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Volumn 9, Issue 11, 2010, Pages 5739-5747

Proteomic approach identifies alterations in cytoskeletal remodelling proteins during decidualization of human endometrial stromal cells

Author keywords

decidualization; human endometrial stromal cells; src substrate cortactin 8

Indexed keywords

ALPHA TROPOMYOSIN; CALDESMON; CALDESMON 1; CONTACTIN; CYCLIC AMP; CYTOSKELETON PROTEIN; LIM PROTEIN; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE ISOMERASE 1A; PROTEIN SH3; SRC SUBSTRATE CONTACTIN 8; TROPOMYOSIN ALPHA 4 CHAIN; UNCLASSIFIED DRUG;

EID: 78149364699     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100525a     Document Type: Article
Times cited : (25)

References (55)
  • 1
    • 0035829844 scopus 로고    scopus 로고
    • Implantation and the survival of early pregnancy
    • Norwitz, E. R.; Schust, D. J.; Fisher, S. J. Implantation and the survival of early pregnancy N. Engl. J. Med. 2001, 345 (19) 1400-8
    • (2001) N. Engl. J. Med. , vol.345 , Issue.19 , pp. 1400-8
    • Norwitz, E.R.1    Schust, D.J.2    Fisher, S.J.3
  • 2
    • 0141851028 scopus 로고    scopus 로고
    • Decidualization of the human endometrial stromal cell: An enigmatic transformation
    • Dunn, C. L.; Kelly, R. W.; Critchley, H. O. Decidualization of the human endometrial stromal cell: an enigmatic transformation Reprod. Biomed. Online 2003, 7 (2) 151-61
    • (2003) Reprod. Biomed. Online , vol.7 , Issue.2 , pp. 151-61
    • Dunn, C.L.1    Kelly, R.W.2    Critchley, H.O.3
  • 4
    • 0025730996 scopus 로고
    • Regulation of insulin-like growth factor-binding protein-1 synthesis and secretion by progestin and relaxin in long term cultures of human endometrial stromal cells
    • Bell, S. C.; Jackson, J. A.; Ashmore, J.; Zhu, H. H.; Tseng, L. Regulation of insulin-like growth factor-binding protein-1 synthesis and secretion by progestin and relaxin in long term cultures of human endometrial stromal cells J. Clin. Endocrinol. Metab. 1991, 72 (5) 1014-24
    • (1991) J. Clin. Endocrinol. Metab. , vol.72 , Issue.5 , pp. 1014-24
    • Bell, S.C.1    Jackson, J.A.2    Ashmore, J.3    Zhu, H.H.4    Tseng, L.5
  • 5
    • 0025102715 scopus 로고
    • Differential effects of progestin and relaxin on the synthesis and secretion of immunoreactive prolactin in long term culture of human endometrial stromal cells
    • Zhu, H. H.; Huang, J. R.; Mazella, J.; Rosenberg, M.; Tseng, L. Differential effects of progestin and relaxin on the synthesis and secretion of immunoreactive prolactin in long term culture of human endometrial stromal cells J. Clin. Endocrinol. Metab. 1990, 71 (4) 889-99
    • (1990) J. Clin. Endocrinol. Metab. , vol.71 , Issue.4 , pp. 889-99
    • Zhu, H.H.1    Huang, J.R.2    Mazella, J.3    Rosenberg, M.4    Tseng, L.5
  • 6
    • 0141842624 scopus 로고    scopus 로고
    • Cyclic AMP and progesterone receptor cross-talk in human endometrium: A decidualizing affair
    • Gellersen, B.; Brosens, J. Cyclic AMP and progesterone receptor cross-talk in human endometrium: a decidualizing affair J. Endocrinol. 2003, 178 (3) 357-72
    • (2003) J. Endocrinol. , vol.178 , Issue.3 , pp. 357-72
    • Gellersen, B.1    Brosens, J.2
  • 7
    • 0036359095 scopus 로고    scopus 로고
    • Molecules in blastocyst implantation: Uterine and embryonic perspectives
    • Lim, H.; Song, H.; Paria, B. C.; Reese, J.; Das, S. K.; Dey, S. K. Molecules in blastocyst implantation: uterine and embryonic perspectives Vitam. Horm. 2002, 64, 43-76
    • (2002) Vitam. Horm. , vol.64 , pp. 43-76
    • Lim, H.1    Song, H.2    Paria, B.C.3    Reese, J.4    Das, S.K.5    Dey, S.K.6
  • 8
    • 14044257952 scopus 로고    scopus 로고
    • Requirement for proprotein convertase 5/6 during decidualization of human endometrial stromal cells in vitro
