메뉴 건너뛰기




Volumn 89, Issue 10, 2011, Pages 2995-3007

Modulation of nicotinamide adenine dinucleotide phosphate oxidase activity through sequential posttranslational modifications of p22 phagocytic oxidase during capacitation and acrosome reaction in goat spermatozoa

Author keywords

Acrosome reaction; Capacitation; Goat spermatozoa; Nicotinamide adenine dinucleotide phosphate oxidase family; Phagocytic oxidase; Reactive oxygen species

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 80053033653     PISSN: 00218812     EISSN: 15253163     Source Type: Journal    
DOI: 10.2527/jas.2010-3731     Document Type: Article
Times cited : (8)

References (61)
  • 1
    • 0032842621 scopus 로고    scopus 로고
    • Regional heterogeneity in intracellular distribution of superoxide and hydrogen peroxide within the sperm and its relation to sperm development
    • Agnihotri, S., S. B. Purohit, M. Laloraya, and G. P. Kumar. 1999. Regional heterogeneity in intracellular distribution of superoxide and hydrogen peroxide within the sperm and its relation to sperm development. Arch. Androl. 43:113-121.
    • (1999) Arch. Androl , vol.43 , pp. 113-121
    • Agnihotri, S.1    Purohit, S.B.2    Laloraya, M.3    Kumar, G.P.4
  • 2
    • 0023617012 scopus 로고
    • Cellular basis of defective sperm function and its association with the genesis of reactive oxygen species by human spermatozoa
    • Aitken, R. J., and J. S. Clarkson. 1987. Cellular basis of defective sperm function and its association with the genesis of reactive oxygen species by human spermatozoa. J. Reprod. Fertil. 81:459-469.
    • (1987) J. Reprod. Fertil , vol.81 , pp. 459-469
    • Aitken, R.J.1    Clarkson, J.S.2
  • 3
    • 0031007755 scopus 로고    scopus 로고
    • Reactive oxygen species generation by human spermatozoa is induced by exogenous NADPH and inhibited by the flavoprotein inhibitors diphenylene iodonium and quinacrine
    • Aitken, R. J., H. M. Fisher, N. Fulton, E. Gomez, W. Knox, B. Lewis, and S. Irvine. 1997. Reactive oxygen species generation by human spermatozoa is induced by exogenous NADPH and inhibited by the flavoprotein inhibitors diphenylene iodonium and quinacrine. Mol. Reprod. Dev. 47:468-482.
    • (1997) Mol. Reprod. Dev , vol.47 , pp. 468-482
    • Aitken, R.J.1    Fisher, H.M.2    Fulton, N.3    Gomez, E.4    Knox, W.5    Lewis, B.6    Irvine, S.7
  • 4
    • 0032227033 scopus 로고    scopus 로고
    • Maturation of redox regulatory mechanisms in the epididymis
    • Aitken, R. J., and P. Vernet. 1998. Maturation of redox regulatory mechanisms in the epididymis. J. Reprod. Fertil. Suppl. 53:109-118.
    • (1998) J. Reprod. Fertil. Suppl , vol.53 , pp. 109-118
    • Aitken, R.J.1    Vernet, P.2
  • 6
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROSgenerating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K., and K. H. Krause. 2007. The NOX family of ROSgenerating NADPH oxidases: Physiology and pathophysiology. Physiol. Rev. 87:245-313.
    • (2007) Physiol. Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 7
    • 3042695344 scopus 로고    scopus 로고
    • Distinct ligand-dependent roles for p38 MAPK in priming and activation of the neutrophil NADPH oxidase
    • Brown, G. E., M. Q. Stewart, S. A. Bissonnette, A. E. Elia, E. Wilker, and M. B. Yaffe. 2004. Distinct ligand-dependent roles for p38 MAPK in priming and activation of the neutrophil NADPH oxidase. J. Biol. Chem. 279:27059-27068.
    • (2004) J. Biol. Chem , vol.279 , pp. 27059-27068
    • Brown, G.E.1    Stewart, M.Q.2    Bissonnette, S.A.3    Elia, A.E.4    Wilker, E.5    Yaffe, M.B.6
  • 8
    • 0027716055 scopus 로고
    • Exorbitantly enhanced protein gyration and erroneous membrane modification programs in spermatozoa after vasectomy: A biophysical basis for low infertility revival after vasectomy
    • Chatterjee, S., M. Laloraya, and G. P. Kumar. 1993. Exorbitantly enhanced protein gyration and erroneous membrane modification programs in spermatozoa after vasectomy: A biophysical basis for low infertility revival after vasectomy. Biochem. Biophys. Res. Commun. 197:450-456.
