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Volumn 40, Issue 4, 2013, Pages 3213-3230

New insights to the ubiquitin-proteasome pathway (UPP) mechanism during spermatogenesis

Author keywords

Acrosome; Midpiece; Mitochondria; Spermatogenesis; Ubiquitin; Ubiquitination

Indexed keywords

PROTEASOME; PROTEINASE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E1; UBIQUITIN PROTEIN LIGASE E2; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

EID: 84878404112     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-012-2397-y     Document Type: Article
Times cited : (67)

References (163)
  • 1
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • 9759494 1:CAS:528:DyaK1cXlsFOmsLc%3D 10.1146/annurev.biochem.67.1.425
    • Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67:425-479
    • (1998) Annu Rev Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 2
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • 15571809 1:CAS:528:DC%2BD2cXhtVantbzO 10.1016/j.bbamcr.2004.09.019
    • Pickart CM, Eddins MJ (2004) Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695(1-3):55-72
    • (2004) Biochim Biophys Acta , vol.1695 , Issue.1-3 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 3
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • 6305978 1:CAS:528:DyaL3sXksV2nsLc%3D
    • Hershko A, Heller H, Elias S, Ciechanover A (1983) Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem 258(13):8206-8214
    • (1983) J Biol Chem , vol.258 , Issue.13 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 4
    • 0016798328 scopus 로고
    • The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells
    • 1170880 1:CAS:528:DyaE2MXkt1ersrk%3D 10.1021/bi00681a026
    • Schlesinger DH, Goldstein G, Niall HD (1975) The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells. Biochemistry 14(10):2214-2218
    • (1975) Biochemistry , vol.14 , Issue.10 , pp. 2214-2218
    • Schlesinger, D.H.1    Goldstein, G.2    Niall, H.D.3
  • 5
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • 19325621 1:CAS:528:DC%2BD1MXjs1Klsbg%3D 10.1038/nature07958
    • Hochstrasser M (2009) Origin and function of ubiquitin-like proteins. Nature 458(7237):422-429
    • (2009) Nature , vol.458 , Issue.7237 , pp. 422-429
    • Hochstrasser, M.1
  • 6
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • 10934491 1:CAS:528:DC%2BD3cXlslymtrc%3D 10.1038/35019643
    • Hochstrasser M (2000) Evolution and function of ubiquitin-like protein-conjugation systems. Nat Cell Biol 2:E153-E157
    • (2000) Nat Cell Biol , vol.2
    • Hochstrasser, M.1
  • 7
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • 11917093 1:CAS:528:DC%2BD38XjtFOnsL4%3D
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82(2):373-428
    • (2002) Physiol Rev , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 8
    • 79151480727 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and mitochondria - Reciprocity
    • 20674813
    • Livnat-Levanon N, Glickman MH (2010) Ubiquitin-proteasome system and mitochondria - reciprocity. Biochim Biophys Acta 1809(2):80-87
    • (2010) Biochim Biophys Acta , vol.1809 , Issue.2 , pp. 80-87
    • Livnat-Levanon, N.1    Glickman, M.H.2
  • 9
    • 3242708461 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system: Past, present and future
    • 15224179 1:CAS:528:DC%2BD2cXntlCktLc%3D 10.1007/s00018-004-4128-6
    • Hilt W, Wolf DH (2004) The ubiquitin-proteasome system: past, present and future. Cell Mol Life Sci 61(13):1545
    • (2004) Cell Mol Life Sci , vol.61 , Issue.13 , pp. 1545
    • Hilt, W.1    Wolf, D.H.2
  • 10
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • 9357313 1:CAS:528:DyaK2sXntFeltLY%3D 10.1016/S0968-0004(97)01122-5
    • Varshavsky A (1997) The ubiquitin system. Trends Biochem Sci 22:383-387
    • (1997) Trends Biochem Sci , vol.22 , pp. 383-387
    • Varshavsky, A.1
  • 11
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • 19489727 1:CAS:528:DC%2BD1MXos1Ghurw%3D 10.1146/annurev.biochem.78. 081507.101607
    • Finley D (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78:477-513
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 12
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • 14570567 1:CAS:528:DC%2BD3sXpsFamtrk%3D 10.1146/annurev.cellbio.19. 110701.154617
    • Hicke L, Dunn R (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19:141-172
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 13
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • 11919637 1:CAS:528:DC%2BD38XislamtrY%3D 10.1038/416451a
    • Polo S, Sigismund S, Faretta M, Guidi M, Capua MR, Bossi G, Chen H, De Camilli P, Di Fiore PP (2002) A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416:451-455
    • (2002) Nature , vol.416 , pp. 451-455
    • Polo, S.1    Sigismund, S.2    Faretta, M.3    Guidi, M.4    Capua, M.R.5    Bossi, G.6    Chen, H.7    De Camilli, P.8    Di Fiore, P.P.9
  • 14
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • 1323239 1:CAS:528:DyaK38Xlt1KmsLc%3D 10.1146/annurev.bi.61.070192.003553
    • Hershko A, Ciechanover A (1992) The ubiquitin system for protein degradation. Annu Rev Biochem 61:761-807
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 15
    • 77950923479 scopus 로고    scopus 로고
    • Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 4: Intercellular bridges, mitochondria, nuclear envelope, apoptosis, ubiquitination, membrane/voltage-gated channels, methylation/acetylation, and transcription factors
    • 19941288 1:CAS:528:DC%2BC3cXlsFSlurs%3D 10.1002/jemt.20783
    • Hermo L, Pelletier RM, Cyr DG, Smith CE (2010) Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 4: intercellular bridges, mitochondria, nuclear envelope, apoptosis, ubiquitination, membrane/voltage-gated channels, methylation/acetylation, and transcription factors. Microsc Res Tech 73(4):364-408
    • (2010) Microsc Res Tech , vol.73 , Issue.4 , pp. 364-408
    • Hermo, L.1    Pelletier, R.M.2    Cyr, D.G.3    Smith, C.E.4
  • 16
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • 11395416 1:CAS:528:DC%2BD3MXlsVehtLw%3D 10.1146/annurev.biochem.70.1.503
    • Pickart C (2001) Mechanisms underlying ubiquitination. Annu Rev Biochem 70:503-533
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.1
  • 17
    • 0037405064 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: Killing three birds with one stone
    • 12672125 1:CAS:528:DC%2BD3sXjslymt7k%3D 10.1002/jemt.10319
    • Sutovsky P (2003) Ubiquitin-dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: killing three birds with one stone. Microsc Res Tech 61:88-102
    • (2003) Microsc Res Tech , vol.61 , pp. 88-102
    • Sutovsky, P.1
  • 18
    • 73949148801 scopus 로고    scopus 로고
    • Spermatogenesis and cycle of the seminiferous epithelium
    • 19856159 10.1007/978-0-387-09597-4-1
    • Hess RA, Renato de Franca L (2008) Spermatogenesis and cycle of the seminiferous epithelium. Adv Exp Med Biol 636:1-15
    • (2008) Adv Exp Med Biol , vol.636 , pp. 1-15
    • Hess, R.A.1    Renato De Franca, L.2
  • 19
    • 0014884736 scopus 로고
    • A comparative view of sperm ultrastructure
    • 12254595 1:STN:280:DC%2BD38rgsFSqug%3D%3D 10.1095/biolreprod2.Supplement- 2.90
    • Fawcett DW (1970) A comparative view of sperm ultrastructure. Biol Reprod Suppl 2:90-127
    • (1970) Biol Reprod Suppl , vol.2 , pp. 90-127
    • Fawcett, D.W.1
  • 20
    • 0028915583 scopus 로고
    • The making of a spermatozoon: A molecular perspective
    • 7736670 1:STN:280:DyaK2M3lsVOnuw%3D%3D 10.1002/dvg.1020160202
    • Hecht NB (1995) The making of a spermatozoon: a molecular perspective. Dev Genet 16:95-103
    • (1995) Dev Genet , vol.16 , pp. 95-103
    • Hecht, N.B.1
  • 21
    • 0017278570 scopus 로고
    • The ultrastructural relationships between Sertoli cells and spermatogenic cells in the rat
    • 931781 1:STN:280:DyaE283ht1Ogsg%3D%3D
    • Kaya M, Harrison RG (1976) The ultrastructural relationships between Sertoli cells and spermatogenic cells in the rat. J Anat 121:279-290
    • (1976) J Anat , vol.121 , pp. 279-290
    • Kaya, M.1    Harrison, R.G.2
  • 22
    • 79955457638 scopus 로고    scopus 로고
    • RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis
    • 1:CAS:528:DC%2BC3MXlt1Gns74%3D 10.1093/abbs/gmr016
    • Ma T, Keller JA, Yu X (2011) RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis. Acta Biochim Biophys Sin (Shanghai) 43(5):339-345
    • (2011) Acta Biochim Biophys Sin (Shanghai) , vol.43 , Issue.5 , pp. 339-345
    • Ma, T.1    Keller, J.A.2    Yu, X.3
  • 23
    • 0010115729 scopus 로고    scopus 로고
    • Ubiquitination of histone H3 in elongating spermatids of rat testes
