메뉴 건너뛰기




Volumn 13, Issue 12, 2014, Pages 5670-5684

Identification of proteins involved in human sperm motility using high-throughput differential proteomics

Author keywords

Human sperm motility; male infertility; pathways analysis; quantitative proteomics; TMT labeling

Indexed keywords

CYTOSKELETON PROTEIN; MITOCHONDRIAL PROTEIN; PROTEOME;

EID: 84915748593     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr500652y     Document Type: Article
Times cited : (144)

References (77)
  • 1
    • 79951508691 scopus 로고    scopus 로고
    • Contemporary concepts in the evaluation and management of male infertility
    • Hwang, K.; Walters, R. C.; Lipshultz, L. I. Contemporary concepts in the evaluation and management of male infertility Nat. Rev. Urol. 2011, 8, 86-94
    • (2011) Nat. Rev. Urol. , vol.8 , pp. 86-94
    • Hwang, K.1    Walters, R.C.2    Lipshultz, L.I.3
  • 4
    • 84884564637 scopus 로고    scopus 로고
    • Sperm quality and its relationship to natural and assisted conception: British Fertility Society guidelines for practice
    • Tomlinson, M.; Lewis, S.; Morroll, D. Sperm quality and its relationship to natural and assisted conception: British Fertility Society guidelines for practice Hum. Fertil. 2013, 16, 175-193
    • (2013) Hum. Fertil. , vol.16 , pp. 175-193
    • Tomlinson, M.1    Lewis, S.2    Morroll, D.3
  • 5
    • 29244476879 scopus 로고    scopus 로고
    • Moving to the beat: A review of mammalian sperm motility regulation
    • Turner, R. M. Moving to the beat: a review of mammalian sperm motility regulation Reprod. Fertil. Dev. 2006, 18, 25-38
    • (2006) Reprod. Fertil. Dev. , vol.18 , pp. 25-38
    • Turner, R.M.1
  • 6
    • 33745272289 scopus 로고    scopus 로고
    • Knockout mouse models of sperm flagellum anomalies
    • Escalier, D. Knockout mouse models of sperm flagellum anomalies Hum. Reprod. Update 2006, 12, 449-461
    • (2006) Hum. Reprod. Update , vol.12 , pp. 449-461
    • Escalier, D.1
  • 7
    • 79960557909 scopus 로고    scopus 로고
    • Sperm flagella: Comparative and phylogenetic perspectives of protein components
    • Inaba, K. Sperm flagella: comparative and phylogenetic perspectives of protein components Mol. Hum. Reprod. 2011, 17, 524-538
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 524-538
    • Inaba, K.1
  • 8
    • 80055094651 scopus 로고    scopus 로고
    • Rediscovering sperm ion channels with the patch-clamp technique
    • Kirichok, Y.; Lishko, P. V. Rediscovering sperm ion channels with the patch-clamp technique Mol. Hum. Reprod. 2011, 17, 478-499
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 478-499
    • Kirichok, Y.1    Lishko, P.V.2
  • 9
    • 80055076248 scopus 로고    scopus 로고
    • Mathematical modeling of calcium signaling during sperm hyperactivation
    • Olson, S. D.; Fauci, L. J.; Suarez, S. S. Mathematical modeling of calcium signaling during sperm hyperactivation Mol. Hum. Reprod. 2011, 17, 500-510
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 500-510
    • Olson, S.D.1    Fauci, L.J.2    Suarez, S.S.3
  • 10
    • 80055068447 scopus 로고    scopus 로고
    • Sperm motility: Is viscosity fundamental to progress?
    • Kirkman-Brown, J. C.; Smith, D. J. Sperm motility: is viscosity fundamental to progress? Mol. Hum. Reprod. 2011, 17, 539-544
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 539-544
    • Kirkman-Brown, J.C.1    Smith, D.J.2
  • 12
    • 80055067653 scopus 로고    scopus 로고
    • Sperm motility: Things are moving in the lab!
