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Volumn 346, Issue 1, 2011, Pages 1-9

Proteasomal degradation of ubiquitinated proteins in oocyte meiosis and fertilization in mammals

Author keywords

Fertilization; Meiosis; Oocyte; Proteasome; Ubiquitin

Indexed keywords

ANAPHASE PROMOTING COMPLEX; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; PROTEASOME; UBIQUITIN;

EID: 80053345641     PISSN: 0302766X     EISSN: 14320878     Source Type: Journal    
DOI: 10.1007/s00441-011-1235-1     Document Type: Review
Times cited : (28)

References (86)
  • 1
    • 0027948083 scopus 로고
    • Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization
    • T Baba S Azuma S Kashiwabara Y Toyoda 1994 Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization J Biol Chem 269 31845 31849 7989357 1:CAS:528:DyaK2cXmvFOkt7g%3D (Pubitemid 24379557)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.50 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.-I.3    Toyoda, Y.4
  • 2
    • 46049094886 scopus 로고    scopus 로고
    • The rat sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification
    • DOI 10.1002/pmic.200700876
    • MA Baker L Hetherington G Reeves J Müller RJ Aitken 2008 The rat sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification Proteomics 8 2312 2321 18528845 10.1002/pmic.200700876 1:CAS:528:DC%2BD1cXotVeitbk%3D (Pubitemid 351898035)
    • (2008) Proteomics , vol.8 , Issue.11 , pp. 2312-2321
    • Baker, M.A.1    Hetherington, L.2    Reeves, G.3    Muller, J.4    Aitken, R.J.5
  • 3
    • 46049094886 scopus 로고    scopus 로고
    • The mouse sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification
    • DOI 10.1002/pmic.200701020
    • MA Baker L Hetherington GM Reeves RJ Aitken 2008 The mouse sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification Proteomics 8 1720 1730 18340633 10.1002/pmic.200701020 1:CAS:528: DC%2BD1cXlsVWit7s%3D (Pubitemid 351580215)
    • (2008) Proteomics , vol.8 , Issue.8 , pp. 1720-1730
    • Baker, M.A.1    Hetherington, L.2    Reeves, G.M.3    Aitken, R.J.4
  • 5
    • 25444517778 scopus 로고    scopus 로고
    • Involvement of the SCF complex in the control of Cdh1 degradation in S-phase
    • R Benmaamar M Pagano 2005 Involvement of the SCF complex in the control of Cdh1 degradation in S-phase Cell Cycle 4 1230 1232 16123585 10.4161/cc.4.9.2048 1:CAS:528:DC%2BD28XktVCgtb4%3D (Pubitemid 41365394)
    • (2005) Cell Cycle , vol.4 , Issue.9 , pp. 1230-1232
    • Benmaamar, R.1    Pagano, M.2
  • 6
    • 79251596169 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic roles of ubiquitin and the ubiquitin proteasome system in transcriptional regulation
    • 21184853 1:CAS:528:DC%2BC3MXhtleis7w%3D
    • KP Bhat SF Greer 2011 Proteolytic and non-proteolytic roles of ubiquitin and the ubiquitin proteasome system in transcriptional regulation Biochim Biophys Acta 1809 150 155 21184853 1:CAS:528:DC%2BC3MXhtleis7w%3D
    • (2011) Biochim Biophys Acta , vol.1809 , pp. 150-155
    • Bhat, K.P.1    Greer, S.F.2
  • 8
    • 0028934581 scopus 로고
    • Oocyte and follicular morphology as determining characteristics for developmental competence in bovine oocytes
    • 7619506 10.1002/mrd.1080410109 1:CAS:528:DyaK2MXlsVagsrs%3D
    • P Blondin MA Sirard 1995 Oocyte and follicular morphology as determining characteristics for developmental competence in bovine oocytes Mol Reprod Dev 41 54 62 7619506 10.1002/mrd.1080410109 1:CAS:528:DyaK2MXlsVagsrs%3D
    • (1995) Mol Reprod Dev , vol.41 , pp. 54-62
    • Blondin, P.1    Sirard, M.A.2
  • 9
    • 41049104393 scopus 로고    scopus 로고
    • Role of proteasomal activity in the induction of acrosomal exocytosis in human spermatozoa
    • S Chakravarty P Bansal P Sutovsky SK Gupta 2008 Role of proteasomal activity in the induction of acrosomal exocytosis in human spermatozoa Reprod Biomed Online 16 391 400 18339263 10.1016/S1472-6483(10)60601-3 1:CAS:528:DC%2BD1cXks1Sqt7c%3D (Pubitemid 351419459)
    • (2008) Reproductive BioMedicine Online , vol.16 , Issue.3 , pp. 391-400
    • Chakravarty, S.1    Bansal, P.2    Sutovsky, P.3    Gupta, S.K.4
  • 10
    • 0028958186 scopus 로고
    • The Drosophila cell cycle gene fizzy is required for normal degradation of cyclins A and B during mitosis and has homology to the CDC20 gene of Saccharomyces cerevisiae
    • 7730407 10.1083/jcb.129.3.725 1:CAS:528:DyaK2MXlt1Wrs74%3D
    • IA Dawson S Roth S Artavanis-Tsakonas 1995 The Drosophila cell cycle gene fizzy is required for normal degradation of cyclins A and B during mitosis and has homology to the CDC20 gene of Saccharomyces cerevisiae J Cell Biol 129 725 737 7730407 10.1083/jcb.129.3.725 1:CAS:528:DyaK2MXlt1Wrs74%3D
    • (1995) J Cell Biol , vol.129 , pp. 725-737
    • Dawson, I.A.1    Roth, S.2    Artavanis-Tsakonas, S.3
  • 12
    • 17044431753 scopus 로고    scopus 로고
    • Cellular, biochemical and molecular mechanisms regulating oocyte maturation