    • 9582357 1:CAS:528:DyaK1cXjsVGjtbk%3D 10.1074/jbc.273.21.13165
    • Chen HY, Sun JM, Zhang Y, Davie JR, Meistrich ML (1998) Ubiquitination of histone H3 in elongating spermatids of rat testes. J Biol Chem 273(21):13165-13169
    • (1998) J Biol Chem , vol.273 , Issue.21 , pp. 13165-13169
    • Chen, H.Y.1    Sun, J.M.2    Zhang, Y.3    Davie, J.R.4    Meistrich, M.L.5
  • 25
    • 8744306041 scopus 로고    scopus 로고
    • Ubiquitin signals in the developing acrosome during spermatogenesis of rat testis: An immunoelectron microscopic study
    • 15505334 1:CAS:528:DC%2BD2cXhtVWgs7nI 10.1369/jhc.4A6275.2004
    • Haraguchi CM, Mabuchi T, Hirata S, Shoda T, Hoshi K, Yokota S (2004) Ubiquitin signals in the developing acrosome during spermatogenesis of rat testis: an immunoelectron microscopic study. J Histochem Cytochem 52(11):1393-1403
    • (2004) J Histochem Cytochem , vol.52 , Issue.11 , pp. 1393-1403
    • Haraguchi, C.M.1    Mabuchi, T.2    Hirata, S.3    Shoda, T.4    Hoshi, K.5    Yokota, S.6
  • 26
    • 0030845347 scopus 로고    scopus 로고
    • The heterotrimeric motor protein kinesin-II localizes to the midpiece and flagellum of sea urchin and sand dollar sperm
    • 9295139 1:CAS:528:DyaK2sXmtVyjtbo%3D 10.1002/(SICI)1097-0169(1997)38: 1<29: AID-CM4>3.0.CO;2-C
    • Henson JH, Cole DG, Roesener CD, Capuano S, Mendola RJ, Scholey JM (1997) The heterotrimeric motor protein kinesin-II localizes to the midpiece and flagellum of sea urchin and sand dollar sperm. Cell Motil Cytoskeleton 38(1):29-37
    • (1997) Cell Motil Cytoskeleton , vol.38 , Issue.1 , pp. 29-37
    • Henson, J.H.1    Cole, D.G.2    Roesener, C.D.3    Capuano, S.4    Mendola, R.J.5    Scholey, J.M.6
  • 27
    • 0035139841 scopus 로고    scopus 로고
    • The possible biological and reproductive functions of ubiquitin
    • 11212067 1:CAS:528:DC%2BD3MXhtlamtLs%3D 10.1093/humupd/7.1.102
    • Bebington C, Doherty FJ, Fleming SD (2001) The possible biological and reproductive functions of ubiquitin. Hum Reprod Update 7(1):102-111
    • (2001) Hum Reprod Update , vol.7 , Issue.1 , pp. 102-111
    • Bebington, C.1    Doherty, F.J.2    Fleming, S.D.3
  • 28
    • 0036087331 scopus 로고    scopus 로고
    • Control of ubiquitination of proteins in rat tissues by ubiquitin conjugating enzymes and isopeptidases
    • 11882492 1:CAS:528:DC%2BD38XivVemu7o%3D
    • Rajapurohitam V, Bedard N, Wing SS (2002) Control of ubiquitination of proteins in rat tissues by ubiquitin conjugating enzymes and isopeptidases. Am J Physiol Endocrinol Metab 282(4):E739-E745
    • (2002) Am J Physiol Endocrinol Metab , vol.282 , Issue.4
    • Rajapurohitam, V.1    Bedard, N.2    Wing, S.S.3
  • 29
    • 0033178830 scopus 로고    scopus 로고
    • Activation of a UBC4-dependent pathway of ubiquitin conjugation during postnatal development of the rat testis
    • 10419697 1:CAS:528:DyaK1MXksFygsb8%3D 10.1006/dbio.1999.9342
    • Rajapurohitam V, Morales CR, El-Alfy M, Lefrançois S, Bedard N, Wing SS (1999) Activation of a UBC4-dependent pathway of ubiquitin conjugation during postnatal development of the rat testis. Dev Biol 212(1):217-228
    • (1999) Dev Biol , vol.212 , Issue.1 , pp. 217-228
    • Rajapurohitam, V.1    Morales, C.R.2    El-Alfy, M.3    Lefrançois, S.4    Bedard, N.5    Wing, S.S.6
  • 30
    • 77955418014 scopus 로고    scopus 로고
    • Mitochondria, spermatogenesis and male infertility
    • 20595008 1:CAS:528:DC%2BC3cXpvFOnt7g%3D 10.1016/j.mito.2010.05.015
    • Rajender S, Rahul P, Mahdi AA (2010) Mitochondria, spermatogenesis and male infertility. Mitochondrion 10(5):419-428
    • (2010) Mitochondrion , vol.10 , Issue.5 , pp. 419-428
    • Rajender, S.1    Rahul, P.2    Mahdi, A.A.3
  • 32
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • 10366593 1:CAS:528:DyaK1MXjvVKiurs%3D 10.1083/jcb.145.6.1199
    • Fisk HA, Yaffe MP (1999) A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J Cell Biol 145(6):1199-1208
    • (1999) J Cell Biol , vol.145 , Issue.6 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 33
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • 16672980 1:CAS:528:DC%2BD28Xmtlaiu70%3D 10.1038/nature04788
    • Park J, Lee SB, Lee S, Kim Y, Song S, Kim S, Bae E, Kim J, Shong M, Kim JM, Chung J (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441(7097):1157-1161
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6    Bae, E.7    Kim, J.8    Shong, M.9    Kim, J.M.10    Chung, J.11
  • 34
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • 16672981 1:CAS:528:DC%2BD28Xmtlaiu78%3D 10.1038/nature04779
    • Clark IE, Dodson MW, Jiang C, Cao JH, Huh JR, Seol JH, Yoo SJ, Hay BA, Guo M (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441(7097):1162-1166
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 35
    • 33846898753 scopus 로고    scopus 로고
    • The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis
    • 17123504 1:CAS:528:DC%2BD2sXhvVGgsLw%3D 10.1016/j.ydbio.2006.10.038
    • Riparbelli MG, Callaini G (2007) The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis. Dev Biol 303(1):108-120
    • (2007) Dev Biol , vol.303 , Issue.1 , pp. 108-120
    • Riparbelli, M.G.1    Callaini, G.2
  • 36
    • 0014804860 scopus 로고
    • Considerations of volume, mass, DNA, and arrangement of mitochondria in the midpiece of bull spermatozoa
    • 5422964 1:STN:280:DyaE3c3htlahsQ%3D%3D 10.1016/0014-4827(70)90526-4
    • Bahr GF, Engler WF (1970) Considerations of volume, mass, DNA, and arrangement of mitochondria in the midpiece of bull spermatozoa. Exp Cell Res 60(3):338-340
    • (1970) Exp Cell Res , vol.60 , Issue.3 , pp. 338-340
    • Bahr, G.F.1    Engler, W.F.2
  • 37
    • 0035995241 scopus 로고    scopus 로고
    • Can mitochondrial DNA mutations cause sperm dysfunction?
    • 12149402 1:CAS:528:DC%2BD38XmvFOrsbw%3D 10.1093/molehr/8.8.719
    • Spiropoulos J, Turnbull DM, Chinnery PF (2002) Can mitochondrial DNA mutations cause sperm dysfunction? Mol Hum Reprod 8:719-721
    • (2002) Mol Hum Reprod , vol.8 , pp. 719-721
    • Spiropoulos, J.1    Turnbull, D.M.2    Chinnery, P.F.3
  • 38
    • 0031768690 scopus 로고    scopus 로고
    • Mitochondrial DNA in mammalian reproduction
    • 9829552 1:CAS:528:DyaK1cXntlaltbk%3D 10.1530/ror.0.0030172
    • Cummins J (1998) Mitochondrial DNA in mammalian reproduction. Rev Reprod 3:172-182
    • (1998) Rev Reprod , vol.3 , pp. 172-182
    • Cummins, J.1
  • 39
    • 77954206550 scopus 로고    scopus 로고
    • The role of mitochondrial DNA copy number in mammalian fertility
    • 20130269 1:CAS:528:DC%2BC3cXotlWqtLo%3D 10.1095/biolreprod.109.080887
    • Wai T, Ao A, Zhang X, Cyr D, Dufort D, Shoubridge EA (2010) The role of mitochondrial DNA copy number in mammalian fertility. Biol Reprod 83(1):52-62
    • (2010) Biol Reprod , vol.83 , Issue.1 , pp. 52-62
    • Wai, T.1    Ao, A.2    Zhang, X.3    Cyr, D.4    Dufort, D.5    Shoubridge, E.A.6
  • 40
    • 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
    • 17339235 1:CAS:528:DC%2BD2sXot1ejt7c%3D 10.1093/humrep/dem030
    • Amaral A, Ramalho-Santos J, St John JC (2007) The expression of polymerase gamma and mitochondrial transcription factor A and the regulation of mitochondrial DNA content in mature human sperm. Hum Reprod 22(6):1585-1596
    • (2007) Hum Reprod , vol.22 , Issue.6 , pp. 1585-1596
    • Amaral, A.1    Ramalho-Santos, J.2    St John, J.C.3
  • 41
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • 20194754 1:CAS:528:DC%2BC3cXjvFGnt7k%3D 10.1073/pnas.0913485107
    • Ziviani E, Tao RN, Whitworth AJ (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci USA 107(11):5018-5023
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.11 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 43
    • 73949112709 scopus 로고    scopus 로고
    • Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation
    • 19741096 1:CAS:528:DC%2BD1MXhsVSksL3L 10.1091/mbc.E09-02-0112
    • Yonashiro R, Sugiura A, Miyachi M, Fukuda T, Matsushita N, Inatome R, Ogata Y, Suzuki T, Dohmae N, Yanagi S (2009) Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation. Mol Biol Cell 20(21):4524-4530
    • (2009) Mol Biol Cell , vol.20 , Issue.21 , pp. 4524-4530
    • Yonashiro, R.1    Sugiura, A.2    Miyachi, M.3    Fukuda, T.4    Matsushita, N.5    Inatome, R.6    Ogata, Y.7    Suzuki, T.8    Dohmae, N.9    Yanagi, S.10
  • 44
    • 0027203710 scopus 로고
    • Expression of prohibitin in rat seminiferous epithelium
    • 8373953 1:CAS:528:DyaK2cXlsFWq 10.1095/biolreprod49.2.300
    • Choongkittaworn NM, Kim KH, Danner DB, Griswold MD (1993) Expression of prohibitin in rat seminiferous epithelium. Biol Reprod 49(2):300-310
    • (1993) Biol Reprod , vol.49 , Issue.2 , pp. 300-310