    • Publicover, S. J.; Barratt, C. L. R. Sperm motility: things are moving in the lab! Mol. Hum. Reprod. 2011, 17, 453-456
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 453-456
    • Publicover, S.J.1    Barratt, C.L.R.2
  • 13
    • 45949103424 scopus 로고    scopus 로고
    • Proteomics in the study of the sperm cell composition, differentiation and function
    • Oliva, R.; Martínez-Heredia, J.; Estanyol, J. M. Proteomics in the study of the sperm cell composition, differentiation and function Syst. Biol. Reprod. Med. 2008, 54, 23-36
    • (2008) Syst. Biol. Reprod. Med. , vol.54 , pp. 23-36
    • Oliva, R.1    Martínez-Heredia, J.2    Estanyol, J.M.3
  • 15
    • 33846632407 scopus 로고    scopus 로고
    • Identification of several proteins involved in regulation of sperm motility by proteomic analysis
    • Zhao, C.; Huo, R.; Wang, F.-Q.; Lin, M.; Zhou, Z.-M.; Sha, J.-H. Identification of several proteins involved in regulation of sperm motility by proteomic analysis Fertil. Steril. 2007, 87, 436-438
    • (2007) Fertil. Steril. , vol.87 , pp. 436-438
    • Zhao, C.1    Huo, R.2    Wang, F.-Q.3    Lin, M.4    Zhou, Z.-M.5    Sha, J.-H.6
  • 19
    • 84866285287 scopus 로고    scopus 로고
    • Sperm phosphoproteome profiling by ultra performance liquid chromatography followed by data independent analysis (LC-MS(E)) reveals altered proteomic signatures in asthenozoospermia
    • Parte, P. P.; Rao, P.; Redij, S.; Lobo, V.; D'Souza, S. J.; Gajbhiye, R.; Kulkarni, V. Sperm phosphoproteome profiling by ultra performance liquid chromatography followed by data independent analysis (LC-MS(E)) reveals altered proteomic signatures in asthenozoospermia J. Proteomics 2012, 75, 5861-5871
    • (2012) J. Proteomics , vol.75 , pp. 5861-5871
    • Parte, P.P.1    Rao, P.2    Redij, S.3    Lobo, V.4    D'Souza, S.J.5    Gajbhiye, R.6    Kulkarni, V.7
  • 20
    • 84889633604 scopus 로고    scopus 로고
    • The combined human sperm proteome: Cellular pathways and implications for basic and clinical science
    • Amaral, A.; Castillo, J.; Ramalho-Santos, J.; Oliva, R. The combined human sperm proteome: cellular pathways and implications for basic and clinical science Hum. Reprod. Update 2014, 20, 40-62
    • (2014) Hum. Reprod. Update , vol.20 , pp. 40-62
    • Amaral, A.1    Castillo, J.2    Ramalho-Santos, J.3    Oliva, R.4
  • 21
    • 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.; Müller, J.; Baur, I.; 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    Müller, J.4    Baur, I.5    Aitken, R.J.6
  • 24
    • 84934443766 scopus 로고    scopus 로고
    • Spermatogenesis
    • In; Carrell, D. T. Aston, K. I. Humana Press: Totowa, NJ, Vol
    • De Mateo, S.; Estanyol, J. M.; Oliva, R. Spermatogenesis. In Methods in Molecular Biology; Carrell, D. T.; Aston, K. I., Eds.; Humana Press: Totowa, NJ, 2013; Vol. 927, pp 411-422.