    • 15836949 10.1016/j.mce.2004.09.010 1:CAS:528:DC%2BD2MXjt1SqtL8%3D
    • N Dekel 2005 Cellular, biochemical and molecular mechanisms regulating oocyte maturation Mol Cell Endocrinol 234 19 25 15836949 10.1016/j.mce.2004.09. 010 1:CAS:528:DC%2BD2MXjt1SqtL8%3D
    • (2005) Mol Cell Endocrinol , vol.234 , pp. 19-25
    • Dekel, N.1
  • 13
    • 31044453144 scopus 로고    scopus 로고
    • The Evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor Emi1
    • DOI 10.1016/j.cell.2005.10.038, PII S0092867405013231
    • AG Eldridge AV Loktev DV Hansen EW Verschuren JD Reimann PK Jackson 2006 The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1 Cell 124 367 380 16439210 10.1016/j.cell.2005.10.038 1:CAS:528:DC%2BD28Xht1Kktb0%3D (Pubitemid 43121984)
    • (2006) Cell , vol.124 , Issue.2 , pp. 367-380
    • Eldridge, A.G.1    Loktev, A.V.2    Hansen, D.V.3    Verschuren, E.W.4    Reimann, J.D.R.5    Jackson, P.K.6
  • 14
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • S Fang AM Weissman 2004 A field guide to ubiquitylation Cell Mol Life Sci 61 1546 1561 15224180 10.1007/s00018-004-4129-5 1:CAS:528:DC%2BD2cXntlCktb4%3D (Pubitemid 38962038)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.13 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 16
    • 75749150366 scopus 로고    scopus 로고
    • P-body loss is concomitant with formation of a messenger RNA storage domain in mouse oocytes
    • 20075394 10.1095/biolreprod.109.082057 1:CAS:528:DC%2BC3cXlt1Khtb4%3D
    • M Flemr J Ma RM Schultz P Svoboda 2010 P-body loss is concomitant with formation of a messenger RNA storage domain in mouse oocytes Biol Reprod 82 1008 1017 20075394 10.1095/biolreprod.109.082057 1:CAS:528:DC%2BC3cXlt1Khtb4%3D
    • (2010) Biol Reprod , vol.82 , pp. 1008-1017
    • Flemr, M.1    Ma, J.2    Schultz, R.M.3    Svoboda, P.4
  • 17
    • 80052717417 scopus 로고    scopus 로고
    • Ubiquitylation and the Fanconi anemia pathway
    • in press doi: 10.1016/j.febslet.2011.04.078)
    • Garner E, Smogorzewska A (2011) Ubiquitylation and the Fanconi anemia pathway. FEBS Lett, in press (doi: 10.1016/j.febslet.2011.04.078 )
    • (2011) FEBS Lett
    • Garner, E.1    Smogorzewska, A.2
  • 18
    • 0025012866 scopus 로고
    • Cyclin is a component of maturation-promoting factor from xenopus
    • DOI 10.1016/0092-8674(90)90599-A
    • J Gautier J Minshull M Lohka M Glotzer T Hunt JL Maller 1990 Cyclin is a component of maturation-promoting factor from Xenopus Cell 60 487 494 1967981 10.1016/0092-8674(90)90599-A 1:CAS:528:DyaK3cXhslClt7o%3D (Pubitemid 20060877)
    • (1990) Cell , vol.60 , Issue.3 , pp. 487-494
    • Gautier, J.1    Minshull, J.2    Lohka, M.3    Glotzer, M.4    Hunt, T.5    Maller, J.L.6
  • 19
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • M Glotzer AW Murray MW Kirschner 1991 Cyclin is degraded by the ubiquitin pathway Nature 349 132 138 1846030 10.1038/349132a0 1:CAS:528: DyaK3MXps12jtA%3D%3D (Pubitemid 21912025)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 20
    • 2442551473 scopus 로고    scopus 로고
    • Deubiquitinating enzymes are IN(trinsic to proteasome function)
    • DOI 10.2174/1389203043379756
    • A Guterman MH Glickman 2004 Deubiquitinating enzymes are IN/(trinsic to proteasome function) Curr Protein Pept Sci 5 201 211 15188770 10.2174/1389203043379756 1:CAS:528:DC%2BD2cXktFCjsbg%3D (Pubitemid 38647473)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.3 , pp. 201-211
    • Guterman, A.1    Glickman, M.H.2
  • 21
    • 0028029983 scopus 로고
    • CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation
    • DOI 10.1016/0092-8674(94)90547-9
    • LE Hake JD Richter 1994 CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation Cell 79 617 627 7954828 10.1016/0092-8674(94)90547-9 1:CAS:528:DyaK2MXit1Gksr8%3D (Pubitemid 24363805)
    • (1994) Cell , vol.79 , Issue.4 , pp. 617-627
    • Hake, L.E.1    Richter, J.D.2
  • 22
    • 31444440363 scopus 로고    scopus 로고
    • CaMKII and Polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit
    • DOI 10.1073/pnas.0509549102
    • DV Hansen JJ Tung PK Jackson 2006 CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit Proc Natl Acad Sci USA 103 608 613 16407128 10.1073/pnas.0509549102 1:CAS:528:DC%2BD28XhtVOiurs%3D (Pubitemid 43153073)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.3 , pp. 608-613
    • Hansen, D.V.1    Tung, J.J.2    Jackson, P.K.3
  • 23
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • DOI 10.1146/annurev.biochem.67.1.425
    • A Hershko A Ciechanover 1998 The ubiquitin system Annu Rev Biochem 67 425 479 9759494 10.1146/annurev.biochem.67.1.425 1:CAS:528:DyaK1cXlsFOmsLc%3D (Pubitemid 28411135)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 24
  • 25
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • DOI 10.1038/35056583
    • L Hicke 2001 Protein regulation by monoubiquitin Nat Rev Mol Cell Biol 2 195 201 11265249 10.1038/35056583 1:CAS:528:DC%2BD3MXhvFKqt7c%3D (Pubitemid 33675744)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.3 , pp. 195-201
