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Volumn 8, Issue 8, 2008, Pages 1720-1730

The mouse sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification

Author keywords

Epididymis; IPGphor; Liquid chromatography tandem mass spectrometry; Mass spectra; Spermatogenesis

Indexed keywords

PROTEIN ACR; PROTEIN ACRBP; PROTEIN ACRV1; PROTEIN CATSPER4; PROTEIN CYLC2; PROTEIN IZUMO; PROTEIN ODF1; PROTEIN ODF2; PROTEIN SMCP; PROTEIN SPA17; PROTEIN SPACA 1; PROTEIN SPACA 3; PROTEIN SPACA 5; PROTEIN SPAG 16; PROTEIN SPAG 17; PROTEIN SPAG 6; PROTEIN SPAM 1; PROTEIN SPATA 18; PROTEIN SPATA 19; PROTEIN SPATA 6; PROTEIN SPESP1; PROTEIN TCP 1; PROTEIN ZONADHESIN; PROTEIN ZP3R; PROTEIN ZPBP 1; PROTEIN ZPBP 2; PROTEOME; RAB PROTEIN; UNCLASSIFIED DRUG;

EID: 42549145478     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200701020     Document Type: Article
Times cited : (72)

References (73)
  • 3
    • 0036796113 scopus 로고    scopus 로고
    • Contraception - past and future
    • Glasie, A., Contraception - past and future. Nat. Cell Biol. 2002, 4, s3-s6.
    • (2002) Nat. Cell Biol , vol.4
    • Glasie, A.1
  • 4
    • 42549089960 scopus 로고    scopus 로고
    • UNDP/UNFPA/WHO, World Bank Special Programme of Research, Development & Research Training in Human Reproduction, World Health Organization, Geneva, Switzerland 1998.
    • UNDP/UNFPA/WHO, World Bank Special Programme of Research, Development & Research Training in Human Reproduction, World Health Organization, Geneva, Switzerland 1998.
  • 6
    • 37049034594 scopus 로고    scopus 로고
    • Identification of gene products present in triton X-100 soluble and insoluble fractions of human spermatozoa lysates using LC-MS/MS analysis
    • Baker, M. A., Reeves, G., Hetherington, L., Aitken, R. J., Identification of gene products present in triton X-100 soluble and insoluble fractions of human spermatozoa lysates using LC-MS/MS analysis. Proteomics Clin. Appl. 2007, 1, 524-532.
    • (2007) Proteomics Clin. Appl , vol.1 , pp. 524-532
    • Baker, M.A.1    Reeves, G.2    Hetherington, L.3    Aitken, R.J.4
  • 7
    • 0043245880 scopus 로고    scopus 로고
    • Expression of testicular germ cell genes identified by differential display analysis
    • Anway, M. D., Li, Y., Ravindranath, N., Dym, M., Griswold, M. D., Expression of testicular germ cell genes identified by differential display analysis. J. Androl. 2003, 24, 173-184.
    • (2003) J. Androl , vol.24 , pp. 173-184
    • Anway, M.D.1    Li, Y.2    Ravindranath, N.3    Dym, M.4    Griswold, M.D.5
  • 8
    • 0031085297 scopus 로고    scopus 로고
    • Differential display to identify and isolate novel genes expressed during spermatogenesis
    • Catalano, R. D., Vlad, M., Kennedy, R. C., Differential display to identify and isolate novel genes expressed during spermatogenesis. Mol. Hum. Reprod. 1997, 3, 215-221.
    • (1997) Mol. Hum. Reprod , vol.3 , pp. 215-221
    • Catalano, R.D.1    Vlad, M.2    Kennedy, R.C.3
  • 9
    • 0042916338 scopus 로고    scopus 로고
    • Identification of developmentally regulated genes in the somatic cells of the mouse testis using serial analysis of gene expression
    • O'Shaughnessy, P. J., Fleming, L., Baker, P. J., Jackson, G., Johnston, H., Identification of developmentally regulated genes in the somatic cells of the mouse testis using serial analysis of gene expression. Biol. Reprod. 2003, 69, 797-808.