    • (2013) Methods in Molecular Biology , vol.927 , pp. 411-422
    • De Mateo, S.1    Estanyol, J.M.2    Oliva, R.3
  • 26
    • 84899128858 scopus 로고    scopus 로고
    • Sperm nuclear proteome and its epigenetic potential
    • Castillo, J.; Amaral, A.; Oliva, R. Sperm nuclear proteome and its epigenetic potential Andrology 2014, 2, 326-338
    • (2014) Andrology , vol.2 , pp. 326-338
    • Castillo, J.1    Amaral, A.2    Oliva, R.3
  • 27
  • 28
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson, A.; Schäfer, J.; Kuhn, K.; Kienle, S.; Schwarz, J.; Schmidt, G.; Neumann, T.; Hamon, C. Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS Anal. Chem. 2003, 75, 1895-1904
    • (2003) Anal. Chem. , vol.75 , pp. 1895-1904
    • Thompson, A.1    Schäfer, J.2    Kuhn, K.3    Kienle, S.4    Schwarz, J.5    Schmidt, G.6    Neumann, T.7    Hamon, C.8
  • 29
    • 77951533012 scopus 로고    scopus 로고
    • From relative to absolute quantification of tryptic peptides with tandem mass tags: Application to cerebrospinal fluid
    • Dayon, L.; Turck, N.; Scherl, A.; Hochstrasser, D. F.; Burkhard, P. R.; Sanchez, J.-C. From relative to absolute quantification of tryptic peptides with tandem mass tags: application to cerebrospinal fluid Chimia 2010, 64, 132-135
    • (2010) Chimia , vol.64 , pp. 132-135
    • Dayon, L.1    Turck, N.2    Scherl, A.3    Hochstrasser, D.F.4    Burkhard, P.R.5    Sanchez, J.-C.6
  • 30
    • 79961174266 scopus 로고    scopus 로고
    • Quantitative profiling of serum samples using TMT protein labelling, fractionation and LC-MS/MS
    • Sinclair, J.; Timms, J. F. Quantitative profiling of serum samples using TMT protein labelling, fractionation and LC-MS/MS Methods 2011, 54, 361-369
    • (2011) Methods , vol.54 , pp. 361-369
    • Sinclair, J.1    Timms, J.F.2
  • 31
    • 84861811029 scopus 로고    scopus 로고
    • Characterization of breast cancer interstitial fluids by TmT labeling, LTQ-Orbitrap Velos mass spectrometry, and pathway analysis
    • Raso, C.; Cosentino, C.; Gaspari, M.; Malara, N.; Han, X.; McClatchy, D.; Park, S. K.; Renne, M.; Vadalà, N.; Prati, U. Characterization of breast cancer interstitial fluids by TmT labeling, LTQ-Orbitrap Velos mass spectrometry, and pathway analysis J. Proteome Res. 2012, 11, 3199-3210
    • (2012) J. Proteome Res. , vol.11 , pp. 3199-3210
    • Raso, C.1    Cosentino, C.2    Gaspari, M.3    Malara, N.4    Han, X.5    McClatchy, D.6    Park, S.K.7    Renne, M.8    Vadalà, N.9    Prati, U.10
  • 32
    • 84878659474 scopus 로고    scopus 로고
    • Increasing throughput in targeted proteomics assays: 54-plex quantitation in a single mass spectrometry run
    • Everley, R. A.; Kunz, R. C.; McAllister, F. E.; Gygi, S. P. Increasing throughput in targeted proteomics assays: 54-plex quantitation in a single mass spectrometry run Anal. Chem. 2013, 85, 5340-5346
    • (2013) Anal. Chem. , vol.85 , pp. 5340-5346
    • Everley, R.A.1    Kunz, R.C.2    McAllister, F.E.3    Gygi, S.P.4
  • 33
    • 84900793731 scopus 로고    scopus 로고
    • High-throughput sperm differential proteomics suggests that epigenetic alterations contribute to failed assisted reproduction