    • Hicke, L.1
  • 26
    • 4243077561 scopus 로고    scopus 로고
    • Regulation of ubiquitin-proteasome pathway on pig oocyte meiotic maturation and fertilization
    • DOI 10.1095/biolreprod.104.028134
    • LJ Huo HY Fan CG Liang LZ Yu ZS Zhong DY Chen QY Sun 2004 Regulation of ubiquitin-proteasome pathway on pig oocyte meiotic maturation and fertilization Biol Reprod 71 853 862 15115724 10.1095/biolreprod.104.028134 1:CAS:528:DC%2BD2cXntFejurw%3D (Pubitemid 39108646)
    • (2004) Biology of Reproduction , vol.71 , Issue.3 , pp. 853-862
    • Huo, L.-J.1    Fan, H.-Y.2    Liang, C.-G.3    Yu, L.-Z.4    Zhong, Z.-S.5    Chen, D.-Y.6    Sun, Q.-Y.7
  • 27
    • 77956096971 scopus 로고    scopus 로고
    • Mice lacking two sperm serine proteases, ACR and PRSS21, are subfertile, but the mutant sperm are infertile in vitro
    • 20484738 10.1095/biolreprod.109.083089 1:CAS:528:DC%2BC3cXhtVyrsrrK
    • N Kawano W Kang M Yamashita Y Koga T Yamazaki T Hata K Miyado T Baba 2010 Mice lacking two sperm serine proteases, ACR and PRSS21, are subfertile, but the mutant sperm are infertile in vitro Biol Reprod 83 359 369 20484738 10.1095/biolreprod.109.083089 1:CAS:528:DC%2BC3cXhtVyrsrrK
    • (2010) Biol Reprod , vol.83 , pp. 359-369
    • Kawano, N.1    Kang, W.2    Yamashita, M.3    Koga, Y.4    Yamazaki, T.5    Hata, T.6    Miyado, K.7    Baba, T.8
  • 28
    • 79151472282 scopus 로고    scopus 로고
    • Structure characterization of the 26S proteasome
    • 20800708 1:CAS:528:DC%2BC3MXhtleis7g%3D
    • HM Kim Y Yu Y Cheng 2011 Structure characterization of the 26S proteasome Biochim Biophys Acta 1809 67 79 20800708 1:CAS:528:DC%2BC3MXhtleis7g%3D
    • (2011) Biochim Biophys Acta , vol.1809 , pp. 67-79
    • Kim, H.M.1    Yu, Y.2    Cheng, Y.3
  • 29
    • 0024342438 scopus 로고
    • MPF from starfish oocytes at first meiotic metaphase is a heterodimer containing one molecule of cdc2 and one molecule of cyclin B
    • JC Labbé JP Capony D Caput JC Cavadore J Derancourt M Kaghad JM Lelias A Picard M Dorée 1989 MPF from starfish oocytes at first meiotic metaphase is a heterodimer containing one molecule of cdc2 and one molecule of cyclin B EMBO J 8 3053 3058 2531073 (Pubitemid 19275008)
    • (1989) EMBO Journal , vol.8 , Issue.10 , pp. 3053-3058
    • Labbe, J.-C.1    Capony, J.-P.2    Caput, D.3    Cavadore, J.-C.4    Derancourt, J.5    Kaghad, M.6    Lelias, J.-M.7    Picard, A.8    Doree, M.9
  • 30
    • 11444265827 scopus 로고    scopus 로고
    • Influence of antral follicle size on oocyte characteristics and embryo development in the bovine
    • DOI 10.1016/j.theriogenology.2004.05.015, PII S0093691X04001815
    • AS Lequarre C Vigneron F Ribaucour P Holm I Donnay R Dalbiès-Tran H Callesen P Mermillod 2005 Influence of antral follicle size on oocyte characteristics and embryo development in the bovine Theriogenology 63 841 859 15629802 10.1016/j.theriogenology.2004.05.015 (Pubitemid 40078156)
    • (2005) Theriogenology , vol.63 , Issue.3 , pp. 841-859
    • Lequarre, A.-S.1    Vigneron, C.2    Ribaucour, F.3    Holm, P.4    Donnay, I.5    Dalbies-Tran, R.6    Callesen, H.7    Mermillod, P.8
  • 31
    • 23944518069 scopus 로고    scopus 로고
    • Calcium elevation at fertilization coordinates phosphorylation of XErp1/Emi2 by Plx1 and CaMK II to release metaphase arrest by cytostatic factor
    • DOI 10.1016/j.cub.2005.07.030, PII S0960982205007748
    • J Liu JL Maller 2005 Calcium elevation at fertilization coordinates phosphorylation of XErp1/Emi2 by Plx1 and CaMK II to release metaphase arrest by cytostatic factor Curr Biol 15 1458 1468 16040245 10.1016/j.cub.2005.07.030 1:CAS:528:DC%2BD2MXos1ajtrw%3D (Pubitemid 41187484)
    • (2005) Current Biology , vol.15 , Issue.16 , pp. 1458-1468
    • Liu, J.1    Maller, J.L.2
  • 32
    • 0024609244 scopus 로고
    • Mitotic control by metaphase-promoting factor and cdc proteins
    • 2674165
    • MJ Lohka 1989 Mitotic control by metaphase-promoting factor and cdc proteins J Cell Sci 92 131 135 2674165
    • (1989) J Cell Sci , vol.92 , pp. 131-135
    • Lohka, M.J.1
  • 33
    • 33748565597 scopus 로고    scopus 로고
    • Mouse Emi2 is required to enter meiosis II by reestablishing cyclin B1 during interkinesis
    • DOI 10.1083/jcb.200604140
    • S Madgwick DV Hansen M Levasseur PK Jackson KT Jones 2006 Mouse Emi2 is required to enter meiosis II by reestablishing cyclin B1 during interkinesis J Cell Biol 174 791 801 16966421 10.1083/jcb.200604140 1:CAS:528: DC%2BD28XpvVGhur4%3D (Pubitemid 44373729)
    • (2006) Journal of Cell Biology , vol.174 , Issue.6 , pp. 791-801
    • Madgwick, S.1    Hansen, D.V.2    Levasseur, M.3    Jackson, P.K.4    Jones, K.T.5
  • 34
    • 43149112331 scopus 로고    scopus 로고
    • Securin regulates entry into M-phase by modulating the stability of cyclin B