    • (2003) Biol. Reprod , vol.69 , pp. 797-808
    • O'Shaughnessy, P.J.1    Fleming, L.2    Baker, P.J.3    Jackson, G.4    Johnston, H.5
  • 10
    • 2642578283 scopus 로고    scopus 로고
    • Analysis of cell-type-specific gene expression during mouse spermatogenesis
    • Almstrup, K., Nielsen, J. E., Hansen, M. A., Tanaka, M. et al., Analysis of cell-type-specific gene expression during mouse spermatogenesis. Biol. Reprod. 2004, 70, 1751-1761.
    • (2004) Biol. Reprod , vol.70 , pp. 1751-1761
    • Almstrup, K.1    Nielsen, J.E.2    Hansen, M.A.3    Tanaka, M.4
  • 11
    • 0942298000 scopus 로고    scopus 로고
    • Stage-specific and tissue-specific expression characteristics of differentially expressed genes during mouse spermatogenesis
    • Guo, R., Yu, Z., Guan, J., Ge, Y. et al., Stage-specific and tissue-specific expression characteristics of differentially expressed genes during mouse spermatogenesis. Mol. Reprod. Dev. 2004, 67, 264-272.
    • (2004) Mol. Reprod. Dev , vol.67 , pp. 264-272
    • Guo, R.1    Yu, Z.2    Guan, J.3    Ge, Y.4
  • 12
    • 0034967424 scopus 로고    scopus 로고
    • Expression of stress response genes in germ cells during spermatogenesis
    • Aguilar-Mahecha, A., Hales, B. F., Robaire, B., Expression of stress response genes in germ cells during spermatogenesis. Biol. Reprod. 2001, 65, 119-127.
    • (2001) Biol. Reprod , vol.65 , pp. 119-127
    • Aguilar-Mahecha, A.1    Hales, B.F.2    Robaire, B.3
  • 13
    • 0038790159 scopus 로고    scopus 로고
    • Gene expression profiles in different stages of mouse spermatogenic cells during spermatogenesis
    • Yu, Z., Guo, R., Ge, Y., Ma, J. et al., Gene expression profiles in different stages of mouse spermatogenic cells during spermatogenesis. Biol. Reprod. 2003, 69, 37-47.
    • (2003) Biol. Reprod , vol.69 , pp. 37-47
    • Yu, Z.1    Guo, R.2    Ge, Y.3    Ma, J.4
  • 14
    • 3142748299 scopus 로고    scopus 로고
    • Identification of cytochrome P450-reductase as the enzyme responsible for NADPH-dependent lucigenin and tetrazolium salt reduction in rat epididymal sperm preparations
    • Baker, M. A., Krutskikh, A., Curry, B. J., McLaughlin, E. A., Aitken, R. J., Identification of cytochrome P450-reductase as the enzyme responsible for NADPH-dependent lucigenin and tetrazolium salt reduction in rat epididymal sperm preparations. Biol. Reprod. 2004, 71, 307-318.
    • (2004) Biol. Reprod , vol.71 , pp. 307-318
    • Baker, M.A.1    Krutskikh, A.2    Curry, B.J.3    McLaughlin, E.A.4    Aitken, R.J.5
  • 15
    • 1042301383 scopus 로고    scopus 로고
    • VDAC1 is a transplasma membrane NADH:ferricyanide reductase
    • Baker, M. A., Lane, D. J., Ly, J. D., De Pinto, V., Lawen, A., VDAC1 is a transplasma membrane NADH:ferricyanide reductase. J. Biol. Chem. 2004, 279, 4811-4819.
    • (2004) J. Biol. Chem , vol.279 , pp. 4811-4819
    • Baker, M.A.1    Lane, D.J.2    Ly, J.D.3    De Pinto, V.4    Lawen, A.5
  • 16
    • 22544461313 scopus 로고    scopus 로고
    • Identification of cytochrome-b5 reductase as the enzyme responsible for NADH-dependent lucigenin chemiluminescence in human spermatozoa
    • Baker, M. A., Krutskikh, A., Curry, B. J., Hetherington, L., Aitken, R. J., Identification of cytochrome-b5 reductase as the enzyme responsible for NADH-dependent lucigenin chemiluminescence in human spermatozoa. Biol. Reprod. 2005, 73, 334-342.
