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Volumn 2014, Issue , 2014, Pages

Molecular chaperones, cochaperones, and ubiquitination/deubiquitination system: Involvement in the production of high quality spermatozoa

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DEUBIQUITINASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; MSJ 1 PROTEIN; PROTEIN DNAJ; UBIQUITIN SPECIFIC PROCESSING PROTEASE GAMMA; UNCLASSIFIED DRUG; DNAJB6 PROTEIN, HUMAN; ESCRT PROTEIN; NERVE PROTEIN; PROTEINASE; UBIQUITIN THIOLESTERASE; USP8 PROTEIN, HUMAN;

EID: 84904114928     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2014/561426     Document Type: Review
Times cited : (32)

References (113)
  • 2
    • 79960557909 scopus 로고    scopus 로고
    • Sperm flagella: Comparative and phylogenetic perspectives of protein components
    • 2-s2.0-79960557909 10.1093/molehr/gar034
    • Inaba K., Sperm flagella: comparative and phylogenetic perspectives of protein components. Molecular Human Reproduction 2011 17 8 524 538 2-s2.0-79960557909 10.1093/molehr/gar034
    • (2011) Molecular Human Reproduction , vol.17 , Issue.8 , pp. 524-538
    • Inaba, K.1
  • 3
    • 0036023086 scopus 로고    scopus 로고
    • Evolutionary aspects of cellular communication in the vertebrate hypothalamo-hypophysio-gonadal axis
    • DOI 10.1016/S0074-7696(02)18012-0
    • Pierantoni R., Cobellis G., Meccariello R., Fasano S., Evolutionary aspects of cellular communication in the vertebrate hypothalamo-hypophysio- gonadal axis. International Review of Cytology 2002 218 69 141 2-s2.0-0036023086 10.1016/S0074-7696(02)18012-0 (Pubitemid 34863239)
    • (2002) International Review of Cytology , vol.218 , pp. 69-141
    • Pierantoni, R.1    Cobellis, G.2    Meccariello, R.3    Fasano, S.4
  • 4
    • 0344851636 scopus 로고    scopus 로고
    • Intratesticular signals for progression of germ cell stages in vertebrates
    • DOI 10.1016/S0016-6480(03)00281-8
    • Cobellis G., Meccariello R., Pierantoni R., Fasano S., Intratesticular signals for progression of germ cell stages in vertebrates. General and Comparative Endocrinology 2003 134 3 220 228 2-s2.0-0344851636 10.1016/S0016-6480(03)00281-8 (Pubitemid 37443477)
    • (2003) General and Comparative Endocrinology , vol.134 , Issue.3 , pp. 220-228
    • Cobellis, G.1    Meccariello, R.2    Pierantoni, R.3    Fasano, S.4
  • 6
    • 84904103061 scopus 로고    scopus 로고
    • Intratesticular signals regulate germ cell progression and production of qualitatively mature spermatozoa in vertebrates
    • article 69 10.3389/fendo.2014.00069
    • Meccariello R., Chianese R., Chioccarelli T., Ciaramella V., Fasano S., Pierantoni R., Cobellis G., Intratesticular signals regulate germ cell progression and production of qualitatively mature spermatozoa in vertebrates. Frontiers in Endocrinology 2014 5 article 69 10.3389/fendo.2014.00069
    • (2014) Frontiers in Endocrinology , vol.5
    • Meccariello, R.1    Chianese, R.2    Chioccarelli, T.3    Ciaramella, V.4    Fasano, S.5    Pierantoni, R.6    Cobellis, G.7
  • 7
    • 0033064556 scopus 로고    scopus 로고
    • Role of heat shock protein HSP70-2 in spermatogenesis
    • DOI 10.1530/ror.0.0040023
    • Eddy E. M., Role of heat shock protein HSP70-2 in spermatogenesis. Reviews of Reproduction 1999 4 1 23 30 2-s2.0-0033064556 10.1530/ror.0.0040023 (Pubitemid 29078541)
    • (1999) Reviews of Reproduction , vol.4 , Issue.1 , pp. 23-30
    • Eddy, E.M.1
  • 8
    • 84878404112 scopus 로고    scopus 로고
    • New insights to the ubiquitin-proteasome pathway (UPP) mechanism during spermatogenesis
    • 2-s2.0-84878404112 10.1007/s11033-012-2397-y
    • Hou C.-C., Yang W.-X., New insights to the ubiquitin-proteasome pathway (UPP) mechanism during spermatogenesis. Molecular Biology Reports 2013 40 4 3213 3220 2-s2.0-84878404112 10.1007/s11033-012-2397-y
    • (2013) Molecular Biology Reports , vol.40 , Issue.4 , pp. 3213-3220
    • Hou, C.-C.1    Yang, W.-X.2
  • 9
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • 2-s2.0-0027333423
    • Georgopoulos C., Welch W. J., Role of the major heat shock proteins as molecular chaperones. Annual Review of Cell Biology 1993 9 601 634 2-s2.0-0027333423
    • (1993) Annual Review of Cell Biology , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 10
    • 0029741321 scopus 로고    scopus 로고
    • Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40
    • DOI 10.1074/jbc.271.32.19617
    • Minami Y., Höhfeld J., Ohtsuka K., Hartl F.-U., Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. Journal of Biological Chemistry 1996 271 32 19617 19624 2-s2.0-0029741321 10.1074/jbc.271.32.19617 (Pubitemid 26271642)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.32 , pp. 19617-19624
    • Minami, Y.1    Hohfeld, J.2    Ohtsuka, K.3    Hartl, F.-U.4
  • 11
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • DOI 10.1016/0968-0004(94)90281-X
    • Cyr D. M., Langer T., Douglas M. G., DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends in Biochemical Sciences 1994 19 4 176 181 2-s2.0-0028353336 10.1016/0968-0004(94)90281-X (Pubitemid 24115434)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.4 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 12
    • 33751265748 scopus 로고    scopus 로고
    • The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
    • DOI 10.1007/s00018-006-6192-6
    • Qiu X.-B., Shao Y.-M., Miao S., Wang L., The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cellular and Molecular Life Sciences 2006 63 22 2560 2570 2-s2.0-33751265748 10.1007/s00018-006-6192-6 (Pubitemid 44800711)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.22 , pp. 2560-2570
    • Qiu, X.-B.1    Shao, Y.-M.2    Miao, S.3    Wang, L.4
  • 14
    • 84904105686 scopus 로고    scopus 로고
    • Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function
    • Bishop O. T., Edkins A. L., Blatch G. L., Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function. Journal of Experimental Zoology 2013 9999 1 20
    • (2013) Journal of Experimental Zoology , vol.9999 , pp. 1-20
    • Bishop, O.T.1    Edkins, A.L.2    Blatch, G.L.3
  • 15
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • DOI 10.1038/nature02264
    • Selkoe D. J., Folding proteins in fatal ways. Nature 2003 426 6968 900 904 2-s2.0-0347987853 10.1038/nature02264 (Pubitemid 38056883)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 16
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • DOI 10.1038/nrn1587
    • Muchowski P. J., Wacker J. L., Modulation of neurodegeneration by molecular chaperones. Nature Reviews Neuroscience 2005 6 1 11 22 2-s2.0-11144243412 10.1038/nrn1587 (Pubitemid 40052135)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.1 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 17