    • 18364698 10.1038/ncb1707 1:CAS:528:DC%2BD1cXktVGqtr8%3D
    • P Marangos J Carroll 2008 Securin regulates entry into M-phase by modulating the stability of cyclin B Nat Cell Biol 10 445 451 18364698 10.1038/ncb1707 1:CAS:528:DC%2BD1cXktVGqtr8%3D
    • (2008) Nat Cell Biol , vol.10 , pp. 445-451
    • Marangos, P.1    Carroll, J.2
  • 35
    • 33845994023 scopus 로고    scopus 로고
    • Cdh1
    • DOI 10.1083/jcb.200607070
    • P Marangos EW Verschuren R Chen PK Jackson J Carroll 2007 Prophase I arrest and progression to metaphase I in mouse oocytes are controlled by Emi1-dependent regulation of APC(Cdh1) J Cell Biol 176 65 75 17190794 10.1083/jcb.200607070 1:CAS:528:DC%2BD2sXktVOmsQ%3D%3D (Pubitemid 46041681)
    • (2007) Journal of Cell Biology , vol.176 , Issue.1 , pp. 65-75
    • Marangos, P.1    Verschuren, E.W.2    Chen, R.3    Jackson, P.K.4    Carroll, J.5
  • 36
    • 0016017003 scopus 로고
    • Biochemistry of mammalian fertilization
    • 4211837 10.1146/annurev.bi.43.070174.004021 1:CAS:528:DyaE2cXltVWjsbc%3D
    • RA McRorie WL Williams 1974 Biochemistry of mammalian fertilization Annu Rev Biochem 43 777 803 4211837 10.1146/annurev.bi.43.070174.004021 1:CAS:528:DyaE2cXltVWjsbc%3D
    • (1974) Annu Rev Biochem , vol.43 , pp. 777-803
    • McRorie, R.A.1    Williams, W.L.2
  • 37
    • 0037007233 scopus 로고    scopus 로고
    • Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction
    • DOI 10.1093/emboj/21.7.1833
    • R Mendez D Barnard JD Richter 2002 Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction EMBO J 21 1833 1844 11927567 10.1093/emboj/21.7.1833 1:CAS:528:DC%2BD38XjtVOgtb4%3D (Pubitemid 34614639)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1833-1844
    • Mendez, R.1    Barnard, D.2    Richter, J.D.3
  • 38
    • 0033253928 scopus 로고    scopus 로고
    • Aspects of follicular and oocyte maturation that affect the developmental potential of embryos
    • 10692875 1:STN:280:DC%2BD3c7lslaltg%3D%3D
    • P Mermillod B Oussaid Y Cognié 1999 Aspects of follicular and oocyte maturation that affect the developmental potential of embryos J Reprod Fertil Suppl 54 449 460 10692875 1:STN:280:DC%2BD3c7lslaltg%3D%3D
    • (1999) J Reprod Fertil Suppl , vol.54 , pp. 449-460
    • Mermillod, P.1    Oussaid, B.2    Cognié, Y.3
  • 39
    • 0037722762 scopus 로고    scopus 로고
    • Participation of the sperm proteasome in human fertilization
    • DOI 10.1093/humrep/deg111
    • P Morales M Kong E Pizarro C Pasten 2003 Participation of the sperm proteasome in human fertilization Hum Reprod 18 1010 1017 12721178 10.1093/humrep/deg111 1:CAS:528:DC%2BD3sXkslyjsr0%3D (Pubitemid 36592043)
    • (2003) Human Reproduction , vol.18 , Issue.5 , pp. 1010-1017
    • Morales, P.1    Kong, M.2    Pizarro, E.3    Pasten, C.4
  • 40
    • 1842427905 scopus 로고    scopus 로고
    • Extracellular Localization of Proteasomes in Human Sperm
    • DOI 10.1002/mrd.20052
    • P Morales E Pizarro M Kong M Jara 2004 Extracellular localization of proteasomes in human sperm Mol Reprod Dev 68 115 124 15039955 10.1002/mrd.20052 1:CAS:528:DC%2BD2cXivFyrsrg%3D (Pubitemid 38420526)
    • (2004) Molecular Reproduction and Development , vol.68 , Issue.1 , pp. 115-124
    • Morales, P.1    Pizarro, E.2    Kong, M.3    Jara, M.4
  • 41
    • 34548818472 scopus 로고    scopus 로고
    • Ubiquitin proteasome pathway gene expression varies in rhesus monkey oocytes and embryos of different developmental potential
    • DOI 10.1152/physiolgenomics.00040.2007
    • NR Mtango KE Latham 2007 Ubiquitin proteasome pathway gene expression varies in rhesus monkey oocytes and embryos of different developmental potential Physiol Genomics 31 1 14 17550997 10.1152/physiolgenomics.00040.2007 1:CAS:528:DC%2BD2sXhtl2rtrfK (Pubitemid 47443843)
    • (2007) Physiological Genomics , vol.31 , Issue.1 , pp. 1-14
    • Mtango, N.R.1    Latham, K.E.2
  • 42
    • 80755184572 scopus 로고    scopus 로고
    • Essential role of maternal UCHL1 and UCHL3 in fertilization and preimplantation embryo development
    • in press (doi: 10.1002/jcp.22876)
    • Mtango NR, Sutovsky M, Susor A, Zhong Z, Latham KE, Sutovsky P (2011) Essential role of maternal UCHL1 and UCHL3 in fertilization and preimplantation embryo development. J Cell Physiol, in press (doi: 10.1002/jcp.22876 )
    • (2011) J Cell Physiol
    • Mtango, N.R.1    Sutovsky, M.2    Susor, A.3    Zhong, Z.4    Latham, K.E.5    Sutovsky, P.6
  • 43
    • 80052416177 scopus 로고    scopus 로고
    • The BRCA1 ubiquitin ligase and homologous recombination repair
    • in press (doi: 10.1016/j.febslet.2011.05.005)
    • Ohta T, Sato K, Wu W (2011) The BRCA1 ubiquitin ligase and homologous recombination repair. FEBS Lett, in press (doi: 10.1016/j.febslet.2011.05.005 )
    • (2011) FEBS Lett
    • Ohta, T.1    Sato, K.2    Wu, W.3
  • 44
    • 0026587969 scopus 로고
    • Fertilization and developmental competence of bovine oocytes derived from different categories of antral follicles