    • (2005) Biol. Reprod , vol.73 , pp. 334-342
    • Baker, M.A.1    Krutskikh, A.2    Curry, B.J.3    Hetherington, L.4    Aitken, R.J.5
  • 17
    • 33644861546 scopus 로고    scopus 로고
    • Immobilized pH gradient isoelectric focusing as a first-dimension separation in shotgun proteomics
    • Cargile, B. J., Sevinsky, J. R., Essader, A. S., Stephenson, J. L., Jr., Bundy, J. L., Immobilized pH gradient isoelectric focusing as a first-dimension separation in shotgun proteomics. J. Biomol. Tech. 2005, 16, 181-189.
    • (2005) J. Biomol. Tech , vol.16 , pp. 181-189
    • Cargile, B.J.1    Sevinsky, J.R.2    Essader, A.S.3    Stephenson Jr., J.L.4    Bundy, J.L.5
  • 18
    • 13244271374 scopus 로고    scopus 로고
    • A comparison of immobilized pH gradient isoelectric focusing and strong-cation-exchange chromatography as a first dimension in shotgun proteomics
    • Essader, A. S., Cargile, B. J., Bundy, J. L., Stephenson, J. L., Jr., A comparison of immobilized pH gradient isoelectric focusing and strong-cation-exchange chromatography as a first dimension in shotgun proteomics. Proteomics 2005, 5, 24-34.
    • (2005) Proteomics , vol.5 , pp. 24-34
    • Essader, A.S.1    Cargile, B.J.2    Bundy, J.L.3    Stephenson Jr., J.L.4
  • 19
    • 33646949472 scopus 로고    scopus 로고
    • Proteomic profiling of accessory structures from the mouse sperm flagellum
    • Cao, W., Gerton, G. L., Moss, S. B., Proteomic profiling of accessory structures from the mouse sperm flagellum. Mol. Cell. Proteomics 2006, 5, 801-810.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 801-810
    • Cao, W.1    Gerton, G.L.2    Moss, S.B.3
  • 20
    • 0035846092 scopus 로고    scopus 로고
    • A sperm ion channel required for sperm motility and male fertility
    • Ren, D., Navarro, B., Perez, G., Jackson, A. C. et al., A sperm ion channel required for sperm motility and male fertility. Nature 2001, 413, 603-609.
    • (2001) Nature , vol.413 , pp. 603-609
    • Ren, D.1    Navarro, B.2    Perez, G.3    Jackson, A.C.4
  • 21
    • 33846613308 scopus 로고    scopus 로고
    • All four CatSper ion channel proteins are required for male fertility and sperm cell hyperactivated motility
    • Qi, H., Moran, M. M., Navarro, B., Chong, J. A. et al., All four CatSper ion channel proteins are required for male fertility and sperm cell hyperactivated motility. Proc. Natl. Acad. Sci. USA 2007, 104, 1219-1223.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1219-1223
    • Qi, H.1    Moran, M.M.2    Navarro, B.3    Chong, J.A.4
  • 23
    • 10744227299 scopus 로고    scopus 로고
    • Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins
    • Hemelaar, J., Borodovsky, A., Kessler, B. M., Reverter, D. et al., Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins. Mol. Cell. Biol. 2004, 24, 84-95.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 84-95
    • Hemelaar, J.1    Borodovsky, A.2    Kessler, B.M.3    Reverter, D.4
  • 24
    • 0036085759 scopus 로고    scopus 로고
    • Role of sperm surface arylsulfatase A in mouse sperm-zona pellucida binding
    • Tantibhedhyangkul, J., Weerachatyanukul, W., Carmona, E., Xu, H. et al., Role of sperm surface arylsulfatase A in mouse sperm-zona pellucida binding. Biol. Reprod. 2002, 67, 212-219.
    • (2002) Biol. Reprod , vol.67 , pp. 212-219
    • Tantibhedhyangkul, J.1    Weerachatyanukul, W.2    Carmona, E.3    Xu, H.4
  • 25
    • 34548483869 scopus 로고    scopus 로고
    • Sperm surface arylsulfatase A can disperse the cumulus matrix of cumulus oocyte complexes
    • Wu, A., Anupriwan, A., Iamsaard, S., Chakrabandhu, K. et al., Sperm surface arylsulfatase A can disperse the cumulus matrix of cumulus oocyte complexes. J. Cell Physiol. 2007, 213, 201-211.
