메뉴 건너뛰기




Volumn 30, Issue 9, 2013, Pages 1187-1202

Unraveling the sperm proteome and post-genomic pathways associated with sperm nuclear DNA fragmentation

Author keywords

Biomarkers; DNA fragmentation; Proteomics; Sperm

Indexed keywords

BIOLOGICAL MARKER; CELL NUCLEUS DNA; PROTEOME; TRIACYLGLYCEROL;

EID: 84886585755     PISSN: 10580468     EISSN: 15737330     Source Type: Journal    
DOI: 10.1007/s10815-013-0054-6     Document Type: Article
Times cited : (55)

References (112)
  • 1
    • 1242269766 scopus 로고    scopus 로고
    • Male factor infertility: Evaluation and management
    • 15049583
    • Brugh VM, Lipshultz LI. Male factor infertility: evaluation and management. Med Clin North Am. 2004;88:367-85.
    • (2004) Med Clin North Am , vol.88 , pp. 367-385
    • Brugh, V.M.1    Lipshultz, L.I.2
  • 3
    • 0037834778 scopus 로고    scopus 로고
    • Negative effects of increased sperm DNA damage in relation to seminal oxidative stress in men with idiopathic and male factor infertility
    • 12801566
    • Saleh RA, Agarwal A, Nada EA, EI-Tonsy MH, Sharma RK, Meyer A, et al. Negative effects of increased sperm DNA damage in relation to seminal oxidative stress in men with idiopathic and male factor infertility. Fertil Steril. 2003;79(S3):1597-605.
    • (2003) Fertil Steril , vol.79 , Issue.S3 , pp. 1597-1605
    • Saleh, R.A.1    Agarwal, A.2    Nada, E.A.3    Ei-Tonsy, M.H.4    Sharma, R.K.5    Meyer, A.6    Nelson, D.R.7    Thomas, A.J.8
  • 5
    • 0034091122 scopus 로고    scopus 로고
    • Analysis of DNA fragmentation, plasma membrane translocation of phosphatidylserine and oxidative stress in human spermatozoa
    • 10831565 1:CAS:528:DC%2BD3cXksVCluro%3D
    • Barroso G, Morshedi M, Oehninger S. Analysis of DNA fragmentation, plasma membrane translocation of phosphatidylserine and oxidative stress in human spermatozoa. Hum Reprod. 2000;15:1338-44.
    • (2000) Hum Reprod , vol.15 , pp. 1338-1344
    • Barroso, G.1    Morshedi, M.2    Oehninger, S.3
  • 6
    • 0036196244 scopus 로고    scopus 로고
    • Nature of DNA damage in ejaculated human spermatozoa and the possible involvement of apoptosis
    • Sakkas D, Moffatt O, Manicardi GC, Mariethoz E, Tarozzi N, Bizzaro D. Nature of DNA damage in ejaculated human spermatozoa and the possible involvement of apoptosis. Biol Reprod. 2003;66:1061-7.
    • (2003) Biol Reprod , vol.66 , pp. 1061-1067
    • Sakkas, D.1    Moffatt, O.2    Manicardi, G.C.3    Mariethoz, E.4    Tarozzi, N.5    Bizzaro, D.6
  • 7
    • 0033567961 scopus 로고    scopus 로고
    • Abnormal sperm parameters in humans are indicative of an abortive apoptotic mechanism linked to the Fas-mediated pathway
    • 10471320 1:CAS:528:DyaK1MXlsFyhsrk%3D
    • Sakkas D, Mariethoz E, St John JC. Abnormal sperm parameters in humans are indicative of an abortive apoptotic mechanism linked to the Fas-mediated pathway. Exp Cell Res. 1999;251(2):350-5.
    • (1999) Exp Cell Res. , vol.251 , Issue.2 , pp. 350-355
    • Sakkas, D.1    Mariethoz, E.2    St John, J.C.3
  • 8
    • 12844260663 scopus 로고    scopus 로고
    • Sperm DNA integrity and male infertility
    • 15667855
    • O'Brien J, Zini A. Sperm DNA integrity and male infertility. Urology. 2005;65:16-22.
    • (2005) Urology , vol.65 , pp. 16-22
    • O'Brien, J.1    Zini, A.2
  • 9
    • 0038060337 scopus 로고    scopus 로고
    • Sperm DNA fragmentation decreases the pregnancy rate in an assisted reproductive technique
    • 12721180
    • Benchaib M, Braun V, Lornage J, Hadj S, Salle B, Lejeune H, et al. Sperm DNA fragmentation decreases the pregnancy rate in an assisted reproductive technique. Hum Reprod. 2003;18(5):1023-8.
    • (2003) Hum Reprod , vol.18 , Issue.5 , pp. 1023-1028
    • Benchaib, M.1    Braun, V.2    Lornage, J.3    Hadj, S.4    Salle, B.5    Lejeune, H.6    Guérin, J.F.7
  • 10
    • 33845676306 scopus 로고    scopus 로고
    • Sperm DNA integrity assessment in prediction of assisted reproduction technology outcome
    • 16921163 1:CAS:528:DC%2BD28XhtlChtbzN
    • Bungum M, Humaidan P, Axmon A, Spano M, Bungum L, Erenpreiss J, et al. Sperm DNA integrity assessment in prediction of assisted reproduction technology outcome. Hum Reprod. 2007;22:174-9.
    • (2007) Hum Reprod , vol.22 , pp. 174-179
    • Bungum, M.1    Humaidan, P.2    Axmon, A.3    Spano, M.4    Bungum, L.5    Erenpreiss, J.6    Giwercman, A.7
  • 12
    • 46649109138 scopus 로고    scopus 로고
    • Evaluation of nuclear DNA damage in human spermatozoa in men opting for assisted reproduction
    • 18403788 1:CAS:528:DC%2BD1cXlsVeqtLY%3D
    • Shamsi MB, Kumar R, Dada R. Evaluation of nuclear DNA damage in human spermatozoa in men opting for assisted reproduction. Indian J Med Res. 2008;127:115-23.
    • (2008) Indian J Med Res , vol.127 , pp. 115-123
    • Shamsi, M.B.1    Kumar, R.2    Dada, R.3
  • 13
    • 0036069482 scopus 로고    scopus 로고
    • Embryo quality and IVF treatment outcomes may correlate with different sperm comet assay parameters
    • 12093852 1:STN:280:DC%2BD38vhtlylsA%3D%3D
    • Tomsu M, Sharma V, Miller D. Embryo quality and IVF treatment outcomes may correlate with different sperm comet assay parameters. Hum Reprod. 2002;17(7):1856-62.