    • 1562328 10.1002/mrd.1080310111 1:STN:280:DyaK383it1Gqtw%3D%3D
    • A Pavlok A Lucas-Hahn H Niemann 1992 Fertilization and developmental competence of bovine oocytes derived from different categories of antral follicles Mol Reprod Dev 31 63 67 1562328 10.1002/mrd.1080310111 1:STN:280:DyaK383it1Gqtw%3D%3D
    • (1992) Mol Reprod Dev , vol.31 , pp. 63-67
    • Pavlok, A.1    Lucas-Hahn, A.2    Niemann, H.3
  • 45
    • 49849098630 scopus 로고    scopus 로고
    • Regulation of APC/C activators in mitosis and meiosis
    • 18598214 10.1146/annurev.cellbio.041408.115949 1:CAS:528: DC%2BD1cXhtlOgtbfO
    • JA Pesin TL Orr-Weaver 2008 Regulation of APC/C activators in mitosis and meiosis Annu Rev Cell Dev Biol 24 475 499 18598214 10.1146/annurev.cellbio. 041408.115949 1:CAS:528:DC%2BD1cXhtlOgtbfO
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 475-499
    • Pesin, J.A.1    Orr-Weaver, T.L.2
  • 46
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • DOI 10.1016/S1097-2765(02)00540-3
    • JM Peters 2002 The anaphase-promoting complex: proteolysis in mitosis and beyond Mol Cell 9 931 943 12049731 10.1016/S1097-2765(02)00540-3 1:CAS:528:DC%2BD38XksFKjtL8%3D (Pubitemid 34626665)
    • (2002) Molecular Cell , vol.9 , Issue.5 , pp. 931-943
    • Peters, J.-M.1
  • 47
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: A machine designed to destroy
    • DOI 10.1038/nrm1988, PII NRM1988
    • JM Peters 2006 The anaphase promoting complex/cyclosome: a machine designed to destroy Nat Rev Mol Cell Biol 7 644 656 16896351 10.1038/nrm1988 1:CAS:528:DC%2BD28Xot12ju7s%3D (Pubitemid 44268210)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.9 , pp. 644-656
    • Peters, J.-M.1
  • 48
    • 0032543552 scopus 로고    scopus 로고
    • The regulation of Cdc20 proteolysis reveals a role for the APC components Cdc23 and Cdc27 during S phase and early mitosis
    • S Prinz ES Hwang R Visintin A Amon 1998 The regulation of Cdc20 proteolysis reveals a role for APC components Cdc23 and Cdc27 during S phase and early mitosis Curr Biol 8 750 760 9651679 10.1016/S0960-9822(98)70298-2 1:CAS:528:DyaK1cXktVKqs78%3D (Pubitemid 28301161)
    • (1998) Current Biology , vol.8 , Issue.13 , pp. 750-760
    • Prinz, S.1    Hwang, E.S.2    Visintin, R.3    Amon, A.4
  • 49
    • 36849019627 scopus 로고    scopus 로고
    • Effects of follicle size and stages of maturation on mRNA expression in bovine in vitro matured oocytes
    • DOI 10.1002/mrd.20770
    • SE Racedo C Wrenzycki D Herrmann D Salamone H Niemann 2008 Effects of follicle size and stages of maturation on mRNA expression in bovine in vitro matured oocytes Mol Reprod Dev 75 17 25 17546584 10.1002/mrd.20770 (Pubitemid 350223986)
    • (2008) Molecular Reproduction and Development , vol.75 , Issue.1 , pp. 17-25
    • Racedo, S.E.1    Wrenzycki, C.2    Herrmann, D.3    Salamone, D.4    Niemann, H.5
  • 50
    • 59849098237 scopus 로고    scopus 로고
    • Dynamics of microtubules, motor proteins and 20S proteasomes during bovine oocyte IVM
    • 19210921 10.1071/RD08111 1:CAS:528:DC%2BD1MXhtVensLc%3D
    • SE Racedo MC Branzini D Salamone C Wójcik VY Rawe H Niemann 2009 Dynamics of microtubules, motor proteins and 20S proteasomes during bovine oocyte IVM Reprod Fertil Dev 21 304 312 19210921 10.1071/RD08111 1:CAS:528:DC%2BD1MXhtVensLc%3D
    • (2009) Reprod Fertil Dev , vol.21 , pp. 304-312
    • Racedo, S.E.1    Branzini, M.C.2    Salamone, D.3    Wójcik, C.4    Rawe, V.Y.5    Niemann, H.6
  • 51
    • 0036249649 scopus 로고    scopus 로고
    • Follicle size and oocyte diameter in relation to developmental competence of buffalo oocytes in vitro
    • DOI 10.1071/RD01060
    • HM Raghu S Nandi SM Reddy 2002 Follicle size and oocyte diameter in relation to developmental competence of buffalo oocytes in vitro Reprod Fertil Dev 14 55 61 12051523 10.1071/RD01060 1:STN:280:DC%2BD38zgvFemsg%3D%3D (Pubitemid 34506265)
    • (2002) Reproduction, Fertility and Development , vol.14 , Issue.1-2 , pp. 55-61
    • Raghu, H.M.1    Nandi, S.2    Reddy, S.M.3
  • 52
    • 33744984782 scopus 로고    scopus 로고
    • APCcdh1 activity in mouse oocytes prevents entry into the first meiotic division
    • 16715549 10.1038/ncb1406 1:CAS:528:DC%2BD28XksVGnu74%3D
    • A Reis HY Chang M Levasseur KT Jones 2006 APCcdh1 activity in mouse oocytes prevents entry into the first meiotic division Nat Cell Biol 8 539 540 16715549 10.1038/ncb1406 1:CAS:528:DC%2BD28XksVGnu74%3D
    • (2006) Nat Cell Biol , vol.8 , pp. 539-540
    • Reis, A.1    Chang, H.Y.2    Levasseur, M.3    Jones, K.T.4
  • 53
    • 33749243774 scopus 로고    scopus 로고
    • cdh1-dependent degron in mammalian cdc20
    • DOI 10.1038/sj.embor.7400772, PII 7400772
    • A Reis M Levasseur HY Chang DJ Elliott KT Jones 2006 The CRY box: a second APCcdh1-dependent degron in mammalian cdc20 EMBO Rep 7 1040 1045 16878123 10.1038/sj.embor.7400772 1:CAS:528:DC%2BD28XhtVajsbfE (Pubitemid 44480521)