    • 33746020449 scopus 로고    scopus 로고
    • Oligozoospermia and heat-shock protein expression in ejaculated spermatozoa
    • DOI 10.1093/humrep/del055
    • Cedenho A. P., Lima S. B., Cenedeze M. A., Spaine D. M., Ortiz V., Oehninger S., Oligozoospermia and heat-shock protein expression in ejaculated spermatozoa. Human Reproduction 2006 21 7 1791 1794 2-s2.0-33746020449 10.1093/humrep/del055 (Pubitemid 44063239)
    • (2006) Human Reproduction , vol.21 , Issue.7 , pp. 1791-1794
    • Cedenho, A.P.1    Lima, S.B.2    Cenedeze, M.A.3    Spaine, D.M.4    Ortiz, V.5    Oehninger, S.6
  • 18
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • DOI 10.1038/sj.emboj.7600808, PII 7600808
    • Haglund K., Dikic I., Ubiquitylation and cell signaling. EMBO Journal 2005 24 19 3353 3359 2-s2.0-27144529182 10.1038/sj.emboj.7600808 (Pubitemid 41486773)
    • (2005) EMBO Journal , vol.24 , Issue.19 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 19
    • 0016798328 scopus 로고
    • The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells
    • 2-s2.0-0016798328
    • Schlesinger D. H., Goldstein G., Niall H. D., The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells. Biochemistry 1975 14 10 2214 2218 2-s2.0-0016798328
    • (1975) Biochemistry , vol.14 , Issue.10 , pp. 2214-2218
    • Schlesinger, D.H.1    Goldstein, G.2    Niall, H.D.3
  • 20
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • DOI 10.1146/annurev.biochem.67.1.425
    • Hershko A., Ciechanover A., The ubiquitin system. Annual Review of Biochemistry 1998 67 425 479 2-s2.0-0031657807 10.1146/annurev.biochem.67.1.425 (Pubitemid 28411135)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 21
    • 33750302074 scopus 로고    scopus 로고
    • Endocytosis: The DUB version
    • DOI 10.1016/j.tcb.2006.09.002, PII S0962892406002388
    • Clague M. J., Urbé S., Endocytosis: the DUB version. Trends in Cell Biology 2006 16 11 551 559 2-s2.0-33750302074 10.1016/j.tcb.2006.09.002 (Pubitemid 44636216)
    • (2006) Trends in Cell Biology , vol.16 , Issue.11 , pp. 551-559
    • Clague, M.J.1    Urbe, S.2
  • 22
    • 0035139841 scopus 로고    scopus 로고
    • The possible biological and reproductive functions of ubiquitin
    • DOI 10.1093/humupd/7.1.102
    • Bebington C., Doherty F. J., Fleming S. D., The possible biological and reproductive functions of ubiquitin. Human Reproduction Update 2001 7 1 102 111 2-s2.0-0035139841 10.1093/humupd/7.1.102 (Pubitemid 32111976)
    • (2001) Human Reproduction Update , vol.7 , Issue.1 , pp. 102-111
    • Bebington, C.1    Doherty, F.J.2    Fleming, S.D.3
  • 23
    • 0037405064 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: Killing three birds with one stone
    • DOI 10.1002/jemt.10319
    • Sutovsky P., Ubiquitin-dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: killing three birds with one stone. Microscopy Research and Technique 2003 61 1 88 102 2-s2.0-0037405064 10.1002/jemt.10319 (Pubitemid 36469238)
    • (2003) Microscopy Research and Technique , vol.61 , Issue.1 , pp. 88-102
    • Sutovsky, P.1
  • 25
    • 84863477544 scopus 로고    scopus 로고
    • The role of molecular chaperones in spermatogenesis and the post-testicular maturation of mammalian spermatozoa
    • 2-s2.0-84863477544 10.1093/humupd/dms009
    • Dun M. D., Aitken R. J., Nixon B., The role of molecular chaperones in spermatogenesis and the post-testicular maturation of mammalian spermatozoa. Human Reproduction Update 2012 18 4 420 435 2-s2.0-84863477544 10.1093/humupd/dms009
    • (2012) Human Reproduction Update , vol.18 , Issue.4 , pp. 420-435
    • Dun, M.D.1    Aitken, R.J.2    Nixon, B.3
  • 26
    • 31544467573 scopus 로고    scopus 로고
    • The Hsp60C gene in the 25F cytogenetic region in Drosophila melanogaster is essential for tracheal development and fertility
    • Sarkar S., Lakhotia S. C., The Hsp60C gene in the 25F cytogenetic region in Drosophila melanogaster is essential for tracheal development and fertility. Journal of Genetics 2005 84 3 265 281 2-s2.0-31544467573 10.1007/BF02715797 (Pubitemid 43161525)
    • (2005) Journal of Genetics , vol.84 , Issue.3 , pp. 265-281
    • Sarkar, S.1    Lakhotia, S.C.2
  • 27
    • 0035067292 scopus 로고    scopus 로고
    • The hsp60B gene of Drosophila melanogaster is essential for the spermatid individualization process
    • DOI 10.1379/1466-1268(2001)006<0071:THGODM>2.0.CO;2
    • Timakov B., Zhang P., The hsp60B gene of Drosophila melanogaster is essential for the spermatid individualization process. Cell Stress Chaperones 2001 6 1 71 77 (Pubitemid 32275331)
    • (2001) Cell Stress and Chaperones , vol.6 , Issue.1 , pp. 71-77
    • Timakov, B.1    Zhang, P.2
  • 28
    • 84155180911 scopus 로고    scopus 로고
    • Corrigendum to 'Characterization of heat shock protein 70 in the red claw crayfish (Cherax quadricarinatus): Evidence for its role in regulating spermatogenesis'
    • 2-s2.0-84861788265 10.1016/j.gene.2012.04.034
    • Fang D.-A., Wang Q., He L., Wang J., Wang Y., Corrigendum to 'Characterization of heat shock protein 70 in the red claw crayfish (Cherax quadricarinatus): evidence for its role in regulating spermatogenesis'. Gene 2012 492 1 138 147 2-s2.0-84861788265 10.1016/j.gene.2012.04.034
    • (2012) Gene , vol.492 , Issue.1 , pp. 138-147
    • Fang, D.-A.1    Wang, Q.2    He, L.3    Wang, J.4    Wang, Y.5
  • 29
    • 84875623999 scopus 로고    scopus 로고
    • Role of HSP70 in the regulation of the testicular apoptosis in a seasonal breeding teleost Prochilodus argenteus from the São Francisco river, Brazil
    • 2-s2.0-84875623999 10.1002/jemt.22173
    • Domingos F. F. T., Thomé R. G., Martinelli P. M., Sato Y., Bazzoli N., Rizzo E., Role of HSP70 in the regulation of the testicular apoptosis in a seasonal breeding teleost Prochilodus argenteus from the São Francisco river, Brazil. Microscopy Research and Technique 2013 76 4 350 356 2-s2.0-84875623999 10.1002/jemt.22173
    • (2013) Microscopy Research and Technique , vol.76 , Issue.4 , pp. 350-356
    • Domingos, F.F.T.1    Thomé, R.G.2    Martinelli, P.M.3    Sato, Y.4    Bazzoli, N.5    Rizzo, E.6
  • 30
    • 33748785716 scopus 로고    scopus 로고
    • HSP90β is involved in signaling prolactin-induced apoptosis in newt testis
    • DOI 10.1016/j.bbrc.2006.08.143, PII S0006291X0601922X
    • Saribek B., Jin Y., Saigo M., Eto K., Abe S.-I., HSP90 β is involved in signaling prolactin-induced apoptosis in newt testis. Biochemical and Biophysical Research Communications 2006 349 4 1190 1197 2-s2.0-33748785716 10.1016/j.bbrc.2006.08.143 (Pubitemid 44416387)
    • (2006) Biochemical and Biophysical Research Communications , vol.349 , Issue.4 , pp. 1190-1197