    • Choongkittaworn, N.M.1    Kim, K.H.2    Danner, D.B.3    Griswold, M.D.4
  • 45
    • 0033883489 scopus 로고    scopus 로고
    • Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos
    • 10906068 1:CAS:528:DC%2BD3cXltl2gurw%3D 10.1095/biolreprod63.2.582
    • Sutovsky P, Moreno RD, Ramalho-Santos J, Dominko T, Simerly C, Schatten G (2000) Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos. Biol Reprod 63(2):582-590
    • (2000) Biol Reprod , 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
  • 46
    • 0037774827 scopus 로고    scopus 로고
    • Ubiquitination of prohibitin in mammalian sperm mitochondria: Possible roles in the regulation of mitochondrial inheritance and sperm quality control
    • 12646488 1:CAS:528:DC%2BD3sXkvFCntb4%3D 10.1095/biolreprod.102.010975
    • Thompson WE, Ramalho-Santos J, Sutovsky P (2003) Ubiquitination of prohibitin in mammalian sperm mitochondria: possible roles in the regulation of mitochondrial inheritance and sperm quality control. Biol Reprod 69(1):254-260
    • (2003) Biol Reprod , vol.69 , Issue.1 , pp. 254-260
    • Thompson, W.E.1    Ramalho-Santos, J.2    Sutovsky, P.3
  • 47
    • 33749253910 scopus 로고    scopus 로고
    • MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology
    • 16936636 1:CAS:528:DC%2BD28XhtVajtr7I 10.1038/sj.embor.7400790
    • Nakamura N, Kimura Y, Tokuda M, Honda S, Hirose S (2006) MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep 7(10):1019-1022
    • (2006) EMBO Rep , vol.7 , Issue.10 , pp. 1019-1022
    • Nakamura, N.1    Kimura, Y.2    Tokuda, M.3    Honda, S.4    Hirose, S.5
  • 48
    • 76649142385 scopus 로고    scopus 로고
    • Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1
    • 20103533 1:CAS:528:DC%2BC3cXjs1Kku7Y%3D 10.1242/jcs.061481
    • Park YY, Lee S, Karbowski M, Neutzner A, Youle RJ, Cho H (2010) Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1. J Cell Sci 123(Pt 4):619-626
    • (2010) J Cell Sci , vol.123 , Issue.PART 4 , pp. 619-626
    • Park, Y.Y.1    Lee, S.2    Karbowski, M.3    Neutzner, A.4    Youle, R.J.5    Cho, H.6
  • 50
    • 0035012044 scopus 로고    scopus 로고
    • A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis
    • 11309198 1:CAS:528:DC%2BD3MXjslyquro%3D
    • Sutovsky P, Moreno R, Ramalho-Santos J, Dominko T, Thompson WE, Schatten G (2001) A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis. J Cell Sci 114(Pt 9):1665-1675
    • (2001) J Cell Sci , vol.114 , Issue.PART 9 , pp. 1665-1675
    • Sutovsky, P.1    Moreno, R.2    Ramalho-Santos, J.3    Dominko, T.4    Thompson, W.E.5    Schatten, G.6
  • 51
    • 0033535345 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event
    • 10085288 1:CAS:528:DyaK1MXhs1yqtbk%3D 10.1083/jcb.144.5.883
    • Martinou I, Desagher S, Eskes R, Antonsson B, Andre E, Fakan S, Martinou JC (1999) The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event. J Cell Biol 144:883-889
    • (1999) J Cell Biol , vol.144 , pp. 883-889
    • Martinou, I.1    Desagher, S.2    Eskes, R.3    Antonsson, B.4    Andre, E.5    Fakan, S.6    Martinou, J.C.7
  • 52
    • 0242298739 scopus 로고    scopus 로고
    • C-terminal kinesin motor KIFC1 participates in acrosome biogenesis and vesicle transport
    • 12826589 1:CAS:528:DC%2BD3sXosV2rs7s%3D 10.1095/biolreprod.102.014878
    • Yang WX, Sperry AO (2003) C-terminal kinesin motor KIFC1 participates in acrosome biogenesis and vesicle transport. Biol Reprod 69(5):1719-1729
    • (2003) Biol Reprod , vol.69 , Issue.5 , pp. 1719-1729
    • Yang, W.X.1    Sperry, A.O.2
  • 53
    • 0037024344 scopus 로고    scopus 로고
    • A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2 alpha and BRG-1/hSNF2 beta and localizes in the Golgi apparatus
    • 12044884 1:CAS:528:DC%2BD38XktFOgtL8%3D 10.1016/S0014-5793(02)02803-X
    • Mori K, Kato H (2002) A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2 alpha and BRG-1/hSNF2 beta and localizes in the Golgi apparatus. FEBS Lett 520:127-132
    • (2002) FEBS Lett , vol.520 , pp. 127-132
    • Mori, K.1    Kato, H.2
  • 54
    • 66149121840 scopus 로고    scopus 로고
    • TMF/ARA160 downregulates proangiogenic genes and attenuates the progression of PC3 xenografts
    • 19330832 1:CAS:528:DC%2BD1MXmslCgtLs%3D 10.1002/ijc.24277
    • Abrham G, Volpe M, Shpungin S, Nir U (2009) TMF/ARA160 downregulates proangiogenic genes and attenuates the progression of PC3 xenografts. Int J Cancer 125(1):43-53
    • (2009) Int J Cancer , vol.125 , Issue.1 , pp. 43-53
    • Abrham, G.1    Volpe, M.2    Shpungin, S.3    Nir, U.4
  • 57
    • 34548349295 scopus 로고    scopus 로고
    • MARCH-XI, a novel transmembrane ubiquitin ligase implicated in ubiquitin-dependent protein sorting in developing spermatids
    • 17604280 1:CAS:528:DC%2BD2sXpt1Slsbc%3D 10.1074/jbc.M700414200
    • Morokuma Y, Nakamura N, Kato A, Notoya M, Yamamoto Y, Sakai Y, Fukuda H, Yamashina S, Hirata Y, Hirose S (2007) MARCH-XI, a novel transmembrane ubiquitin ligase implicated in ubiquitin-dependent protein sorting in developing spermatids. J Biol Chem 282(34):24806-24815
    • (2007) J Biol Chem , vol.282 , Issue.34 , pp. 24806-24815
    • Morokuma, Y.1    Nakamura, N.2    Kato, A.3    Notoya, M.4    Yamamoto, Y.5    Sakai, Y.6    Fukuda, H.7    Yamashina, S.8    Hirata, Y.9    Hirose, S.10
  • 58
    • 84857640110 scopus 로고    scopus 로고
    • Identification of SAMT family proteins as substrates of MARCH11 in mouse spermatids
    • 22075566 1:CAS:528:DC%2BC38Xit1Omug%3D%3D 10.1007/s00418-011-0887-y
    • Yogo K, Tojima H, Ohno JY, Ogawa T, Nakamura N, Hirose S, Takeya T, Kohsaka T (2012) Identification of SAMT family proteins as substrates of MARCH11 in mouse spermatids. Histochem Cell Biol 137(1):53-65
    • (2012) Histochem Cell Biol , vol.137 , Issue.1 , pp. 53-65
    • Yogo, K.1    Tojima, H.2    Ohno, J.Y.3    Ogawa, T.4    Nakamura, N.5    Hirose, S.6    Takeya, T.7    Kohsaka, T.8
  • 59
    • 0021097528 scopus 로고
    • Changes in nuclear content of protein conjugate histone H2A-ubiquitin during rooster spermatogenesis
    • 6303842 1:CAS:528:DyaL3sXktlKiur0%3D 10.1016/0014-5793(82)80604-2
    • Agell N, Chiva M, Mezquita C (1983) Changes in nuclear content of protein conjugate histone H2A-ubiquitin during rooster spermatogenesis. FEBS Lett 155(2):209-212
    • (1983) FEBS Lett , vol.155 , Issue.2 , pp. 209-212
    • Agell, N.1    Chiva, M.2    Mezquita, C.3
  • 61
    • 15044354179 scopus 로고    scopus 로고
    • Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones
    • 15767685 1:CAS:528:DC%2BD2MXis12ju7o%3D 10.1128/MCB.25.7.2819-2831.2005
    • Liu Z, Oughtred R, Wing SS (2005) Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones. Mol Cell Biol 25(7):2819-2831
    • (2005) Mol Cell Biol , vol.25 , Issue.7 , pp. 2819-2831
    • Liu, Z.1    Oughtred, R.2    Wing, S.S.3
  • 62
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • 8982460 1:CAS:528:DyaK2sXht1yk 10.1146/annurev.genet.30.1.405
    • Hochstrasser M (1996) Ubiquitin-dependent protein degradation. Annu Rev Genet 30:405-439
    • (1996) Annu Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 63
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • 11265246 1:CAS:528:DC%2BD3MXhvFKrs74%3D 10.1038/35056563
    • Weissman AM (2001) Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2(3):169-178
    • (2001) Nat Rev Mol Cell Biol , vol.2 , Issue.3 , pp. 169-178
    • Weissman, A.M.1
  • 64
    • 2442529664 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family
    • 15071497 1:CAS:528:DC%2BD2cXjt1Cls78%3D 10.1038/sj.emboj.7600186
    • Pintard L, Willems A, Peter M (2004) Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family. EMBO J 23(8):1681-1687
    • (2004) EMBO J , vol.23 , Issue.8 , pp. 1681-1687
    • Pintard, L.1    Willems, A.2    Peter, M.3
  • 65
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • 1336336 1:CAS:528:DyaK3sXit1ygsro%3D 10.1146/annurev.ge.26.120192.001143
    • Jentsch S (1992) The ubiquitin-conjugation system. Annu Rev Genet 26:179-207
    • (1992) Annu Rev Genet , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 66
    • 27944475244 scopus 로고    scopus 로고
    • Isolation and characterization of ubiquitin-activating enzyme E1-domain containing 1, UBE1DC1
    • 16328888 1:CAS:528:DC%2BD2MXht1enu77O 10.1007/s11033-005-4822-y
    • Dou T, Gu S, Liu J, Chen F, Zeng L, Guo L, Xie Y, Mao Y (2005) Isolation and characterization of ubiquitin-activating enzyme E1-domain containing 1, UBE1DC1. Mol Biol Rep 32(4):265-271
    • (2005) Mol Biol Rep , vol.32 , Issue.4 , pp. 265-271
    • Dou, T.1    Gu, S.2    Liu, J.3    Chen, F.4    Zeng, L.5    Guo, L.6    Xie, Y.7    Mao, Y.8
  • 68
    • 84858285540 scopus 로고    scopus 로고
