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Volumn 71, Issue 4, 2005, Pages 272-281

Identification of novel endometrial targets for contraception

Author keywords

Calbindin; HtrA3; MNSF ; Proprotein convertase 6; SC35 splicing factor

Indexed keywords

CALBINDIN; SERINE PROTEINASE; SUPPRESSOR FACTOR;

EID: 15744400044     PISSN: 00107824     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.contraception.2004.12.019     Document Type: Article
Times cited : (18)

References (55)
  • 1
    • 0026768292 scopus 로고
    • Blastocyst implantation depends on maternal expression of leukaemia inhibitory factor
    • C.L. Stewart, P. Kaspar, and L.J. Brunet Blastocyst implantation depends on maternal expression of leukaemia inhibitory factor Nature 359 1992 76 79
    • (1992) Nature , vol.359 , pp. 76-79
    • Stewart, C.L.1    Kaspar, P.2    Brunet, L.J.3
  • 2
    • 0030702122 scopus 로고    scopus 로고
    • Multiple female reproductive failures in cyclooxygenase 2-deficient mice
    • H. Lim, B.C. Paria, and S.K. Das Multiple female reproductive failures in cyclooxygenase 2-deficient mice Cell 91 1997 197 208
    • (1997) Cell , vol.91 , pp. 197-208
    • Lim, H.1    Paria, B.C.2    Das, S.K.3
  • 3
    • 0031916723 scopus 로고    scopus 로고
    • Infertility in female mice lacking the receptor for interleukin 11 is due to a defective uterine response to implantation
    • L. Robb, R. Li, L. Hartley, H.H. Nandurkar, F. Koentgen, and C.G. Begley Infertility in female mice lacking the receptor for interleukin 11 is due to a defective uterine response to implantation Nat. Med. 4 1998 303 308
    • (1998) Nat. Med. , vol.4 , pp. 303-308
    • Robb, L.1    Li, R.2    Hartley, L.3    Nandurkar, H.H.4    Koentgen, F.5    Begley, C.G.6
  • 4
    • 0032523915 scopus 로고    scopus 로고
    • Abdominal B (AbdB) Hoxa genes: Regulation in adult uterus by estrogen and progesterone and repression in mullerian duct by the synthetic estrogen diethylstilbestrol (DES)
    • L. Ma, G.V. Benson, H. Lim, S.K. Dey, and R.L. Maas Abdominal B (AbdB) Hoxa genes: Regulation in adult uterus by estrogen and progesterone and repression in mullerian duct by the synthetic estrogen diethylstilbestrol (DES) Dev. Biol. 197 1998 141 154
    • (1998) Dev. Biol. , vol.197 , pp. 141-154
    • Ma, L.1    Benson, G.V.2    Lim, H.3    Dey, S.K.4    Maas, R.L.5
  • 5
    • 0033304625 scopus 로고    scopus 로고
    • Hoxa-10 regulates uterine stromal cell responsiveness to progesterone during implantation and decidualization in the mouse
    • H. Lim, L. Ma, W.G. Ma, R.L. Maas, and S.K. Dey Hoxa-10 regulates uterine stromal cell responsiveness to progesterone during implantation and decidualization in the mouse Mol. Endocrinol. 13 1999 1005 1017
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1005-1017
    • Lim, H.1    Ma, L.2    Ma, W.G.3    Maas, R.L.4    Dey, S.K.5
  • 6
    • 0034531041 scopus 로고    scopus 로고
    • The role of the endometrium during embryo implantation
    • B.A. Lessey The role of the endometrium during embryo implantation Hum. Reprod. 15 Suppl. 6 2000 39 50
    • (2000) Hum. Reprod. , vol.15 , Issue.6 SUPPL. , pp. 39-50
    • Lessey, B.A.1
  • 7
    • 0141842624 scopus 로고    scopus 로고
    • Cyclic AMP and progesterone receptor cross-talk in human endometrium: A decidualizing affair
    • B. Gellersen, and J. Brosens Cyclic AMP and progesterone receptor cross-talk in human endometrium: A decidualizing affair J. Endocrinol. 178 2003 357 372
    • (2003) J. Endocrinol. , vol.178 , pp. 357-372
    • Gellersen, B.1    Brosens, J.2
  • 8
    • 0032524834 scopus 로고    scopus 로고