    • (2007) J. Cell Physiol , vol.213 , pp. 201-211
    • Wu, A.1    Anupriwan, A.2    Iamsaard, S.3    Chakrabandhu, K.4
  • 26
    • 4444254836 scopus 로고    scopus 로고
    • Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition
    • Asquith, K. L., Baleato, R. M., McLaughlin, E. A., Nixon, B., Aitken, R. J., Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition. J. Cell Sci. 2004, 117, 3645-3657.
    • (2004) J. Cell Sci , vol.117 , pp. 3645-3657
    • Asquith, K.L.1    Baleato, R.M.2    McLaughlin, E.A.3    Nixon, B.4    Aitken, R.J.5
  • 27
    • 16344379736 scopus 로고    scopus 로고
    • Identification of post-translational modifications that occur during sperm maturation using difference in 2D-gel electrophoresis
    • Baker, M. A., Witherdin, R., Hetherington, L., Cunningham-Smith, K., Aitken, R. J., Identification of post-translational modifications that occur during sperm maturation using difference in 2D-gel electrophoresis. Proteomics Suppl. 2005, 5, 1003-1012.
    • (2005) Proteomics Suppl , vol.5 , pp. 1003-1012
    • Baker, M.A.1    Witherdin, R.2    Hetherington, L.3    Cunningham-Smith, K.4    Aitken, R.J.5
  • 29
    • 0031044330 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoretic analysis of vectorially labeled surface proteins of human spermatozoa
    • Naaby-Hansen, S., Flickinger, C. J., Herr, J. C., Two-dimensional gel electrophoretic analysis of vectorially labeled surface proteins of human spermatozoa. Biol. Reprod. 1997, 56, 771-787.
    • (1997) Biol. Reprod , vol.56 , pp. 771-787
    • Naaby-Hansen, S.1    Flickinger, C.J.2    Herr, J.C.3
  • 30
    • 33646863600 scopus 로고    scopus 로고
    • Proteomic analysis of sperm regions that mediate sperm-egg interactions
    • Stein, K. K., Go, J. C., Lane, W. S., Primakoff, P., Myles, D. G., Proteomic analysis of sperm regions that mediate sperm-egg interactions. Proteomics 2006, 6, 3533-3543.
    • (2006) Proteomics , vol.6 , pp. 3533-3543
    • Stein, K.K.1    Go, J.C.2    Lane, W.S.3    Primakoff, P.4    Myles, D.G.5
  • 31
    • 33746307519 scopus 로고    scopus 로고
    • Multiple glycolytic enzymes are tightly bound to the fibrous sheath of mouse spermatozoa
    • Krisfalusi, M., Miki, K., Magyar, P. L., O'Brien, D. A., Multiple glycolytic enzymes are tightly bound to the fibrous sheath of mouse spermatozoa. Biol. Reprod. 2006, 75, 270-278.
    • (2006) Biol. Reprod , vol.75 , pp. 270-278
    • Krisfalusi, M.1    Miki, K.2    Magyar, P.L.3    O'Brien, D.A.4
  • 32
    • 33748374699 scopus 로고    scopus 로고
    • Identification of the proteins present in the bull sperm cytosolic fraction enriched in tyrosine kinase activity: A proteomic approach
    • Lalancette, C., Faure, R. L., Leclerc, P., Identification of the proteins present in the bull sperm cytosolic fraction enriched in tyrosine kinase activity: A proteomic approach. Proteomics 2006, 4523-4540.
    • (2006) Proteomics , pp. 4523-4540
    • Lalancette, C.1    Faure, R.L.2    Leclerc, P.3
  • 33
    • 33748316506 scopus 로고    scopus 로고
    • Identification of pp60c-src as a key PKA-stimulated tyrosine kinase involved in the capacitation and hyperactivation of murine spermatozoa
    • Baker, M. A., Aitken, R. J., Identification of pp60c-src as a key PKA-stimulated tyrosine kinase involved in the capacitation and hyperactivation of murine spermatozoa. J. Cell Sci. 2006, 119, 3182-3192.
    • (2006) J. Cell Sci , vol.119 , pp. 3182-3192
    • Baker, M.A.1    Aitken, R.J.2
  • 34
    • 34447307399 scopus 로고    scopus 로고
    • Application of proteomic methods for identification of sperm immunogenic antigens
    • Domagala, A., Pulido, S., Kurpisz, M., Herr, J. C., Application of proteomic methods for identification of sperm immunogenic antigens. Mol. Hum. Reprod. 2007, 13, 437-444.