    • Identification and characterization of a spermatogenesis-related gene Ube1 in rat testis
    • 18560730 1:CAS:528:DC%2BD1MXlvFeqtr0%3D
    • Du Y, Liu ML, Jia MC (2008) Identification and characterization of a spermatogenesis-related gene Ube1 in rat testis. Sheng Li Xue Bao 60(3):382-390
    • (2008) Sheng Li Xue Bao , vol.60 , Issue.3 , pp. 382-390
    • Du, Y.1    Liu, M.L.2    Jia, M.C.3
  • 70
    • 0029898412 scopus 로고    scopus 로고
    • A novel rat homologue of the S. Cerevisiae ubiquitin conjugating enzyme UBC4 with distinct biochemical features is induced during spermatogenesis
    • 8754804 1:CAS:528:DyaK28XksValtr0%3D
    • Wing SS, Bedard N, Morales C, Hingamp P, Trasler J (1996) A novel rat homologue of the S. Cerevisiae ubiquitin conjugating enzyme UBC4 with distinct biochemical features is induced during spermatogenesis. Mol Cell Biol 16:4064-4072
    • (1996) Mol Cell Biol , vol.16 , pp. 4064-4072
    • Wing, S.S.1    Bedard, N.2    Morales, C.3    Hingamp, P.4    Trasler, J.5
  • 71
    • 0029982968 scopus 로고    scopus 로고
    • Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes
    • 8610150 1:CAS:528:DyaK28XitVCitLk%3D 10.1073/pnas.93.7.2958
    • Kovalenko OV, Plug AW, Haaf T, Gonda DK, Ashley T, Ward DC, Radding CM, Golub EI (1996) Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc Natl Acad Sci 93(7):2958-2963
    • (1996) Proc Natl Acad Sci , vol.93 , Issue.7 , pp. 2958-2963
    • Kovalenko, O.V.1    Plug, A.W.2    Haaf, T.3    Gonda, D.K.4    Ashley, T.5    Ward, D.C.6    Radding, C.M.7    Golub, E.I.8
  • 72
    • 0016189174 scopus 로고
    • Lack of chemically induced mutation in repair-deficient mutants of yeast
    • 4376097 1:CAS:528:DyaE2MXkslalsLc%3D
    • Prakash L (1974) Lack of chemically induced mutation in repair-deficient mutants of yeast. Genetics 78(4):1101-1118
    • (1974) Genetics , vol.78 , Issue.4 , pp. 1101-1118
    • Prakash, L.1
  • 73
    • 0030021770 scopus 로고    scopus 로고
    • Expression of the ubiquitin-conjugating DNA repair enzymes HHR6A and B suggests a role in spermatogenesis and chromatin modification
    • 8575614 1:CAS:528:DyaK28XotFaitQ%3D%3D 10.1006/dbio.1996.0011
    • Koken MH, Hoogerbrugge JW, Jasper-Dekker I, de Wit J, Willemsen R, Roest HP, Grootegoed JA, Hoeijmakers JH (1996) Expression of the ubiquitin-conjugating DNA repair enzymes HHR6A and B suggests a role in spermatogenesis and chromatin modification. Dev Biol 173:119-132
    • (1996) Dev Biol , vol.173 , pp. 119-132
    • Koken, M.H.1    Hoogerbrugge, J.W.2    Jasper-Dekker, I.3    De Wit, J.4    Willemsen, R.5    Roest, H.P.6    Grootegoed, J.A.7    Hoeijmakers, J.H.8
  • 74
    • 0033063745 scopus 로고    scopus 로고
    • Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis
    • 10373550 1:CAS:528:DyaK1MXktVCgt7g%3D
    • Pati D, Meistrich ML, Plon SE (1999) Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis. Mol Cell Biol 19:5001-5013
    • (1999) Mol Cell Biol , vol.19 , pp. 5001-5013
    • Pati, D.1    Meistrich, M.L.2    Plon, S.E.3
  • 75
    • 0028813764 scopus 로고
    • Molecular cloning, expression and characterization of a ubiquitin conjugation enzyme (E2(17)kB) highly expressed in rat testis
    • 7826319 1:CAS:528:DyaK2MXjtFeltLw%3D
    • Wing SS, Jain P (1995) Molecular cloning, expression and characterization of a ubiquitin conjugation enzyme (E2(17)kB) highly expressed in rat testis. Biochem J 305:125-132
    • (1995) Biochem J , vol.305 , pp. 125-132
    • Wing, S.S.1    Jain, P.2
  • 77
    • 0033755145 scopus 로고    scopus 로고
    • Specific aspects of the ubiquitin system in spermatogenesis
    • 11079455 1:CAS:528:DC%2BD3cXotVWrurk%3D
    • Baarends WM, van der Laan R, Grootegoed JA (2000) Specific aspects of the ubiquitin system in spermatogenesis. J Endocrinol Invest 23:597-604
    • (2000) J Endocrinol Invest , vol.23 , pp. 597-604
    • Baarends, W.M.1    Van Der Laan, R.2    Grootegoed, J.A.3
  • 79
    • 77955618370 scopus 로고    scopus 로고
    • Identification of testis-specific ubiquitin-conjugating enzyme in the ascidian Ciona intestinalis
    • 20578064 1:CAS:528:DC%2BC3cXotVahsLk%3D 10.1002/mrd.21198
    • Yokota N, Harada Y, Sawada H (2010) Identification of testis-specific ubiquitin-conjugating enzyme in the ascidian Ciona intestinalis. Mol Reprod Dev 77(7):640-647
    • (2010) Mol Reprod Dev , vol.77 , Issue.7 , pp. 640-647
    • Yokota, N.1    Harada, Y.2    Sawada, H.3
  • 80
    • 67649585990 scopus 로고    scopus 로고
    • Rnf19a, a ubiquitin protein ligase, and Psmc3, a component of the 26S proteasome, tether to the acrosome membranes and the head-tail coupling apparatus during rat spermatid development
    • 19517565 1:CAS:528:DC%2BD1MXovV2msro%3D 10.1002/dvdy.22004
    • Rivkin E, Kierszenbaum AL, Gil M, Tres LL (2009) Rnf19a, a ubiquitin protein ligase, and Psmc3, a component of the 26S proteasome, tether to the acrosome membranes and the head-tail coupling apparatus during rat spermatid development. Dev Dyn 238(7):1851-1861
    • (2009) Dev Dyn , vol.238 , Issue.7 , pp. 1851-1861
    • Rivkin, E.1    Kierszenbaum, A.L.2    Gil, M.3    Tres, L.L.4
  • 81
    • 46749155472 scopus 로고    scopus 로고
    • Mouse RING finger protein Rnf133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase
    • 18574499 1:CAS:528:DC%2BD1cXnvFyhsbY%3D 10.1038/cr.2008.73
    • Nian H, Zhang W, Shi H, Zhao Q, Xie Q, Liao S, Zhang Y, Zhang Z, Wang C, Han C (2008) Mouse RING finger protein Rnf133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase. Cell Res 18(7):800-802
    • (2008) Cell Res , vol.18 , Issue.7 , pp. 800-802
    • Nian, H.1    Zhang, W.2    Shi, H.3    Zhao, Q.4    Xie, Q.5    Liao, S.6    Zhang, Y.7    Zhang, Z.8    Wang, C.9    Han, C.10
  • 82
    • 34548026107 scopus 로고    scopus 로고
    • RNF151, a testis-specific RING finger protein, interacts with dysbindin
    • 17577571 1:CAS:528:DC%2BD2sXpsFGhtLY%3D 10.1016/j.abb.2007.05.013
    • Nian H, Fan C, Liao S, Shi Y, Zhang K, Liu Y, Han C (2007) RNF151, a testis-specific RING finger protein, interacts with dysbindin. Arch Biochem Biophys 465(1):157-163
    • (2007) Arch Biochem Biophys , vol.465 , Issue.1 , pp. 157-163
    • Nian, H.1    Fan, C.2    Liao, S.3    Shi, Y.4    Zhang, K.5    Liu, Y.6    Han, C.7
  • 83
    • 41149103625 scopus 로고    scopus 로고
    • Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-bound ubiquitin ligase
    • 18363970 1:CAS:528:DC%2BD1cXkvFegtL0%3D 10.1111/j.1365-2443.2008.01169.x
    • Ogawa M, Mizugishi K, Ishiguro A, Koyabu Y, Imai Y, Takahashi R, Mikoshiba K, Aruga J (2008) Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-bound ubiquitin ligase. Genes Cells 13(4):397-409
    • (2008) Genes Cells , vol.13 , Issue.4 , pp. 397-409
    • Ogawa, M.1    Mizugishi, K.2    Ishiguro, A.3    Koyabu, Y.4    Imai, Y.5    Takahashi, R.6    Mikoshiba, K.7    Aruga, J.8
  • 84
    • 76049113545 scopus 로고    scopus 로고
    • RNF8-dependent histone modifications regulate nucleosome removal during spermatogenesis
    • 20153262 1:CAS:528:DC%2BC3cXlsVSht78%3D 10.1016/j.devcel.2010.01.010
    • Lu LY, Wu J, Ye L, Gavrilina GB, Saunders TL, Yu X (2010) RNF8-dependent histone modifications regulate nucleosome removal during spermatogenesis. Dev Cell 18(3):371-384
    • (2010) Dev Cell , vol.18 , Issue.3 , pp. 371-384
    • Lu, L.Y.1    Wu, J.2    Ye, L.3    Gavrilina, G.B.4    Saunders, T.L.5    Yu, X.6
  • 85
    • 77956440333 scopus 로고    scopus 로고
    • Human RING finger protein ZNF645 is a novel testis-specific E3 ubiquitin ligase
    • 20657603 1:CAS:528:DC%2BC3cXhtFaitr3N 10.1038/aja.2010.54
    • Liu YQ, Bai G, Zhang H, Su D, Tao DC, Yang Y, Ma YX, Zhang SZ (2010) Human RING finger protein ZNF645 is a novel testis-specific E3 ubiquitin ligase. Asian J Androl 12(5):658-666
    • (2010) Asian J Androl , vol.12 , Issue.5 , pp. 658-666
    • Liu, Y.Q.1    Bai, G.2    Zhang, H.3    Su, D.4    Tao, D.C.5    Yang, Y.6    Ma, Y.X.7    Zhang, S.Z.8
  • 86
    • 33744974570 scopus 로고    scopus 로고
    • MEX is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis
    • 16522193 1:CAS:528:DC%2BD28XltVWmu7Y%3D 10.1042/BJ20051814
    • Nishito Y, Hasegawa M, Inohara N, Núñez G (2006) MEX is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis. Biochem J 396(3):411-417
    • (2006) Biochem J , vol.396 , Issue.3 , pp. 411-417
    • Nishito, Y.1    Hasegawa, M.2    Inohara, N.3    Núñez, G.4
  • 87
    • 77649153374 scopus 로고    scopus 로고
    • Spermatogenesis rescue in a mouse deficient for the ubiquitin ligase SCF{beta}-TrCP by single substrate depletion
    • 20194439 1:CAS:528:DC%2BC3cXjtFaiur8%3D 10.1101/gad.551610