    • (1993) Biochem. Biophys. Res. Commun , vol.197 , pp. 450-456
    • Chatterjee, S.1    Laloraya, M.2    Kumar, G.P.3
  • 9
    • 0027396562 scopus 로고
    • Human sperm hyperactivation and capacitation as parts of an oxidative process
    • de Lamirande, E., and C. Gagnon. 1993. Human sperm hyperactivation and capacitation as parts of an oxidative process. Free Radic. Biol. Med. 14:157-166.
    • (1993) Free Radic. Biol. Med , vol.14 , pp. 157-166
    • de Lamirande, E.1    Gagnon, C.2
  • 10
    • 0028918676 scopus 로고
    • Capacitation-associated production of superoxide anion by human spermatozoa
    • de Lamirande, E., and C. Gagnon. 1995. Capacitation-associated production of superoxide anion by human spermatozoa. Free Radic. Biol. Med. 18:487-495.
    • (1995) Free Radic. Biol. Med , vol.18 , pp. 487-495
    • de Lamirande, E.1    Gagnon, C.2
  • 11
    • 0036169665 scopus 로고    scopus 로고
    • The extracellular signalregulated kinase (ERK) pathway is involved in human sperm function and modulated by the superoxide anion
    • de Lamirande, E., and C. Gagnon. 2002. The extracellular signalregulated kinase (ERK) pathway is involved in human sperm function and modulated by the superoxide anion. Mol. Hum. Reprod. 8:124-135.
    • (2002) Mol. Hum. Reprod , vol.8 , pp. 124-135
    • de Lamirande, E.1    Gagnon, C.2
  • 13
    • 58649120059 scopus 로고    scopus 로고
    • Reactive oxygen-induced reactive oxygen formation during human sperm capacitation
    • de Lamirande, E., and G. Lamothe. 2009. Reactive oxygen-induced reactive oxygen formation during human sperm capacitation. Free Radic. Biol. Med. 46:502-510.
    • (2009) Free Radic. Biol. Med , vol.46 , pp. 502-510
    • de Lamirande, E.1    Lamothe, G.2
  • 14
    • 64649101898 scopus 로고    scopus 로고
    • Control of superoxide and nitric oxide formation during human sperm capacitation
    • de Lamirande, E., G. Lamothe, and M. Villemure. 2009. Control of superoxide and nitric oxide formation during human sperm capacitation. Free Radic. Biol. Med. 46:1420-1427.
    • (2009) Free Radic. Biol. Med , vol.46 , pp. 1420-1427
    • de Lamirande, E.1    Lamothe, G.2    Villemure, M.3
  • 15
    • 0031793041 scopus 로고    scopus 로고
    • Involvement of reactive oxygen species in human sperm arcosome reaction induced by A23187, lysophosphatidylcholine, and biological fluid ultrafiltrates
    • de Lamirande, E., C. Tsai, A. Harakat, and C. Gagnon. 1998. Involvement of reactive oxygen species in human sperm arcosome reaction induced by A23187, lysophosphatidylcholine, and biological fluid ultrafiltrates. J. Androl. 19:585-594.
    • (1998) J. Androl , vol.19 , pp. 585-594
    • de Lamirande, E.1    Tsai, C.2    Harakat, A.3    Gagnon, C.4
  • 16
    • 0034607821 scopus 로고    scopus 로고
    • Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly
    • DeLeo, F. R., J. B. Burritt, L. Yu, A. J. Jesaitis, M. C. Dinauer, and W. M. Nauseef. 2000. Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly. J. Biol. Chem. 275:13986-13993.
    • (2000) J. Biol. Chem , vol.275 , pp. 13986-13993
    • Deleo, F.R.1    Burritt, J.B.2    Yu, L.3    Jesaitis, A.J.4    Dinauer, M.C.5    Nauseef, W.M.6
  • 17
    • 0031127073 scopus 로고    scopus 로고
    • Comparative analysis of the ability of precursor germ cells and epididymal spermatozoa to generate reactive oxygen metabolites
    • Fisher, H. M., and R. J. Aitken. 1997. Comparative analysis of the ability of precursor germ cells and epididymal spermatozoa to generate reactive oxygen metabolites. J. Exp. Zool. 277:390-400.