    • Azpiazu, R.; Amaral, A.; Castillo, J.; Estanyol, J. M.; Guimerà, M.; Ballescà, J. L.; Balasch, J.; Oliva, R. High-throughput sperm differential proteomics suggests that epigenetic alterations contribute to failed assisted reproduction Hum. Reprod. 2014, 29, 1225-1237
    • (2014) Hum. Reprod. , vol.29 , pp. 1225-1237
    • Azpiazu, R.1    Amaral, A.2    Castillo, J.3    Estanyol, J.M.4    Guimerà, M.5    Ballescà, J.L.6    Balasch, J.7    Oliva, R.8
  • 36
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, D. W.; Sherman, B. T.; Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources Nat. Protoc. 2009, 4, 44-57
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 37
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • Huang, D. W.; Sherman, B. T.; Lempicki, R. A. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists Nucleic Acids Res. 2009, 37, 1-13
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 38
    • 16344389891 scopus 로고    scopus 로고
    • PermutMatrix: A graphical environment to arrange gene expression profiles in optimal linear order
    • Caraux, G.; Pinloche, S. PermutMatrix: a graphical environment to arrange gene expression profiles in optimal linear order Bioinformatics 2005, 21, 1280-1281
    • (2005) Bioinformatics , vol.21 , pp. 1280-1281
    • Caraux, G.1    Pinloche, S.2
  • 40
    • 55249093249 scopus 로고    scopus 로고
    • The tektin family of microtubule-stabilizing proteins
    • Amos, L. A. The tektin family of microtubule-stabilizing proteins Genome Biol. 2008, 9, 229
    • (2008) Genome Biol. , vol.9 , pp. 229
    • Amos, L.A.1
  • 42
    • 0942297998 scopus 로고    scopus 로고
    • Tektin3 encodes an evolutionarily conserved putative testicular microtubules-related protein expressed preferentially in male germ cells
    • Roy, A.; Yan, W.; Burns, K. H.; Matzuk, M. M. Tektin3 encodes an evolutionarily conserved putative testicular microtubules-related protein expressed preferentially in male germ cells Mol. Reprod. Dev. 2004, 67, 295-302
    • (2004) Mol. Reprod. Dev. , vol.67 , pp. 295-302
    • Roy, A.1    Yan, W.2    Burns, K.H.3    Matzuk, M.M.4
  • 43
    • 79251509219 scopus 로고    scopus 로고
    • Characterization of a novel tektin member, TEKT5, in mouse sperm
    • Cao, W.; Ijiri, T. W.; Huang, A. P.; Gerton, G. L. Characterization of a novel tektin member, TEKT5, in mouse sperm J. Androl. 2011, 32, 55-69
    • (2011) J. Androl. , vol.32 , pp. 55-69
    • Cao, W.1    Ijiri, T.W.2    Huang, A.P.3    Gerton, G.L.4
  • 45
    • 84894095539 scopus 로고    scopus 로고
    • Localization of Tektin 1 at both acrosome and flagella of mouse and bull spermatozoa
    • Oiki, S.; Hiyama, E.; Gotoh, T.; Iida, H. Localization of Tektin 1 at both acrosome and flagella of mouse and bull spermatozoa Zool. Sci. 2014, 31, 101-107
    • (2014) Zool. Sci. , vol.31 , pp. 101-107
    • Oiki, S.1    Hiyama, E.2    Gotoh, T.3    Iida, H.4
  • 46
    • 33744753472 scopus 로고    scopus 로고
    • Tektin 4 is located on outer dense fibers, not associated with axonemal tubulins of flagella in rodent spermatozoa
    • Iida, H.; Honda, Y.; Matsuyama, T.; Shibata, Y.; Inai, T. Tektin 4 is located on outer dense fibers, not associated with axonemal tubulins of flagella in rodent spermatozoa Mol. Reprod. Dev. 2006, 73, 929-936