    • (2007) Mol. Hum. Reprod , vol.13 , pp. 437-444
    • Domagala, A.1    Pulido, S.2    Kurpisz, M.3    Herr, J.C.4
  • 35
    • 33745104040 scopus 로고    scopus 로고
    • Large-scale and high-confidence proteomic analysis of human seminal plasma
    • Pilch, B., Mann, M., Large-scale and high-confidence proteomic analysis of human seminal plasma. Genome Biol. 2006, 7, R40.
    • (2006) Genome Biol , vol.7
    • Pilch, B.1    Mann, M.2
  • 37
    • 0035816608 scopus 로고    scopus 로고
    • A human mitochondrial ferritin encoded by an intronless gene
    • Levi, S., Corsi, B., Bosisio, M., Invernizzi, R. et al., A human mitochondrial ferritin encoded by an intronless gene. J. Biol. Chem. 2001, 276, 24437-24440.
    • (2001) J. Biol. Chem , vol.276 , pp. 24437-24440
    • Levi, S.1    Corsi, B.2    Bosisio, M.3    Invernizzi, R.4
  • 38
    • 42549127662 scopus 로고
    • Spermatozoa mitochondiral ferritin (MtF) content is related to sperm motility
    • Calzi, F., Levi, S., Santambrogio, P., De Santis, L. et al., Spermatozoa mitochondiral ferritin (MtF) content is related to sperm motility. Fertil. Steril. 1993, 80, 31.
    • (1993) Fertil. Steril , vol.80 , pp. 31
    • Calzi, F.1    Levi, S.2    Santambrogio, P.3    De Santis, L.4
  • 39
    • 0024477563 scopus 로고
    • The role of free oxygen radicals and sperm function
    • Aitken, R. J., The role of free oxygen radicals and sperm function. Int. J. Androl. 1989, 12, 95-97.
    • (1989) Int. J. Androl , vol.12 , pp. 95-97
    • Aitken, R.J.1
  • 40
    • 0029451739 scopus 로고
    • Free radicals, lipid peroxidation and sperm function
    • Aitken, R. J., Free radicals, lipid peroxidation and sperm function. Reprod. Fertil. Dev. 1995, 7, 659-668.
    • (1995) Reprod. Fertil. Dev , vol.7 , pp. 659-668
    • Aitken, R.J.1
  • 41
    • 1942532710 scopus 로고    scopus 로고
    • The importance of redox regulated pathways in sperm cell biology
    • Baker, M. A., Aitken, R. J., The importance of redox regulated pathways in sperm cell biology. Mol. Cell. Endocrinol. 2004, 216, 47-54.
    • (2004) Mol. Cell. Endocrinol , vol.216 , pp. 47-54
    • Baker, M.A.1    Aitken, R.J.2
  • 42
    • 28844474824 scopus 로고    scopus 로고
    • Reactive oxygen species in spermatozoa: Methods for monitoring and significance for the origins of genetic disease and infertility
    • Baker, M. A., Aitken, R. J., Reactive oxygen species in spermatozoa: Methods for monitoring and significance for the origins of genetic disease and infertility. Reprod. Biol. Endocrinol. 2005, 3, 67.
    • (2005) Reprod. Biol. Endocrinol , vol.3 , pp. 67
    • Baker, M.A.1    Aitken, R.J.2
  • 43
    • 0019133661 scopus 로고
    • Mutations affecting segment number and polarity in Drosophila
    • Nusslein-Volhard, C., Wieschaus, E., Mutations affecting segment number and polarity in Drosophila. Nature 1980, 287, 795-801.
    • (1980) Nature , vol.287 , pp. 795-801
    • Nusslein-Volhard, C.1    Wieschaus, E.2
  • 44
    • 0030297553 scopus 로고    scopus 로고
    • Dual roles for patched in sequestering and transducing Hedgehog
    • Chen, Y., Struhl, G., Dual roles for patched in sequestering and transducing Hedgehog. Cell 1996, 87, 553-563.