    • Precursor convertases: An evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins
    • N. Seidah, R. Day, M. Marcinkiewicz, and M. Chretien Precursor convertases: An evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins Ann. N. Y. Acad. Sci. 839 1998 9 24
    • (1998) Ann. N. Y. Acad. Sci. , vol.839 , pp. 9-24
    • Seidah, N.1    Day, R.2    Marcinkiewicz, M.3    Chretien, M.4
  • 9
    • 0033452452 scopus 로고    scopus 로고
    • Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides
    • N. Seidah, and M. Chretien Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides Brain Res. 848 1999 45 62
    • (1999) Brain Res. , vol.848 , pp. 45-62
    • Seidah, N.1    Chretien, M.2
  • 10
    • 0038461962 scopus 로고    scopus 로고
    • Curbing activation: Proprotein convertases in homeostasis and pathology
    • N.A. Taylor, W.J.M. Van De Van, and J.W.M. Creemers Curbing activation: Proprotein convertases in homeostasis and pathology FASEB J. 17 2003 1215 1227
    • (2003) FASEB J. , vol.17 , pp. 1215-1227
    • Taylor, N.A.1    Van De Van, W.J.M.2    Creemers, J.W.M.3
  • 11
    • 0029836967 scopus 로고    scopus 로고
    • Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4+ cell lines
    • E. Decroly, S. Wouters, C. Di Bello, C. Lazure, J.-M. Ruysschaert, and N. Seidah Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4+ cell lines J. Biol. Chem. 271 1996 30442 30450
    • (1996) J. Biol. Chem. , vol.271 , pp. 30442-30450
    • Decroly, E.1    Wouters, S.2    Di Bello, C.3    Lazure, C.4    Ruysschaert, J.-M.5    Seidah, N.6
  • 12
    • 0029842866 scopus 로고    scopus 로고
    • Isolation of the human PC6 gene encoding the putative host proteases for HIV-1 gp160 processing in CD4+ T lymphocytes
    • L. Miranda, J. Wolf, S. Pichuantes, R. Duke, and A. Franzusoff Isolation of the human PC6 gene encoding the putative host proteases for HIV-1 gp160 processing in CD4+ T lymphocytes Proc. Natl. Acad. Sci. U. S. A. 93 1996 7695 7700
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7695-7700
    • Miranda, L.1    Wolf, J.2    Pichuantes, S.3    Duke, R.4    Franzusoff, A.5
  • 13
    • 0037743535 scopus 로고    scopus 로고
    • The crystal structure of the proprotein processing proteinase furin explains its stringent specificity
    • S. Henrich, A. Cameron, and G.P. Bourenkov The crystal structure of the proprotein processing proteinase furin explains its stringent specificity Nat. Struct. Biol. 10 2003 520 526
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 520-526
    • Henrich, S.1    Cameron, A.2    Bourenkov, G.P.3
  • 14
    • 0027296764 scopus 로고
    • Identification of an isoform with an extremely large Cys-rich region of PC6, a kex2-like processing endoprotease
    • T. Nakagawa, K. Murakami, and K. Nakayama Identification of an isoform with an extremely large Cys-rich region of PC6, a kex2-like processing endoprotease FEBS Lett. 327 1993 165 171
    • (1993) FEBS Lett. , vol.327 , pp. 165-171
    • Nakagawa, T.1    Murakami, K.2    Nakayama, K.3
  • 15
    • 0030443840 scopus 로고    scopus 로고
    • The isoforms of proprotein convertase PC5 are sorted to different subcellular compartments
    • I. De Bie, M. Marcinkiewicz, and D. Malide The isoforms of proprotein convertase PC5 are sorted to different subcellular compartments J. Cell Biol. 135 1996 1261 1275
    • (1996) J. Cell Biol. , vol.135 , pp. 1261-1275
    • De Bie, I.1    Marcinkiewicz, M.2    Malide, D.3
  • 16
    • 0029907237 scopus 로고    scopus 로고
    • Prohormone convertase PC5 is a candidate processing enzyme for prorennin in the human adrenal cortex