    • (2006) Mol. Reprod. Dev. , vol.73 , pp. 929-936
    • Iida, H.1    Honda, Y.2    Matsuyama, T.3    Shibata, Y.4    Inai, T.5
  • 47
    • 40049093698 scopus 로고    scopus 로고
    • Tektin5, a new Tektin family member, is a component of the middle piece of flagella in rat spermatozoa
    • Murayama, E.; Yamamoto, E.; Kaneko, T.; Shibata, Y.; Inai, T.; Iida, H. Tektin5, a new Tektin family member, is a component of the middle piece of flagella in rat spermatozoa Mol. Reprod. Dev. 2008, 75, 650-658
    • (2008) Mol. Reprod. Dev. , vol.75 , pp. 650-658
    • Murayama, E.1    Yamamoto, E.2    Kaneko, T.3    Shibata, Y.4    Inai, T.5    Iida, H.6
  • 48
    • 4444289801 scopus 로고    scopus 로고
    • Mice deficient in the axonemal protein Tektin-t exhibit male infertility and immotile-cilium syndrome due to impaired inner arm dynein function
    • Tanaka, H.; Iguchi, N.; Toyama, Y.; Kitamura, K.; Takahashi, T.; Kaseda, K.; Maekawa, M.; Nishimune, Y. Mice deficient in the axonemal protein Tektin-t exhibit male infertility and immotile-cilium syndrome due to impaired inner arm dynein function Mol. Cell. Biol. 2004, 24, 7958-7964
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7958-7964
    • Tanaka, H.1    Iguchi, N.2    Toyama, Y.3    Kitamura, K.4    Takahashi, T.5    Kaseda, K.6    Maekawa, M.7    Nishimune, Y.8
  • 49
    • 33947655346 scopus 로고    scopus 로고
    • Absence of tektin 4 causes asthenozoospermia and subfertility in male mice
    • Roy, A.; Lin, Y.-N.; Agno, J. E.; DeMayo, F. J.; Matzuk, M. M. Absence of tektin 4 causes asthenozoospermia and subfertility in male mice FASEB J. 2007, 21, 1013-1025
    • (2007) FASEB J. , vol.21 , pp. 1013-1025
    • Roy, A.1    Lin, Y.-N.2    Agno, J.E.3    Demayo, F.J.4    Matzuk, M.M.5
  • 50
    • 43249090398 scopus 로고    scopus 로고
    • A possible association of a human tektin-t gene mutation (A229V) with isolated non-syndromic asthenozoospermia: Case report
    • Zuccarello, D.; Ferlin, A.; Garolla, A.; Pati, M. a; Moretti, A.; Cazzadore, C.; Francavilla, S.; Foresta, C. A possible association of a human tektin-t gene mutation (A229V) with isolated non-syndromic asthenozoospermia: case report Hum. Reprod. 2008, 23, 996-1001
    • (2008) Hum. Reprod. , vol.23 , pp. 996-1001
    • Zuccarello, D.1    Ferlin, A.2    Garolla, A.3    Pati, M.A.4    Moretti, A.5    Cazzadore, C.6    Francavilla, S.7    Foresta, C.8
  • 53
    • 84880448771 scopus 로고    scopus 로고
    • KIF3A is essential for sperm tail formation and manchette function
    • Lehti, M. S.; Kotaja, N.; Sironen, A. KIF3A is essential for sperm tail formation and manchette function Mol. Cell. Endocrinol. 2013, 377, 44-55
    • (2013) Mol. Cell. Endocrinol. , vol.377 , pp. 44-55
    • Lehti, M.S.1    Kotaja, N.2    Sironen, A.3
  • 54
    • 69049087814 scopus 로고    scopus 로고
    • Mitochondrial functionality in reproduction: From gonads and gametes to embryos and embryonic stem cells
    • Ramalho-Santos, J.; Varum, S.; Amaral, S.; Mota, P. C.; Sousa, A. P.; Amaral, A. Mitochondrial functionality in reproduction: from gonads and gametes to embryos and embryonic stem cells Hum. Reprod. Update 2009, 15, 553-572