    • Saribek, B.1    Jin, Y.2    Saigo, M.3    Eto, K.4    Abe, S.-i.5
  • 31
    • 84878658224 scopus 로고    scopus 로고
    • Identification of a testis-enriched heat shock protein and fourteen members of Hsp70 family in the swamp Eel
    • 2-s2.0-84878658224 10.1371/journal.pone.0065269 e65269
    • He Y., Luo M., Yi M., Sheng Y., Cheng Y., Zhou R., Cheng H., Identification of a testis-enriched heat shock protein and fourteen members of Hsp70 family in the swamp Eel. PLoS ONE 2013 8 6 2-s2.0-84878658224 10.1371/journal.pone.0065269 e65269
    • (2013) PLoS ONE , vol.8 , Issue.6
    • He, Y.1    Luo, M.2    Yi, M.3    Sheng, Y.4    Cheng, Y.5    Zhou, R.6    Cheng, H.7
  • 32
    • 0023959196 scopus 로고
    • A novel hsp70-like protein (P70) is present in mouse spermatogenic cells
    • 2-s2.0-0023959196
    • Allen R. L., O'Brien D. A., Eddy E. M., A novel hsp70-like protein (P70) is present in mouse spermatogenic cells. Molecular and Cellular Biology 1988 8 2 828 832 2-s2.0-0023959196
    • (1988) Molecular and Cellular Biology , vol.8 , Issue.2 , pp. 828-832
    • Allen, R.L.1    O'Brien, D.A.2    Eddy, E.M.3
  • 33
    • 0025058935 scopus 로고
    • Cloning of a hsp70-related gene expressed in mouse spermatids
    • DOI 10.1016/0006-291X(90)91909-C
    • Matsumoto M., Fujimoto H., Cloning of a hsp70-related gene expressed in mouse spermatids. Biochemical and Biophysical Research Communications 1990 166 1 43 49 2-s2.0-0025058935 10.1016/0006-291X(90)91909-C (Pubitemid 20040150)
    • (1990) Biochemical and Biophysical Research Communications , vol.166 , Issue.1 , pp. 43-49
    • Matsumoto, M.1    Fujimoto, H.2
  • 34
    • 0030721027 scopus 로고    scopus 로고
    • HSP70-2 is required for desynapsis of synaptonemal complexes during meiotic prophase in juvenile and adult mouse spermatocytes
    • Dix D. J., Allen J. W., Collins B. W., Poorman-Allen P., Mori C., Blizard D. R., Brown P. R., Goulding E. H., Strong B. D., Eddy E. M., HSP70-2 is required for desynapsis of synaptonemal complexes during meiotic prophase in juvenile and adult mouse spermatocytes. Development 1997 124 22 4595 4603 2-s2.0-0030721027 (Pubitemid 27519254)
    • (1997) Development , vol.124 , Issue.22 , pp. 4595-4603
    • Dix, D.J.1    Allen, J.W.2    Collins, B.W.3    Poorman-Allen, P.4    Mori, C.5    Blizard, D.R.6    Brown, P.R.7    Goulding, E.H.8    Strong, B.D.9    Eddy, E.M.10
  • 35
    • 65249185665 scopus 로고    scopus 로고
    • Diminished reproductive potential of male mice in response to selenium-induced oxidative stress: Involvement of HSP70, HSP70-2, and MSJ-1
    • 2-s2.0-65249185665 10.1002/jbt.20276
    • Kaushal N., Bansal M. P., Diminished reproductive potential of male mice in response to selenium-induced oxidative stress: involvement of HSP70, HSP70-2, and MSJ-1. Journal of Biochemical and Molecular Toxicology 2009 23 2 125 136 2-s2.0-65249185665 10.1002/jbt.20276
    • (2009) Journal of Biochemical and Molecular Toxicology , vol.23 , Issue.2 , pp. 125-136
    • Kaushal, N.1    Bansal, M.P.2
  • 37
    • 84870562813 scopus 로고    scopus 로고
    • The molecular chaperone HSPA2 plays a key role in regulating the expression of sperm surface receptors that mediate sperm-egg recognition
    • 2-s2.0-84870562813 10.1371/journal.pone.0050851 e50851
    • Redgrove K. A., Nixon B., Baker M. A., Hetherington L., Baker G., Liu D.-Y., Aitken R. J., The molecular chaperone HSPA2 plays a key role in regulating the expression of sperm surface receptors that mediate sperm-egg recognition. PLoS ONE 2012 7 11 2-s2.0-84870562813 10.1371/journal.pone.0050851 e50851
    • (2012) PLoS ONE , vol.7 , Issue.11
    • Redgrove, K.A.1    Nixon, B.2    Baker, M.A.3    Hetherington, L.4    Baker, G.5    Liu, D.-Y.6    Aitken, R.J.7
  • 38
    • 74349083062 scopus 로고    scopus 로고
    • Localization of Hsp60 and Grp78 in the human testis, epididymis and mature spermatozoa
    • 2-s2.0-74349083062 10.1111/j.1365-2605.2008.00948.x
    • Lachance C., Fortier M., Thimon V., Sullivan R., Bailey J. L., Leclerc P., Localization of Hsp60 and Grp78 in the human testis, epididymis and mature spermatozoa. International Journal of Andrology 2010 33 1 33 44 2-s2.0-74349083062 10.1111/j.1365-2605.2008.00948.x
    • (2010) International Journal of Andrology , vol.33 , Issue.1 , pp. 33-44
    • Lachance, C.1    Fortier, M.2    Thimon, V.3    Sullivan, R.4    Bailey, J.L.5    Leclerc, P.6
  • 39
    • 48249091339 scopus 로고    scopus 로고
    • Comparative immunolocalization of heat shock proteins (Hsp)-60, -70, -90 in boar, stallion, dog and cat spermatozoa
    • 2-s2.0-48249091339 10.1111/j.1439-0531.2007.00918.x
    • Volpe S., Galeati G., Bernardini C., Tamanini C., Mari G., Zambelli D., Seren E., Spinaci M., Comparative immunolocalization of heat shock proteins (Hsp)-60, -70, -90 in boar, stallion, dog and cat spermatozoa. Reproduction in Domestic Animals 2008 43 4 385 392 2-s2.0-48249091339 10.1111/j.1439-0531.2007. 00918.x
    • (2008) Reproduction in Domestic Animals , vol.43 , Issue.4 , pp. 385-392
    • Volpe, S.1    Galeati, G.2    Bernardini, C.3    Tamanini, C.4    Mari, G.5    Zambelli, D.6    Seren, E.7    Spinaci, M.8
  • 40
    • 79958254987 scopus 로고    scopus 로고
    • Developmental expression of heat shock proteins 60, 70, 90, and A2 in rabbit testis
    • 2-s2.0-79958254987 10.1007/s00441-011-1151-4
    • Wu Y., Pei Y., Qin Y., Developmental expression of heat shock proteins 60, 70, 90, and A2 in rabbit testis. Cell and Tissue Research 2011 344 2 355 363 2-s2.0-79958254987 10.1007/s00441-011-1151-4
    • (2011) Cell and Tissue Research , vol.344 , Issue.2 , pp. 355-363
    • Wu, Y.1    Pei, Y.2    Qin, Y.3
  • 41
    • 84878764864 scopus 로고    scopus 로고
    • Heat shock protein 90 functions to stabilize and activate the testis-specific serine/threonine kinases, a family of kinases essential for male fertility
    • 2-s2.0-84878764864 10.1074/jbc.M112.400978
    • Jha K. N., Coleman A. R., Wong L., Salicioni A. M., Howcroft E., Johnson G. R., Heat shock protein 90 functions to stabilize and activate the testis-specific serine/threonine kinases, a family of kinases essential for male fertility. Journal of Biological Chemistry 2013 288 23 16308 16320 2-s2.0-84878764864 10.1074/jbc.M112.400978
    • (2013) Journal of Biological Chemistry , vol.288 , Issue.23 , pp. 16308-16320
    • Jha, K.N.1    Coleman, A.R.2    Wong, L.3    Salicioni, A.M.4    Howcroft, E.5    Johnson, G.R.6
  • 42
    • 39049180198 scopus 로고    scopus 로고
    • Expression of androgen receptor and heat shock protein 90alpha in the testicular biopsy specimens of infertile patients with spermatogenic arrest
    • 2-s2.0-39049180198