    • C. Mercure, I. Jutras, R. Day, N. Seidah, and T.L. Reudelhuber Prohormone convertase PC5 is a candidate processing enzyme for prorennin in the human adrenal cortex Hypertension 28 1996 840 846
    • (1996) Hypertension , vol.28 , pp. 840-846
    • Mercure, C.1    Jutras, I.2    Day, R.3    Seidah, N.4    Reudelhuber, T.L.5
  • 17
    • 0032566775 scopus 로고    scopus 로고
    • PC5-A-mediated processing of pro-neurotensin in early compartments of the regulated secretory pathway of PC5-transfected PC12 cells
    • P. Barbero, C. Rovere, I. De Bie, N. Seidah, A. Beaudet, and P. Kitabgi PC5-A-mediated processing of pro-neurotensin in early compartments of the regulated secretory pathway of PC5-transfected PC12 cells J. Biol. Chem. 273 1998 25339 25346
    • (1998) J. Biol. Chem. , vol.273 , pp. 25339-25346
    • Barbero, P.1    Rovere, C.2    De Bie, I.3    Seidah, N.4    Beaudet, A.5    Kitabgi, P.6
  • 18
    • 0037855769 scopus 로고    scopus 로고
    • The proprotein convertase PC5A and a metalloprotease are involved in the proteolytic processing of the neural adhesion molecule L1
    • I. Kalus, B. Schnegelsberg, N.G. Seidah, R. Kleene, and M. Schachner The proprotein convertase PC5A and a metalloprotease are involved in the proteolytic processing of the neural adhesion molecule L1 J. Biol. Chem. 278 2003 10381 10388
    • (2003) J. Biol. Chem. , vol.278 , pp. 10381-10388
    • Kalus, I.1    Schnegelsberg, B.2    Seidah, N.G.3    Kleene, R.4    Schachner, M.5
  • 19
    • 0034652182 scopus 로고    scopus 로고
    • Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7
    • J.-C. Lissitzky, J. Luis, and J.S. Munzer Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7 Biochem. J. 346 2000 133 138
    • (2000) Biochem. J. , vol.346 , pp. 133-138
    • Lissitzky, J.-C.1    Luis, J.2    Munzer, J.S.3
  • 20
    • 0035877662 scopus 로고    scopus 로고
    • Lefty proteins exhibit unique processing and activate the MAPK pathway
    • L. Ulloa, J.W. Creemers, S. Roy, S. Liu, J. Mason, and S. Tabibzadeh Lefty proteins exhibit unique processing and activate the MAPK pathway J. Biol. Chem. 276 2001 21387 21396
    • (2001) J. Biol. Chem. , vol.276 , pp. 21387-21396
    • Ulloa, L.1    Creemers, J.W.2    Roy, S.3    Liu, S.4    Mason, J.5    Tabibzadeh, S.6
  • 21
    • 0038481179 scopus 로고    scopus 로고
    • The secretory proprotein convertases furin, PC5, and PC7 activate VEGF-C to induce tumorigenesis
    • G. Siegfried, A. Basak, and J.A. Cromlish The secretory proprotein convertases furin, PC5, and PC7 activate VEGF-C to induce tumorigenesis J. Clin. Invest. 111 2003 1723 1732
    • (2003) J. Clin. Invest. , vol.111 , pp. 1723-1732
    • Siegfried, G.1    Basak, A.2    Cromlish, J.A.3
  • 22
    • 0037307159 scopus 로고    scopus 로고
    • Specific and transient up-regulation of proprotein convertase 6 at the site of embryo implantation and identification of a unique transcript in mouse uterus during early pregnancy
    • G.Y. Nie, Y. Li, H. Minoura, J.K. Findlay, and L.A. Salamonsen Specific and transient up-regulation of proprotein convertase 6 at the site of embryo implantation and identification of a unique transcript in mouse uterus during early pregnancy Biol. Reprod. 68 2003 439 447
    • (2003) Biol. Reprod. , vol.68 , pp. 439-447
    • Nie, G.Y.1    Li, Y.2    Minoura, H.3    Findlay, J.K.4    Salamonsen, L.A.5
  • 23
    • 15744375398 scopus 로고    scopus 로고
    • Inhibiting uterine PC6 blocks embryo implantation: An obligatory role for a proprotein convertase in fertility
    • G. Nie, M. Wang, and Y.X. Liu Inhibiting uterine PC6 blocks embryo implantation: An obligatory role for a proprotein convertase in fertility Biol. Reprod. Dec. 15 2004 [Epub ahead of print]