    • (2009) Hum. Reprod. Update , vol.15 , pp. 553-572
    • Ramalho-Santos, J.1    Varum, S.2    Amaral, S.3    Mota, P.C.4    Sousa, A.P.5    Amaral, A.6
  • 55
    • 80053337018 scopus 로고    scopus 로고
    • Exogenous glucose improves long-standing human sperm motility, viability, and mitochondrial function
    • Amaral, A.; Paiva, C.; Baptista, M.; Sousa, A. P.; Ramalho-Santos, J. Exogenous glucose improves long-standing human sperm motility, viability, and mitochondrial function Fertil. Steril. 2011, 96, 848-850
    • (2011) Fertil. Steril. , vol.96 , pp. 848-850
    • Amaral, A.1    Paiva, C.2    Baptista, M.3    Sousa, A.P.4    Ramalho-Santos, J.5
  • 57
    • 34447303791 scopus 로고    scopus 로고
    • The expression of polymerase gamma and mitochondrial transcription factor A and the regulation of mitochondrial DNA content in mature human sperm
    • Amaral, A.; Ramalho-Santos, J.; St John, J. C. The expression of polymerase gamma and mitochondrial transcription factor A and the regulation of mitochondrial DNA content in mature human sperm Hum. Reprod. 2007, 22, 1585-1596
    • (2007) Hum. Reprod. , vol.22 , pp. 1585-1596
    • Amaral, A.1    Ramalho-Santos, J.2    St John, J.C.3
  • 58
    • 74349089527 scopus 로고    scopus 로고
    • Assessment of mitochondrial potential: Implications for the correct monitoring of human sperm function
    • Amaral, A.; Ramalho-Santos, J. Assessment of mitochondrial potential: implications for the correct monitoring of human sperm function Int. J. Androl. 2010, 33, e180-6
    • (2010) Int. J. Androl. , vol.33 , pp. 180-186
    • Amaral, A.1    Ramalho-Santos, J.2
  • 61
    • 16244366793 scopus 로고    scopus 로고
    • The impact of mitochondrial genetics on male infertility
    • St John, J. C.; Jokhi, R. P.; Barratt, C. L. R. The impact of mitochondrial genetics on male infertility Int. J. Androl. 2005, 28, 65-73
    • (2005) Int. J. Androl. , vol.28 , pp. 65-73
    • St John, J.C.1    Jokhi, R.P.2    Barratt, C.L.R.3
  • 62
    • 0020181886 scopus 로고
    • Fatty acid synthesis in isolated spermatocytes and spermatids of mouse testis
    • Grogan, W. M.; Lam, J. W. Fatty acid synthesis in isolated spermatocytes and spermatids of mouse testis Lipids 1982, 17, 604-611
    • (1982) Lipids , vol.17 , pp. 604-611
    • Grogan, W.M.1    Lam, J.W.2
  • 64
    • 0032697684 scopus 로고    scopus 로고
    • Specific expression of heat shock protein HspA2 in human male germ cells
    • Son, W. Y.; Hwang, S. H.; Han, C. T.; Lee, J. H.; Kim, S.; Kim, Y. C. Specific expression of heat shock protein HspA2 in human male germ cells Mol. Hum. Reprod. 1999, 5, 1122-1126
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 1122-1126
    • Son, W.Y.1    Hwang, S.H.2    Han, C.T.3    Lee, J.H.4    Kim, S.5    Kim, Y.C.6
  • 68
    • 0033837992 scopus 로고    scopus 로고
    • Putative creatine kinase M-isoform in human sperm is identifiedas the 70-kilodalton heat shock protein HspA2
    • Huszar, G.; Stone, K.; Dix, D.; Vigue, L. Putative creatine kinase M-isoform in human sperm is identifiedas the 70-kilodalton heat shock protein HspA2 Biol. Reprod. 2000, 63, 925-932
    • (2000) Biol. Reprod. , vol.63 , pp. 925-932
    • Huszar, G.1    Stone, K.2    Dix, D.3    Vigue, L.4