    • (1996) Cell , vol.87 , pp. 553-563
    • Chen, Y.1    Struhl, G.2
  • 45
    • 0032780648 scopus 로고    scopus 로고
    • Lessons from animal models
    • The patched signaling pathway in tumorigenesis and development
    • Hahn, H., Wojnowski, L., Miller, G., Zimmer, A., The patched signaling pathway in tumorigenesis and development: Lessons from animal models. J. Mol. Med. 1999, 77, 459-468.
    • (1999) J. Mol. Med , vol.77 , pp. 459-468
    • Hahn, H.1    Wojnowski, L.2    Miller, G.3    Zimmer, A.4
  • 46
    • 0030901264 scopus 로고    scopus 로고
    • Drosophila CBP is a co-activator of cubitus interruptus in hedgehog signalling
    • Akimaru, H., Chen, Y., Dai, P., Hou, D. X. et al., Drosophila CBP is a co-activator of cubitus interruptus in hedgehog signalling. Nature 1997, 386, 735-738.
    • (1997) Nature , vol.386 , pp. 735-738
    • Akimaru, H.1    Chen, Y.2    Dai, P.3    Hou, D.X.4
  • 48
    • 33646191319 scopus 로고    scopus 로고
    • Odorant receptors and olfactory-like signaling mechanisms in mammalian sperm
    • Spehr, M., Schwane, K., Riffeil, J. A., Zimmer, R. K., Hatt, H., Odorant receptors and olfactory-like signaling mechanisms in mammalian sperm. Mol. Cell. Endocrinol. 2006, 250, 128-136.
    • (2006) Mol. Cell. Endocrinol , vol.250 , pp. 128-136
    • Spehr, M.1    Schwane, K.2    Riffeil, J.A.3    Zimmer, R.K.4    Hatt, H.5
  • 49
    • 0032103774 scopus 로고    scopus 로고
    • Immunohistochemical analysis of the expression of two serine-threonine kinases in the maturing mouse testis
    • Nayak, S., Galili, N., Buck, C. A., Immunohistochemical analysis of the expression of two serine-threonine kinases in the maturing mouse testis. Mech. Dev. 1998, 74, 171-174.
    • (1998) Mech. Dev , vol.74 , pp. 171-174
    • Nayak, S.1    Galili, N.2    Buck, C.A.3
  • 50
    • 18144369690 scopus 로고    scopus 로고
    • Identification and characterization of SSTK, a serine/threonine protein kinase essential for male fertility
    • Spiridonov, N. A., Wong, L., Zerfas, P. M., Starost, M. F. et al., Identification and characterization of SSTK, a serine/threonine protein kinase essential for male fertility. Mol. Cell Biol. 2005, 25, 4250-4261.
    • (2005) Mol. Cell Biol , vol.25 , pp. 4250-4261
    • Spiridonov, N.A.1    Wong, L.2    Zerfas, P.M.3    Starost, M.F.4
  • 51
    • 0345169713 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
    • Ecroyd, H., Jones, R. C., Aitken, R. J., Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation. Biol. Reprod. 2003, 69, 1801-1807.
    • (2003) Biol. Reprod , vol.69 , pp. 1801-1807
    • Ecroyd, H.1    Jones, R.C.2    Aitken, R.J.3
  • 54
    • 0035831474 scopus 로고    scopus 로고
    • Functional relationships between capacitation-dependent cell signaling and compartmentalized metabolic pathways in murine spermatozoa
    • Travis, A. J., Jorgez, C. J., Merdiushev, T., Jones, B. H. et al., Functional relationships between capacitation-dependent cell signaling and compartmentalized metabolic pathways in murine spermatozoa. J. Biol. Chem. 2001, 276, 7630-7636.
    • (2001) J. Biol. Chem , vol.276 , pp. 7630-7636
    • Travis, A.J.1    Jorgez, C.J.2    Merdiushev, T.3    Jones, B.H.4
  • 55
    • 1642462435 scopus 로고    scopus 로고
    • Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation
    • Baker, M. A., Hetherington, L., Ekroyd, H., Roman, S. D., Aitken, R. J., Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation. J. Cell Sci. 2004, 117, 211-222.