    • (1997) J. Exp. Zool , vol.277 , pp. 390-400
    • Fisher, H.M.1    Aitken, R.J.2
  • 18
    • 0035914317 scopus 로고    scopus 로고
    • Identification of a spectrally stable proteolytic fragment of human neutrophil flavocytochrome b composed of the NH2-terminal regions of gp91(phox) and p22(phox)
    • Foubert, T. R., J. B. Bleazard, J. B. Burritt, J. M. Gripentrog, D. Baniulis, R. M. Taylor, and A. J. Jesaitis. 2001. Identification of a spectrally stable proteolytic fragment of human neutrophil flavocytochrome b composed of the NH2-terminal regions of gp91(phox) and p22(phox). J. Biol. Chem. 276:38852-38861.
    • (2001) J. Biol. Chem , vol.276 , pp. 38852-38861
    • Foubert, T.R.1    Bleazard, J.B.2    Burritt, J.B.3    Gripentrog, J.M.4    Baniulis, D.5    Taylor, R.M.6    Jesaitis, A.J.7
  • 21
    • 0030820190 scopus 로고    scopus 로고
    • Reactive oxygen species and human spermatozoa: Physiology and pathology
    • Griveau, J. F., and L. D. Le. 1997. Reactive oxygen species and human spermatozoa: Physiology and pathology. Int. J. Androl. 20:61-69.
    • (1997) Int. J. Androl , vol.20 , pp. 61-69
    • Griveau, J.F.1    Le, L.D.2
  • 24
    • 0020434623 scopus 로고
    • Production of superoxide and activity of superoxide dismutase in rabbit epididymal spermatozoa
    • Holland, M. K., J. G. Alvarez, and B. T. Storey. 1982. Production of superoxide and activity of superoxide dismutase in rabbit epididymal spermatozoa. Biol. Reprod. 27:1109-1118.
    • (1982) Biol. Reprod , vol.27 , pp. 1109-1118
    • Holland, M.K.1    Alvarez, J.G.2    Storey, B.T.3
  • 25
  • 26
    • 0018341406 scopus 로고
    • Peroxidative breakdown of phospholipids in human spermatozoa, spermicidal properties of fatty acid peroxides, and protective action of seminal plasma
    • Jones, R., T. Mann, and R. Sherins. 1979. Peroxidative breakdown of phospholipids in human spermatozoa, spermicidal properties of fatty acid peroxides, and protective action of seminal plasma. Fertil. Steril. 31:531-537.
    • (1979) Fertil. Steril , vol.31 , pp. 531-537
    • Jones, R.1    Mann, T.2    Sherins, R.3
  • 28
    • 0030860591 scopus 로고    scopus 로고
    • Calcium requirement and time course of capacitation of goat spermatozoa assessed by chlortetracycline assay
    • Kaul, G., S. Singh, K. K. Gandhi, and S. R. Anand. 1997. Calcium requirement and time course of capacitation of goat spermatozoa assessed by chlortetracycline assay. Andrologia 29:243-251.
    • (1997) Andrologia , vol.29 , pp. 243-251
    • Kaul, G.1    Singh, S.2    Gandhi, K.K.3    Anand, S.R.4
  • 29
    • 24744468043 scopus 로고    scopus 로고
    • Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation
    • Kawahara, T., D. Ritsick, G. Cheng, and J. D. Lambeth. 2005. Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation. J. Biol. Chem. 280:31859-31869.
    • (2005) J. Biol. Chem , vol.280 , pp. 31859-31869
    • Kawahara, T.1    Ritsick, D.2    Cheng, G.3    Lambeth, J.D.4
  • 30
    • 0026533102 scopus 로고
    • Characterization of a phagocyte cytochrome b558 91-kilodalton subunit functional domain: Identification of peptide sequence and amino acids essential for activity
    • Kleinberg, M. E., D. Mital, D. Rotrosen, and H. L. Malech. 1992. Characterization of a phagocyte cytochrome b558 91-kilodalton subunit functional domain: Identification of peptide sequence and amino acids essential for activity. Biochemistry 31:2686-2690.
    • (1992) Biochemistry , vol.31 , pp. 2686-2690
    • Kleinberg, M.E.1    Mital, D.2    Rotrosen, D.3    Malech, H.L.4
  • 31
    • 9144257277 scopus 로고    scopus 로고
    • Tissue distribution and putative physiological function of NOX family NADPH oxidases
    • Krause, K. H. 2004. Tissue distribution and putative physiological function of NOX family NADPH oxidases. Jpn. J. Infect. Dis. 57:S28-S29.