    • Kanarek N, Horwitz E, Mayan I, Leshets M, Cojocaru G, Davis M, Tsuberi BZ, Pikarsky E, Pagano M, Ben-Neriah Y (2010) Spermatogenesis rescue in a mouse deficient for the ubiquitin ligase SCF{beta}-TrCP by single substrate depletion. Genes Dev 24(5):470-477
    • (2010) Genes Dev , vol.24 , Issue.5 , pp. 470-477
    • Kanarek, N.1    Horwitz, E.2    Mayan, I.3    Leshets, M.4    Cojocaru, G.5    Davis, M.6    Tsuberi, B.Z.7    Pikarsky, E.8    Pagano, M.9    Ben-Neriah, Y.10
  • 88
    • 36549074062 scopus 로고    scopus 로고
    • Disruption of the ubiquitin ligase HERC4 causes defects in spermatozoon maturation and impaired fertility
    • 17967448 1:CAS:528:DC%2BD2sXhsVSktrvP 10.1016/j.ydbio.2007.09.053
    • Rodriguez CI, Stewart CL (2007) Disruption of the ubiquitin ligase HERC4 causes defects in spermatozoon maturation and impaired fertility. Dev Biol 312(2):501-508
    • (2007) Dev Biol , vol.312 , Issue.2 , pp. 501-508
    • Rodriguez, C.I.1    Stewart, C.L.2
  • 89
    • 35649007879 scopus 로고    scopus 로고
    • A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila
    • 17880263 10.1371/journal.pbio.0050251 1:CAS:528:DC%2BD2sXhsVersrrI
    • Arama E, Bader M, Rieckhof GE, Steller H (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10):e251
    • (2007) PLoS Biol , vol.5 , Issue.10 , pp. 251
    • Arama, E.1    Bader, M.2    Rieckhof, G.E.3    Steller, H.4
  • 90
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • 16678110 10.1016/j.molcel.2006.03.035 1:CAS:528:DC%2BD28XkvVChsb8%3D
    • Wang H, Zhai L, Xu J, Joo HY, Jackson S, Erdjument-Bromage H, Tempst P, Xiong Y, Zhang Y (2006) Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell 22(3):383-394
    • (2006) Mol Cell , vol.22 , Issue.3 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.Y.4    Jackson, S.5    Erdjument-Bromage, H.6    Tempst, P.7    Xiong, Y.8    Zhang, Y.9
  • 91
    • 79953023825 scopus 로고    scopus 로고
    • Cul4A is essential for spermatogenesis and male fertility
    • 21291880 1:CAS:528:DC%2BC3MXjvV2ms7g%3D 10.1016/j.ydbio.2011.01.028
    • Kopanja D, Roy N, Stoyanova T, Hess RA, Bagchi S, Raychaudhuri P (2011) Cul4A is essential for spermatogenesis and male fertility. Dev Biol 352(2):278-287
    • (2011) Dev Biol , vol.352 , Issue.2 , pp. 278-287
    • Kopanja, D.1    Roy, N.2    Stoyanova, T.3    Hess, R.A.4    Bagchi, S.5    Raychaudhuri, P.6
  • 93
    • 0036773058 scopus 로고    scopus 로고
    • Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase induced in germ cells of the rat testis and similar to the Drosophila hyperplastic discs gene
    • 12239083 1:CAS:528:DC%2BD38Xnt1ygs7g%3D 10.1210/en.2002-220262
    • Oughtred R, Bedard N, Adegoke OA, Morales CR, Trasler J, Rajapurohitam V, Wing SS (2002) Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase induced in germ cells of the rat testis and similar to the Drosophila hyperplastic discs gene. Endocrinology 143(10):3740-3747
    • (2002) Endocrinology , vol.143 , Issue.10 , pp. 3740-3747
    • Oughtred, R.1    Bedard, N.2    Adegoke, O.A.3    Morales, C.R.4    Trasler, J.5    Rajapurohitam, V.6    Wing, S.S.7
  • 94
    • 67349172917 scopus 로고    scopus 로고
    • The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases
    • 19013150 1:CAS:528:DC%2BD1MXltVyqurs%3D 10.1016/j.yexcr.2008.10.026
    • Nathan JA, Lehner PJ (2009) The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases. Exp Cell Res 315(9):1593-1600
    • (2009) Exp Cell Res , vol.315 , Issue.9 , pp. 1593-1600
    • Nathan, J.A.1    Lehner, P.J.2
  • 95
    • 80655125026 scopus 로고    scopus 로고
    • Membrane-associated RING-CH 10 (MARCH10 protein) is a microtubule-associated E3 ubiquitin ligase of the spermatid flagella
    • 21937444 1:CAS:528:DC%2BC3MXhsVSqt7bI 10.1074/jbc.M111.256875
    • Iyengar PV, Hirota T, Hirose S, Nakamura N (2011) Membrane-associated RING-CH 10 (MARCH10 protein) is a microtubule-associated E3 ubiquitin ligase of the spermatid flagella. J Biol Chem 286(45):39082-39090
    • (2011) J Biol Chem , vol.286 , Issue.45 , pp. 39082-39090
    • Iyengar, P.V.1    Hirota, T.2    Hirose, S.3    Nakamura, N.4
  • 96
    • 35348953150 scopus 로고    scopus 로고
    • Regulated expression of the ubiquitin protein ligase, E3(Histone)/LASU1/Mule/ARF-BP1/HUWE1, during spermatogenesis
    • 17823942 1:CAS:528:DC%2BD2sXhtlels77J 10.1002/dvdy.21302
    • Liu Z, Miao D, Xia Q, Hermo L, Wing SS (2007) Regulated expression of the ubiquitin protein ligase, E3(Histone)/LASU1/Mule/ARF-BP1/HUWE1, during spermatogenesis. Dev Dyn 236(10):2889-2898
    • (2007) Dev Dyn , vol.236 , Issue.10 , pp. 2889-2898
    • Liu, Z.1    Miao, D.2    Xia, Q.3    Hermo, L.4    Wing, S.S.5
  • 99
    • 0036021262 scopus 로고    scopus 로고
    • Ran, a GTP-binding protein involved in nucleocytoplasmic transport and microtubule nucleation, relocates from the manchette to the centrosome region during rat spermiogenesis
    • 12211070 1:CAS:528:DC%2BD38XmtVemtrs%3D 10.1002/mrd.10164
    • Kierszenbaum AL, Gil M, Rivkin E, Tres LL (2002) Ran, a GTP-binding protein involved in nucleocytoplasmic transport and microtubule nucleation, relocates from the manchette to the centrosome region during rat spermiogenesis. Mol Reprod Dev 63(1):131-140
    • (2002) Mol Reprod Dev , vol.63 , Issue.1 , pp. 131-140
    • Kierszenbaum, A.L.1    Gil, M.2    Rivkin, E.3    Tres, L.L.4
  • 100
    • 0344851636 scopus 로고    scopus 로고
    • Intratesticular signals for progression of germ cell stages in vertebrates
    • 14636628 1:CAS:528:DC%2BD3sXptVektb8%3D 10.1016/S0016-6480(03)00281-8
    • Cobellis G, Meccariello R, Pierantoni R, Fasano S (2003) Intratesticular signals for progression of germ cell stages in vertebrates. Gen Comp Endocrinol 134(3):220-228
    • (2003) Gen Comp Endocrinol , vol.134 , Issue.3 , pp. 220-228
    • Cobellis, G.1    Meccariello, R.2    Pierantoni, R.3    Fasano, S.4
  • 101
    • 20444374433 scopus 로고    scopus 로고
    • Novel mutations in testis-specific ubiquitin protease 26 gene may cause male infertility and hypogonadism
    • 15970005 10.1016/S1472-6483(10)61119-4
    • Paduch DA, Mielnik A, Schlegel PN (2005) Novel mutations in testis-specific ubiquitin protease 26 gene may cause male infertility and hypogonadism. Reprod Biomed Online 10(6):747-754
    • (2005) Reprod Biomed Online , vol.10 , Issue.6 , pp. 747-754
    • Paduch, D.A.1    Mielnik, A.2    Schlegel, P.N.3
  • 102
    • 14944354066 scopus 로고    scopus 로고
    • Possible role of USP26 in patients with severely impaired spermatogenesis
    • 15562280 1:CAS:528:DC%2BD2MXhsVOmsL0%3D 10.1038/sj.ejhg.5201335
    • Stouffs K, Lissens W, Tournaye H, Van Steirteghem A, Liebaers I (2005) Possible role of USP26 in patients with severely impaired spermatogenesis. Eur J Hum Genet 13(3):336-340
    • (2005) Eur J Hum Genet , vol.13 , Issue.3 , pp. 336-340
    • Stouffs, K.1    Lissens, W.2    Tournaye, H.3    Van Steirteghem, A.4    Liebaers, I.5
  • 104
    • 33750795592 scopus 로고    scopus 로고
    • The expression of Usp42 during embryogenesis and spermatogenesis in mouse
    • 16904385 1:CAS:528:DC%2BD28Xht1agsbrO 10.1016/j.modgep.2006.06.006
    • Kim YK, Kim YS, Yoo KJ, Lee HJ, Lee DR, Yeo CY, Baek KH (2007) The expression of Usp42 during embryogenesis and spermatogenesis in mouse. Gene Expr Patterns 7(1-2):143-148
    • (2007) Gene Expr Patterns , vol.7 , Issue.1-2 , pp. 143-148
    • Kim, Y.K.1    Kim, Y.S.2    Yoo, K.J.3    Lee, H.J.4    Lee, D.R.5    Yeo, C.Y.6    Baek, K.H.7
  • 105
    • 0032727618 scopus 로고    scopus 로고
    • An azoospermic man with a de novo point mutation in the Y-chromosomal gene USP9Y
    • 10581029 1:CAS:528:DyaK1MXnvFOktbs%3D 10.1038/70539
    • Sun C, Skaletsky H, Birren B, Devon K, Tang Z, Silber S, Oates R, Page DC (1999) An azoospermic man with a de novo point mutation in the Y-chromosomal gene USP9Y. Nat Genet 23(4):429-432
    • (1999) Nat Genet , vol.23 , Issue.4 , pp. 429-432
    • Sun, C.1    Skaletsky, H.2    Birren, B.3    Devon, K.4    Tang, Z.5    Silber, S.6    Oates, R.7    Page, D.C.8
  • 107
    • 77349084837 scopus 로고    scopus 로고
    • Expression and localization of the deubiquitinating enzyme mUBPy in wobbler mouse testis during spermiogenesis
    • 19800341 10.1016/j.ygcen.2009.09.014 1:CAS:528:DC%2BC3cXjtVCgtLg%3D
    • Chianese R, Scarpa D, Berruti G, Cobellis G, Pierantoni R, Fasano S, Meccariello R (2009) Expression and localization of the deubiquitinating enzyme mUBPy in wobbler mouse testis during spermiogenesis. Gen Comp Endocrinol 166(2):289-295
    • (2009) Gen Comp Endocrinol , vol.166 , Issue.2 , pp. 289-295
    • Chianese, R.1    Scarpa, D.2    Berruti, G.3    Cobellis, G.4    Pierantoni, R.5    Fasano, S.6    Meccariello, R.7