    • Okada, H.; Nie, G.; Salamonsen, L. A. Requirement for proprotein convertase 5/6 during decidualization of human endometrial stromal cells in vitro J. Clin. Endocrinol. Metab. 2005, 90 (2) 1028-34
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , Issue.2 , pp. 1028-34
    • Okada, H.1    Nie, G.2    Salamonsen, L.A.3
  • 11
    • 0033643577 scopus 로고    scopus 로고
    • Implantation defect in endometriosis: Endometrium or peritoneal fluid
    • Selam, B.; Arici, A. Implantation defect in endometriosis: endometrium or peritoneal fluid J. Reprod. Fertil., Suppl. 2000, 55, 121-8
    • (2000) J. Reprod. Fertil., Suppl. , vol.55 , pp. 121-8
    • Selam, B.1    Arici, A.2
  • 12
    • 0032908870 scopus 로고    scopus 로고
    • Insulin-like growth factor binding protein-1 expression in baboon endometrial stromal cells: Regulation by filamentous actin and requirement for de novo protein synthesis
    • Kim, J. J.; Jaffe, R. C.; Fazleabas, A. T. Insulin-like growth factor binding protein-1 expression in baboon endometrial stromal cells: regulation by filamentous actin and requirement for de novo protein synthesis Endocrinology 1999, 140 (2) 997-1004
    • (1999) Endocrinology , vol.140 , Issue.2 , pp. 997-1004
    • Kim, J.J.1    Jaffe, R.C.2    Fazleabas, A.T.3
  • 13
    • 0034456460 scopus 로고    scopus 로고
    • Discovery of new inducible genes in in vitro decidualized human endometrial stromal cells using microarray technology
    • Popovici, R. M.; Kao, L. C.; Giudice, L. C. Discovery of new inducible genes in in vitro decidualized human endometrial stromal cells using microarray technology Endocrinology 2000, 141 (9) 3510-3
    • (2000) Endocrinology , vol.141 , Issue.9 , pp. 3510-3
    • Popovici, R.M.1    Kao, L.C.2    Giudice, L.C.3
  • 14
    • 0346109672 scopus 로고    scopus 로고
    • Gene induction and categorical reprogramming during in vitro human endometrial fibroblast decidualization
    • Brar, A. K.; Handwerger, S.; Kessler, C. A.; Aronow, B. J. Gene induction and categorical reprogramming during in vitro human endometrial fibroblast decidualization Physiol. Genomics 2001, 7 (2) 135-48
    • (2001) Physiol. Genomics , vol.7 , Issue.2 , pp. 135-48
    • Brar, A.K.1    Handwerger, S.2    Kessler, C.A.3    Aronow, B.J.4
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 1976, 72, 248-54
    • (1976) Anal. Biochem. , vol.72 , pp. 248-54
    • Bradford, M.M.1
  • 17
    • 70449397854 scopus 로고    scopus 로고
    • Proteomic identification of caldesmon as a physiological substrate of proprotein convertase 6 in human uterine decidual cells essential for pregnancy establishment
    • Kilpatrick, L. M.; Stephens, A. N.; Hardman, B. M.; Salamonsen, L. A.; Li, Y.; Stanton, P. G.; Nie, G. Proteomic identification of caldesmon as a physiological substrate of proprotein convertase 6 in human uterine decidual cells essential for pregnancy establishment J. Proteome Res. 2009, 8 (11) 4983-92
    • (2009) J. Proteome Res. , vol.8 , Issue.11 , pp. 4983-92
    • Kilpatrick, L.M.1    Stephens, A.N.2    Hardman, B.M.3    Salamonsen, L.A.4    Li, Y.5    Stanton, P.G.6    Nie, G.7
  • 18
    • 34249320529 scopus 로고    scopus 로고
    • Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia
    • Clark, E. S.; Whigham, A. S.; Yarbrough, W. G.; Weaver, A. M. Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia Cancer Res. 2007, 67 (9) 4227-35
    • (2007) Cancer Res. , vol.67 , Issue.9 , pp. 4227-35
    • Clark, E.S.1    Whigham, A.S.2    Yarbrough, W.G.3    Weaver, A.M.4
  • 19
    • 34547670979 scopus 로고    scopus 로고
    • Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans
    • Winter, A. D.; McCormack, G.; Page, A. P. Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans Dev. Biol. 2007, 308 (2) 449-61