    • (2004) Jpn. J. Infect. Dis , vol.57
    • Krause, K.H.1
  • 32
    • 0025812798 scopus 로고
    • Superoxide radical level and superoxide dismutase activity changes in maturing mammalian spermatozoa
    • Kumar, P. G., M. Laloraya, and M. M. Laloraya. 1991. Superoxide radical level and superoxide dismutase activity changes in maturing mammalian spermatozoa. Andrologia 23:171-175.
    • (1991) Andrologia , vol.23 , pp. 171-175
    • Kumar, P.G.1    Laloraya, M.2    Laloraya, M.M.3
  • 33
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J. D. 2004. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4:181-189.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 34
    • 77449086400 scopus 로고    scopus 로고
    • hosphorylation of p22phox on threonine147 enhances NADPH oxidase activity by promoting p47phox binding
    • Lewis, E. M., S. Sergeant, B. Ledford, N. Stull, M. C. Dinauer, and. C. McPhail, 2010. hosphorylation of p22phox on threonine147 enhances NADPH oxidase activity by promoting p47phox binding. J. Biol. Chem. 285:2959-2967.
    • (2010) J. Biol. Chem , vol.285 , pp. 2959-2967
    • Lewis, E.M.1    Sergeant, S.2    Ledford, B.3    Stull, N.4    Dinauer, M.C.5    McPhail, C.6
  • 35
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • Li, J. M., and A. M. Shah. 2002. Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells. J. Biol. Chem. 277:19952-19960.
    • (2002) J. Biol. Chem , vol.277 , pp. 19952-19960
    • Li, J.M.1    Shah, A.M.2
  • 36
    • 54849175900 scopus 로고    scopus 로고
    • Downregulation of p22phox in retinal pigment epithelial cells inhibits choroidal neovascularization in mice
    • Li, Q., A. Dinculescu, Z. Shan, R. Miller, J. Pang, A. S. Lewin, M. K. Raizada, and W. W. Hauswirth. 2008. Downregulation of p22phox in retinal pigment epithelial cells inhibits choroidal neovascularization in mice. Mol. Ther. 16:1688-1694.
    • (2008) Mol. Ther , vol.16 , pp. 1688-1694
    • Li, Q.1    Dinculescu, A.2    Shan, Z.3    Miller, R.4    Pang, J.5    Lewin, A.S.6    Raizada, M.K.7    Hauswirth, W.W.8
  • 38
    • 18744371911 scopus 로고    scopus 로고
    • Sperm ubiquitination positively correlates to normal morphology in human semen
    • Muratori, M., S. Marchiani, G. Forti, and E. Baldi. 2005. Sperm ubiquitination positively correlates to normal morphology in human semen. Hum. Reprod. 20:1035-1043.
    • (2005) Hum. Reprod , vol.20 , pp. 1035-1043
    • Muratori, M.1    Marchiani, S.2    Forti, G.3    Baldi, E.4
  • 40
    • 33645401924 scopus 로고    scopus 로고
    • Expression of NADPH oxidase in rabbit corneal epithelial and stromal cells in culture
    • O'Brien, W. J., C. Krema, T. Heimann, and H. Zhao. 2006. Expression of NADPH oxidase in rabbit corneal epithelial and stromal cells in culture. Invest. Ophthalmol. Vis. Sci. 47:853-863.
    • (2006) Invest. Ophthalmol. Vis. Sci , vol.47 , pp. 853-863
    • O'Brien, W.J.1    Krema, C.2    Heimann, T.3    Zhao, H.4
  • 41
    • 0037386320 scopus 로고    scopus 로고
    • Participation of superoxide anion in the capacitation of cryopreserved bovine sperm
    • O'Flaherty, C., N. Beorlegui, and M. T. Beconi. 2003. Participation of superoxide anion in the capacitation of cryopreserved bovine sperm. Int. J. Androl. 26:109-114.
    • (2003) Int. J. Androl , vol.26 , pp. 109-114
    • O'Flaherty, C.1    Beorlegui, N.2    Beconi, M.T.3
  • 42
    • 33746077694 scopus 로고    scopus 로고
    • Positive role of reactive oxygen species in mammalian sperm capacitation: Triggering and modulation of phosphorylation events
    • O'Flaherty, C., E. de Lamirande, and C. Gagnon. 2006. Positive role of reactive oxygen species in mammalian sperm capacitation: Triggering and modulation of phosphorylation events. Free Radic. Biol. Med. 41:528-540.