    • Liu Z., Wang G., Pan Y., Zhu C., Expression of androgen receptor and heat shock protein 90alpha in the testicular biopsy specimens of infertile patients with spermatogenic arrest. Zhonghua Nan Ke Xue 2004 10 9 662 666 2-s2.0-39049180198
    • (2004) Zhonghua Nan Ke Xue , vol.10 , Issue.9 , pp. 662-666
    • Liu, Z.1    Wang, G.2    Pan, Y.3    Zhu, C.4
  • 43
    • 79251495443 scopus 로고    scopus 로고
    • The molecular chaperone hsp90a is required for meiotic progression of spermatocytes beyond pachytene in the mouse
    • 2-s2.0-79251495443 10.1371/journal.pone.0015770 e15770
    • Grad I., Cederroth C. R., Walicki J., Grey C., Barluenga S., Winssinger N., de Massy B., Nef S., Picard D., The molecular chaperone hsp90a is required for meiotic progression of spermatocytes beyond pachytene in the mouse. PLoS ONE 2010 5 12 2-s2.0-79251495443 10.1371/journal.pone.0015770 e15770
    • (2010) PLoS ONE , vol.5 , Issue.12
    • Grad, I.1    Cederroth, C.R.2    Walicki, J.3    Grey, C.4    Barluenga, S.5    Winssinger, N.6    De Massy, B.7    Nef, S.8    Picard, D.9
  • 44
    • 0030794618 scopus 로고    scopus 로고
    • Regulation of hsp expression during rodent spermatogenesis
    • DOI 10.1007/PL00000591
    • Sarge K. D., Cullen K. E., Regulation of hsp expression during rodent spermatogenesis. Cellular and Molecular Life Sciences 1997 53 2 191 197 2-s2.0-0030794618 10.1007/PL00000591 (Pubitemid 27365891)
    • (1997) Cellular and Molecular Life Sciences , vol.53 , Issue.2 , pp. 191-197
    • Sarge, K.D.1    Cullen, K.E.2
  • 45
    • 0038320258 scopus 로고    scopus 로고
    • Targeted disruption of the heat shock transcription factor (hsf)-2 gene results in increased embryonic lethality, neuronal defects, and reduced spermatogenesis
    • DOI 10.1002/gene.10200
    • Wang G., Zhang J., Moskophidis D., Mivechi N. F., Targeted disruption of the heat shock transcription factor (hsf)-2 gene results in increased embryonic lethality, neuronal defects, and reduced spermatogenesis. Genesis 2003 36 1 48 61 2-s2.0-0038320258 10.1002/gene.10200 (Pubitemid 36666238)
    • (2003) Genesis , vol.36 , Issue.1 , pp. 48-61
    • Wang, G.1    Zhang, J.2    Moskophidis, D.3    Mivechi, N.F.4
  • 46
    • 1542327630 scopus 로고    scopus 로고
    • Essential Requirement for Both hsf1 and hsf2 Transcriptional Activity in Spermatogenesis and Male Fertility
    • DOI 10.1002/gene.20005
    • Wang G., Ying Z., Jin X., Tu N., Zhang Y., Phillips M., Moskophidis D., Mivechi N. F., Essential requirement for both hsf1 and hsf2 transcriptional activity in spermatogenesis and male fertility. Genesis 2004 38 2 66 80 2-s2.0-1542327630 10.1002/gene.20005 (Pubitemid 38327894)
    • (2004) Genesis , vol.38 , Issue.2 , pp. 66-80
    • Wang, G.1    Ying, Z.2    Jin, X.3    Tu, N.4    Zhang, Y.5    Phillips, M.6    Moskophidis, D.7    Mivechi, N.F.8
  • 48
    • 34248231741 scopus 로고    scopus 로고
    • The new function of two ubiquitin C-terminal hydrolase isozymes as reciprocal modulators of germ cell apoptosis
    • DOI 10.1538/expanim.56.71
    • Kwon J., The new function of two ubiquitin C-terminal hydrolase isozymes as reciprocal modulators of germ cell apoptosis. Experimental Animals 2007 56 2 71 77 2-s2.0-34248231741 10.1538/expanim.56.71 (Pubitemid 46711790)
    • (2007) Experimental Animals , vol.56 , Issue.2 , pp. 71-77
    • Kwon, J.1
  • 52
    • 84877104355 scopus 로고    scopus 로고
    • MARCH7 E3 ubiquitin ligase is highly expressed in developing spermatids of rats and its possible involvement in head and tail formation
    • 2-s2.0-84877104355 10.1007/s00418-012-1043-z
    • Zhao B., Ito K., Iyengar P. V., Hirose S., Nakamura N., MARCH7 E3 ubiquitin ligase is highly expressed in developing spermatids of rats and its possible involvement in head and tail formation. Histochemistry and Cell Biology 2013 139 3 447 460 2-s2.0-84877104355 10.1007/s00418-012-1043-z
    • (2013) Histochemistry and Cell Biology , vol.139 , Issue.3 , pp. 447-460
    • Zhao, B.1    Ito, K.2    Iyengar, P.V.3    Hirose, S.4    Nakamura, N.5
  • 54
    • 0027293226 scopus 로고
    • Immunoreactive ubiquitin in human seminal plasma
    • Lippert T. H., Seeger H., Schieferstein G., Voelter W., Immunoreactive ubiquitin in human seminal plasma. Journal of Andrology 1993 14 2 130 131 2-s2.0-0027293226 (Pubitemid 23264408)
    • (1993) Journal of Andrology , vol.14 , Issue.2 , pp. 130-131
    • Lippert, T.H.1    Seeger, H.2    Schieferstein, G.3    Voelter, W.4
  • 55
    • 0035012044 scopus 로고    scopus 로고
    • A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis
    • Sutovsky P., Moreno R., Ramalho-Santos J., Dominko T., Thompson W. E., Schatten G., A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis. Journal of Cell Science 2001 114 9 1665 1675 2-s2.0-0035012044 (Pubitemid 32454665)
    • (2001) Journal of Cell Science , vol.114 , Issue.9 , pp. 1665-1675
    • Sutovsky, P.1    Moreno, R.2    Ramalho-Santos, J.3    Dominko, T.4    Thompson, W.E.5    Schatten, G.6
  • 56
    • 84869388997 scopus 로고    scopus 로고
    • Expression of the ubiquitin proteasome system in neonatal rat gonocytes and spermatogonia: Role in gonocyte differentiation1
    • 2-s2.0-84869388997 10.1095/biolreprod.112.099143
    • Manku G., Wing S. S., Culty M., Expression of the ubiquitin proteasome system in neonatal rat gonocytes and spermatogonia: role in gonocyte differentiation1. Biology of Reproduction 2012 87 2, article 44 2-s2.0-84869388997 10.1095/biolreprod.112.099143
    • (2012) Biology of Reproduction , vol.87 , Issue.2 ARTICLE 44
    • Manku, G.1    Wing, S.S.2    Culty, M.3
  • 57
    • 0036786058 scopus 로고    scopus 로고
    • Control of membrane fusion during spermiogenesis and the acrosome reaction
    • 2-s2.0-0036786058
    • Ramalho-Santos J., Schatten G., Moreno R. D., Control of membrane fusion during spermiogenesis and the acrosome reaction. Biology of Reproduction 2002 67 4 1043 1051 2-s2.0-0036786058
    • (2002) Biology of Reproduction , vol.67 , Issue.4 , pp. 1043-1051
    • Ramalho-Santos, J.1    Schatten, G.2    Moreno, R.D.3
  • 58
    • 0029809447 scopus 로고    scopus 로고
    • Oocyte penetration by fresh or stored diluted boar spermatozoa before and after in vitro capacitation treatments
    • Martinez E. A., Vazquez J. M., Matas C., Gadea J., Alonso M. I., Roca J., Oocyte penetration by fresh or stored diluted boar spermatozoa before and after in vitro capacitation treatments. Biology of Reproduction 1996 55 1 134 140 2-s2.0-0029809447 (Pubitemid 26293150)
    • (1996) Biology of Reproduction , vol.55 , Issue.1 , pp. 134-140
    • Martinez, E.A.1    Vazquez, J.M.2    Matas, C.3    Gadea, J.4    Alonso, M.I.5    Roca, J.6
  • 59
    • 0033944267 scopus 로고    scopus 로고