    • (2002) Hum Reprod , vol.17 , Issue.7 , pp. 1856-1862
    • Tomsu, M.1    Sharma, V.2    Miller, D.3
  • 14
    • 33749993552 scopus 로고    scopus 로고
    • Sperm DNA fragmentation: Paternal effect on early post-implantation embryo development in ART
    • 16793992 1:STN:280:DC%2BD28ngt12ruw%3D%3D
    • Borini A, Tarozzi N, Bizzaro D, Bonu MA, Fava L, Flamigni C, et al. Sperm DNA fragmentation: paternal effect on early post-implantation embryo development in ART. Hum Reprod. 2006;21(11):2876-81.
    • (2006) Hum Reprod , vol.21 , Issue.11 , pp. 2876-2881
    • Borini, A.1    Tarozzi, N.2    Bizzaro, D.3    Bonu, M.A.4    Fava, L.5    Flamigni, C.6    Coticchio, G.7
  • 15
    • 4143065747 scopus 로고    scopus 로고
    • Extent of nuclear DNA damage in ejaculated spermatozoa impacts on blastocyst development after in vitro fertilization
    • 15302287
    • Seli E, Gardner DK, Schoolcraft WB, Moffatt O, Sakkas D. Extent of nuclear DNA damage in ejaculated spermatozoa impacts on blastocyst development after in vitro fertilization. Fertil Steril. 2004;82:378-83.
    • (2004) Fertil Steril , vol.82 , pp. 378-383
    • Seli, E.1    Gardner, D.K.2    Schoolcraft, W.B.3    Moffatt, O.4    Sakkas, D.5
  • 16
    • 84864445196 scopus 로고    scopus 로고
    • Diagnostic evaluation of the infertile male: A committee opinion
    • Practice Committee of American Society for Reproductive Medicine
    • Practice Committee of American Society for Reproductive Medicine. Diagnostic evaluation of the infertile male: a committee opinion. Fertil Steril. 2012;98(2):294-301.
    • (2012) Fertil Steril , vol.98 , Issue.2 , pp. 294-301
  • 17
    • 0019296108 scopus 로고
    • Relation of mammalian sperm chromatin heterogeneity to fertility
    • 7444440 1:CAS:528:DyaL3MXivVGjsg%3D%3D
    • Evenson DP, Darzynkiewicz Z, Melamed MR. Relation of mammalian sperm chromatin heterogeneity to fertility. Science. 1980;210:1131-3.
    • (1980) Science , vol.210 , pp. 1131-1133
    • Evenson, D.P.1    Darzynkiewicz, Z.2    Melamed, M.R.3
  • 19
    • 65549116879 scopus 로고    scopus 로고
    • Are tests of sperm DNA damage clinically useful- pros and cons
    • 19059901 1:CAS:528:DC%2BD1MXlvFOjtbw%3D
    • Zini A, Sigman M. Are tests of sperm DNA damage clinically useful? pros and cons. J Androl. 2009;30(3):219-29.
    • (2009) J Androl , vol.30 , Issue.3 , pp. 219-229
    • Zini, A.1    Sigman, M.2
  • 20
    • 0031951882 scopus 로고    scopus 로고
    • Cytoplasmic extrusion and the switch from creatine kinase B to M isoform are completed by the commencement of epididymal transport in human and stallion spermatozoa
    • 9537287 1:CAS:528:DyaK1cXhs1aisb4%3D
    • Huszar G, Patrizio P, Vigue L, Willets M, Wilker C, Adhoot D, et al. Cytoplasmic extrusion and the switch from creatine kinase B to M isoform are completed by the commencement of epididymal transport in human and stallion spermatozoa. J Androl. 1998;19(1):11-20.
    • (1998) J Androl , vol.19 , Issue.1 , pp. 11-20
    • Huszar, G.1    Patrizio, P.2    Vigue, L.3    Willets, M.4    Wilker, C.5    Adhoot, D.6    Johnson, L.7
  • 21
    • 84876407305 scopus 로고    scopus 로고
    • Novel technologies for selecting the best sperm for in vitro fertilization and intracytoplasmic sperm injection
    • 10.1016/j.fertnstert.2012.12.025
    • Sakkas D. Novel technologies for selecting the best sperm for in vitro fertilization and intracytoplasmic sperm injection. Fertil Steril. 2013. doi: 10.1016/j.fertnstert.2012.12.025.
    • (2013) Fertil Steril
    • Sakkas, D.1
  • 22
    • 0000212362 scopus 로고
    • Regulation of Spermatogenesis
    • E. Knobil J.D. Neil (eds) 2 Raven Press, Ltd. New York
    • Sharpe RM. Regulation of Spermatogenesis. In: Knobil E, Neil JD, editors. The physiology of reproduction. 2nd ed. New York: Raven Press, Ltd.; 1994. p. 1363-434.
    • (1994) The Physiology of Reproduction , pp. 1363-1434
    • Sharpe, R.M.1
  • 23
    • 0036107443 scopus 로고    scopus 로고
    • Detection of apoptotic alterations in sperm in subfertile patients and their correlations with sperm quality
    • 11980750
    • Shen HM, Dai J, Chia SE, Lim A, Ong CN. Detection of apoptotic alterations in sperm in subfertile patients and their correlations with sperm quality. Hum Reprod. 2002;17(5):1266-73.
    • (2002) Hum Reprod , vol.17 , Issue.5 , pp. 1266-1273
    • Shen, H.M.1    Dai, J.2    Chia, S.E.3    Lim, A.4    Ong, C.N.5
  • 24
    • 84870659836 scopus 로고    scopus 로고
    • Types, causes, detection and repair of DNA fragmentation in animal and human sperm cells
    • 23203048
    • González-Marín C, Gosálvez J, Roy R. Types, causes, detection and repair of DNA fragmentation in animal and human sperm cells. Int J Mol Sci. 2012;13(11):14026-52.
    • (2012) Int J Mol Sci , vol.13 , Issue.11 , pp. 14026-14052
    • González-Marín, C.1    Gosálvez, J.2    Roy, R.3
  • 25
    • 1542723120 scopus 로고    scopus 로고
    • Incidence of Fas positivity and deoxyribonucleic acid double-stranded breaks in human ejaculated sperm
    • 15019807 1:CAS:528:DC%2BD2MXitFGhs70%3D
    • McVicar CM, McClure N, Williamson K, Dalzell LH, Lewis SE. Incidence of Fas positivity and deoxyribonucleic acid double-stranded breaks in human ejaculated sperm. Fertil Steril. 2004;81 Suppl 1:767-74.