    • (2004) J. Cell Sci , vol.117 , pp. 211-222
    • Baker, M.A.1    Hetherington, L.2    Ekroyd, H.3    Roman, S.D.4    Aitken, R.J.5
  • 56
    • 1942476757 scopus 로고    scopus 로고
    • The acroplaxome is the docking site of Golgi-derived myosin Va/Rab27a/b- containing proacrosomal vesicles in wild-type and Hrb mutant mouse spermatids
    • Kierszenbaum, A. L., Tres, L. L., Rivkin, E., Kang-Decker, N., van Deursen, J. M., The acroplaxome is the docking site of Golgi-derived myosin Va/Rab27a/b- containing proacrosomal vesicles in wild-type and Hrb mutant mouse spermatids. Biol. Reprod. 2004, 70, 1400-1410.
    • (2004) Biol. Reprod , vol.70 , pp. 1400-1410
    • Kierszenbaum, A.L.1    Tres, L.L.2    Rivkin, E.3    Kang-Decker, N.4    van Deursen, J.M.5
  • 57
    • 0030581190 scopus 로고    scopus 로고
    • rab 3-peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A2 metabolites
    • Garde, J., Roldan, E. R., rab 3-peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A2 metabolites. FEBS Lett. 1996, 391, 263-268.
    • (1996) FEBS Lett , vol.391 , pp. 263-268
    • Garde, J.1    Roldan, E.R.2
  • 58
    • 0033762476 scopus 로고    scopus 로고
    • Fusion of membranes during acosome reaction: A tale of two SNAREs
    • Kierszanbaum, A. L., Fusion of membranes during acosome reaction: A tale of two SNAREs. Mol. Reprod. Dev. 2000, 57, 309-310.
    • (2000) Mol. Reprod. Dev , vol.57 , pp. 309-310
    • Kierszanbaum, A.L.1
  • 59
    • 38449115722 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane fusion during acrosomal exocytosis
    • Tomes, C. N., Molecular mechanisms of membrane fusion during acrosomal exocytosis. Soc. Reprod. Fertil. Suppl. 2007, 65, 275-291.
    • (2007) Soc. Reprod. Fertil. Suppl , vol.65 , pp. 275-291
    • Tomes, C.N.1
  • 61
    • 0032563119 scopus 로고    scopus 로고
    • Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release?
    • Takagi, H., Shi, D., Ha, Y., Allewell, N. M., Theil, E. C., Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J. Biol. Chem. 1998, 273, 18685-18688.
    • (1998) J. Biol. Chem , vol.273 , pp. 18685-18688
    • Takagi, H.1    Shi, D.2    Ha, Y.3    Allewell, N.M.4    Theil, E.C.5
  • 62
    • 0027245545 scopus 로고
    • Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets
    • Lu, G., Villalba, M., Coscia, M. R., Hoffman, D. R., King, T. P., Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets. J. Immunol. 1993, 150, 2823-2830.
    • (1993) J. Immunol , vol.150 , pp. 2823-2830
    • Lu, G.1    Villalba, M.2    Coscia, M.R.3    Hoffman, D.R.4    King, T.P.5
  • 63
    • 0026788322 scopus 로고
    • Mouse submandibular glands express an androgen-regulated transcript encoding an acidic epididymal glycoprotein-like molecule
    • Mizuki, N., Kasahara, M., Mouse submandibular glands express an androgen-regulated transcript encoding an acidic epididymal glycoprotein-like molecule. Mol. Cell. Endocrinol. 1992, 89, 25-32.
    • (1992) Mol. Cell. Endocrinol , vol.89 , pp. 25-32
    • Mizuki, N.1    Kasahara, M.2
  • 64
    • 0024742682 scopus 로고
    • Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene
    • Kasahara, M., Gutknecht, J., Brew, K., Spurr, N., Goodfellow, P. N., Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. Genomics 1989, 5, 527-534.
    • (1989) Genomics , vol.5 , pp. 527-534
    • Kasahara, M.1    Gutknecht, J.2    Brew, K.3    Spurr, N.4    Goodfellow, P.N.5
  • 65
    • 0031754774 scopus 로고    scopus 로고
    • The armadillo family of structural proteins
    • Hatzfeld, M., The armadillo family of structural proteins. Int. Rev. Cytol. 1999, 186, 179-224.
    • (1999) Int. Rev. Cytol , vol.186 , pp. 179-224
    • Hatzfeld, M.1
  • 66
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?
    • Bork, P., Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally? Proteins 1993, 17, 363-374.