    • Vesicular traffic and Golgi apparatus dynamics during mammalian spermatogenesis: Implications for acrosome architecture
    • Moreno R. D., Ramalho-Santos J., Sutovsky P., Chan E. K. L., Schatten G., Vesicular traffic and Golgi apparatus dynamics during mammalian spermatogenesis: implications for acrosome architecture. Biology of Reproduction 2000 63 1 89 98 2-s2.0-0033944267 (Pubitemid 30429389)
    • (2000) Biology of Reproduction , vol.63 , Issue.1 , pp. 89-98
    • Moreno, R.D.1    Ramalho-Santos, J.2    Sutovsky, P.3    Chan, E.K.L.4    Schatten, G.5
  • 60
    • 33748852206 scopus 로고    scopus 로고
    • The mammalian acrosome as a secretory lysosome: New and old evidence
    • DOI 10.1002/mrd.20581
    • Moreno R. D., Alvarado C. P., The mammalian acrosome as a secretory lysosome: new and old evidence. Molecular Reproduction and Development 2006 73 11 1430 1434 2-s2.0-33748852206 10.1002/mrd.20581 (Pubitemid 44423732)
    • (2006) Molecular Reproduction and Development , vol.73 , Issue.11 , pp. 1430-1434
    • Moreno, R.D.1    Alvarado, C.P.2
  • 61
    • 0029816615 scopus 로고    scopus 로고
    • Brefeldin A and mannose 6-phosphate regulation of acrosomic related vesicular trafficking
    • West A. P., Willison K. R., Brefeldin A and mannose 6-phosphate regulation of acrosomic related vesicular trafficking. European Journal of Cell Biology 1996 70 4 315 321 2-s2.0-0029816615 (Pubitemid 26268234)
    • (1996) European Journal of Cell Biology , vol.70 , Issue.4 , pp. 315-321
    • West, A.P.1    Willison, K.R.2
  • 62
    • 0035398602 scopus 로고    scopus 로고
    • Membrane trafficking machinery components associated with the mammalian acrosome during spermiogenesis
    • DOI 10.1006/excr.2000.5119
    • Ramalho-Santos J., Moreno R. D., Wessel G. M., Chan E. K. L., Schatten G., Membrane trafficking machinery components associated with the mammalian acrosome during spermiogenesis. Experimental Cell Research 2001 267 1 45 60 2-s2.0-0035398602 10.1006/excr.2000.5119 (Pubitemid 32579140)
    • (2001) Experimental Cell Research , vol.267 , Issue.1 , pp. 45-60
    • Ramalho-Santos, J.1    Moreno, R.D.2    Wessel, G.M.3    Chan, E.K.L.4    Schatten, G.5
  • 63
    • 0034924081 scopus 로고    scopus 로고
    • MSJ-1, a mouse testis-specific DnaJ protein, is highly expressed in haploid male germ cells and interacts with the testis-specific heat shock protein Hsp70-2
    • Berruti G., Martegani E., MSJ-1, a mouse testis-specific DnaJ protein, is highly expressed in haploid male germ cells and interacts with the testis-specific heat shock protein Hsp70-2. Biology of Reproduction 2001 65 2 488 495 2-s2.0-0034924081 (Pubitemid 32702313)
    • (2001) Biology of Reproduction , vol.65 , Issue.2 , pp. 488-495
    • Berruti, G.1    Martegani, E.2
  • 65
    • 0031741426 scopus 로고    scopus 로고
    • Molecular cloning and developmental pattern of expression of MSJ-1, a new male germ cell-specific DNAJ homologue
    • Berruti G., Perego L., Martegani E., Molecular cloning and developmental pattern of expression of MSJ-1, a new male germ cell-specific DNAJ homologue. Advances in Experimental Medicine and Biology 1998 444 145 150 2-s2.0-0031741426 (Pubitemid 128700425)
    • (1998) Advances in Experimental Medicine and Biology , vol.444 , pp. 145-150
    • Berruti, G.1    Perego, L.2    Martegani, E.3
  • 66
    • 0036963485 scopus 로고    scopus 로고
    • MUBPy and MSJ-1, a deubiquitinating enzyme and a molecular chaperone specifically expressed in testis, associate with the acrosome and centrosome in mouse germ cells
    • Berruti G., Martegani E., mUBPy and MSJ-1, a deubiquitinating enzyme and a molecular chaperone specifically expressed in testis, associate with the acrosome and centrosome in mouse germ cells. Annals of the New York Academy of Sciences 2002 973 5 7 2-s2.0-0036963485 (Pubitemid 36124969)
    • (2002) Annals of the New York Academy of Sciences , vol.973 , pp. 5-7
    • Berruti, G.1    Martegani, E.2
  • 67
    • 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
    • DOI 10.1095/biolreprod.104.030866
    • Berruti G., Martegani E., 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. Biology of Reproduction 2005 72 1 14 21 2-s2.0-10944270585 10.1095/biolreprod.104.030866 (Pubitemid 40013749)
    • (2005) Biology of Reproduction , vol.72 , Issue.1 , pp. 14-21
    • Berruti, G.1    Martegani, E.2
  • 69
    • 0025873873 scopus 로고
    • Defect of sperm assembly in a neurological mutant of the mouse, wobbler (WR)
    • 2-s2.0-0025873873
    • Heimann P., Laage S., Jockusch H., Defect of sperm assembly in a neurological mutant of the mouse, wobbler (WR). Differentiation 1991 47 2 77 83 2-s2.0-0025873873
    • (1991) Differentiation , vol.47 , Issue.2 , pp. 77-83
    • Heimann, P.1    Laage, S.2    Jockusch, H.3
  • 71
    • 33745366486 scopus 로고    scopus 로고
    • Domains within the GARP subunit Vps54 confer separate functions in complex assembly and early endosome recognition
    • DOI 10.1091/mbc.E05-11-1002
    • Quenneville N. R., Chao T.-Y., McCaffery J. M., Conibear E., Domains within the GARP subunit Vps54 confer separate functions in complex assembly and early endosome recognition. Molecular Biology of the Cell 2006 17 4 1859 1870 2-s2.0-33745366486 10.1091/mbc.E05-11-1002 (Pubitemid 44011601)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1859-1870
    • Quenneville, N.R.1    Chao, T.-Y.2    McCaffery, J.M.3    Conibear, E.4
  • 72
    • 0016422334 scopus 로고
    • The fine structure of the cervical spinal cord, ventral root and brachial nerves in the wobbler (wr) mouse
    • 2-s2.0-0016422334
    • Andrews J. M., The fine structure of the cervical spinal cord, ventral root and brachial nerves in the wobbler (wr) mouse. Journal of Neuropathology and Experimental Neurology 1975 34 1 12 27 2-s2.0-0016422334
    • (1975) Journal of Neuropathology and Experimental Neurology , vol.34 , Issue.1 , pp. 12-27
    • Andrews, J.M.1
  • 73
    • 84897389268 scopus 로고    scopus 로고
    • Pathoproteomics of testicular tissue deficient in the GARP component VPS54: The wobbler mouse model of globozoospermia
    • Jockusch H., Holland A., Staunton L., Schmitt-John T., Heimann P., Dowling P., Ohlendieck K., Pathoproteomics of testicular tissue deficient in the GARP component VPS54: the wobbler mouse model of globozoospermia. Proteomics 2014 14 7-8 839 852
    • (2014) Proteomics , vol.14 , Issue.7-8 , pp. 839-852
    • Jockusch, H.1    Holland, A.2    Staunton, L.3    Schmitt-John, T.4    Heimann, P.5    Dowling, P.6    Ohlendieck, K.7
  • 74
    • 0037056001 scopus 로고    scopus 로고
    • Early defect in the expression of mouse sperm DNAJ 1, a member of the DNAJ/heat shock protein 40 chaperone protein family, in the spinal cord of the wobbler mouse, a murine model of motoneuronal degeneration