    • (2006) EMBO Reports , vol.7 , Issue.10 , pp. 1040-1045
    • Reis, A.1    Levasseur, M.2    Chang, H.-Y.3    Elliott, D.J.4    Jones, K.T.5
  • 54
    • 34848893367 scopus 로고    scopus 로고
    • cdh1 activity prevents non-disjunction in mammalian oocytes
    • DOI 10.1038/ncb1640, PII NCB1640
    • A Reis S Madgwick HY Chang I Nabti M Levasseur KT Jones 2007 Prometaphase APCcdh1 activity prevents non-disjunction in mammalian oocytes Nat Cell Biol 9 1192 1198 17891138 10.1038/ncb1640 1:CAS:528:DC%2BD2sXhtFSntb%2FN (Pubitemid 47500496)
    • (2007) Nature Cell Biology , vol.9 , Issue.10 , pp. 1192-1198
    • Reis, A.1    Madgwick, S.2    Chang, H.-Y.3    Nabti, I.4    Levasseur, M.5    Jones, K.T.6
  • 55
    • 0035869581 scopus 로고    scopus 로고
    • CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome
    • DOI 10.1006/dbio.2001.0153
    • CG Reverte MD Ahearn LE Hake 2001 CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome Dev Biol 231 447 458 11237472 10.1006/dbio.2001.0153 1:CAS:528:DC%2BD3MXhsFOht7g%3D (Pubitemid 32217584)
    • (2001) Developmental Biology , vol.231 , Issue.2 , pp. 447-458
    • Reverte, C.G.1    Ahearn, M.D.2    Hake, L.E.3
  • 56
    • 34249908103 scopus 로고    scopus 로고
    • CPEB: A life in translation
    • DOI 10.1016/j.tibs.2007.04.004, PII S0968000407000928
    • JD Richter 2007 CPEB: a life in translation Trends Biochem Sci 32 279 285 17481902 10.1016/j.tibs.2007.04.004 1:CAS:528:DC%2BD2sXmtlahsbw%3D (Pubitemid 46874928)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.6 , pp. 279-285
    • Richter, J.D.1
  • 57
    • 51449095832 scopus 로고    scopus 로고
    • A quantitative assessment of follicle size on oocyte developmental competence
    • 18249377 10.1016/j.fertnstert.2007.02.011
    • MP Rosen S Shen AT Dobson PF Rinaudo CE McCulloch MI Cedars 2008 A quantitative assessment of follicle size on oocyte developmental competence Fertil Steril 90 684 690 18249377 10.1016/j.fertnstert.2007.02.011
    • (2008) Fertil Steril , vol.90 , pp. 684-690
    • Rosen, M.P.1    Shen, S.2    Dobson, A.T.3    Rinaudo, P.F.4    McCulloch, C.E.5    Cedars, M.I.6
  • 58
    • 1542375145 scopus 로고    scopus 로고
    • Non-traditional roles of ubiquitin-proteasome system in fertilization and gametogenesis
    • DOI 10.1016/S1357-2725(03)00263-2, PII S1357272503002632
    • N Sakai MT Sawada H Sawada 2004 Non-traditional roles of ubiquitin-proteasome system in fertilization and gametogenesis Int J Biochem Cell Biol 36 776 784 15006630 10.1016/S1357-2725(03)00263-2 1:CAS:528: DC%2BD2cXhvFSmtLo%3D (Pubitemid 38299393)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.5 , pp. 776-784
    • Sakai, N.1    Sawada, M.T.2    Sawada, H.3
  • 59
    • 0031782520 scopus 로고    scopus 로고
    • Participation of sperm proteasome in fertilization of the phlebobranch ascidian Ciona intestinalis
    • DOI 10.1002/(SICI)1098-2795(199808)50:4<493::AID-MRD13>3.0.CO;2-3
    • H Sawada MR Pinto R De Santis 1998 Participation of sperm proteasome in fertilization of the phlebobranch ascidian Ciona intestinalis Mol Reprod Dev 50 493 498 9669533 10.1002/(SICI)1098-2795(199808)50:4<493::AID-MRD13>3.0. CO;2-3 1:CAS:528:DyaK1cXktlKru7w%3D (Pubitemid 28294791)
    • (1998) Molecular Reproduction and Development , vol.50 , Issue.4 , pp. 493-498
    • Sawada, H.1    Pinto, M.R.2    De Santis, R.3
  • 61
    • 0030738748 scopus 로고    scopus 로고
    • Yeast Hct1 is a regulator of Cib2 cyclin proteolysis
    • DOI 10.1016/S0092-8674(00)80529-2
    • M Schwab AS Lutum W Seufert 1997 Yeast Hct1 is a regulator of Clb2 cyclin proteolysis Cell 90 683 693 9288748 10.1016/S0092-8674(00)80529-2 1:CAS:528:DyaK2sXlvFKmtbk%3D (Pubitemid 27357960)
    • (1997) Cell , vol.90 , Issue.4 , pp. 683-693
    • Schwab, M.1    Lutum, A.S.2    Seufert, W.3
  • 64
    • 0030835478 scopus 로고    scopus 로고
    • Drosophila fizzy-related down-regulates mitotic cyclins and is required for cell proliferation arrest and entry into endocycles
    • DOI 10.1016/S0092-8674(00)80528-0
    • SJ Sigrist CF Lehner 1997 Drosophila fizzy-related down-regulates mitotic cyclins and is required for cell proliferation arrest and entry into endocycles Cell 90 671 681 9288747 10.1016/S0092-8674(00)80528-0 1:CAS:528: DyaK2sXlvFKmtbg%3D (Pubitemid 27357959)
    • (1997) Cell , vol.90 , Issue.4 , pp. 671-681
    • Sigrist, S.J.1    Lehner, C.F.2
  • 66
    • 35048812953 scopus 로고    scopus 로고
    • Proteomic analysis of porcine oocytes during in vitro maturation reveals essential role for the ubiquitin C-terminal hydrolase-L1
    • DOI 10.1530/REP-07-0079
    • A Susor Z Ellederova L Jelinkova P Halada D Kavan M Kubelka H Kovarova 2007 Proteomic analysis of porcine oocytes during in vitro maturation reveals essential role for the ubiquitin C-terminal hydrolase-L1 Reproduction 134 559 568 17890291 10.1530/REP-07-0079 1:CAS:528:DC%2BD2sXht1Knur3K (Pubitemid 47555049)
    • (2007) Reproduction , vol.134 , Issue.4 , pp. 559-568