    • (2006) Free Radic. Biol. Med , vol.41 , pp. 528-540
    • O'Flaherty, C.1    de Lamirande, E.2    Gagnon, C.3
  • 43
    • 33846130574 scopus 로고    scopus 로고
    • Bone-marrow derived hematopoietic stem/progenitor cells express multiple isoforms of NADPH oxidase and produce constitutively reactive oxygen species
    • Piccoli, C., A. D'Aprile, M. Ripoli, R. Scrima, L. Lecce, D. Boffoli, A. Tabilio, and N. Capitanio. 2007. Bone-marrow derived hematopoietic stem/progenitor cells express multiple isoforms of NADPH oxidase and produce constitutively reactive oxygen species. Biochem. Biophys. Res. Commun. 353:965-972.
    • (2007) Biochem. Biophys. Res. Commun , vol.353 , pp. 965-972
    • Piccoli, C.1    D'aprile, A.2    Ripoli, M.3    Scrima, R.4    Lecce, L.5    Boffoli, D.6    Tabilio, A.7    Capitanio, N.8
  • 44
    • 49349108756 scopus 로고    scopus 로고
    • Ubiquitination and its influence in boar sperm physiology and cryopreservation
    • Purdy, P. H. 2008. Ubiquitination and its influence in boar sperm physiology and cryopreservation. Theriogenology 70:818-826.
    • (2008) Theriogenology , vol.70 , pp. 818-826
    • Purdy, P.H.1
  • 45
    • 0033188490 scopus 로고    scopus 로고
    • Role of ions and ion channels in capacitation and acrosome reaction of spermatozoa
    • Purohit, S. B., M. Laloraya, and G. P. Kumar. 1999. Role of ions and ion channels in capacitation and acrosome reaction of spermatozoa. Asian J. Androl. 1:95-107.
    • (1999) Asian J. Androl , vol.1 , pp. 95-107
    • Purohit, S.B.1    Laloraya, M.2    Kumar, G.P.3
  • 46
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases
    • Quinn, M. T., and K. A. Gauss. 2004. Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases. J. Leukoc. Biol. 76:760-781.
    • (2004) J. Leukoc. Biol , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 47
    • 0034664253 scopus 로고    scopus 로고
    • Phosphorylation of p22phox is mediated by phospholipase d-dependent and -independent mechanisms. Correlation of NADPH oxidase activity and p22phox phosphorylation
    • Regier, D. S., D. G. Greene, S. Sergeant, A. J. Jesaitis, and L. C. McPhail. 2000. Phosphorylation of p22phox is mediated by phospholipase d-dependent and -independent mechanisms. Correlation of NADPH oxidase activity and p22phox phosphorylation. J. Biol. Chem. 275:28406-28412.
    • (2000) J. Biol. Chem , vol.275 , pp. 28406-28412
    • Regier, D.S.1    Greene, D.G.2    Sergeant, S.3    Jesaitis, A.J.4    McPhail, L.C.5
  • 49
    • 9644289356 scopus 로고    scopus 로고
    • Nitric oxide-induced capacitation of cryopreserved bull spermatozoa and assessment of participating regulatory pathways
    • Rodriguez, P. C., C. M. O'Flaherty, M. T. Beconi, and N. B. Beorlegui. 2005. Nitric oxide-induced capacitation of cryopreserved bull spermatozoa and assessment of participating regulatory pathways. Anim. Reprod. Sci. 85:231-242.
    • (2005) Anim. Reprod. Sci , vol.85 , pp. 231-242
    • Rodriguez, P.C.1    O'Flaherty, C.M.2    Beconi, M.T.3    Beorlegui, N.B.4
  • 50
    • 36549058341 scopus 로고    scopus 로고
    • Production of superoxide anion and hydrogen peroxide by capacitating buffalo (Bubalus bubalis) spermatozoa
    • Roy, S. C., and S. K. Atreja. 2008. Production of superoxide anion and hydrogen peroxide by capacitating buffalo (Bubalus bubalis) spermatozoa. Anim. Reprod. Sci. 103:260-270.