    • (2004) Fertil Steril , vol.81 , Issue.SUPPL. 1 , pp. 767-774
    • McVicar, C.M.1    McClure, N.2    Williamson, K.3    Dalzell, L.H.4    Lewis, S.E.5
  • 26
    • 0020856342 scopus 로고
    • Sequence of sperm cell surface differentiation and its relationship to exogenous fluid proteins in the ram epididymis
    • 6640035 1:CAS:528:DyaL2cXitFSjtA%3D%3D
    • Dacheux JL, Voglmayr JK. Sequence of sperm cell surface differentiation and its relationship to exogenous fluid proteins in the ram epididymis. Biol Reprod. 1983;29:1033-46.
    • (1983) Biol Reprod , vol.29 , pp. 1033-1046
    • Dacheux, J.L.1    Voglmayr, J.K.2
  • 29
    • 62449125901 scopus 로고    scopus 로고
    • Effect of leukocytospermia and processing by discontinuous density gradient on sperm nuclear DNA fragmentation and mitochondrial activity
    • 19184399
    • Fariello RM, Del Giudice PT, Spaine DM, Fraietta R, Bertolla RP, Cedenho AP. Effect of leukocytospermia and processing by discontinuous density gradient on sperm nuclear DNA fragmentation and mitochondrial activity. J Assist Reprod Genet. 2009;26:151-7.
    • (2009) J Assist Reprod Genet , vol.26 , pp. 151-157
    • Fariello, R.M.1    Del Giudice, P.T.2    Spaine, D.M.3    Fraietta, R.4    Bertolla, R.P.5    Cedenho, A.P.6
  • 30
    • 50949105076 scopus 로고    scopus 로고
    • Comet assay analysis of single-stranded DNA breaks in circulating leukocytes of glaucoma patients
    • 18769648 1:CAS:528:DC%2BD1cXht1SjsL7E
    • Mozaffarieh M, Schoetzau A, Sauter M, Grieshaber M, Orgül S, Golubnitschaja O, et al. Comet assay analysis of single-stranded DNA breaks in circulating leukocytes of glaucoma patients. Mol Vis. 2008;14:1584-8.
    • (2008) Mol Vis , vol.14 , pp. 1584-1588
    • Mozaffarieh, M.1    Schoetzau, A.2    Sauter, M.3    Grieshaber, M.4    Orgül, S.5    Golubnitschaja, O.6    Flammer, J.7
  • 31
    • 84871217649 scopus 로고    scopus 로고
    • Unbiased label-free quantitative proteomic profiling and enriched proteomic pathways in seminal plasma of adult men before and after varicocelectomy
    • 23042794 1:CAS:528:DC%2BC38XhvVGms77I
    • Camargo M, Intasqui Lopes P, Del Giudice PT, Carvalho VM, Cardozo KH, Andreoni C, et al. Unbiased label-free quantitative proteomic profiling and enriched proteomic pathways in seminal plasma of adult men before and after varicocelectomy. Hum Reprod. 2013;28(1):33-46.
    • (2013) Hum Reprod , vol.28 , Issue.1 , pp. 33-46
    • Camargo, M.1    Intasqui Lopes, P.2    Del Giudice, P.T.3    Carvalho, V.M.4    Cardozo, K.H.5    Andreoni, C.6    Fraietta, R.7    Bertolla, R.P.8
  • 34
    • 77954378406 scopus 로고    scopus 로고
    • Amniotic fluid proteome analysis from down syndrome pregnancies for biomarker discovery
    • 20459121 1:CAS:528:DC%2BC3cXmsVCqurk%3D
    • Cho CK, Smith CR, Diamandis EP. Amniotic fluid proteome analysis from down syndrome pregnancies for biomarker discovery. J Proteome Res. 2010;9(7):3574-82.
    • (2010) J Proteome Res , vol.9 , Issue.7 , pp. 3574-3582
    • Cho, C.K.1    Smith, C.R.2    Diamandis, E.P.3
  • 36
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2.8: New features for data integration and network visualization
    • 21149340 1:CAS:528:DC%2BC3MXhs1GisL0%3D
    • Smoot ME, Ono K, Ruscheinski J, Wang PL, Ideker T. Cytoscape 2.8: new features for data integration and network visualization. Bioinformatics. 2011;27(3):431-2.
    • (2011) Bioinformatics , vol.27 , Issue.3 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3    Wang, P.L.4    Ideker, T.5
  • 38
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • da Huang W, Sherman BT, Lempicki RA. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 2009;37(1):1-13.
    • (2009) Nucleic Acids Res , vol.37 , Issue.1 , pp. 1-13
    • Da Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 39
    • 34249752597 scopus 로고    scopus 로고
    • Extracting biology from high-dimensional biological data
    • 17449816 1:CAS:528:DC%2BD2sXnt1Gku7k%3D
    • Quackenbush J. Extracting biology from high-dimensional biological data. J Exp Biol. 2007;210:1507-17.
    • (2007) J Exp Biol , vol.210 , pp. 1507-1517
    • Quackenbush, J.1
  • 40
    • 84876410606 scopus 로고    scopus 로고
    • The use of genomics, proteomics, and metabolomics in identifying biomarkers of male infertility
    • 10.1016/j.fertnstert.2013.01.111
    • Kovac JR, Pastuszak AW, Lamb DJ. The use of genomics, proteomics, and metabolomics in identifying biomarkers of male infertility. Fertil Steril. 2013. doi: 10.1016/j.fertnstert.2013.01.111.
    • (2013) Fertil Steril
    • Kovac, J.R.1    Pastuszak, A.W.2    Lamb, D.J.3
  • 41
    • 33749426382 scopus 로고    scopus 로고
    • Reactive oxygen species as an independent marker of male factor infertility
    • 17027357 1:CAS:528:DC%2BD28Xht1eht7%2FK
    • Agarwal A, Sharma RK, Nallella KP, Thomas AJ, Alvarez JG, Sikka SC. Reactive oxygen species as an independent marker of male factor infertility. Fertil Steril. 2006;86(4):878-85.
    • (2006) Fertil Steril , vol.86 , Issue.4 , pp. 878-885
    • Agarwal, A.1    Sharma, R.K.2    Nallella, K.P.3    Thomas, A.J.4    Alvarez, J.G.5    Sikka, S.C.6
  • 42
    • 0025040520 scopus 로고
    • Dense fibers protect mammalian sperm against damage
    • 2271730 1:STN:280:DyaK3M7gsFagsw%3D%3D
    • Baltz JM, Williams PO, Cone RA. Dense fibers protect mammalian sperm against damage. Biol Reprod. 1990;43:485-91.
