로고
    • Male fertility is linked to the selenoprotein phospholipid hydroperoxide glutathione peroxidase
    • Foresta C, Flohé L, Garolla A, Roveri A, Ursini F, Maiorino M: Male fertility is linked to the selenoprotein phospholipid hydroperoxide glutathione peroxidase. Biol Reprod 2002, 67:967-971.
    • (2002) Biol Reprod , vol.67 , pp. 967-971
    • Foresta, C.1    Flohé, L.2    Garolla, A.3    Roveri, A.4    Ursini, F.5    Maiorino, M.6
  • 45
    • 0022969384 scopus 로고
    • Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex
    • Jilka JM, Rahmatulla M, Roche TE: Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex. J Biol Chem 1986, 261:1858-1867.
    • (1986) J Biol Chem , vol.261 , pp. 1858-1867
    • Jilka, J.M.1    Rahmatulla, M.2    Roche, T.E.3
  • 47
    • 0037501375 scopus 로고    scopus 로고
    • Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation
    • Ficarro S, Chertihin O, Westbrook VA, White F, Jayes F, Kalab P, Marto JA, Shabanowitz J, Herr JC, Hunt DF, Visconti PE: Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. J Biol Chem 2003, 278:11579-11589.
    • (2003) J Biol Chem , vol.278 , pp. 11579-11589
    • Ficarro, S.1    Chertihin, O.2    Westbrook, V.A.3    White, F.4    Jayes, F.5    Kalab, P.6    Marto, J.A.7    Shabanowitz, J.8    Herr, J.C.9    Hunt, D.F.10    Visconti, P.E.11
  • 50
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee SG, Chae HZ, Kim K: Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 2005, 38:1543-1552.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 51
    • 78751689485 scopus 로고    scopus 로고
    • Hydrogen peroxide modifies human sperm peroxiredoxins in a dose-dependent manner
    • O'Flaherty C, de Souza AR: Hydrogen peroxide modifies human sperm peroxiredoxins in a dose-dependent manner. Biol Reprod 2011, 84:238-247.
    • (2011) Biol Reprod , vol.84 , pp. 238-247
    • O'Flaherty, C.1    de Souza, A.R.2
  • 52
    • 34447312189 scopus 로고    scopus 로고
    • Multiple proteins present in purified porcine sperm apical plasma membranes interact with the zona pellucida of the oocyte
    • van Gestel RA, Brewis IA, Ashton PR, Brouwers JF, Gadella BM: Multiple proteins present in purified porcine sperm apical plasma membranes interact with the zona pellucida of the oocyte. Mol Hum Reprod 2007, 13:445-454.
    • (2007) Mol Hum Reprod , vol.13 , pp. 445-454
    • van Gestel, R.A.1    Brewis, I.A.2    Ashton, P.R.3    Brouwers, J.F.4    Gadella, B.M.5
  • 53
    • 0025240799 scopus 로고
    • Bovine oviductal fluid components and their potential role in sperm cholesterol efflux
    • Ehrenwald E, Foote RH, Parks JE: Bovine oviductal fluid components and their potential role in sperm cholesterol efflux. Mol Reprod Dev 1990, 25:195-204.
    • (1990) Mol Reprod Dev , vol.25 , pp. 195-204
    • Ehrenwald, E.1    Foote, R.H.2    Parks, J.E.3
  • 55
    • 0036740048 scopus 로고    scopus 로고
    • The role of cholesterol efflux in regulating the fertilization potential of mammalian spermatozoa
    • Travis AJ, Kopf GS: The role of cholesterol efflux in regulating the fertilization potential of mammalian spermatozoa. J Clin Invest 2002, 110:731-736.
    • (2002) J Clin Invest , vol.110 , pp. 731-736
    • Travis, A.J.1    Kopf, G.S.2
  • 56
    • 0030827648 scopus 로고    scopus 로고
    • Major proteins of bovine seminal plasma modulate sperm capacitation by high-density lipoprotein
    • Thérien I, Soubeyrand S, Manjunath P: Major proteins of bovine seminal plasma modulate sperm capacitation by high-density lipoprotein. Biol Reprod 1997, 57:1080-1088.
    • (1997) Biol Reprod , vol.57 , pp. 1080-1088
    • Thérien, I.1    Soubeyrand, S.2    Manjunath, P.3
  • 57
    • 84887260860 scopus 로고    scopus 로고
    • Proteomic revolution to improve tools for evaluating male fertility in animals
    • Park YJ, Kim J, You YA, Pang MG: Proteomic revolution to improve tools for evaluating male fertility in animals. J Proteome Res 2013, 12:4738-4747.