  • 108
    • 77953838066 scopus 로고    scopus 로고
    • USP8, a regulator of endosomal sorting, is involved in mouse acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules
    • 20130268 1:CAS:528:DC%2BC3cXlt1KhtLw%3D 10.1095/biolreprod.109.081679
    • Berruti G, Ripolone M, Ceriani M (2010) USP8, a regulator of endosomal sorting, is involved in mouse acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Biol Reprod 82(5):930-939
    • (2010) Biol Reprod , vol.82 , Issue.5 , pp. 930-939
    • Berruti, G.1    Ripolone, M.2    Ceriani, M.3
  • 109
    • 10944270585 scopus 로고    scopus 로고
    • The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: The relation with the proteasome, acrosome, and centrosome in mouse male germ cells
    • 15342353 10.1095/biolreprod.104.030866 1:CAS:528:DC%2BD2MXmtlGq
    • Berruti G, Martegani E (2004) The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and centrosome in mouse male germ cells. Biol Reprod 72(1):14-21
    • (2004) Biol Reprod , vol.72 , Issue.1 , pp. 14-21
    • Berruti, G.1    Martegani, E.2
  • 110
    • 0034809856 scopus 로고    scopus 로고
    • Cloning, expression, and mapping of a mouse gene, Uchl4, highly homologous to human and mouse Uchl3
    • 11341770 1:CAS:528:DC%2BD3MXjt1GntL4%3D 10.1006/bbrc.2001.4841
    • Osawa Y, Wang YL, Osaka H, Aoki S, Wada K (2001) Cloning, expression, and mapping of a mouse gene, Uchl4, highly homologous to human and mouse Uchl3. Biochem Biophys Res Commun 283:627-633
    • (2001) Biochem Biophys Res Commun , vol.283 , pp. 627-633
    • Osawa, Y.1    Wang, Y.L.2    Osaka, H.3    Aoki, S.4    Wada, K.5
  • 112
    • 0035444169 scopus 로고    scopus 로고
    • Loss of Uch-L1 and Uch-L3 leads to neurodegeneration, posterior paralysis and dysphagia
    • 11555633 1:CAS:528:DC%2BD3MXntlSgsbY%3D 10.1093/hmg/10.18.1963
    • Kurihara LJ, Kikuchi T, Wada K, Tilghman SM (2001) Loss of Uch-L1 and Uch-L3 leads to neurodegeneration, posterior paralysis and dysphagia. Hum Mol Genet 10:1963-1970
    • (2001) Hum Mol Genet , vol.10 , pp. 1963-1970
    • Kurihara, L.J.1    Kikuchi, T.2    Wada, K.3    Tilghman, S.M.4
  • 113
    • 12344261439 scopus 로고    scopus 로고
    • Localization of ubiquitin carboxyl-terminal hydrolase-L1 in cynomolgus monkey placentas
    • 15664418 1:CAS:528:DC%2BD2MXms1Gqug%3D%3D 10.1016/j.placenta.2004.05.007
    • Sekiguchi S, Takatori A, Negishi T, Kwon J, Kokubo T, Ishii Y, Kyuwa S, Yoshikawa Y (2005) Localization of ubiquitin carboxyl-terminal hydrolase-L1 in cynomolgus monkey placentas. Placenta 26(1):99-103
    • (2005) Placenta , vol.26 , Issue.1 , pp. 99-103
    • Sekiguchi, S.1    Takatori, A.2    Negishi, T.3    Kwon, J.4    Kokubo, T.5    Ishii, Y.6    Kyuwa, S.7    Yoshikawa, Y.8
  • 114
    • 0029060311 scopus 로고
    • Ultrastructural localization of PGP 9.5 and ubiquitin immunoreactivities in rat ductus epididymidis epithelium
    • 7558892
    • Martín R, Santamaría L, Fraile B, Paniagua R, Polak JM (1995) Ultrastructural localization of PGP 9.5 and ubiquitin immunoreactivities in rat ductus epididymidis epithelium. Histochem J 27(6):431-439
    • (1995) Histochem J , vol.27 , Issue.6 , pp. 431-439
    • Martín, R.1    Santamaría, L.2    Fraile, B.3    Paniagua, R.4    Polak, J.M.5
  • 115
    • 37849045569 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase-L1 (Uch-L1) correlates with gonadal transformation in the rice field eel
    • 18076650 1:CAS:528:DC%2BD1cXhtFejtrs%3D 10.1111/j.1742-4658.2007.06194.x
    • Sun J, Shang X, Tian Y, Zhao W, He Y, Chen K, Cheng H, Zhou R (2008) Ubiquitin C-terminal hydrolase-L1 (Uch-L1) correlates with gonadal transformation in the rice field eel. FEBS J 275(2):242-249
    • (2008) FEBS J , vol.275 , Issue.2 , pp. 242-249
    • Sun, J.1    Shang, X.2    Tian, Y.3    Zhao, W.4    He, Y.5    Chen, K.6    Cheng, H.7    Zhou, R.8
  • 116
    • 7444236389 scopus 로고    scopus 로고
    • Effects of endocrine-disrupting chemicals on expression of ubiquitin C-terminal hydrolase mRNA in testis and brain of the Japanese common goby
    • 15522430 1:CAS:528:DC%2BD2cXptFKqtrg%3D 10.1016/j.aquatox.2004.08.001
    • Mochida K, Ohkubo N, Matsubara T, Ito K, Kakuno A, Fujii K, Aquat Toxicol (2004) Effects of endocrine-disrupting chemicals on expression of ubiquitin C-terminal hydrolase mRNA in testis and brain of the Japanese common goby. Aquat Toxicol 70(2):123-136
    • (2004) Aquat Toxicol , vol.70 , Issue.2 , pp. 123-136
    • Mochida, K.1    Ohkubo, N.2    Matsubara, T.3    Ito, K.4    Kakuno, A.5    Fujii, K.6    Aquat, T.7
  • 117
    • 0036711565 scopus 로고    scopus 로고
    • Molecular cloning and immunohistochemical localization of ubiquitin C-Terminal hydrolase expressed in testis of a teleost, the Nile Tilapia, Oreochromis niloticus
    • 12210120 1:CAS:528:DC%2BD38XnsVSrs70%3D 10.1002/jez.10136
    • Mochida K, Matsubara T, Kudo H, Andoh T, Ueda H, Adachi S, Yamauchi K (2002) Molecular cloning and immunohistochemical localization of ubiquitin C-Terminal hydrolase expressed in testis of a teleost, the Nile Tilapia, Oreochromis niloticus. J Exp Zool 293(4):368-383
    • (2002) J Exp Zool , vol.293 , Issue.4 , pp. 368-383
    • Mochida, K.1    Matsubara, T.2    Kudo, H.3    Andoh, T.4    Ueda, H.5    Adachi, S.6    Yamauchi, K.7
  • 118
    • 0037676148 scopus 로고    scopus 로고
    • Characterization of the testis in congenitally ubiquitin carboxy-terminal hydrolase-1 (Uch-L1) defective (gad) mice
    • 12638230 1:CAS:528:DC%2BD3sXhvFSqtbc%3D 10.1538/expanim.52.1
    • Kwon J, Kikuchi T, Setsuie R, Ishii Y, Kyuwa S, Yoshikawa Y (2003) Characterization of the testis in congenitally ubiquitin carboxy-terminal hydrolase-1 (Uch-L1) defective (gad) mice. Exp Anim 52(1):1-9
    • (2003) Exp Anim , vol.52 , Issue.1 , pp. 1-9
    • Kwon, J.1    Kikuchi, T.2    Setsuie, R.3    Ishii, Y.4    Kyuwa, S.5    Yoshikawa, Y.6
  • 119
    • 0032708518 scopus 로고    scopus 로고
    • Expression of protein gene product 9.5, a neuronal ubiquitin C-terminal hydrolase, and its developing change in Sertoli cells of mouse testis
    • 10542373 1:CAS:528:DyaK1MXntFCltLw%3D 10.1002/(SICI)1098-2795(199912)54: 4<333: AID-MRD3>3.0.CO;2-8
    • Kon Y, Endoh D, Iwanaga T (1999) Expression of protein gene product 9.5, a neuronal ubiquitin C-terminal hydrolase, and its developing change in Sertoli cells of mouse testis. Mol Reprod Dev 54(4):333-341
    • (1999) Mol Reprod Dev , vol.54 , Issue.4 , pp. 333-341
    • Kon, Y.1    Endoh, D.2    Iwanaga, T.3
  • 120
    • 0029739625 scopus 로고    scopus 로고
    • Light and electron microscopic immunohistochemical localization of protein gene product 9.5 and ubiquitin immunoreactivities in the human epididymis and vas deferens
    • 8828831 1:CAS:528:DyaK28XltlGit70%3D 10.1095/biolreprod55.2.291
    • Fraile B, Martin R, De Miguel MP, Arenas MI, Bethencourt FR, Peinado F, Paniagua R, Santamaria L (1996) Light and electron microscopic immunohistochemical localization of protein gene product 9.5 and ubiquitin immunoreactivities in the human epididymis and vas deferens. Biol Reprod 55(2):291-297
    • (1996) Biol Reprod , vol.55 , Issue.2 , pp. 291-297
    • Fraile, B.1    Martin, R.2    De Miguel, M.P.3    Arenas, M.I.4    Bethencourt, F.R.5    Peinado, F.6    Paniagua, R.7    Santamaria, L.8
  • 121
    • 20844437611 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase L-1 is essential for the early apoptotic wave of germinal cells and for sperm quality control during spermatogenesis
    • 15744022 1:CAS:528:DC%2BD2MXls1Srtro%3D 10.1095/biolreprod.104.037077
    • Kwon J, Mochida K, Wang YL, Sekiguchi S, Sankai T, Aoki S, Ogura A, Yoshikawa Y, Wada K (2005) Ubiquitin C-terminal hydrolase L-1 is essential for the early apoptotic wave of germinal cells and for sperm quality control during spermatogenesis. Biol Reprod 73(1):29-35
    • (2005) Biol Reprod , vol.73 , Issue.1 , pp. 29-35
    • Kwon, J.1    Mochida, K.2    Wang, Y.L.3    Sekiguchi, S.4    Sankai, T.5    Aoki, S.6    Ogura, A.7    Yoshikawa, Y.8    Wada, K.9
  • 122
    • 33644806314 scopus 로고    scopus 로고
    • The region-specific functions of two ubiquitin C-terminal hydrolase isozymes along the epididymis
    • 16508210 1:CAS:528:DC%2BD28XisFKmtb8%3D 10.1538/expanim.55.35
    • Kwon J, Sekiguchi S, Wang YL, Setsuie R, Yoshikawa Y, Wada K (2006) The region-specific functions of two ubiquitin C-terminal hydrolase isozymes along the epididymis. Exp Anim 55(1):35-43
    • (2006) Exp Anim , vol.55 , Issue.1 , pp. 35-43
    • Kwon, J.1    Sekiguchi, S.2    Wang, Y.L.3    Setsuie, R.4    Yoshikawa, Y.5    Wada, K.6
  • 123
    • 28744440612 scopus 로고    scopus 로고