    • Susor, A.1    Ellederova, Z.2    Jelinkova, L.3    Halada, P.4    Kavan, D.5    Kubelka, M.6    Kovarova, H.7
  • 67
    • 77953815862 scopus 로고    scopus 로고
    • Role of ubiquitin C-terminal hydrolase-L1 in antipolyspermy defense of mammalian oocytes
    • 20164442 10.1095/biolreprod.109.081547 1:CAS:528:DC%2BC3cXmvVCgt7Y%3D
    • A Susor L Liskova T Toralova A Pavlok K Pivonkova P Karabinova M Lopatarova P Sutovsky M Kubelka 2010 Role of ubiquitin C-terminal hydrolase-L1 in antipolyspermy defense of mammalian oocytes Biol Reprod 82 1151 1161 20164442 10.1095/biolreprod.109.081547 1:CAS:528:DC%2BC3cXmvVCgt7Y%3D
    • (2010) Biol Reprod , vol.82 , pp. 1151-1161
    • Susor, A.1    Liskova, L.2    Toralova, T.3    Pavlok, A.4    Pivonkova, K.5    Karabinova, P.6    Lopatarova, M.7    Sutovsky, P.8    Kubelka, M.9
  • 68
    • 0033883489 scopus 로고    scopus 로고
    • Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos
    • P Sutovsky RD Moreno J Ramalho-Santos T Dominko C Simerly G Schatten 2000 Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos Biol Reprod 63 582 590 10906068 10.1095/biolreprod63.2.582 1:CAS:528:DC%2BD3cXltl2gurw%3D (Pubitemid 30639950)
    • (2000) Biology of Reproduction , vol.63 , Issue.2 , pp. 582-590
    • Sutovsky, P.1    Moreno, R.D.2    Ramalho-Santos, J.3    Dominko, T.4    Simerly, C.5    Schatten, G.6
  • 69
    • 5144231426 scopus 로고    scopus 로고
    • Proteasomal interference prevents zona pellucida penetration and fertilization in mammals
    • DOI 10.1095/biolreprod.104.032532
    • P Sutovsky G Manandhar TC McCauley JN Caamaño M Sutovsky WE Thompson BN Day 2004 Proteasomal interference prevents zona pellucida penetration and fertilization in mammals Biol Reprod 71 1625 1637 15253927 10.1095/biolreprod.104.032532 1:CAS:528:DC%2BD2cXpt1yisbc%3D (Pubitemid 39403259)
    • (2004) Biology of Reproduction , vol.71 , Issue.5 , pp. 1625-1637
    • Sutovsky, P.1    Manandhar, G.2    McCauley, T.C.3    Caamano, J.N.4    Sutovsky, M.5    Thompson, W.E.6    Day, B.N.7
  • 70
    • 0037442540 scopus 로고    scopus 로고
    • Role of cdc2 kinase phosphorylation and conserved N-terminal proteolysis motifs in cytoplasmic polyadenylation-element-binding protein (CPEB) complex dissociation and degradation
    • DOI 10.1042/BJ20021462
    • G Thom N Minshall A Git J Argasinska N Standart 2003 Role of cdc2 kinase phosphorylation and conserved N-terminal proteolysis motifs in cytoplasmic polyadenylation-element-binding protein (CPEB) complex dissociation and degradation Biochem J 370 91 100 12401129 10.1042/BJ20021462 1:CAS:528:DC%2BD3sXhtVKkurk%3D (Pubitemid 36259422)
    • (2003) Biochemical Journal , vol.370 , Issue.1 , pp. 91-100
    • Thom, G.1    Minshall, N.2    Git, A.3    Argasinska, J.4    Standart, N.5
  • 71
    • 0031301877 scopus 로고    scopus 로고
    • Purification and characterization of 26S proteasomes from human and mouse spermatozoa
    • CP Tipler SP Hutchon K Hendil K Tanaka S Fishel RJ Mayer 1997 Purification and characterization of 26S proteasomes from human and mouse spermatozoa Mol Hum Reprod 3 1053 1060 9464850 10.1093/molehr/3.12.1053 1:CAS:528:DyaK1cXoslentg%3D%3D (Pubitemid 127509911)
    • (1997) Molecular Human Reproduction , vol.3 , Issue.12 , pp. 1053-1060
    • Tipler, C.P.1    Hutchon, S.P.2    Hendil, K.3    Tanaka, K.4    Fishel, S.5    Mayer, R.J.6
  • 73
    • 0037444220 scopus 로고    scopus 로고
    • Under arrest: Cytostatic factor (CSF)-mediated metaphase arrest in vertebrate eggs
    • DOI 10.1101/gad.1071303
    • BJ Tunquist JL Maller 2003 Under arrest: cytostatic factor (CSF)-mediated metaphase arrest in vertebrate eggs Genes Dev 17 683 710 12651887 10.1101/gad.1071303 1:CAS:528:DC%2BD3sXivVWmsLk%3D (Pubitemid 36359187)
    • (2003) Genes and Development , vol.17 , Issue.6 , pp. 683-710
    • Tunquist, B.J.1    Maller, J.L.2
  • 74
    • 80052702417 scopus 로고    scopus 로고
    • Timing and spacing of ubiquitin-dependent DNA damage bypass
    • in press (doi: 10.1016/j.febslet.2011.05.028)
    • Ulrich HD (2011) Timing and spacing of ubiquitin-dependent DNA damage bypass. FEBS Lett, in press (doi: 10.1016/j.febslet.2011.05.028 )
    • (2011) FEBS Lett
    • Ulrich, H.D.1
  • 75
    • 38549128208 scopus 로고    scopus 로고
    • Spatio-temporal expression patterns of Aurora kinases A, B, and C and cytoplasmic polyadenylation-element-binding protein in bovine oocytes during meiotic maturation
    • DOI 10.1095/biolreprod.107.061036
    • S Uzbekova Y Arlot-Bonnemains J Dupont R Dalbiès-Tran P Papillier S Pennetier A Thélie C Perreau P Mermillod C Prigent R Uzbekov 2008 Spatio-temporal expression patterns of aurora kinases a, B, and C and cytoplasmic polyadenylation-element-binding protein in bovine oocytes during meiotic maturation Biol Reprod 78 218 233 17687118 10.1095/biolreprod.107.061036 1:CAS:528:DC%2BD1cXht1Kru7w%3D (Pubitemid 351159978)