    • (1990) Biol Reprod , vol.43 , pp. 485-491
    • Baltz, J.M.1    Williams, P.O.2    Cone, R.A.3
  • 43
    • 0026322455 scopus 로고
    • Poor development of outer dense fibers as a major cause of tail abnormalities in the spermatozoa of asthenoteratozoospermic men
    • 1770140 1:STN:280:DyaK387itFeqtw%3D%3D
    • Haidl G, Becker A, Henkel R. Poor development of outer dense fibers as a major cause of tail abnormalities in the spermatozoa of asthenoteratozoospermic men. Hum Reprod. 1991;6:1431-8.
    • (1991) Hum Reprod , vol.6 , pp. 1431-1438
    • Haidl, G.1    Becker, A.2    Henkel, R.3
  • 44
    • 0032467365 scopus 로고    scopus 로고
    • Human outer dense fiber gene, ODF2, localizes to chromosome 9q34
    • 10072582 1:CAS:528:DyaK1MXitFCjtb4%3D
    • Shao X, Murthy S, Demetrick DJ, van der Hoorn FA. Human outer dense fiber gene, ODF2, localizes to chromosome 9q34. Cytogenet Cell Genet. 1998;83(3-4):221-3.
    • (1998) Cytogenet Cell Genet , vol.83 , Issue.3-4 , pp. 221-223
    • Shao, X.1    Murthy, S.2    Demetrick, D.J.3    Van Der Hoorn, F.A.4
  • 45
    • 3042592721 scopus 로고    scopus 로고
    • Sperm proteome mapping of a patient who experienced failed fertilization at IVF reveals altered expression of at least 20 proteins compared with fertile donors: Case report
    • 15105389
    • Pixton KL, Deeks ED, Flesch FM, Moseley FL, Björndahl L, Ashton PR, et al. Sperm proteome mapping of a patient who experienced failed fertilization at IVF reveals altered expression of at least 20 proteins compared with fertile donors: case report. Hum Reprod. 2004;19:1438-47.
    • (2004) Hum Reprod , vol.19 , pp. 1438-1447
    • Pixton, K.L.1    Deeks, E.D.2    Flesch, F.M.3    Moseley, F.L.4    Björndahl, L.5    Ashton, P.R.6    Barratt, C.L.7    Brewis, I.A.8
  • 46
    • 43249115593 scopus 로고    scopus 로고
    • The role of proteomics in understanding sperm cell biology
    • 1:CAS:528:DC%2BD1cXnsFOnu7k%3D
    • Aitken RJ, Baker MA. The role of proteomics in understanding sperm cell biology. Int JAndrol. 2008;31:295-302.
    • (2008) Int JAndrol , vol.31 , pp. 295-302
    • Aitken, R.J.1    Baker, M.A.2
  • 47
    • 0037359564 scopus 로고    scopus 로고
    • The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins
    • 12820655 1:CAS:528:DC%2BD3sXjsFWjsL8%3D
    • Fontaine JM, Rest JS, Welsh MJ, Benndorf R. The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins. Cell Stress Chaperones. 2003;8(1):62-9.
    • (2003) Cell Stress Chaperones , vol.8 , Issue.1 , pp. 62-69
    • Fontaine, J.M.1    Rest, J.S.2    Welsh, M.J.3    Benndorf, R.4
  • 48
    • 0036359558 scopus 로고    scopus 로고
    • Small stress proteins: Modulation of intracellular redox state and protection against oxidative stress
    • 11908058 1:CAS:528:DC%2BD38XivVGru78%3D
    • Arrigo AP, Paul C, Ducasse C, Sauvageot O, Kretz-Remy C. Small stress proteins: modulation of intracellular redox state and protection against oxidative stress. Prog Mol Subcell Biol. 2002;28:171-84.
    • (2002) Prog Mol Subcell Biol , vol.28 , pp. 171-184
    • Arrigo, A.P.1    Paul, C.2    Ducasse, C.3    Sauvageot, O.4    Kretz-Remy, C.5
  • 50
    • 0036357776 scopus 로고    scopus 로고
    • Chaperone function of sHsps
    • 11908065 1:CAS:528:DC%2BD38XivVGrurs%3D
    • Haslbeck M, Buchner J. Chaperone function of sHsps. Prog Mol Subcell Biol. 2002;28:37-59.
    • (2002) Prog Mol Subcell Biol , vol.28 , pp. 37-59
    • Haslbeck, M.1    Buchner, J.2
  • 51
    • 84886582414 scopus 로고    scopus 로고
    • Gene Ontology (GO:0050821)
    • Gene Ontology (GO:0050821), http://amigo.geneontology.org/cgi-bin/amigo/ term-details?term=GO:0050821&session-id=5683amigo1336408572
  • 52
    • 20944445990 scopus 로고    scopus 로고
    • Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway
    • 15938716 1:CAS:528:DC%2BD2MXpvF2lt70%3D
    • Nagamori I, Yabuta N, Fujii T, Tanaka H, Yomogida K, Nishimune Y, et al. Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway. Genes Cells. 2005;10(6):575-94.
    • (2005) Genes Cells , vol.10 , Issue.6 , pp. 575-594
    • Nagamori, I.1    Yabuta, N.2    Fujii, T.3    Tanaka, H.4    Yomogida, K.5    Nishimune, Y.6    Nojima, H.7
  • 53
    • 0033064556 scopus 로고    scopus 로고
    • Role of heat shock protein HSP70-2 in spermatogenesis
    • 10051099 1:CAS:528:DyaK1MXhtVeht7s%3D
    • Eddy EM. Role of heat shock protein HSP70-2 in spermatogenesis. Rev Reprod. 1999;4:23-30.
    • (1999) Rev Reprod , vol.4 , pp. 23-30
    • Eddy, E.M.1
  • 54
    • 84870562813 scopus 로고    scopus 로고
    • The molecular chaperone HSPA2 plays a key role in regulating the expression of sperm surface receptors that mediate sperm-egg recognition
    • 23209833 1:CAS:528:DC%2BC38XhvVKqsbjN
    • Redgrove KA, Nixon B, Baker MA, Hetherington L, Baker G, Liu DY, et al. The molecular chaperone HSPA2 plays a key role in regulating the expression of sperm surface receptors that mediate sperm-egg recognition. PLoS One. 2012;7:e50851.