  • 69
    • 0034076573 scopus 로고    scopus 로고
    • Repression of hspA2 messenger RNA in human testes with abnormal spermatogenesis
    • Son, W. Y.; Han, C. T.; Hwang, S. H.; Lee, J. H.; Kim, S.; Kim, Y. C. Repression of hspA2 messenger RNA in human testes with abnormal spermatogenesis Fertil. Steril. 2000, 73, 1138-1144
    • (2000) Fertil. Steril. , vol.73 , pp. 1138-1144
    • Son, W.Y.1    Han, C.T.2    Hwang, S.H.3    Lee, J.H.4    Kim, S.5    Kim, Y.C.6
  • 70
    • 18644368855 scopus 로고    scopus 로고
    • WDRPUH, a novel WD-repeat-containing protein, is highly expressed in human hepatocellular carcinoma and involved in cell proliferation
    • Silva, F. P.; Hamamoto, R.; Nakamura, Y.; Furukawa, Y. WDRPUH, a novel WD-repeat-containing protein, is highly expressed in human hepatocellular carcinoma and involved in cell proliferation Neoplasia 2005, 7, 348-355
    • (2005) Neoplasia , vol.7 , pp. 348-355
    • Silva, F.P.1    Hamamoto, R.2    Nakamura, Y.3    Furukawa, Y.4
  • 71
    • 79960447102 scopus 로고    scopus 로고
    • Sperm proteasome and fertilization
    • Sutovsky, P. Sperm proteasome and fertilization Reproduction 2011, 142, 1-14
    • (2011) Reproduction , vol.142 , pp. 1-14
    • Sutovsky, P.1
  • 72
    • 84878404112 scopus 로고    scopus 로고
    • New insights to the ubiquitin-proteasome pathway (UPP) mechanism during spermatogenesis
    • Hou, C.-C.; Yang, W.-X. New insights to the ubiquitin-proteasome pathway (UPP) mechanism during spermatogenesis Mol. Biol. Rep. 2013, 40, 3213-3230
    • (2013) Mol. Biol. Rep. , vol.40 , pp. 3213-3230
    • Hou, C.-C.1    Yang, W.-X.2
  • 73
    • 54249087642 scopus 로고    scopus 로고
    • Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation
    • Arcelay, E.; Salicioni, A. M.; Wertheimer, E.; Visconti, P. E. Identification of proteins undergoing tyrosine phosphorylation during mouse sperm capacitation Int. J. Dev. Biol. 2008, 52, 463-472
    • (2008) Int. J. Dev. Biol. , vol.52 , pp. 463-472
    • Arcelay, E.1    Salicioni, A.M.2    Wertheimer, E.3    Visconti, P.E.4
  • 74
    • 0036929129 scopus 로고    scopus 로고
    • NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases
    • Liu, J.; Furukawa, M.; Matsumoto, T.; Xiong, Y. NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases Mol. Cell 2002, 10, 1511-1518
    • (2002) Mol. Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 76
    • 84866558307 scopus 로고    scopus 로고
    • CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer
    • Korzeniewski, N.; Hohenfellner, M.; Duensing, S. CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer Neoplasia 2012, 14, 799-806
    • (2012) Neoplasia , vol.14 , pp. 799-806
    • Korzeniewski, N.1    Hohenfellner, M.2    Duensing, S.3
  • 77
    • 20444385146 scopus 로고    scopus 로고
    • SNARE proteins and caveolin-1 in stallion spermatozoa: Possible implications for fertility
    • Gamboa, S.; Ramalho-Santos, J. SNARE proteins and caveolin-1 in stallion spermatozoa: possible implications for fertility Theriogenology 2005, 64, 275-291
    • (2005) Theriogenology , vol.64 , pp. 275-291
    • Gamboa, S.1    Ramalho-Santos, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.