    • DOI 10.1016/S0306-4522(02)00235-X, PII S030645220200235X
    • Boillée S., Berruti G., Meccariello R., Grannec G., Razan F., Pierantoni R., Fasano S., Junier M. P., Early defect in the expression of mouse sperm DNAJ 1, a member of the DNAJ/heat shock protein 40 chaperone protein family, in the spinal cord of the wobbler mouse, a murine model of motoneuronal degeneration. Neuroscience 2002 113 4 825 835 2-s2.0-0037056001 10.1016/S0306-4522(02)00235-X (Pubitemid 35245252)
    • (2002) Neuroscience , vol.113 , Issue.4 , pp. 825-835
    • Boillee, S.1    Berruti, G.2    Meccariello, R.3    Grannec, G.4    Razan, F.5    Pierantoni, R.6    Fasano, S.7    Junier, M.P.8
  • 76
    • 2342640311 scopus 로고    scopus 로고
    • Detection of msj-1 Gene Expression in the Frog, Rana esculenta Testis, Brain, and Spinal Cord
    • DOI 10.1002/mrd.20066
    • Meccariello R., Cobellis G., Scarpa D., Fienga G., Pierantoni R., Fasano S., Detection of msj-1 gene expression in the frog, rana esculenta testis, brain, and spinal cord. Molecular Reproduction and Development 2004 68 2 149 158 2-s2.0-2342640311 10.1002/mrd.20066 (Pubitemid 38569243)
    • (2004) Molecular Reproduction and Development , vol.68 , Issue.2 , pp. 149-158
    • Meccariello, R.1    Cobellis, G.2    Scarpa, D.3    Fienga, G.4    Pierantoni, R.5    Fasano, S.6
  • 78
    • 0026746411 scopus 로고
    • Mapping of the mouse bilirubin UDP-glucuronosyltransferase gene (Gnt-1) to chromosome 1 by restriction fragment length variations
    • 2-s2.0-0026746411 10.1007/BF00569325
    • Sato H., Sakai Y., Koiwai O., Watanabe T., Mapping of the mouse bilirubin UDP-glucuronosyltransferase gene (Gnt-1) to chromosome 1 by restriction fragment length variations. Biochemical Genetics 1992 30 7-8 347 352 2-s2.0-0026746411 10.1007/BF00569325
    • (1992) Biochemical Genetics , vol.30 , Issue.7-8 , pp. 347-352
    • Sato, H.1    Sakai, Y.2    Koiwai, O.3    Watanabe, T.4
  • 79
    • 33646846293 scopus 로고    scopus 로고
    • The complexity of antisense transcription revealed by the study of developing male germ cells
    • DOI 10.1016/j.ygeno.2005.12.006, PII S0888754305003691
    • Chan W.-Y., Wu S.-M., Ruszczyk L., Law E., Lee T.-L., Baxendale V., Lap-Yin Pang A., Rennert O. M., The complexity of antisense transcription revealed by the study of developing male germ cells. Genomics 2006 87 6 681 692 2-s2.0-33646846293 10.1016/j.ygeno.2005.12.006 (Pubitemid 43776874)
    • (2006) Genomics , vol.87 , Issue.6 , pp. 681-692
    • Chan, W.-Y.1    Wu, S.-M.2    Ruszczyk, L.3    Law, E.4    Lee, T.-L.5    Baxendale, V.6    Lap-Yin Pang, A.7    Rennert, O.M.8
  • 80
    • 0035914321 scopus 로고    scopus 로고
    • Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the ras guanine nucleotide exchange factor CDC25 Mm/Ras-GRF1
    • 2-s2.0-0035914321 10.1074/jbc.M103454200
    • Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R., Sturani E., Borgonovo B., Berruti G., Martegani E., Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the ras guanine nucleotide exchange factor CDC25 Mm/Ras-GRF1. Journal of Biological Chemistry 2001 276 42 39448 39454 2-s2.0-0035914321 10.1074/jbc.M103454200
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.42 , pp. 39448-39454
    • Gnesutta, N.1    Ceriani, M.2    Innocenti, M.3    Mauri, I.4    Zippel, R.5    Sturani, E.6    Borgonovo, B.7    Berruti, G.8    Martegani, E.9
  • 81
    • 27644438783 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes
    • DOI 10.1091/mbc.E05-06-0560
    • Mizuno E., Iura T., Mukai A., Yoshimori T., Kitamura N., Komada M., Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes. Molecular Biology of the Cell 2005 16 11 5163 5174 2-s2.0-27644438783 10.1091/mbc.E05-06-0560 (Pubitemid 41566829)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.11 , pp. 5163-5174
    • Mizuno, E.1    Iura, T.2    Mukai, A.3    Yoshimori, T.4    Kitamura, N.5    Komada, M.6
  • 82
    • 33745754789 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes
    • 2-s2.0-33745754789 10.1111/j.1600-0854.2006.00452.x
    • Mizuno E., Kobayashi K., Yamamoto A., Kitamura N., Komada M., A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes. Traffic 2006 7 8 1017 1031 2-s2.0-33745754789 10.1111/j.1600-0854. 2006.00452.x
    • (2006) Traffic , vol.7 , Issue.8 , pp. 1017-1031
    • Mizuno, E.1    Kobayashi, K.2    Yamamoto, A.3    Kitamura, N.4    Komada, M.5
  • 83
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation
    • DOI 10.1074/jbc.M512615200
    • Row P. E., Prior I. A., McCullough J., Clague M. J., Urbé S., The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. Journal of Biological Chemistry 2006 281 18 12618 12624 2-s2.0-33646788800 10.1074/jbc.M512615200 (Pubitemid 43855351)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbe, S.5
  • 84
    • 34347346071 scopus 로고    scopus 로고
    • Essential role of ubiquitin-specific protease 8 for receptor tyrosine kinase stability and endocytic trafficking in vivo
    • DOI 10.1128/MCB.01566-06
    • Niendorf S., Oksche A., Kisser A., Löhler J., Prinz M., Schorle H., Feller S., Lewitzky M., Horak I., Knobeloch K.-P., Essential role of ubiquitin-specific protease 8 for receptor tyrosine kinase stability and endocytic trafficking in vivo. Molecular and Cellular Biology 2007 27 13 5029 5039 2-s2.0-34347346071 10.1128/MCB.01566-06 (Pubitemid 47016150)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.13 , pp. 5029-5039
    • Niendorf, S.1    Oksche, A.2    Kisser, A.3    Lohler, J.4    Prinz, M.5    Schorle, H.6    Feller, S.7    Lewitzky, M.8    Horak, I.9    Knobeloch, K.-P.10
  • 85
    • 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
    • 2-s2.0-77953838066 10.1095/biolreprod.109.081679
    • Berruti G., Ripolone M., Ceriani M., USP8, a regulator of endosomal sorting, is involved in mouse acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Biology of Reproduction 2010 82 5 930 939 2-s2.0-77953838066 10.1095/biolreprod.109.081679
    • (2010) Biology of Reproduction , vol.82 , Issue.5 , pp. 930-939
    • Berruti, G.1    Ripolone, M.2    Ceriani, M.3
  • 86
    • 34547122739 scopus 로고    scopus 로고
    • UBPy/MSJ-1 system during male germ cell progression in the frog, Rana esculenta
    • DOI 10.1016/j.ygcen.2006.10.004, PII S001664800600325X
    • Meccariello R., Chianese R., Scarpa D., Berruti G., Cobellis G., Pierantoni R., Fasano S., UBPy/MSJ-1 system during male germ cell progression in the frog, Rana esculenta. General and Comparative Endocrinology 2007 153 1-3 275 279 2-s2.0-34547122739 10.1016/j.ygcen.2006.10.004 (Pubitemid 47102315)
    • (2007) General and Comparative Endocrinology , vol.153 , Issue.1-3 , pp. 275-279