    • (2012) PLoS One , vol.7 , pp. 50851
    • Redgrove, K.A.1    Nixon, B.2    Baker, M.A.3    Hetherington, L.4    Baker, G.5    Liu, D.Y.6    Aitken, R.J.7
  • 55
    • 33751170221 scopus 로고    scopus 로고
    • Expression of the HSPA2 gene in ejaculated spermatozoa from adolescents with and without varicocele
    • 17007855 1:CAS:528:DC%2BD2sXkt1aksg%3D%3D
    • Lima SB, Cenedeze MA, Bertolla RP, Filho PA, Oehninger S, Cedenho AP. Expression of the HSPA2 gene in ejaculated spermatozoa from adolescents with and without varicocele. Fertil Steril. 2006;86(6):1659-963.
    • (2006) Fertil Steril , vol.86 , Issue.6 , pp. 1659-1963
    • Lima, S.B.1    Cenedeze, M.A.2    Bertolla, R.P.3    Filho, P.A.4    Oehninger, S.5    Cedenho, A.P.6
  • 56
    • 1542711820 scopus 로고    scopus 로고
    • Late, but not early, paternal effect on human embryo development is related to sperm DNA fragmentation
    • 14998960 1:CAS:528:DC%2BD2cXhvFSqtrc%3D
    • Tesarik J, Greco E, Mendoza C. Late, but not early, paternal effect on human embryo development is related to sperm DNA fragmentation. Hum Reprod. 2004;19(3):611-5.
    • (2004) Hum Reprod , vol.19 , Issue.3 , pp. 611-615
    • Tesarik, J.1    Greco, E.2    Mendoza, C.3
  • 57
    • 0036041264 scopus 로고    scopus 로고
    • Targeted disruption of the Akap4 gene causes defects in sperm flagellum and motility
    • 12167408 1:CAS:528:DC%2BD38XlvFSqtLo%3D
    • Miki K, Willis WD, Brown PR, Goulding EH, Fulcher KD, Eddy EM. Targeted disruption of the Akap4 gene causes defects in sperm flagellum and motility. Dev Biol. 2002;248(2):331-42.
    • (2002) Dev Biol , vol.248 , Issue.2 , pp. 331-342
    • Miki, K.1    Willis, W.D.2    Brown, P.R.3    Goulding, E.H.4    Fulcher, K.D.5    Eddy, E.M.6
  • 58
    • 79952399131 scopus 로고    scopus 로고
    • Proteomic analysis of seminal plasma from normal volunteers and post-vasectomy patients identifies over 2000 proteins and candidate biomarkers of the urogenital system
    • 21142078 1:CAS:528:DC%2BC3MXhvVymurg%3D
    • Batruch I, Lecker I, Kagedan D, Smith CR, Mullen BJ, Grober E, et al. Proteomic analysis of seminal plasma from normal volunteers and post-vasectomy patients identifies over 2000 proteins and candidate biomarkers of the urogenital system. J Proteome Res. 2011;10(3):941-53.
    • (2011) J Proteome Res , vol.10 , Issue.3 , pp. 941-953
    • Batruch, I.1    Lecker, I.2    Kagedan, D.3    Smith, C.R.4    Mullen, B.J.5    Grober, E.6    Lo, K.C.7    Diamandis, E.P.8    Jarvi, K.A.9
  • 59
    • 0030610318 scopus 로고    scopus 로고
    • Prostasome fraction of human seminal plasma prevents sperm from becoming acrosomally responsive to the agonist progesterone
    • 9202832 1:CAS:528:DyaK2sXks1Sqtrk%3D
    • Cross NL, Mahasreshti P. Prostasome fraction of human seminal plasma prevents sperm from becoming acrosomally responsive to the agonist progesterone. Arch Androl. 1997;39(1):39-44.
    • (1997) Arch Androl , vol.39 , Issue.1 , pp. 39-44
    • Cross, N.L.1    Mahasreshti, P.2
  • 61
    • 81455142498 scopus 로고    scopus 로고
    • Prostasomes: Inhibitors of capacitation and modulators of cellular signalling in human sperm
    • 21029115 1:CAS:528:DC%2BC38XivFOgtrc%3D
    • Pons-Rejraji H, Artonne C, Sion B, Brugnon F, Canis M, Janny L, et al. Prostasomes: inhibitors of capacitation and modulators of cellular signalling in human sperm. Int J Androl. 2011;34:568-80.
    • (2011) Int J Androl , vol.34 , pp. 568-580
    • Pons-Rejraji, H.1    Artonne, C.2    Sion, B.3    Brugnon, F.4    Canis, M.5    Janny, L.6    Grizard, G.7
  • 62
    • 0031828567 scopus 로고    scopus 로고
    • Antioxidant capacity of prostasomes in human semen
    • 9701789 1:CAS:528:DyaK1cXlsVCgsb8%3D
    • Saez F, Motta C, Boucher D, Grizard G. Antioxidant capacity of prostasomes in human semen. Mol Hum Reprod. 1998;4:667-72.
    • (1998) Mol Hum Reprod , vol.4 , pp. 667-672
    • Saez, F.1    Motta, C.2    Boucher, D.3    Grizard, G.4
  • 65
    • 3242759921 scopus 로고    scopus 로고
    • Glycolysis plays a major role for adenosine triphosphate supplementation in mouse sperm flagellar movement
    • 15084484 1:CAS:528:DC%2BD2cXmtFWgur4%3D
    • Mukai C, Okuno M. Glycolysis plays a major role for adenosine triphosphate supplementation in mouse sperm flagellar movement. Biol Reprod. 2004;71(2):540-7.
    • (2004) Biol Reprod , vol.71 , Issue.2 , pp. 540-547
    • Mukai, C.1    Okuno, M.2
  • 67
    • 0031039619 scopus 로고    scopus 로고
    • Absence of glucose decreases human fertilization and sperm movement characteristics in vitro
    • 9043915 1:CAS:528:DyaK2sXhsleiu7c%3D
    • Mahadevan MM, Miller MM, Moutos DM. Absence of glucose decreases human fertilization and sperm movement characteristics in vitro. Hum Reprod. 1997;12:119-23.
    • (1997) Hum Reprod , vol.12 , pp. 119-123
    • Mahadevan, M.M.1    Miller, M.M.2    Moutos, D.M.3
  • 68
    • 0034941785 scopus 로고    scopus 로고
    • The role of glucose in supporting motility and capacitation in human spermatozoa
    • 11451366 1:CAS:528:DC%2BD3MXlsFCmsrs%3D
    • Williams AC, Ford WCL. The role of glucose in supporting motility and capacitation in human spermatozoa. J Androl. 2001;22(4):680-95.