    • (2008) Biology of Reproduction , vol.78 , Issue.2 , pp. 218-233
    • Uzbekova, S.1    Arlot-Bonnemains, Y.2    Dupont, J.3    Dalbies-Tran, R.4    Papillier, P.5    Pennetier, S.6    Thelie, A.7    Perreau, C.8    Mermillod, P.9    Prigent, C.10    Uzbekov, R.11
  • 76
    • 80755184573 scopus 로고    scopus 로고
    • Control of the oocyte-to-embryo transition by the ubiquitin-proteolytic system in mouse and C. elegans
    • MH Verlhac ME Terret L Pintard 2010 Control of the oocyte-to-embryo transition by the ubiquitin-proteolytic system in mouse and C. elegans Nat Rev Cell Biol 22 1 6
    • (2010) Nat Rev Cell Biol , vol.22 , pp. 1-6
    • Verlhac, M.H.1    Terret, M.E.2    Pintard, L.3
  • 78
    • 0030693087 scopus 로고    scopus 로고
    • CDC20 and CDH1: A family of substrate-specific activators of APC- dependent proteolysis
    • DOI 10.1126/science.278.5337.460
    • R Visintin S Prinz A Amon 1997 CDC20 and CDH1: a family of substrate-specific activators of APC-dependent proteolysis Science 278 460 463 9334304 10.1126/science.278.5337.460 1:CAS:528:DyaK2sXmslKiu7w%3D (Pubitemid 27454429)
    • (1997) Science , vol.278 , Issue.5337 , pp. 460-463
    • Visintin, R.1    Prinz, S.2    Amon, A.3
  • 80
    • 0032197525 scopus 로고    scopus 로고
    • P-Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse
    • K Yamagata K Murayama N Kohno S Kashiwabara T Baba 1998 p-Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse Zygote 6 311 319 9921641 10.1017/S0967199498000264 1:CAS:528:DyaK1MXhtVyqu7g%3D (Pubitemid 128574677)
    • (1998) Zygote , vol.6 , Issue.4 , pp. 311-319
    • Yamagata, K.1    Murayama, K.2    Kohno, N.3    Kashiwabara, S.-I.4    Baba, T.5
  • 82
    • 56749116049 scopus 로고    scopus 로고
    • Functions of FZR1 and CDC20, activators of the anaphase-promoting complex, during meiotic maturation of swine oocytes
    • 18753608 10.1095/biolreprod.108.070326 1:CAS:528:DC%2BD1cXhsVCltLzE
    • T Yamamuro K Kano K Naito 2008 Functions of FZR1 and CDC20, activators of the anaphase-promoting complex, during meiotic maturation of swine oocytes Biol Reprod 79 1202 1209 18753608 10.1095/biolreprod.108.070326 1:CAS:528: DC%2BD1cXhsVCltLzE
    • (2008) Biol Reprod , vol.79 , pp. 1202-1209
    • Yamamuro, T.1    Kano, K.2    Naito, K.3
  • 83
    • 35548979382 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization
    • DOI 10.1095/biolreprod.107.061275
    • YJ Yi G Manandhar M Sutovsky R Li V Jonáková R Oko CS Park RS Prather P Sutovsky 2007 Ubiquitin C-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization Biol Reprod 77 780 793 17671268 10.1095/biolreprod.107.061275 1:CAS:528:DC%2BD2sXht1CnurfI (Pubitemid 350014166)
    • (2007) Biology of Reproduction , vol.77 , Issue.5 , pp. 780-793
    • Yi, Y.-J.1    Manandhar, G.2    Sutovsky, M.3    Li, R.4    Jonakova, V.5    Oko, R.6    Park, C.-S.7    Prather, R.S.8    Sutovsky, P.9
  • 84
    • 76749149068 scopus 로고    scopus 로고
    • Inhibition of 19S proteasomal regulatory complex subunit PSMD8 increases polyspermy during porcine fertilization in vitro
    • 20004025 10.1016/j.jri.2009.11.002 1:CAS:528:DC%2BC3cXit1Kiu7w%3D
    • YJ Yi G Manandhar M Sutovsky V Jonáková CS Park P Sutovsky 2010 Inhibition of 19S proteasomal regulatory complex subunit PSMD8 increases polyspermy during porcine fertilization in vitro J Reprod Immunol 84 154 163 20004025 10.1016/j.jri.2009.11.002 1:CAS:528:DC%2BC3cXit1Kiu7w%3D
    • (2010) J Reprod Immunol , vol.84 , pp. 154-163
    • Yi, Y.J.1    Manandhar, G.2    Sutovsky, M.3    Jonáková, V.4    Park, C.S.5    Sutovsky, P.6
  • 85
    • 0036257128 scopus 로고    scopus 로고
    • Proteasome localization and ultrastructure of spermatozoa from patients with varicocele - Immunoelectron microscopic study
    • H Ziemba LP Biały S Fracki L Bablok C Wójcik 2002 Proteasome localization and ultrastructure of spermatozoa from patients with varicocele-immunoelectron microscopic study Folia Histochem Cytobiol 40 169 170 12056629 1:STN:280:DC%2BD38zhsVGjug%3D%3D (Pubitemid 34477133)
    • (2002) Folia Histochemica et Cytobiologica , vol.40 , Issue.2 , pp. 169-170
    • Ziemba, H.1    Bialy, L.P.2    Fracki, S.3    Bablok, L.4    Wojcik, C.5
  • 86
    • 79952032656 scopus 로고    scopus 로고
    • Sperm proteasomes degrade sperm receptor on the egg zona pellucida during mammalian fertilization
    • 21383844 10.1371/journal.pone.0017256 1:CAS:528:DC%2BC3MXivFGgsL8%3D
    • SW Zimmerman G Manandhar YJ Yi SK Gupta M Sutovsky JF Odhiambo MD Powell DJ Miller P Sutovsky 2011 Sperm proteasomes degrade sperm receptor on the egg zona pellucida during mammalian fertilization PLoS One 6 e17256 21383844 10.1371/journal.pone.0017256 1:CAS:528:DC%2BC3MXivFGgsL8%3D
    • (2011) PLoS One , vol.6 , pp. 17256
    • Zimmerman, S.W.1    Manandhar, G.2    Yi, Y.J.3    Gupta, S.K.4    Sutovsky, M.5    Odhiambo, J.F.6    Powell, M.D.7    Miller, D.J.8    Sutovsky, P.9


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