    • Meccariello, R.1    Chianese, R.2    Scarpa, D.3    Berruti, G.4    Cobellis, G.5    Pierantoni, R.6    Fasano, S.7
  • 87
    • 77349084837 scopus 로고    scopus 로고
    • Expression and localization of the deubiquitinating enzyme mUBPy in wobbler mouse testis during spermiogenesis
    • 2-s2.0-77349084837 10.1016/j.ygcen.2009.09.014
    • Chianese R., Scarpa D., Berruti G., Cobellis G., Pierantoni R., Fasano S., Meccariello R., Expression and localization of the deubiquitinating enzyme mUBPy in wobbler mouse testis during spermiogenesis. General and Comparative Endocrinology 2010 166 2 289 295 2-s2.0-77349084837 10.1016/j.ygcen.2009.09.014
    • (2010) General and Comparative Endocrinology , 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
  • 88
    • 85015747917 scopus 로고    scopus 로고
    • Failure of acrosome formation and globozoospermia in the wobbler mouse, a Vps54 spontaneous recessive mutant
    • Pairadi C., Pasini M. E., Gioria M., Berruti G., Failure of acrosome formation and globozoospermia in the wobbler mouse, a Vps54 spontaneous recessive mutant. Spermatogenesis 2011 1 1 52 62
    • (2011) Spermatogenesis , vol.1 , Issue.1 , pp. 52-62
    • Pairadi, C.1    Pasini, M.E.2    Gioria, M.3    Berruti, G.4
  • 89
    • 35648973707 scopus 로고    scopus 로고
    • The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation
    • DOI 10.1074/jbc.M704009200
    • Row P. E., Liu H., Hayes S., Welchman R., Charalabous P., Hofmann K., Clague M. J., Sanderson C. M., Urbé S., The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation. The Journal of Biological Chemistry 2007 282 30929 30937 2-s2.0-67649790218 (Pubitemid 350035210)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.42 , pp. 30929-30937
    • Row, P.E.1    Liu, H.2    Hayes, S.3    Welchman, R.4    Charalabous, P.5    Hofmann, K.6    Clague, M.J.7    Sanderson, C.M.8    Urbe, S.9
  • 90
    • 14844283118 scopus 로고    scopus 로고
    • A type I DnaJ homolog, DjA1, regulates androgen receptor signaling and spermatogenesis
    • DOI 10.1038/sj.emboj.7600549
    • Terada K., Yomogida K., Imai T., Kiyonari H., Takeda N., Kadomatsu T., Yano M., Aizawa S., Mori M., A type I DnaJ homolog, DjA1, regulates androgen receptor signaling and spermatogenesis. EMBO Journal 2005 24 3 611 622 2-s2.0-14844283118 10.1038/sj.emboj.7600549 (Pubitemid 40343262)
    • (2005) EMBO Journal , vol.24 , Issue.3 , pp. 611-622
    • Terada, K.1    Yomogida, K.2    Imai, T.3    Kiyonari, H.4    Takeda, N.5    Kadomatsu, T.6    Yano, M.7    Aizawa, S.8    Mori, M.9
  • 91
    • 33846022368 scopus 로고    scopus 로고
    • Identification of a heat-shock protein Hsp40, DjB1, as an acrosome- and a tail-associated component in rodent spermatozoa
    • DOI 10.1002/mrd.20609
    • Doiguchi M., Kaneko T., Urasoko A., Nishitani H., Iida H., Identification of a heat-shock protein Hsp40, DjB1, as an acrosome- and a tail-associated component in rodent spermatozoa. Molecular Reproduction and Development 2007 74 2 223 232 2-s2.0-33846022368 10.1002/mrd.20609 (Pubitemid 46047993)
    • (2007) Molecular Reproduction and Development , vol.74 , Issue.2 , pp. 223-232
    • Doiguchi, M.1    Kaneko, T.2    Urasoko, A.3    Nishitani, H.4    Iida, H.5
  • 92
    • 0037423697 scopus 로고    scopus 로고
    • Molecular cloning, structure, and testis-specific expression of MFSJ1, a member of the DNAJ protein family, in the Japanese monkey (Macaca fuscata)
    • DOI 10.1016/S0006-291X(02)03035-8
    • Yu S. S., Takenaka O., Molecular cloning, structure, and testis-specific expression of MFSJ1, a member of the DNAJ protein family, in the Japanese monkey (Macaca fuscata). Biochemical and Biophysical Research Communications 2003 301 2 443 449 2-s2.0-0037423697 10.1016/S0006-291X(02)03035-8 (Pubitemid 36279259)
    • (2003) Biochemical and Biophysical Research Communications , vol.301 , Issue.2 , pp. 443-449
    • Yu, S.S.1    Takenaka, O.2
  • 93
    • 26844498010 scopus 로고    scopus 로고
    • Identification and characterization of rDJL, a novel member of the DnaJ protein family, in rat testis
    • DOI 10.1016/j.febslet.2005.09.046, PII S0014579305011671
    • Yang C., Miao S., Zong S., Koide S. S., Wang L., Identification and characterization of rDJL, a novel member of the DnaJ protein family, in rat testis. FEBS Letters 2005 579 25 5734 5740 2-s2.0-26844498010 10.1016/j.febslet.2005.09.046 (Pubitemid 41455656)
    • (2005) FEBS Letters , vol.579 , Issue.25 , pp. 5734-5740
    • Yang, C.1    Miao, S.2    Zong, S.3    Koide, S.S.4    Wang, L.5
  • 94
    • 63849344963 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel transcript variant of Mtsarg1 gene
    • 2-s2.0-63849344963 10.1007/s11033-008-9276-6
    • Li L., Liu G., Fu J.-J., Li L.-Y., Tan X.-J., Yang S., Lu G.-X., Molecular cloning and characterization of a novel transcript variant of Mtsarg1 gene. Molecular Biology Reports 2009 36 5 1023 1032 2-s2.0-63849344963 10.1007/s11033-008-9276-6
    • (2009) Molecular Biology Reports , vol.36 , Issue.5 , pp. 1023-1032
    • Li, L.1    Liu, G.2    Fu, J.-J.3    Li, L.-Y.4    Tan, X.-J.5    Yang, S.6    Lu, G.-X.7
  • 95
    • 27844550504 scopus 로고    scopus 로고
    • Molecular cloning of a novel rat gene Tsarg1, a member of the DnaJ/HSP40 protein family
    • DOI 10.1080/10425170500129736
    • Yang H.-M., Liu G., Nie Z.-Y., Nie D.-S., Deng Y., Lu G.-X., Molecular cloning of a novel rat gene Tsarg1, a member of the DnaJ/HSP40 protein family. DNA Sequence-Journal of DNA Sequencing and Mapping 2005 16 3 166 172 2-s2.0-27844550504 10.1080/10425170500129736 (Pubitemid 41657509)
    • (2005) DNA Sequence - Journal of DNA Sequencing and Mapping , vol.16 , Issue.3 , pp. 166-172
    • Yang, H.-M.1    Liu, G.2    Nie, Z.-Y.3    Nie, D.-S.4    Deng, Y.5    Lu, G.-X.6
  • 96
    • 0037388535 scopus 로고    scopus 로고
    • Molecular cloning of TSARG3 gene related to apoptosis in human spermatogenic cells
    • Liu G., Lu G.-X., Fu J.-J., Liu S.-F., Xing X.-W., Li L.-Y., Molecular cloning of TSARG3 gene related to apoptosis in human spermatogenic cells. Chinese Journal of Medical Genetics 2003 20 2 107 110 2-s2.0-0037388535 (Pubitemid 36427798)
    • (2003) Chinese Journal of Medical Genetics , vol.20 , Issue.2 , pp. 107-110
    • Liu, G.1    Lu, G.-X.2    Fu, J.-J.3    Liu, S.-F.4    Xing, X.-W.5    Li, L.-Y.6
  • 97
    • 16544372479 scopus 로고    scopus 로고
    • Molecular cloning of TSARG6 gene related to apoptosis in human spermatogenic cells
    • Liu G., Lu G.-X., Xing X.-W., Molecular cloning of TSARG6 gene related to apoptosis in human spermatogenic cells. Acta Biochimica et Biophysica Sinica 2004 36 2 93 98 2-s2.0-16544372479 (Pubitemid 38501902)
    • (2004) Acta Biochimica et Biophysica Sinica , vol.36 , Issue.2 , pp. 93-98