    • (2001) J Androl , vol.22 , Issue.4 , pp. 680-695
    • Williams, A.C.1    Ford, W.C.L.2
  • 69
    • 0025602222 scopus 로고
    • Importance of glycolysable substrates for in vitro capacitation of human spermatozoa
    • 2291925 1:CAS:528:DyaK3MXktVSiug%3D%3D
    • Rogers BJ, Perreault SD. Importance of glycolysable substrates for in vitro capacitation of human spermatozoa. Biol Reprod. 1990;43:1064-9.
    • (1990) Biol Reprod , vol.43 , pp. 1064-1069
    • Rogers, B.J.1    Perreault, S.D.2
  • 70
    • 33846621579 scopus 로고    scopus 로고
    • Association between seasonal changes in fatty-acid composition, expression of VLDL receptor and bovine sperm quality
    • 17157373 1:CAS:528:DC%2BD2sXhtlCksbg%3D
    • Argov N, Sklan D, Zeron Y, Roth Z. Association between seasonal changes in fatty-acid composition, expression of VLDL receptor and bovine sperm quality. Theriogenology. 2007;67:878-85.
    • (2007) Theriogenology , vol.67 , pp. 878-885
    • Argov, N.1    Sklan, D.2    Zeron, Y.3    Roth, Z.4
  • 71
  • 74
    • 0035995241 scopus 로고    scopus 로고
    • Can mitochondrial DNA mutations cause sperm dysfunction?
    • 12149402 1:CAS:528:DC%2BD38XmvFOrsbw%3D
    • Spiropoulos J, Turnbull DM, Chinnery PF. Can mitochondrial DNA mutations cause sperm dysfunction? Mol Hum Reprod. 2002;8:719-21.
    • (2002) Mol Hum Reprod , vol.8 , pp. 719-721
    • Spiropoulos, J.1    Turnbull, D.M.2    Chinnery, P.F.3
  • 76
    • 79955010189 scopus 로고    scopus 로고
    • Evaluation of mitochondrial respiratory efficiency during in vitro capacitation of human spermatozoa
    • 20546047 1:CAS:528:DC%2BC3MXot1Cqsrs%3D
    • Stendardi A, Focarelli R, Piomboni P, Palumberi D, Serafini F, Ferramosca A, et al. Evaluation of mitochondrial respiratory efficiency during in vitro capacitation of human spermatozoa. Int J Androl. 2011;34(3):247-55.
    • (2011) Int J Androl , vol.34 , Issue.3 , pp. 247-255
    • Stendardi, A.1    Focarelli, R.2    Piomboni, P.3    Palumberi, D.4    Serafini, F.5    Ferramosca, A.6    Zara, V.7
  • 78
    • 0036314771 scopus 로고    scopus 로고
    • Testis-specific cytochrome c-null mice produce functional sperm but undergo early testicular atrophy
    • Narisawa S, Hecht NB, Goldberg E, Boatright KM, Reed JC, Millán JL. Testis-specific cytochrome c-null mice produce functional sperm but undergo early testicular atrophy. Mol Cell Biol. 2002;15:5554-62.
    • (2002) Mol Cell Biol , vol.15 , pp. 5554-5562
    • Narisawa, S.1    Hecht, N.B.2    Goldberg, E.3    Boatright, K.M.4    Reed, J.C.5    Millán, J.L.6
  • 79
    • 43249106981 scopus 로고    scopus 로고
    • Oxygen uptake by mitochondria in demembranated human spermatozoa: A reliable tool for the evaluation of sperm respiratory efficiency
    • 17573845 1:STN:280:DC%2BD1c3pvFemsg%3D%3D
    • Ferramosca A, Focarelli R, Piomboni P, Coppola L, Zara V. Oxygen uptake by mitochondria in demembranated human spermatozoa: a reliable tool for the evaluation of sperm respiratory efficiency. Int J Androl. 2008;31(3):337-45.
    • (2008) Int J Androl , vol.31 , Issue.3 , pp. 337-345
    • Ferramosca, A.1    Focarelli, R.2    Piomboni, P.3    Coppola, L.4    Zara, V.5
  • 81
    • 0141516719 scopus 로고    scopus 로고
    • Alterations in mitochondria membrane potential and oxidative stress in infertile men: A prospective observational study
    • 14505763
    • Wang X, Sharma RK, Gupta A, George V, Thomas AJ, Falcone T, et al. Alterations in mitochondria membrane potential and oxidative stress in infertile men: a prospective observational study. Fertil Steril. 2003;80:844-50.
    • (2003) Fertil Steril , vol.80 , pp. 844-850
    • Wang, X.1    Sharma, R.K.2    Gupta, A.3    George, V.4    Thomas, A.J.5    Falcone, T.6    Agarwal, A.7
  • 82
    • 0031472327 scopus 로고    scopus 로고
    • CD4-mediated anchoring of the seminal antigen gp17 onto the spermatozoon surface
    • 9438207 1:CAS:528:DyaK1cXksFKltw%3D%3D
    • Bergamo P, Balestrieri M, Cammarota G, Guardiola J, Abrescia P. CD4-mediated anchoring of the seminal antigen gp17 onto the spermatozoon surface. Hum Immunol. 1997;58:30-41.
    • (1997) Hum Immunol , vol.58 , pp. 30-41
    • Bergamo, P.1    Balestrieri, M.2    Cammarota, G.3    Guardiola, J.4    Abrescia, P.5
  • 84
    • 79955457638 scopus 로고    scopus 로고
    • RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis
    • 21444325 1:CAS:528:DC%2BC3MXlt1Gns74%3D
    • Ma T, Keller JA, Yu X. RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis. Acta Biochim Biophys Sin. 2011;43(5):339-45.
    • (2011) Acta Biochim Biophys Sin , vol.43 , Issue.5 , pp. 339-345
    • Ma, T.1    Keller, J.A.2    Yu, X.3
  • 85
    • 41049104393 scopus 로고    scopus 로고
    • Role of proteasomal activity in the induction of acrosomal exocytosis in human spermatozoa
    • 18339263 1:CAS:528:DC%2BD1cXks1Sqt7c%3D
    • Chakravarty S, Bansal P, Sutovsky P, Gupta SK. Role of proteasomal activity in the induction of acrosomal exocytosis in human spermatozoa. Reprod Biomed Online. 2008;16:391-400.