    • (2004) Biol. Reprod. , Issue.DEC. 15
    • Nie, G.1    Wang, M.2    Liu, Y.X.3
  • 24
    • 14044257952 scopus 로고    scopus 로고
    • Requirement for proprotein convertase 6 during decidualization of human endometrial stromal cells in vitro
    • H. Okada, G. Nie, and L.A. Salamonsen Requirement for proprotein convertase 6 during decidualization of human endometrial stromal cells in vitro J. Clin. Endocrinol. Metab. 90 2005 1028 1034
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 1028-1034
    • Okada, H.1    Nie, G.2    Salamonsen, L.A.3
  • 25
    • 0024344467 scopus 로고
    • Vitamin D-dependent calcium binding proteins: Chemistry, distribution, functional considerations and molecular biology
    • S. Christakos, C. Gabrielides, and W.B. Rhoten Vitamin D-dependent calcium binding proteins: Chemistry, distribution, functional considerations and molecular biology Endocr. Rev. 10 1989 3 26
    • (1989) Endocr. Rev. , vol.10 , pp. 3-26
    • Christakos, S.1    Gabrielides, C.2    Rhoten, W.B.3
  • 26
    • 0001786345 scopus 로고
    • Vitamin D-induced calcium binding proteins
    • W.Y. Cheung Academic Press New York
    • R.H. Wasserman, and C.S. Fullmer Vitamin D-induced calcium binding proteins W.Y. Cheung Calcium and cell function 1982 Academic Press New York 175 216
    • (1982) Calcium and Cell Function , pp. 175-216
    • Wasserman, R.H.1    Fullmer, C.S.2
  • 27
    • 0023661038 scopus 로고
    • Structure-function relationships in EF-hand Ca2+-binding proteins. Protein engineering and biophysical studies of calbindin D9k
    • S. Linse, P. Brodin, and T. Drakenberg Structure-function relationships in EF-hand Ca2+-binding proteins. Protein engineering and biophysical studies of calbindin D9k Biochemistry 26 1987 6723 6735
    • (1987) Biochemistry , vol.26 , pp. 6723-6735
    • Linse, S.1    Brodin, P.2    Drakenberg, T.3
  • 28
    • 0030726470 scopus 로고    scopus 로고
    • Domain organization of calbindin D28k as determined from the association of six synthetic EF-hand fragments
    • S. Linse, E. Thulin, and L.K. Gifford Domain organization of calbindin D28k as determined from the association of six synthetic EF-hand fragments Protein Sci. 6 1997 2385 2396
    • (1997) Protein Sci. , vol.6 , pp. 2385-2396
    • Linse, S.1    Thulin, E.2    Gifford, L.K.3
  • 29
    • 0025535794 scopus 로고
    • Calbindin-D9K (CaBP9K) gene: A model for studying the genomic actions of cacitriol and calcium in mammals
    • M. Thomasset, J.M. Dupret, A. Brehier, and C. Perret Calbindin-D9K (CaBP9K) gene: A model for studying the genomic actions of cacitriol and calcium in mammals Adv. Exp. Med. Biol. 269 1990 35 36
    • (1990) Adv. Exp. Med. Biol. , vol.269 , pp. 35-36
    • Thomasset, M.1    Dupret, J.M.2    Brehier, A.3    Perret, C.4
  • 30
    • 0026091082 scopus 로고
    • No decrease of 1,25(OH)2D3 receptors and duodenal calbindin-D9k in uraemic rats
    • A. Szabo, J. Merke, M. Thomasset, and E. Ritz No decrease of 1,25(OH)2D3 receptors and duodenal calbindin-D9k in uraemic rats Eur. J. Clin. Invest. 21 1991 521 526
    • (1991) Eur. J. Clin. Invest. , vol.21 , pp. 521-526
    • Szabo, A.1    Merke, J.2    Thomasset, M.3    Ritz, E.4
  • 31
    • 0026303933 scopus 로고
    • Immunocytochemical localization of calbindin-D28k, calbindin-D9k and parvalbumin in rat kidney
    • R.J. Bindels, A. Hartog, J.A. Timmermans, and C.H. van Os Immunocytochemical localization of calbindin-D28k, calbindin-D9k and parvalbumin in rat kidney Contrib. Nephrol. 91 1991 7 13
    • (1991) Contrib. Nephrol. , vol.91 , pp. 7-13