    • Liu, G.1    Lu, G.-X.2    Xing, X.-W.3
  • 98
    • 47749151047 scopus 로고    scopus 로고
    • A heat-shock protein 40, DNAJB13, is an axoneme-associated component in mouse spermatozoa
    • DOI 10.1002/mrd.20874
    • Guan J., Yuan L., A heat-shock protein 40, DNAJB13, is an axoneme-associated component in mouse spermatozoa. Molecular Reproduction and Development 2008 75 9 1379 1386 2-s2.0-47749151047 10.1002/mrd.20874 (Pubitemid 352032526)
    • (2008) Molecular Reproduction and Development , vol.75 , Issue.9 , pp. 1379-1386
    • Guan, J.1    Yuan, L.2
  • 99
    • 79960457105 scopus 로고    scopus 로고
    • Mice lacking the USP2 deubiquitinating enzyme have severe male subfertility associated with defects in fertilization and sperm motility
    • 2-s2.0-79960457105 10.1095/biolreprod.110.088542
    • Bedard N., Yang Y., Gregory M., Cyr D. G., Suzuki J., Yu X., Chian R.-C., Hermo L., O'Flaherty C., Smith C. E., Clarke H. J., Wing S. S., Mice lacking the USP2 deubiquitinating enzyme have severe male subfertility associated with defects in fertilization and sperm motility. Biology of Reproduction 2011 85 3 594 604 2-s2.0-79960457105 10.1095/biolreprod.110.088542
    • (2011) Biology of Reproduction , vol.85 , Issue.3 , pp. 594-604
    • Bedard, N.1    Yang, Y.2    Gregory, M.3    Cyr, D.G.4    Suzuki, J.5    Yu, X.6    Chian, R.-C.7    Hermo, L.8    O'Flaherty, C.9    Smith, C.E.10    Clarke, H.J.11    Wing, S.S.12
  • 100
    • 0032727618 scopus 로고    scopus 로고
    • An azoospermic man with a de novo point mutation in the Y-chromosomal gene USP9Y
    • 2-s2.0-0032727618 10.1038/70539
    • Sun C., Skaletsky H., Birren B., Devon K., Tang Z., Silber S., Oates R., Page D. C., An azoospermic man with a de novo point mutation in the Y-chromosomal gene USP9Y. Nature Genetics 1999 23 4 429 432 2-s2.0-0032727618 10.1038/70539
    • (1999) Nature Genetics , 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
  • 103
    • 0033572623 scopus 로고    scopus 로고
    • USP25, a novel gene encoding a deubiquitinating enzyme, is located in the gene-poor region 21q11.2
    • DOI 10.1006/geno.1999.6025
    • Valero R., Marfany G., González-Angulo O., González- González G., Puelles L., González-Duarte R., USP25, a novel gene encoding a deubiquitinating enzyme, is located in the gene-poor region 21q11.2. Genomics 1999 62 3 395 405 2-s2.0-0033572623 10.1006/geno.1999.6025 (Pubitemid 30075169)
    • (1999) Genomics , vol.62 , Issue.3 , pp. 395-405
    • Valero, R.1    Marfany, G.2    Gonzalez-Angulo, O.3    Gonzalez-Gonzalez, G.4    Puelles, L.5    Gonzalez-Duarte, R.6
  • 104
  • 105
    • 80053385227 scopus 로고    scopus 로고
    • Localization of ubiquitin specific protease 26 at blood-testis barrier and near Sertoli cell-germ cell interface in mouse testes
    • 2-s2.0-80053385227 10.1111/j.1365-2605.2010.01130.x
    • Lin Y.-W., Hsu T.-H., Yen P. H., Localization of ubiquitin specific protease 26 at blood-testis barrier and near Sertoli cell-germ cell interface in mouse testes. International Journal of Andrology 2011 34 5 e368 e377 2-s2.0-80053385227 10.1111/j.1365-2605.2010.01130.x
    • (2011) International Journal of Andrology , vol.34 , Issue.5
    • Lin, Y.-W.1    Hsu, T.-H.2    Yen, P.H.3
  • 106
    • 33750795592 scopus 로고    scopus 로고
    • The expression of Usp42 during embryogenesis and spermatogenesis in mouse
    • DOI 10.1016/j.modgep.2006.06.006, PII S1567133X06001141
    • Kim Y.-K., Kim Y.-S., Yoo K.-J., Lee H.-J., Lee D.-R., Yeo C. Y., Baek K.-H., The expression of Usp42 during embryogenesis and spermatogenesis in mouse. Gene Expression Patterns 2007 7 1-2 143 148 2-s2.0-33750795592 10.1016/j.modgep.2006.06.006 (Pubitemid 44712736)
    • (2007) Gene Expression 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
  • 107
  • 108
    • 0037676148 scopus 로고    scopus 로고
    • Characterization of the testis in congenitally ubiquitin carboxy-terminal hydrolase-1 (Uch-L1) defective (gad) mice
    • DOI 10.1538/expanim.52.1
    • Kwon J., Kikuchi T., Setsuie R., Ishii Y., Kyuwa S., Yoshikawa Y., Characterization of the testis in congenitally ubiquitin carboxy-terminal hydrolase-1 (Uch-L1) defective (gad) mice. Experimental Animals 2003 52 1 1 9 2-s2.0-0037676148 10.1538/expanim.52.1 (Pubitemid 41349985)
    • (2003) Experimental Animals , 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
  • 109
    • 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
    • DOI 10.1002/(SICI)1098-2795(199912)54:4<333::AID-MRD3>3.0.CO;2-8
    • Kon Y., Endoh D., Iwanaga T., Expression of protein gene product 9. 5, a neuronal ubiquitin C-terminal hydrolase, and its developing change in Sertoli cells of mouse testis. Molecular Reproduction and Development 1999 54 4 333 341 (Pubitemid 29519862)
    • (1999) Molecular Reproduction and Development , vol.54 , Issue.4 , pp. 333-341
    • Kon, Y.1    Endoh, D.2    Iwanaga, T.3
  • 110
    • 0034117284 scopus 로고    scopus 로고
    • Expression and functional analysis of Uch-L3 during mouse development
    • DOI 10.1128/MCB.20.7.2498-2504.2000
    • Kurihara L. J., Semenova E., Levorse J. M., Tilghman S. M., Expression and functional analysis of Uch-L3 during mouse development. Molecular and Cellular Biology 2000 20 7 2498 2504 2-s2.0-0034117284 10.1128/MCB.20.7.2498- 2504.2000 (Pubitemid 30152057)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.7 , pp. 2498-2504
    • Kurihara, L.J.1    Semenova, E.2    Levorse, J.M.3    Tilghman, S.M.4
  • 111
    • 0034809856 scopus 로고    scopus 로고
    • Cloning, expression, and mapping of a mouse gene, Uchl4, highly homologous to human and mouse Uchl3
    • DOI 10.1006/bbrc.2001.4841
    • Osawa Y., Wang Y.-L., Osaka H., Aoki S., Wada K., Cloning, expression, and mapping of a mouse gene, Uchl4, highly homologous to human and mouse Uchl3. Biochemical and Biophysical Research Communications 2001 283 3 627 633 2-s2.0-0034809856 10.1006/bbrc.2001.4841 (Pubitemid 32917935)
    • (2001) Biochemical and Biophysical Research Communications , vol.283 , Issue.3 , pp. 627-633
    • Osawa, Y.1    Wang, Y.-L.2    Osaka, H.3    Aoki, S.4    Wada, K.5
  • 113
    • 35548974703 scopus 로고    scopus 로고
    • Regulation of Early Wave of Germ Cell Apoptosis and Spermatogenesis by Deubiquitinating Enzyme CYLD
    • DOI 10.1016/j.devcel.2007.09.007, PII S1534580707003486
    • Wright A., Reiley W. W., Chang M., Jin W., Lee A. J., Zhang M., Sun S.-C., Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD. Developmental Cell 2007 13 5 705 716 2-s2.0-35548974703 10.1016/j.devcel.2007.09.007 (Pubitemid 350011985)
    • (2007) Developmental 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


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