    • (2008) Reprod Biomed Online , vol.16 , pp. 391-400
    • Chakravarty, S.1    Bansal, P.2    Sutovsky, P.3    Gupta, S.K.4
  • 86
    • 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
    • 19144957 1:CAS:528:DC%2BD1MXlsVajsrY%3D
    • 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(5):1026-35.
    • (2009) Biol Reprod , vol.80 , Issue.5 , pp. 1026-1035
    • Kong, M.1    Diaz, E.S.2    Morales, P.3
  • 88
    • 0035012044 scopus 로고    scopus 로고
    • A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis
    • 11309198 1:CAS:528:DC%2BD3MXjslyquro%3D
    • Sutovsky P, Moreno R, Ramalho-Santos J, Dominko T, Thompson WE, Schatten G. A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis. J Cell Sci. 2001;114:1665-75.
    • (2001) J Cell Sci , vol.114 , pp. 1665-1675
    • Sutovsky, P.1    Moreno, R.2    Ramalho-Santos, J.3    Dominko, T.4    Thompson, W.E.5    Schatten, G.6
  • 89
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • 12586069 1:CAS:528:DC%2BD3sXhsFKntrY%3D
    • Yoshida H, Matsui T, Hosokawa N, Kaufman JR, Nagata K, Mori K. A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell. 2003;4:265-71.
    • (2003) Dev Cell , vol.4 , pp. 265-271
    • Yoshida, H.1    Matsui, T.2    Hosokawa, N.3    Kaufman, J.R.4    Nagata, K.5    Mori, K.6
  • 90
    • 0025825971 scopus 로고
    • Localization of sulfated glycoprotein-2 (clusterin) on spermatozoa and in the reproductive tract of the male rat
    • 1878433 1:CAS:528:DyaK3MXlvVSjsr0%3D
    • Sylvester SR, Morales C, Oko R, Griswold MD. Localization of sulfated glycoprotein-2 (clusterin) on spermatozoa and in the reproductive tract of the male rat. Biol Reprod. 1991;45:195-207.
    • (1991) Biol Reprod , vol.45 , pp. 195-207
    • Sylvester, S.R.1    Morales, C.2    Oko, R.3    Griswold, M.D.4
  • 92
    • 0020590006 scopus 로고
    • Ram rete testis fluid contains a protein (clusterin) which influences cell-cell interaction in vitro
    • 6871313 1:CAS:528:DyaL3sXkt1Sju74%3D
    • Fritz IB, Burdzy K, Setchell B, Blaschuk O. Ram rete testis fluid contains a protein (clusterin) which influences cell-cell interaction in vitro. Biol Reprod. 1983;28:1173-88.
    • (1983) Biol Reprod , vol.28 , pp. 1173-1188
    • Fritz, I.B.1    Burdzy, K.2    Setchell, B.3    Blaschuk, O.4
  • 93
    • 0023931052 scopus 로고
    • SP-40, 40, a newly identified normal human serum protein found in the SC5b-9 complex of complement and in the immune deposits in glomerulonephritis
    • 2454950 1:CAS:528:DyaL1cXkvFSqsbs%3D
    • Murphy BF, Kirszbaum L, Walker ID, d'Apice AJ. SP-40, 40, a newly identified normal human serum protein found in the SC5b-9 complex of complement and in the immune deposits in glomerulonephritis. J Clin Invest. 1988;81:1858-64.
    • (1988) J Clin Invest , vol.81 , pp. 1858-1864
    • Murphy, B.F.1    Kirszbaum, L.2    Walker, I.D.3    D'Apice, A.J.4
  • 94
    • 0025910082 scopus 로고
    • Clusterin (complement lysis inhibitor) forms a high density lipoprotein complex with apolipoprotein A-I in human plasma
    • 1904058 1:CAS:528:DyaK3MXltFagurc%3D
    • Jenne DE, Lowin B, Peitsch MC, Böttcher A, Schmitz G, Tschopp J. Clusterin (complement lysis inhibitor) forms a high density lipoprotein complex with apolipoprotein A-I in human plasma. J Biol Chem. 1991;266:11030-6.
    • (1991) J Biol Chem , vol.266 , pp. 11030-11036
    • Jenne, D.E.1    Lowin, B.2    Peitsch, M.C.3    Böttcher, A.4    Schmitz, G.5    Tschopp, J.6
  • 95
    • 0033764651 scopus 로고    scopus 로고
    • Correlation between clusterin-positive spermatozoa determined by flow cytometry in bull semen and fertility
    • 11105915 1:STN:280:DC%2BD3MzgtlyqtQ%3D%3D
    • Ibrahim NM, Gilbert GR, Loseth KL, Crabo BG. Correlation between clusterin-positive spermatozoa determined by flow cytometry in bull semen and fertility. J Androl. 2000;21:887-94.
    • (2000) J Androl , vol.21 , pp. 887-894
    • Ibrahim, N.M.1    Gilbert, G.R.2    Loseth, K.L.3    Crabo, B.G.4
  • 96
    • 0028137221 scopus 로고
    • The use of anticlusterin monoclonal antibodies for the combined assessment of human sperm morphology and acrosome integrity
    • 7989511
    • O'Bryan MK, Murphy BF, Liu DY, Clarke GN, Baker HW. The use of anticlusterin monoclonal antibodies for the combined assessment of human sperm morphology and acrosome integrity. Hum Reprod. 1994;9:1490-6.
    • (1994) Hum Reprod , vol.9 , pp. 1490-1496
    • O'Bryan, M.K.1    Murphy, B.F.2    Liu, D.Y.3    Clarke, G.N.4    Baker, H.W.5
  • 98
  • 99
    • 0028908876 scopus 로고
    • Detection of cytokines (interleukin-1, interleukin-6, transforming growth factor-beta) and soluble tumor necrosis factor receptors in embryo culture fluids during in-vitro fertilization
    • 7745050 1:CAS:528:DyaK2MXktlars7c%3D
    • Austgulen R, Arntzen KJ, Vatten LJ, Kahn J, Sunde A. Detection of cytokines (interleukin-1, interleukin-6, transforming growth factor-beta) and soluble tumor necrosis factor receptors in embryo culture fluids during in-vitro fertilization. Hum Reprod. 1995;10(1):171-6.
    • (1995) Hum Reprod , vol.10 , Issue.1 , pp. 171-176
    • Austgulen, R.1    Arntzen, K.J.2    Vatten, L.J.3    Kahn, J.4    Sunde, A.5
  • 100
    • 0043204996 scopus 로고    scopus 로고
    • VDAC2 inhibits BAK activation and mitochondrial apoptosis
    • 12881569 1:CAS:528:DC%2BD3sXls1Cqsr4%3D
    • Cheng EH, Sheiko TV, Fisher JK, Craigen WJ, Korsmeyer SJ. VDAC2 inhibits BAK activation and mitochondrial apoptosis. Science. 2003;301(5632):513-7.