    • (2013) J Proteome Res , vol.12 , pp. 4738-4747
    • Park, Y.J.1    Kim, J.2    You, Y.A.3    Pang, M.G.4
  • 58
    • 0019364045 scopus 로고
    • A glycolytic product is obligatory for initiation of the sperm acrosome reaction and whiplash motility required for fertilization in the mouse
    • Fraser LR, Quinn PJ: A glycolytic product is obligatory for initiation of the sperm acrosome reaction and whiplash motility required for fertilization in the mouse. J Reprod Fertil 1981, 61:25-35.
    • (1981) J Reprod Fertil , vol.61 , pp. 25-35
    • Fraser, L.R.1    Quinn, P.J.2
  • 59
    • 84881664329 scopus 로고    scopus 로고
    • Acrosin-binding protein (ACRBP) and triosephosphate isomerase (TPI) are good markers to predict boar sperm freezing capacity
    • Vilagran I, Castillo J, Bonet S, Sancho S, Yeste M, Estanyol JM, Oliva R: Acrosin-binding protein (ACRBP) and triosephosphate isomerase (TPI) are good markers to predict boar sperm freezing capacity. Theriogenology 2013, 80:443-450.
    • (2013) Theriogenology , vol.80 , pp. 443-450
    • Vilagran, I.1    Castillo, J.2    Bonet, S.3    Sancho, S.4    Yeste, M.5    Estanyol, J.M.6    Oliva, R.7
  • 60
    • 0033955805 scopus 로고    scopus 로고
    • Ropporin, a sperm-specific binding protein of rhophilin, that is localized in the fibrous sheath of sperm flagella
    • Fujita A, Nakamura K, Kato T, Watanabe N, Ishizaki T, Kimura K, Mizoguchi A, Narumiya S: Ropporin, a sperm-specific binding protein of rhophilin, that is localized in the fibrous sheath of sperm flagella. J Cell Sci 2000, 113:103-112.
    • (2000) J Cell Sci , vol.113 , pp. 103-112
    • Fujita, A.1    Nakamura, K.2    Kato, T.3    Watanabe, N.4    Ishizaki, T.5    Kimura, K.6    Mizoguchi, A.7    Narumiya, S.8
  • 61
    • 79251497651 scopus 로고    scopus 로고
    • Functional expression of ropporin in human testis and ejaculated spermatozoa
    • Chen J, Wang Y, Wei B, Lai Y, Yan Q, Gui Y, Cai Z: Functional expression of ropporin in human testis and ejaculated spermatozoa. J Androl 2011, 32:26-32.
    • (2011) J Androl , vol.32 , pp. 26-32
    • Chen, J.1    Wang, Y.2    Wei, B.3    Lai, Y.4    Yan, Q.5    Gui, Y.6    Cai, Z.7
  • 63
    • 0032324423 scopus 로고    scopus 로고
    • Immunoelectronmicroscopic imaging of spermadhesin AWN epitopes on boar spermatozoa bound in vivo to the zona pellucida
    • Rodríguez-Martinez H, Iborra A, Martínez P, Calvete JJ: Immunoelectronmicroscopic imaging of spermadhesin AWN epitopes on boar spermatozoa bound in vivo to the zona pellucida. Reprod Fertil Dev 1998, 10:491-497.
    • (1998) Reprod Fertil Dev , vol.10 , pp. 491-497
    • Rodríguez-Martinez, H.1    Iborra, A.2    Martínez, P.3    Calvete, J.J.4
  • 65
    • 0028223555 scopus 로고
    • Quantitation of boar spermadhesins in accessory sex gland fluids and on the surface of epididymal, ejaculated and capacitated spermatozoa
    • Dostàlovà Z, Calvete JJ, Sanz L, Töpfer-Petersen E: Quantitation of boar spermadhesins in accessory sex gland fluids and on the surface of epididymal, ejaculated and capacitated spermatozoa. Biochim Biophys Acta 1994, 1200:48-54.
    • (1994) Biochim Biophys Acta , vol.1200 , pp. 48-54
    • Dostàlovà, Z.1    Calvete, J.J.2    Sanz, L.3    Töpfer-Petersen, E.4
  • 66
    • 0033060654 scopus 로고    scopus 로고
    • Sperm chemotaxis
    • Eisenbach M: Sperm chemotaxis. Rev Reprod 1999, 4:56-66.
    • (1999) Rev Reprod , vol.4 , pp. 56-66
    • Eisenbach, M.1


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