    • Bindels, R.J.1    Hartog, A.2    Timmermans, J.A.3    Van Os, C.H.4
  • 32
    • 0028977897 scopus 로고
    • Calbindin-D9K gene expression in rat chorioallantoic placenta is not regulated by 1,25-dihydroxyvitamin D3
    • J.D. Glazier, E.B. Mawer, and C.P. Sibley Calbindin-D9K gene expression in rat chorioallantoic placenta is not regulated by 1,25-dihydroxyvitamin D3 Pediatr. Res. 37 1995 720 725
    • (1995) Pediatr. Res. , vol.37 , pp. 720-725
    • Glazier, J.D.1    Mawer, E.B.2    Sibley, C.P.3
  • 33
    • 0024283932 scopus 로고
    • Nucleotide sequence of the promoter region of the gene encoding chicken calbindin D28K
    • S. Ferrari, E. Drusiani, R. Battini, and M. Fregni Nucleotide sequence of the promoter region of the gene encoding chicken calbindin D28K Nucleic Acids Res. 16 1988 353
    • (1988) Nucleic Acids Res. , vol.16 , pp. 353
    • Ferrari, S.1    Drusiani, E.2    Battini, R.3    Fregni, M.4
  • 34
    • 0023248725 scopus 로고
    • Developmental and functional studies of parvalbumin and calbindin D28K in hypothalamic neurons grown in serum-free medium
    • G.E. Pfyffer, A. Faivre-Bauman, A. Tixier-Vidal, A.W. Norman, and C.W. Heizmann Developmental and functional studies of parvalbumin and calbindin D28K in hypothalamic neurons grown in serum-free medium J. Neurochem. 49 1987 442 451
    • (1987) J. Neurochem. , vol.49 , pp. 442-451
    • Pfyffer, G.E.1    Faivre-Bauman, A.2    Tixier-Vidal, A.3    Norman, A.W.4    Heizmann, C.W.5
  • 35
    • 0026615814 scopus 로고
    • Calbindin-D9k gene expression during pregnancy and lactation in the rat
    • J. Krisinger, J.L. Dann, E.B. Jeung, and P.C. Leung Calbindin-D9k gene expression during pregnancy and lactation in the rat Mol. Cell. Endocrinol. 88 1992 119 128
    • (1992) Mol. Cell. Endocrinol. , vol.88 , pp. 119-128
    • Krisinger, J.1    Dann, J.L.2    Jeung, E.B.3    Leung, P.C.4
  • 36
    • 0028984250 scopus 로고
    • 9k gene expression in endometrium, myometrium and placenta in the absence of a functional estrogen response element in intron a
    • 9k gene expression in endometrium, myometrium and placenta in the absence of a functional estrogen response element in intron A Biol. Reprod. 52 1995 115 123
    • (1995) Biol. Reprod. , vol.52 , pp. 115-123
    • Krisinger, J.1    Jeung, E.-B.2    Simmen, R.C.M.3    Leung, P.C.K.4
  • 37
    • 0033957528 scopus 로고    scopus 로고
    • Complex regulation of calcium-binding protein D9k (Calbindin-D9k) in the mouse uterus during early pregnancy and at the site of embryo implantation
    • G.-Y. Nie, Y. Li, J. Wang, H. Minoura, J.K. Findlay, and L.A. Salamonsen Complex regulation of calcium-binding protein D9k (Calbindin-D9k) in the mouse uterus during early pregnancy and at the site of embryo implantation Biol. Reprod. 62 2000 27 36
    • (2000) Biol. Reprod. , vol.62 , pp. 27-36
    • Nie, G.-Y.1    Li, Y.2    Wang, J.3    Minoura, H.4    Findlay, J.K.5    Salamonsen, L.A.6
  • 38
    • 0032903244 scopus 로고    scopus 로고
    • Expression of calcium binding protein D-9k messenger RNA in the mouse uterine endometrium during implantation
    • K. Tatsumi, T. Higuchi, and H. Fujiwara Expression of calcium binding protein D-9k messenger RNA in the mouse uterine endometrium during implantation Mol. Hum. Reprod. 5 1999 153 161
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 153-161
    • Tatsumi, K.1    Higuchi, T.2    Fujiwara, H.3
  • 39
    • 2542559734 scopus 로고    scopus 로고
    • Endometrial calbindins are critical for embryo implantation: Evidence from in vivo use of morpholino antisense oligonucleotides