    • (2007) Dev. Biol. , vol.308 , Issue.2 , pp. 449-61
    • Winter, A.D.1    McCormack, G.2    Page, A.P.3
  • 20
    • 34247206573 scopus 로고    scopus 로고
    • Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions
    • Rainey-Barger, E. K.; Mkrtchian, S.; Tsai, B. Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions Mol. Biol. Cell 2007, 18 (4) 1253-60
    • (2007) Mol. Biol. Cell , vol.18 , Issue.4 , pp. 1253-60
    • Rainey-Barger, E.K.1    Mkrtchian, S.2    Tsai, B.3
  • 21
    • 37549005081 scopus 로고    scopus 로고
    • Nuclear localization and cytosolic overexpression of LASP-1 correlates with tumor size and nodal-positivity of human breast carcinoma
    • Grunewald, T. G.; Kammerer, U.; Kapp, M.; Eck, M.; Dietl, J.; Butt, E.; Honig, A. Nuclear localization and cytosolic overexpression of LASP-1 correlates with tumor size and nodal-positivity of human breast carcinoma BMC Cancer 2007, 7, 198
    • (2007) BMC Cancer , vol.7 , pp. 198
    • Grunewald, T.G.1    Kammerer, U.2    Kapp, M.3    Eck, M.4    Dietl, J.5    Butt, E.6    Honig, A.7
  • 22
    • 33645214432 scopus 로고    scopus 로고
    • Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells
    • Grunewald, T. G.; Kammerer, U.; Schulze, E.; Schindler, D.; Honig, A.; Zimmer, M.; Butt, E. Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells Exp. Cell Res. 2006, 312 (7) 974-82
    • (2006) Exp. Cell Res. , vol.312 , Issue.7 , pp. 974-82
    • Grunewald, T.G.1    Kammerer, U.2    Schulze, E.3    Schindler, D.4    Honig, A.5    Zimmer, M.6    Butt, E.7
  • 24
    • 0037168916 scopus 로고    scopus 로고
    • Endometrial function: Cell specific changes in the uterine environment
    • Fazleabas, A. T.; Strakova, Z. Endometrial function: cell specific changes in the uterine environment Mol. Cell. Endocrinol. 2002, 186 (2) 143-7
    • (2002) Mol. Cell. Endocrinol. , vol.186 , Issue.2 , pp. 143-7
    • Fazleabas, A.T.1    Strakova, Z.2
  • 25
    • 0141614998 scopus 로고    scopus 로고
    • Complex regulation of decidualization: A role for cytokines and proteases - A review
    • Salamonsen, L. A.; Dimitriadis, E.; Jones, R. L.; Nie, G. Complex regulation of decidualization: a role for cytokines and proteases - a review Placenta 2003, 24 (Suppl A S76-85
    • (2003) Placenta , vol.24 , Issue.SUPPL. A
    • Salamonsen, L.A.1    Dimitriadis, E.2    Jones, R.L.3    Nie, G.4
  • 27
    • 59349096434 scopus 로고    scopus 로고
    • LIM and SH3 protein 1 (Lasp1) is a novel p53 transcriptional target involved in hepatocellular carcinoma
    • Wang, B.; Feng, P.; Xiao, Z.; Ren, E. C. LIM and SH3 protein 1 (Lasp1) is a novel p53 transcriptional target involved in hepatocellular carcinoma J. Hepatol. 2009, 50 (3) 528-37
    • (2009) J. Hepatol. , vol.50 , Issue.3 , pp. 528-37
    • Wang, B.1    Feng, P.2    Xiao, Z.3    Ren, E.C.4
  • 28
    • 0038521306 scopus 로고    scopus 로고
    • Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146
    • Butt, E.; Gambaryan, S.; Gottfert, N.; Galler, A.; Marcus, K.; Meyer, H. E. Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146 J. Biol. Chem. 2003, 278 (18) 15601-7
    • (2003) J. Biol. Chem. , vol.278 , Issue.18 , pp. 15601-7
    • Butt, E.1    Gambaryan, S.2    Gottfert, N.3    Galler, A.4    Marcus, K.5    Meyer, H.E.6
  • 29
    • 0037115487 scopus 로고    scopus 로고
    • Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo
    • Chew, C. S.; Chen, X.; Parente, J. A., Jr.; Tarrer, S.; Okamoto, C.; Qin, H. Y. Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo J. Cell Sci. 2002, 115 (Pt 24) 4787-99
    • (2002) J. Cell Sci. , vol.115 , Issue.PART 24 , pp. 4787-99
    • Chew, C.S.1    Chen, X.2    Parente, Jr.J.A.3    Tarrer, S.4    Okamoto, C.5    Qin, H.Y.6