    • (1993) Proteins , vol.17 , pp. 363-374
    • Bork, P.1
  • 67
    • 0023795510 scopus 로고
    • Widespread occurrence of calicin, a basic cytoskeletal protein of sperm cells, in diverse mammalian species
    • Paranko, J., Longo, F., Potts, J., Krohne, G., Franke, W. W., Widespread occurrence of calicin, a basic cytoskeletal protein of sperm cells, in diverse mammalian species. Differ Res. Biol. Divers. 1988, 38, 21-27.
    • (1988) Differ Res. Biol. Divers , vol.38 , pp. 21-27
    • Paranko, J.1    Longo, F.2    Potts, J.3    Krohne, G.4    Franke, W.W.5
  • 68
    • 0041861078 scopus 로고    scopus 로고
    • Equatorial segment protein defines a discrete acrosomal subcompartment persisting throughout acrosomal biogenesis
    • Wolkowicz, M. J., Shetty, J., Westbrook, A., Klotz, K. et al., Equatorial segment protein defines a discrete acrosomal subcompartment persisting throughout acrosomal biogenesis. Biol. Reprod. 2003, 69, 735-745.
    • (2003) Biol. Reprod , vol.69 , pp. 735-745
    • Wolkowicz, M.J.1    Shetty, J.2    Westbrook, A.3    Klotz, K.4
  • 69
    • 0039820804 scopus 로고    scopus 로고
    • Characterization of the human NIPSNAP1 gene from 22q12: A member of a novel gene family
    • Seroussi, E., Pan, H. Q., Kedra, D., Roe, B. A., Dumanski, J. P., Characterization of the human NIPSNAP1 gene from 22q12: A member of a novel gene family. Gene 1998, 212, 13-20.
    • (1998) Gene , vol.212 , pp. 13-20
    • Seroussi, E.1    Pan, H.Q.2    Kedra, D.3    Roe, B.A.4    Dumanski, J.P.5
  • 70
    • 33846295573 scopus 로고    scopus 로고
    • Mouse testicular hyaluronidase-like proteins SPAM1 and HYAL5 but not HYALP1 degrade hyaluronan
    • Reitinger, S., Laschober, G. T., Fehrer, C., Greiderer, B., Lepperdinger, G., Mouse testicular hyaluronidase-like proteins SPAM1 and HYAL5 but not HYALP1 degrade hyaluronan. Biochem. J. 2007, 401, 79-85.
    • (2007) Biochem. J , vol.401 , pp. 79-85
    • Reitinger, S.1    Laschober, G.T.2    Fehrer, C.3    Greiderer, B.4    Lepperdinger, G.5
  • 71
    • 0024230925 scopus 로고
    • A single 12.5-kilobase androgen-regulated mRNA encoding multiple proline-rich polypeptides in the ventral prostate of the rat
    • Hemschoote, K., Peeters, B., Dirckx, L., Claessens, F. et al., A single 12.5-kilobase androgen-regulated mRNA encoding multiple proline-rich polypeptides in the ventral prostate of the rat. J. Biol. Chem. 1988, 263, 19159-19165.
    • (1988) J. Biol. Chem , vol.263 , pp. 19159-19165
    • Hemschoote, K.1    Peeters, B.2    Dirckx, L.3    Claessens, F.4
  • 72
    • 0036300780 scopus 로고    scopus 로고
    • Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions
    • Mueller, T. D., Feigon, J., Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. J. Mol. Biol. 2002, 319, 1243-1255.
    • (2002) J. Mol. Biol , vol.319 , pp. 1243-1255
    • Mueller, T.D.1    Feigon, J.2
  • 73
    • 36348946462 scopus 로고    scopus 로고
    • FSCB, a novel protein kinase A-phosphorylated calcium-binding protein, is a CABYR-binding partner involved in late steps of fibrous sheath biogenesis
    • Li, Y. F., He, W., Jha, K. N., Klotz, K. et al., FSCB, a novel protein kinase A-phosphorylated calcium-binding protein, is a CABYR-binding partner involved in late steps of fibrous sheath biogenesis. J. Biol. Chem. 2007, 282, 34104-34119.
    • (2007) J. Biol. Chem , vol.282 , pp. 34104-34119
    • Li, Y.F.1    He, W.2    Jha, K.N.3    Klotz, K.4


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