    • K.C. Luu, G.Y. Nie, and L.A. Salamonsen Endometrial calbindins are critical for embryo implantation: Evidence from in vivo use of morpholino antisense oligonucleotides Proc. Natl. Acad. Sci. U. S. A. 101 2004 8028 8033
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8028-8033
    • Luu, K.C.1    Nie, G.Y.2    Salamonsen, L.A.3
  • 40
    • 6344282883 scopus 로고    scopus 로고
    • Endometrial expression of calbindin-d28k but not -d9k in primates implies evolutionary changes and functional redundancy of calbindins at implantation
    • K. Luu, G. Nie, A. Hampton, G.Q. Fu, Y.-X. Liu, and L.A. Salamonsen Endometrial expression of calbindin-d28k but not -d9k in primates implies evolutionary changes and functional redundancy of calbindins at implantation Reproduction 128 2004 433 441
    • (2004) Reproduction , vol.128 , pp. 433-441
    • Luu, K.1    Nie, G.2    Hampton, A.3    Fu, G.Q.4    Liu, Y.-X.5    Salamonsen, L.A.6
  • 41
    • 0031019589 scopus 로고    scopus 로고
    • Ataxia and altered dendritic calcium signaling in mice carrying a targeted null mutation of the calbindin D28k gene
    • M.S. Airaksinen, J. Eilers, O. Garaschuk, H. Thoenen, A. Konnerth, and M. Meyer Ataxia and altered dendritic calcium signaling in mice carrying a targeted null mutation of the calbindin D28k gene Proc. Natl. Acad. Sci. U. S. A. 94 1997 1488 1493
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1488-1493
    • Airaksinen, M.S.1    Eilers, J.2    Garaschuk, O.3    Thoenen, H.4    Konnerth, A.5    Meyer, M.6
  • 42
    • 0038310595 scopus 로고    scopus 로고
    • A novel serine protease of the mammalian HtrA family is up-regulated in mouse uterus coinciding with placentation
    • G.-Y. Nie, Y. Li, and H. Minoura A novel serine protease of the mammalian HtrA family is up-regulated in mouse uterus coinciding with placentation Mol. Hum. Reprod. 9 2003 279 290
    • (2003) Mol. Hum. Reprod. , vol.9 , pp. 279-290
    • Nie, G.-Y.1    Li, Y.2    Minoura, H.3
  • 43
    • 0037394645 scopus 로고    scopus 로고
    • Identification and cloning of two isoforms of human HtrA3, characterisation of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2
    • G.Y. Nie, A. Hampton, Y. Li, J.K. Findlay, and L.A. Salamonsen Identification and cloning of two isoforms of human HtrA3, characterisation of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2 Biochem. J. 371 2003 39 48
    • (2003) Biochem. J. , vol.371 , pp. 39-48
    • Nie, G.Y.1    Hampton, A.2    Li, Y.3    Findlay, J.K.4    Salamonsen, L.A.5
  • 45
    • 0029767662 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • J.L. Manley, and R. Tacke SR proteins and splicing control Genes Dev. 10 1996 1569 1579
    • (1996) Genes Dev. , vol.10 , pp. 1569-1579
    • Manley, J.L.1    Tacke, R.2
  • 46
    • 0033663922 scopus 로고    scopus 로고
    • Uterine expression of alternatively spliced mRNAs of mouse splicing factor SC35 during early pregnancy
    • G.Y. Nie, Y. Li, and L. Batten Uterine expression of alternatively spliced mRNAs of mouse splicing factor SC35 during early pregnancy Mol. Hum. Reprod. 6 2000 1131 1139
    • (2000) Mol. Hum. Reprod. , vol.6 , pp. 1131-1139
    • Nie, G.Y.1    Li, Y.2    Batten, L.3
  • 47
    • 0036053613 scopus 로고    scopus 로고
    • A potential molecular mechanism for regulating pre-mRNA splicing of implantation-related genes through unique uterine expression of splicing factor SC35 in women and rhesus monkeys
    • G.Y. Nie, A.L. Hampton, G.Q. Fu, Y.X. Liu, J.K. Findlay, and L.A. Salamonsen A potential molecular mechanism for regulating pre-mRNA splicing of implantation-related genes through unique uterine expression of splicing factor SC35 in women and rhesus monkeys Reproduction 124 2002 209 217