    • (2008) Anim. Reprod. Sci , vol.103 , pp. 260-270
    • Roy, S.C.1    Atreja, S.K.2
  • 51
    • 34548046998 scopus 로고    scopus 로고
    • Characterization of NADPH oxidase 5 in equine testis and spermatozoa
    • Sabeur, K., and B. A. Ball. 2007. Characterization of NADPH oxidase 5 in equine testis and spermatozoa. Reproduction 134:263-270.
    • (2007) Reproduction , vol.134 , pp. 263-270
    • Sabeur, K.1    Ball, B.A.2
  • 52
    • 5144226313 scopus 로고    scopus 로고
    • Human sperm superoxide anion generation and correlation with semen quality in patients with male infertility
    • Said, T. M., A. Agarwal, R. K. Sharma, E. Mascha, S. C. Sikka, and A. J. Thomas Jr. 2004. Human sperm superoxide anion generation and correlation with semen quality in patients with male infertility. Fertil. Steril. 82:871-877.
    • (2004) Fertil. Steril , vol.82 , pp. 871-877
    • Said, T.M.1    Agarwal, A.2    Sharma, R.K.3    Mascha, E.4    Sikka, S.C.5    Thomas Jr., A.J.6
  • 54
    • 0032544692 scopus 로고    scopus 로고
    • Increased association of synaptosome-associated protein of 25 kDa with syntaxin and vesicle-associated membrane protein following acrosomal exocytosis of sea urchin sperm
    • Schulz, J. R., J. D. Sasaki, and V. D. Vacquier. 1998. Increased association of synaptosome-associated protein of 25 kDa with syntaxin and vesicle-associated membrane protein following acrosomal exocytosis of sea urchin sperm. J. Biol. Chem. 273:24355-24359.
    • (1998) J. Biol. Chem , vol.273 , pp. 24355-24359
    • Schulz, J.R.1    Sasaki, J.D.2    Vacquier, V.D.3
  • 56
    • 18044365226 scopus 로고    scopus 로고
    • Identification of non-mitochondrial NADPH oxidase and the spatiotemporal organization of its components in mouse spermatozoa
    • Shukla, S., R. K. Jha, M. Laloraya, and P. G. Kumar. 2005. Identification of non-mitochondrial NADPH oxidase and the spatiotemporal organization of its components in mouse spermatozoa. Biochem. Biophys. Res. Commun. 331:476-483.
    • (2005) Biochem. Biophys. Res. Commun , vol.331 , pp. 476-483
    • Shukla, S.1    Jha, R.K.2    Laloraya, M.3    Kumar, P.G.4
  • 57
    • 0034449491 scopus 로고    scopus 로고
    • DNA loop domain organization: The three-dimensional genomic code
    • Sotolongo, B., and W. S. Ward. 2000. DNA loop domain organization: The three-dimensional genomic code. J. Cell Biochem. Suppl. 35:23-26.
    • (2000) J. Cell Biochem. Suppl , vol.35 , pp. 23-26
    • Sotolongo, B.1    Ward, W.S.2
  • 58
    • 1542397212 scopus 로고    scopus 로고
    • Increased levels of sperm ubiquitin correlate with semen quality in men from an andrology laboratory clinic population
    • Sutovsky, P., R. Hauser, and M. Sutovsky. 2004. Increased levels of sperm ubiquitin correlate with semen quality in men from an andrology laboratory clinic population. Hum. Reprod. 19:628-638.
    • (2004) Hum. Reprod , vol.19 , pp. 628-638
    • Sutovsky, P.1    Hauser, R.2    Sutovsky, M.3
  • 60
    • 0034809549 scopus 로고    scopus 로고
    • Analysis of reactive oxygen species generating systems in rat epididymal spermatozoa
    • Vernet, P., N. Fulton, C. Wallace, and R. J. Aitken. 2001. Analysis of reactive oxygen species generating systems in rat epididymal spermatozoa. Biol. Reprod. 65:1102-1113.
    • (2001) Biol. Reprod , vol.65 , pp. 1102-1113
    • Vernet, P.1    Fulton, N.2    Wallace, C.3    Aitken, R.J.4
  • 61
    • 65549107417 scopus 로고    scopus 로고
    • The regulation of NADPH oxidase and its association with cell proliferation in human lens epithelial cells
    • Wang, Y., and M. F. Lou. 2009. The regulation of NADPH oxidase and its association with cell proliferation in human lens epithelial cells. Invest. Ophthalmol. Vis. Sci. 50:2291-2300.
    • (2009) Invest. Ophthalmol. Vis. Sci , vol.50 , pp. 2291-2300
    • Wang, Y.1    Lou, M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.