  • 30
    • 67649646958 scopus 로고    scopus 로고
    • Manipulating actin dynamics affects human in vitro decidualization
    • Ihnatovych, I.; Livak, M.; Reed, J.; de Lanerolle, P.; Strakova, Z. Manipulating actin dynamics affects human in vitro decidualization Biol. Reprod. 2009, 81 (1) 222-30
    • (2009) Biol. Reprod. , vol.81 , Issue.1 , pp. 222-30
    • Ihnatovych, I.1    Livak, M.2    Reed, J.3    De Lanerolle, P.4    Strakova, Z.5
  • 31
    • 33644951350 scopus 로고    scopus 로고
    • Caldesmon phosphorylation in actin cytoskeletal remodeling
    • Hai, C. M.; Gu, Z. Caldesmon phosphorylation in actin cytoskeletal remodeling Eur. J. Cell Biol. 2006, 85 (3-4) 305-9
    • (2006) Eur. J. Cell Biol. , vol.85 , Issue.3-4 , pp. 305-9
    • Hai, C.M.1    Gu, Z.2
  • 32
    • 4444257529 scopus 로고    scopus 로고
    • Caldesmon mutant defective in Ca(2+)-calmodulin binding interferes with assembly of stress fibers and affects cell morphology, growth and motility
    • Li, Y.; Lin, J. L.; Reiter, R. S.; Daniels, K.; Soll, D. R.; Lin, J. J. Caldesmon mutant defective in Ca(2+)-calmodulin binding interferes with assembly of stress fibers and affects cell morphology, growth and motility J. Cell Sci. 2004, 117 (Pt 16) 3593-604
    • (2004) J. Cell Sci. , vol.117 , Issue.PART 16 , pp. 3593-604
    • Li, Y.1    Lin, J.L.2    Reiter, R.S.3    Daniels, K.4    Soll, D.R.5    Lin, J.J.6
  • 33
    • 0026086010 scopus 로고
    • Structural and functional relationships between h- and l-caldesmons
    • Hayashi, K.; Fujio, Y.; Kato, I.; Sobue, K. Structural and functional relationships between h- and l-caldesmons J. Biol. Chem. 1991, 266 (1) 355-61
    • (1991) J. Biol. Chem. , vol.266 , Issue.1 , pp. 355-61
    • Hayashi, K.1    Fujio, Y.2    Kato, I.3    Sobue, K.4
  • 37
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller, J. P.; Helfman, D. M. The molecular basis for tropomyosin isoform diversity Bioessays 1991, 13 (9) 429-37
    • (1991) Bioessays , vol.13 , Issue.9 , pp. 429-37
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 38
    • 0027302402 scopus 로고
    • The essential role of tropomyosin in cooperative regulation of smooth muscle thin filament activity by caldesmon
    • Marston, S. B.; Redwood, C. S. The essential role of tropomyosin in cooperative regulation of smooth muscle thin filament activity by caldesmon J. Biol. Chem. 1993, 268 (17) 12317-20
    • (1993) J. Biol. Chem. , vol.268 , Issue.17 , pp. 12317-20
    • Marston, S.B.1    Redwood, C.S.2
  • 39
    • 11144230917 scopus 로고    scopus 로고
    • Modes of caldesmon binding to actin: Sites of caldesmon contact and modulation of interactions by phosphorylation
    • Foster, D. B.; Huang, R.; Hatch, V.; Craig, R.; Graceffa, P.; Lehman, W.; Wang, C. L. Modes of caldesmon binding to actin: sites of caldesmon contact and modulation of interactions by phosphorylation J. Biol. Chem. 2004, 279 (51) 53387-94
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 53387-94
    • Foster, D.B.1    Huang, R.2    Hatch, V.3    Craig, R.4    Graceffa, P.5    Lehman, W.6    Wang, C.L.7
  • 40
    • 0028268574 scopus 로고
    • Overexpression of human fibroblast caldesmon fragment containing actin-, Ca++/calmodulin-, and tropomyosin-binding domains stabilizes endogenous tropomyosin and microfilaments
    • Warren, K. S.; Lin, J. L.; Wamboldt, D. D.; Lin, J. J. Overexpression of human fibroblast caldesmon fragment containing actin-, Ca++/calmodulin-, and tropomyosin-binding domains stabilizes endogenous tropomyosin and microfilaments J. Cell Biol. 1994, 125 (2) 359-68
    • (1994) J. Cell Biol. , vol.125 , Issue.2 , pp. 359-68
    • Warren, K.S.1    Lin, J.L.2    Wamboldt, D.D.3    Lin, J.J.4
  • 41
    • 0035475450 scopus 로고    scopus 로고