    • (2003) Science , vol.301 , Issue.5632 , pp. 513-517
    • Cheng, E.H.1    Sheiko, T.V.2    Fisher, J.K.3    Craigen, W.J.4    Korsmeyer, S.J.5
  • 101
    • 78651326754 scopus 로고    scopus 로고
    • Analysis and difference of voltage-dependent anion channel mRNA in ejaculated spermatozoa from normozoospermic fertile donors and infertile patients with idiopathic asthenozoospermia
    • 20809416
    • Liu B, Wang P, Wang Z, Jia Y, Niu X, Wang W, et al. Analysis and difference of voltage-dependent anion channel mRNA in ejaculated spermatozoa from normozoospermic fertile donors and infertile patients with idiopathic asthenozoospermia. J Assist Reprod Genet. 2010;27:719-24.
    • (2010) J Assist Reprod Genet , vol.27 , pp. 719-724
    • Liu, B.1    Wang, P.2    Wang, Z.3    Jia, Y.4    Niu, X.5    Wang, W.6    Zhang, W.7
  • 102
    • 2442468057 scopus 로고    scopus 로고
    • Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum
    • 14739283 1:CAS:528:DC%2BD2cXivVKgsLg%3D
    • Hinsch K-D, De Pinto V, Aires VA, Schneider X, Messina A, Hinsch E. Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum. J Biol Chem. 2004;279(15):15281-8.
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 15281-15288
    • Hinsch, K.-D.1    De Pinto, V.2    Aires, V.A.3    Schneider, X.4    Messina, A.5    Hinsch, E.6
  • 103
    • 0024337024 scopus 로고
    • Role of glutathione peroxidase in protecting mammalian spermatozoa from loss of motility caused by spontaneous lipid peroxidation
    • 2545584 1:CAS:528:DyaL1MXksFCrt74%3D
    • Alvarez JG, Storey BT. Role of glutathione peroxidase in protecting mammalian spermatozoa from loss of motility caused by spontaneous lipid peroxidation. Gamete Res. 1989;23:77-90.
    • (1989) Gamete Res , vol.23 , pp. 77-90
    • Alvarez, J.G.1    Storey, B.T.2
  • 104
    • 70350337541 scopus 로고    scopus 로고
    • Ascorbic Acid in human seminal plasma: Determination and its relationship to sperm quality
    • 19794921 1:CAS:528:DC%2BD1MXhtlWrsbvP
    • Colagar AH, Marzony ET. Ascorbic Acid in human seminal plasma: determination and its relationship to sperm quality. J Clin Biochem Nutr. 2009;45:144-9.
    • (2009) J Clin Biochem Nutr , vol.45 , pp. 144-149
    • Colagar, A.H.1    Marzony, E.T.2
  • 105
    • 0037382663 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the pathophysiology of human reproduction
    • 12749418
    • Agarwal A, Saleh RA, Bedaiwy MA. Role of reactive oxygen species in the pathophysiology of human reproduction. Fertil Steril. 2003;79:829-43.
    • (2003) Fertil Steril , vol.79 , pp. 829-843
    • Agarwal, A.1    Saleh, R.A.2    Bedaiwy, M.A.3
  • 106
    • 0030464440 scopus 로고    scopus 로고
    • Role of reactive oxygen species in male infertility
    • 8973665 1:STN:280:DyaK2s7ivFWhtw%3D%3D
    • Sharma RK, Agarwal A. Role of reactive oxygen species in male infertility. Urology. 1996;48:835-50.
    • (1996) Urology , vol.48 , pp. 835-850
    • Sharma, R.K.1    Agarwal, A.2
  • 107
    • 0032904982 scopus 로고    scopus 로고
    • Reactive oxygen species influence the acrosome reaction but not acrosin activity in human spermatozoa
    • 1:CAS:528:DyaK1MXhsV2hsLc%3D
    • Ichikawa T, Oeda T, Ohmori H, Schill W-B. Reactive oxygen species influence the acrosome reaction but not acrosin activity in human spermatozoa. International J Androl. 1999;22:37-42.
    • (1999) International J Androl , vol.22 , pp. 37-42
    • Ichikawa, T.1    Oeda, T.2    Ohmori, H.3    Schill, W.-B.4
  • 108
    • 42449105332 scopus 로고    scopus 로고
    • Oxidative stress and male infertility - A clinical perspective
    • 18281241 1:CAS:528:DC%2BD1cXkvFOqtbc%3D
    • Tremellen K. Oxidative stress and male infertility - a clinical perspective. Hum Reprod Update. 2008;14:243-58.
    • (2008) Hum Reprod Update. , vol.14 , pp. 243-258
    • Tremellen, K.1
  • 109
    • 34748822250 scopus 로고    scopus 로고
    • Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis
    • 17664285 1:CAS:528:DC%2BD2sXhtFSktLzM
    • Lin YN, Roy A, Yan W, Burns KH, Matzuk MM. Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol Cell Biol. 2007;27(19):6794-805.
    • (2007) Mol Cell Biol , vol.27 , Issue.19 , pp. 6794-6805
    • Lin, Y.N.1    Roy, A.2    Yan, W.3    Burns, K.H.4    Matzuk, M.M.5
  • 110
    • 34447635697 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of sperm-egg interaction
    • 17447007 1:CAS:528:DC%2BD2sXovFagtLo%3D
    • Nixon B, Aitken RJ, McLaughlin EA. New insights into the molecular mechanisms of sperm-egg interaction. Cell Mol Life Sci. 2007;64:1805-23.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1805-1823
    • Nixon, B.1    Aitken, R.J.2    McLaughlin, E.A.3
  • 112
    • 0024308967 scopus 로고
    • T he concentration of pepsinogen C in human semen and the physiological activation of zymogen in the vagina
    • 2758094 1:CAS:528:DyaL1MXktVCqtbg%3D
    • Szecsi PB, Dalgaard D, Stakemann G, Wagner G, Foltmann B. T he concentration of pepsinogen C in human semen and the physiological activation of zymogen in the vagina. Biol Reprod. 1989;40(3):653-9.
    • (1989) Biol Reprod , vol.40 , Issue.3 , pp. 653-659
    • Szecsi, P.B.1    Dalgaard, D.2    Stakemann, G.3    Wagner, G.4    Foltmann, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.