    • Overexpression of ubiquitin carboxyl-terminal hydrolase L1 arrests spermatogenesis in transgenic mice
    • 16177983 1:CAS:528:DC%2BD2MXht12ntbzN 10.1002/mrd.20364
    • Wang YL, Liu W, Sun YJ, Kwon J, Setsuie R, Osaka H, Noda M, Aoki S, Yoshikawa Y, Wada K (2006) Overexpression of ubiquitin carboxyl-terminal hydrolase L1 arrests spermatogenesis in transgenic mice. Mol Reprod Dev 73(1):40-49
    • (2006) Mol Reprod Dev , vol.73 , Issue.1 , pp. 40-49
    • Wang, Y.L.1    Liu, W.2    Sun, Y.J.3    Kwon, J.4    Setsuie, R.5    Osaka, H.6    Noda, M.7    Aoki, S.8    Yoshikawa, Y.9    Wada, K.10
  • 124
    • 0034117284 scopus 로고    scopus 로고
    • Expression and functional analysis of Uch-L3 during mouse development
    • 10713173 1:CAS:528:DC%2BD3cXhvFegurc%3D 10.1128/MCB.20.7.2498-2504.2000
    • Kurihara LJ, Semenova E, Levorse JM, Tilghman SM (2000) Expression and functional analysis of Uch-L3 during mouse development. Mol Cell Biol 20(7):2498-2504
    • (2000) Mol Cell Biol , vol.20 , Issue.7 , pp. 2498-2504
    • Kurihara, L.J.1    Semenova, E.2    Levorse, J.M.3    Tilghman, S.M.4
  • 125
    • 77949272190 scopus 로고    scopus 로고
    • UCHL1 (PGP 9.5): Neuronal biomarker and ubiquitin system protein
    • 19879917 1:CAS:528:DC%2BC3cXjtFyhsLw%3D 10.1016/j.pneurobio.2009.10.020
    • Day IN, Thompson RJ (2010) UCHL1 (PGP 9.5): neuronal biomarker and ubiquitin system protein. Prog Neurobiol 90(3):327-362
    • (2010) Prog Neurobiol , vol.90 , Issue.3 , pp. 327-362
    • Day, I.N.1    Thompson, R.J.2
  • 126
    • 35548974703 scopus 로고    scopus 로고
    • Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD
    • 17981138 1:CAS:528:DC%2BD2sXhtlWitrfE 10.1016/j.devcel.2007.09.007
    • Wright A, Reiley WW, Chang M, Jin W, Lee AJ, Zhang M, Sun SC (2007) Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD. Dev Cell 13(5):705-716
    • (2007) Dev Cell , vol.13 , Issue.5 , pp. 705-716
    • Wright, A.1    Reiley, W.W.2    Chang, M.3    Jin, W.4    Lee, A.J.5    Zhang, M.6    Sun, S.C.7
  • 127
    • 0344392821 scopus 로고    scopus 로고
    • Acroplaxome, an F-actin-keratin-containing plate, anchors the acrosome to the nucleus during shaping of the spermatid head
    • 14551252 1:CAS:528:DC%2BD3sXpt1ymtLo%3D 10.1091/mbc.E03-04-0226
    • Kierszenbaum AL, Rivkin E, Tres LL (2003) Acroplaxome, an F-actin-keratin-containing plate, anchors the acrosome to the nucleus during shaping of the spermatid head. Mol Biol Cell 14(11):4628-4640
    • (2003) Mol Biol Cell , vol.14 , Issue.11 , pp. 4628-4640
    • Kierszenbaum, A.L.1    Rivkin, E.2    Tres, L.L.3
  • 128
    • 78649769243 scopus 로고    scopus 로고
    • Knobbed acrosome defect is associated with a region containing the genes STK17b and HECW2 on porcine chromosome 15
    • 21143916 1:CAS:528:DC%2BC3cXhsF2lt73F 10.1186/1471-2164-11-699
    • Sironen A, Uimari P, Nagy S, Paku S, Andersson M, Vilkki J (2010) Knobbed acrosome defect is associated with a region containing the genes STK17b and HECW2 on porcine chromosome 15. BMC Genomics 11:699
    • (2010) BMC Genomics , vol.11 , pp. 699
    • Sironen, A.1    Uimari, P.2    Nagy, S.3    Paku, S.4    Andersson, M.5    Vilkki, J.6
  • 129
    • 0035134182 scopus 로고    scopus 로고
    • Ubiquitin-based sperm assay for the diagnosis of male factor infertility
    • 11157815 1:CAS:528:DC%2BD3MXhsFGrs7k%3D 10.1093/humrep/16.2.250
    • Sutovsky P, Terada Y, Schatten G (2001) Ubiquitin-based sperm assay for the diagnosis of male factor infertility. Hum Reprod 16:250-258
    • (2001) Hum Reprod , vol.16 , pp. 250-258
    • Sutovsky, P.1    Terada, Y.2    Schatten, G.3
  • 130
    • 0036165849 scopus 로고    scopus 로고
    • Ubiquitin-dependent sperm quality control mechanism recognizes spermatozoa with DNA defects as revealed by dual ubiquitin-TUNEL assay
    • 11835586 1:CAS:528:DC%2BD38XhsFCgtbg%3D 10.1002/mrd.10101
    • Sutovsky P, Neuber E, Schatten G (2002) Ubiquitin-dependent sperm quality control mechanism recognizes spermatozoa with DNA defects as revealed by dual ubiquitin-TUNEL assay. Mol Reprod Dev 61:406-413
    • (2002) Mol Reprod Dev , vol.61 , pp. 406-413
    • Sutovsky, P.1    Neuber, E.2    Schatten, G.3
  • 132
    • 25144493349 scopus 로고    scopus 로고
    • Clinical adaptation of the sperm tag immunoassay (SUTI): Relationship of sperm ubiquitylation with sperm quality in gradient-purified semen samples from 93 men from a general infertility clinic population
    • 15817585 1:CAS:528:DC%2BD2MXmt1Gnuro%3D 10.1093/humrep/dei013
    • Ozanon C, Chouteau J, Sutovsky P (2005) Clinical adaptation of the sperm tag immunoassay (SUTI): relationship of sperm ubiquitylation with sperm quality in gradient-purified semen samples from 93 men from a general infertility clinic population. Hum Reprod 20:2271-2278
    • (2005) Hum Reprod , vol.20 , pp. 2271-2278
    • Ozanon, C.1    Chouteau, J.2    Sutovsky, P.3
  • 133
    • 0037307665 scopus 로고    scopus 로고
    • Differential ubiquitination of stallion sperm proteins: Possible implications for infertility and reproductive seasonality
    • 12533436 1:CAS:528:DC%2BD3sXntVCgtA%3D%3D 10.1095/biolreprod.102.005306
    • Sutovsky P, Turner RM, Hameed S, Sutovsky M (2003) Differential ubiquitination of stallion sperm proteins: possible implications for infertility and reproductive seasonality. Biol Reprod 68:688-698
    • (2003) Biol Reprod , vol.68 , pp. 688-698
    • Sutovsky, P.1    Turner, R.M.2    Hameed, S.3    Sutovsky, M.4
  • 134
    • 1942469900 scopus 로고    scopus 로고
    • Immunofluorescence reveals ubiquitination of retained distal cytoplasmic droplets on ejaculated porcine spermatozoa
    • 15064310
    • Kuster CE, Hess RA, Althouse GC (2004) Immunofluorescence reveals ubiquitination of retained distal cytoplasmic droplets on ejaculated porcine spermatozoa. J Androl 25:340-347
    • (2004) J Androl , vol.25 , pp. 340-347
    • Kuster, C.E.1    Hess, R.A.2    Althouse, G.C.3
  • 136
    • 18744371911 scopus 로고    scopus 로고
    • Sperm ubiquitination positively correlates to normal morphology in human semen
    • 15705629 1:CAS:528:DC%2BD2MXis1yjtLw%3D 10.1093/humrep/deh678
    • Muratori M, Marchiani S, Forti G, Baldi E (2005) Sperm ubiquitination positively correlates to normal morphology in human semen. Hum Reprod 20(4):1035-1043
    • (2005) Hum Reprod , vol.20 , Issue.4 , pp. 1035-1043
    • Muratori, M.1    Marchiani, S.2    Forti, G.3    Baldi, E.4
  • 137
    • 39749139563 scopus 로고    scopus 로고
    • Regulation of turnover of tumor suppressor p53 and cell growth by E6-AP, a ubiquitin protein ligase mutated in Angelman mental retardation syndrome
    • 18193166 1:CAS:528:DC%2BD1cXjtVylurs%3D 10.1007/s00018-007-7476-1
    • Mishra A, Jana NR (2008) Regulation of turnover of tumor suppressor p53 and cell growth by E6-AP, a ubiquitin protein ligase mutated in Angelman mental retardation syndrome. Cell Mol Life Sci 65(4):656-666
    • (2008) Cell Mol Life Sci , vol.65 , Issue.4 , pp. 656-666
    • Mishra, A.1    Jana, N.R.2
  • 138
    • 85028121020 scopus 로고    scopus 로고
    • Role of the ubiquitin ligase Fbw7 in cancer progression
    • 10.1007/s10555-011-9330-z
    • Cheng Y, Li G (2011) Role of the ubiquitin ligase Fbw7 in cancer progression. Cancer Metastasis Rev. doi: 10.1007/s10555-011-9330-z
    • (2011) Cancer Metastasis Rev
    • Cheng, Y.1    Li, G.2
  • 139
    • 0020961333 scopus 로고
    • Cyclin: A protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division
    • 6134587 1:CAS:528:DyaL3sXksFSlurs%3D 10.1016/0092-8674(83)90420-8
    • Evans T, Rosenthal ET, Youngblom J, Distel D, Hunt T (1983) Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell 33:389-396
    • (1983) Cell , vol.33 , pp. 389-396
    • Evans, T.1    Rosenthal, E.T.2    Youngblom, J.3    Distel, D.4    Hunt, T.5
  • 140
    • 38549086019 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase: A tumour suppressor at the crossroads of cell division, growth and differentiation
    • 18094723 1:CAS:528:DC%2BD1cXhtVGhs7Y%3D 10.1038/nrc2290
    • Welcker M, Clurman BE (2008) FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation. Nat Rev Cancer 8:83-93
    • (2008) Nat Rev Cancer , vol.8 , pp. 83-93
    • Welcker, M.1    Clurman, B.E.2
  • 141
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cell-cycle control and cancer
    • 16633365 1:CAS:528:DC%2BD28XjslGitb4%3D 10.1038/nrc1881
    • Nakayama KI, Nakayama K (2006) Ubiquitin ligases: cell-cycle control and cancer. Nat Rev Cancer 6:369-381
    • (2006) Nat Rev Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 142
    • 1342275412 scopus 로고    scopus 로고
    • The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling
    • 14739463 1:CAS:528:DC%2BD2cXhsFyrtb8%3D 10.1126/science.1092880