    • (2002) Reproduction , vol.124 , pp. 209-217
    • Nie, G.Y.1    Hampton, A.L.2    Fu, G.Q.3    Liu, Y.X.4    Findlay, J.K.5    Salamonsen, L.A.6
  • 48
    • 0022652069 scopus 로고
    • Isolation and characterization of a monoclonal nonspecific suppressor factor (MNSF) produced by a T cell hybridoma
    • M. Nakamura, H. Ogawa, and T. Tsunematsu Isolation and characterization of a monoclonal nonspecific suppressor factor (MNSF) produced by a T cell hybridoma J. Immunol. 136 1986 2904 2909
    • (1986) J. Immunol. , vol.136 , pp. 2904-2909
    • Nakamura, M.1    Ogawa, H.2    Tsunematsu, T.3
  • 49
    • 0023093435 scopus 로고
    • Characterization of monoclonal nonspecific suppressor factor (MNSF) with the use of a monoclonal antibody
    • M. Nakamura, H. Ogawa, and T. Tsunematsu Characterization of monoclonal nonspecific suppressor factor (MNSF) with the use of a monoclonal antibody J. Immunol. 138 1987 1799 1803
    • (1987) J. Immunol. , vol.138 , pp. 1799-1803
    • Nakamura, M.1    Ogawa, H.2    Tsunematsu, T.3
  • 50
    • 0027952890 scopus 로고
    • Monoclonal nonspecific suppressor factor (MNSF) inhibits the IL-4 secretion by bone marrow-derived mast cell (BMMC)
    • M. Nakamura, R.M. Xavier, and Y. Tanigawa Monoclonal nonspecific suppressor factor (MNSF) inhibits the IL-4 secretion by bone marrow-derived mast cell (BMMC) FEBS Lett. 339 1993 239 242
    • (1993) FEBS Lett. , vol.339 , pp. 239-242
    • Nakamura, M.1    Xavier, R.M.2    Tanigawa, Y.3
  • 51
    • 0029118562 scopus 로고
    • Monoclonal nonspecific suppressor factor beta inhibits the IL-4 secretion by a type-2 helper T cell clone
    • M. Nakamura, R.M. Xavier, and Y. Tanigawa Monoclonal nonspecific suppressor factor beta inhibits the IL-4 secretion by a type-2 helper T cell clone Eur. J. Immunol. 25 1995 2417 2419
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2417-2419
    • Nakamura, M.1    Xavier, R.M.2    Tanigawa, Y.3
  • 52
    • 0034053539 scopus 로고    scopus 로고
    • Identification of monoclonal nonspecific suppressor factor beta (MNSFbeta) as one of the genes differentially expressed at implantation sites compared to interimplantation sites in the mouse uterus
    • G.-Y. Nie, Y. Li, A.L. Hampton, L.A. Salamonsen, J.A. Clements, and J.K. Findlay Identification of monoclonal nonspecific suppressor factor beta (MNSFbeta) as one of the genes differentially expressed at implantation sites compared to interimplantation sites in the mouse uterus Mol. Reprod. Dev. 55 2000 351 363
    • (2000) Mol. Reprod. Dev. , vol.55 , pp. 351-363
    • Nie, G.-Y.1    Li, Y.2    Hampton, A.L.3    Salamonsen, L.A.4    Clements, J.A.5    Findlay, J.K.6
  • 53
    • 85030811303 scopus 로고    scopus 로고
    • [WHO Geneva. (Newsletter of the UNDP/UNFPA/WHO/World Bank Special Programme of Research, Development and Research Training in Human Reproduction)].
    • Prog Reprod Health Res 59, 2002, [WHO Geneva. (Newsletter of the UNDP/UNFPA/WHO/World Bank Special Programme of Research, Development and Research Training in Human Reproduction)].
    • (2002) Prog Reprod Health Res , vol.59
  • 54
    • 0030940884 scopus 로고    scopus 로고
    • Targeted drug delivery in gynaecology: The first uterine pass effect
    • C. Bulletti, D. de Ziegler, and C. Flamigni Targeted drug delivery in gynaecology: The first uterine pass effect Hum. Reprod. 12 1997 1073 1079
    • (1997) Hum. Reprod. , vol.12 , pp. 1073-1079
    • Bulletti, C.1    De Ziegler, D.2    Flamigni, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.