    • Nateri AS, Riera-Sans L, Da Costa C, Behrens A (2004) The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling. Science 303:1374-1378
    • (2004) Science , vol.303 , pp. 1374-1378
    • Nateri, A.S.1    Riera-Sans, L.2    Da Costa, C.3    Behrens, A.4
  • 143
    • 0035812709 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitination of cyclin e by the SCFFbw7 ubiquitin ligase
    • 11533444 1:CAS:528:DC%2BD3MXnsFyit7c%3D 10.1126/science.1065203
    • Koepp DM, Schaefer LK, Ye X, Keyomarsi K, Chu C, Harper JW, Elledge SJ (2001) Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 294:173-177
    • (2001) Science , vol.294 , pp. 173-177
    • Koepp, D.M.1    Schaefer, L.K.2    Ye, X.3    Keyomarsi, K.4    Chu, C.5    Harper, J.W.6    Elledge, S.J.7
  • 144
    • 2942650133 scopus 로고    scopus 로고
    • The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation
    • 15150404 1:CAS:528:DC%2BD2cXltlWqsbo%3D 10.1073/pnas.0402770101
    • Welcker M, Orian A, Jin J, Grim JE, Harper JW, Eisenman RN, Clurman BE (2004) The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc Natl Acad Sci USA 101:9085-9090
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9085-9090
    • Welcker, M.1    Orian, A.2    Jin, J.3    Grim, J.E.4    Harper, J.W.5    Eisenman, R.N.6    Clurman, B.E.7
  • 145
    • 22244476115 scopus 로고    scopus 로고
    • The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase
    • 16023596 1:CAS:528:DC%2BD2MXntVejs70%3D 10.1016/j.ccr.2005.06.005
    • Wei W, Jin J, Schlisio S, Harper JW, Kaelin WG Jr (2005) The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase. Cancer Cell 8:25-33
    • (2005) Cancer Cell , vol.8 , pp. 25-33
    • Wei, W.1    Jin, J.2    Schlisio, S.3    Harper, J.W.4    Kaelin, Jr.W.G.5
  • 146
    • 54049087334 scopus 로고    scopus 로고
    • Notch-dependent cell cycle arrest and apoptosis in mouse embryonic fibroblasts lacking Fbxw7
    • 18641686 1:CAS:528:DC%2BD1cXht1Cms7rP 10.1038/onc.2008.216
    • Ishikawa Y, Onoyama I, Nakayama KI, Nakayama K (2008) Notch-dependent cell cycle arrest and apoptosis in mouse embryonic fibroblasts lacking Fbxw7. Oncogene 27:6164-6174
    • (2008) Oncogene , vol.27 , pp. 6164-6174
    • Ishikawa, Y.1    Onoyama, I.2    Nakayama, K.I.3    Nakayama, K.4
  • 147
    • 77953158826 scopus 로고    scopus 로고
    • The Fbw7 tumor suppressor targets KLF5 for ubiquitin-mediated degradation and suppresses breast cell proliferation
    • 20484041 1:CAS:528:DC%2BC3cXmslWgtbk%3D 10.1158/0008-5472.CAN-10-0040
    • Zhao D, Zheng HQ, Zhou Z, Chen C (2010) The Fbw7 tumor suppressor targets KLF5 for ubiquitin-mediated degradation and suppresses breast cell proliferation. Cancer Res 70:4728-4738
    • (2010) Cancer Res , vol.70 , pp. 4728-4738
    • Zhao, D.1    Zheng, H.Q.2    Zhou, Z.3    Chen, C.4
  • 148
    • 0034624678 scopus 로고    scopus 로고
    • Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
    • 10723139 1:CAS:528:DC%2BD3cXit1ygtbs%3D 10.1038/sj.onc.1203464
    • Honda R, Yasuda H (2000) Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 19:1473-1476
    • (2000) Oncogene , vol.19 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 149
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • 9450543 1:CAS:528:DyaK2sXotVyjtrg%3D 10.1016/S0014-5793(97)01480-4
    • Honda R, Tanaka H, Yasuda H (1997) Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 420:25-27
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 150
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • 9153395 1:CAS:528:DyaK2sXjtlSgtL8%3D 10.1038/387296a0
    • Haupt Y, Maya R, Kazaz A, Oren M (1997) Mdm2 promotes the rapid degradation of p53. Nature 387:296-299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 151
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • 9039259 1:CAS:528:DyaK2sXhtFahtLg%3D 10.1016/S0092-8674(00)81871-1
    • Levine AJ (1997) p53, the cellular gatekeeper for growth and division. Cell 88:323-331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 152
    • 23044506681 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and its role in cancer
    • 16034054 1:CAS:528:DC%2BD2MXotFars7o%3D 10.1200/JCO.2005.05.081
    • Mani A, Gelmann EP (2005) The ubiquitin-proteasome pathway and its role in cancer. J Clin Oncol 23(21):4776-4789
    • (2005) J Clin Oncol , vol.23 , Issue.21 , pp. 4776-4789
    • Mani, A.1    Gelmann, E.P.2
  • 153
    • 84856032790 scopus 로고    scopus 로고
    • Histone H2B ubiquitin ligases RNF20 and RNF40 in androgen signaling and prostate cancer cell growth
    • 22155569 10.1016/j.mce.2011.11.025 1:CAS:528:DC%2BC38XhtFajsrw%3D
    • Jääskeläinen T, Makkonen H, Visakorpi T, Kim J, Roeder RG, Palvimo JJ (2012) Histone H2B ubiquitin ligases RNF20 and RNF40 in androgen signaling and prostate cancer cell growth. Mol Cell Endocrinol 350(1):87-98
    • (2012) Mol Cell Endocrinol , vol.350 , Issue.1 , pp. 87-98
    • Jääskeläinen, T.1    Makkonen, H.2    Visakorpi, T.3    Kim, J.4    Roeder, R.G.5    Palvimo, J.J.6
  • 155
    • 84862805404 scopus 로고    scopus 로고
    • The ubiquitin E3 ligase WWP1 increases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis
    • 22266093 1:CAS:528:DC%2BC38Xjs1yhsrY%3D 10.1016/j.bone.2011.12.022
    • Subik K, Shu L, Wu C, Liang Q, Hicks D, Boyce B, Schiffhauer L, Chen D, Chen C, Tang P, Xing L (2012) The ubiquitin E3 ligase WWP1 increases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis. Bone 50(4):813-823
    • (2012) Bone , vol.50 , Issue.4 , pp. 813-823
    • Subik, K.1    Shu, L.2    Wu, C.3    Liang, Q.4    Hicks, D.5    Boyce, B.6    Schiffhauer, L.7    Chen, D.8    Chen, C.9    Tang, P.10    Xing, L.11
  • 156
    • 4644312604 scopus 로고    scopus 로고
    • Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)
    • 15221015 1:CAS:528:DC%2BD2cXnsFait7w%3D 10.1038/sj.onc.1207885
    • Komuro A, Imamura T, Saitoh M, Yoshida Y, Yamori T, Miyazono K, Miyazawa K (2004) Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1). Oncogene 23(41):6914-6923
    • (2004) Oncogene , vol.23 , Issue.41 , pp. 6914-6923
    • Komuro, A.1    Imamura, T.2    Saitoh, M.3    Yoshida, Y.4    Yamori, T.5    Miyazono, K.6    Miyazawa, K.7
  • 157
    • 29244464672 scopus 로고    scopus 로고
    • Human Kruppel-like factor 5 is a target of the E3 ubiquitin ligase WWP1 for proteolysis in epithelial cells
    • 16223724 1:CAS:528:DC%2BD2MXhtlShsbjN 10.1074/jbc.M506183200
    • Chen C, Sun X, Guo P, Dong XY, Sethi P, Cheng X, Zhou J, Ling J, Simons JW, Lingrel JB, Dong JT (2005) Human Kruppel-like factor 5 is a target of the E3 ubiquitin ligase WWP1 for proteolysis in epithelial cells. J Biol Chem 280(50):41553-41561
    • (2005) J Biol Chem , vol.280 , Issue.50 , pp. 41553-41561
    • Chen, C.1    Sun, X.2    Guo, P.3    Dong, X.Y.4    Sethi, P.5    Cheng, X.6    Zhou, J.7    Ling, J.8    Simons, J.W.9    Lingrel, J.B.10    Dong, J.T.11
  • 159
    • 79956366646 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy
    • 21484190 10.1007/s12079-011-0121-7
    • Crawford LJ, Walker B, Irvine AE (2011) Proteasome inhibitors in cancer therapy. J Cell Commun Signal 5(2):101-110
    • (2011) J Cell Commun Signal , vol.5 , Issue.2 , pp. 101-110
    • Crawford, L.J.1    Walker, B.2    Irvine, A.E.3
  • 160
    • 0029898412 scopus 로고    scopus 로고
    • A novel rat homolog of the Saccharomyces cerevisiae ubiquitin-conjugating enzymes UBC4 and UBC5 with distinct biochemical features is induced during spermatogenesis
    • 8754804 1:CAS:528:DyaK28XksValtr0%3D
    • Wing SS, Bédard N, Morales C, Hingamp P, Trasler J (1996) A novel rat homolog of the Saccharomyces cerevisiae ubiquitin-conjugating enzymes UBC4 and UBC5 with distinct biochemical features is induced during spermatogenesis. Mol Cell Biol 16(8):4064-4072
    • (1996) Mol Cell Biol , vol.16 , Issue.8 , pp. 4064-4072
    • Wing, S.S.1    Bédard, N.2    Morales, C.3    Hingamp, P.4    Trasler, J.5
  • 161
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • 15989956 1:CAS:528:DC%2BD2MXmtF2ntr8%3D 10.1016/j.cell.2005.03.037
    • Chen D, Kon N, Li M, Zhang W, Qin J, Gu W (2005) ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 121(7):1071-1083
    • (2005) Cell , vol.121 , Issue.7 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5    Gu, W.6
  • 163
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • 10.1016/j.cell.2005.06.009 1:CAS:528:DC%2BD2MXmtF2ntrw%3D
    • Zhong Q, Gao W, Du F, Wang X (2005) Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 12(7):1085-1095
    • (2005) Cell , vol.12 , Issue.7 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4


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