    • Cortactin: Coupling membrane dynamics to cortical actin assembly
    • Weed, S. A.; Parsons, J. T. Cortactin: coupling membrane dynamics to cortical actin assembly Oncogene 2001, 20 (44) 6418-34
    • (2001) Oncogene , vol.20 , Issue.44 , pp. 6418-34
    • Weed, S.A.1    Parsons, J.T.2
  • 43
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase
    • Jiang, X. M.; Fitzgerald, M.; Grant, C. M.; Hogg, P. J. Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase J. Biol. Chem. 1999, 274 (4) 2416-23
    • (1999) J. Biol. Chem. , vol.274 , Issue.4 , pp. 2416-23
    • Jiang, X.M.1    Fitzgerald, M.2    Grant, C.M.3    Hogg, P.J.4
  • 44
    • 0029020757 scopus 로고
    • Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: Formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit
    • Helaakoski, T.; Annunen, P.; Vuori, K.; MacNeil, I. A.; Pihlajaniemi, T.; Kivirikko, K. I. Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (10) 4427-31
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.10 , pp. 4427-31
    • Helaakoski, T.1    Annunen, P.2    Vuori, K.3    MacNeil, I.A.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 45
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier, L.; Usherwood, Y. K.; Chung, K. T.; Hendershot, L. M. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins Mol. Biol. Cell 2002, 13 (12) 4456-69
    • (2002) Mol. Biol. Cell , vol.13 , Issue.12 , pp. 4456-69
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 46
    • 0030463481 scopus 로고    scopus 로고
    • Facilitated protein aggregation. Effects of calcium on the chaperone and anti-chaperone activity of protein disulfide-isomerase
    • Primm, T. P.; Walker, K. W.; Gilbert, H. F. Facilitated protein aggregation. Effects of calcium on the chaperone and anti-chaperone activity of protein disulfide-isomerase J. Biol. Chem. 1996, 271 (52) 33664-9
    • (1996) J. Biol. Chem. , vol.271 , Issue.52 , pp. 33664-9
    • Primm, T.P.1    Walker, K.W.2    Gilbert, H.F.3
  • 47
    • 0035979394 scopus 로고    scopus 로고
    • Detection of disulfide bonds in bovine brain tubulin and their role in protein folding and microtubule assembly in vitro: A novel disulfide detection approach
    • Chaudhuri, A. R.; Khan, I. A.; Luduena, R. F. Detection of disulfide bonds in bovine brain tubulin and their role in protein folding and microtubule assembly in vitro: a novel disulfide detection approach Biochemistry 2001, 40 (30) 8834-41
    • (2001) Biochemistry , vol.40 , Issue.30 , pp. 8834-41
    • Chaudhuri, A.R.1    Khan, I.A.2    Luduena, R.F.3
  • 48
    • 15744404413 scopus 로고    scopus 로고
    • Contributions of disulfide bonds in a nested pattern to the structure, stability, and biological functions of endostatin
    • Zhou, H.; Wang, W.; Luo, Y. Contributions of disulfide bonds in a nested pattern to the structure, stability, and biological functions of endostatin J. Biol. Chem. 2005, 280 (12) 11303-12
    • (2005) J. Biol. Chem. , vol.280 , Issue.12 , pp. 11303-12
    • Zhou, H.1    Wang, W.2    Luo, Y.3
  • 49
    • 69249146570 scopus 로고    scopus 로고
    • Society for Reproductive Biology Founders' Lecture 2009. Preparing fertile soil: The importance of endometrial receptivity
    • Salamonsen, L. A.; Nie, G.; Hannan, N. J.; Dimitriadis, E. Society for Reproductive Biology Founders' Lecture 2009. Preparing fertile soil: the importance of endometrial receptivity Reprod. Fertil. Dev. 2009, 21 (7) 923-34
    • (2009) Reprod. Fertil. Dev. , vol.21 , Issue.7 , pp. 923-34
    • Salamonsen, L.A.1    Nie, G.2    Hannan, N.J.3    Dimitriadis, E.4
  • 50
    • 33747734121 scopus 로고    scopus 로고
    • TGF-beta superfamily expression and actions in the endometrium and placenta
    • Jones, R. L.; Stoikos, C.; Findlay, J. K.; Salamonsen, L. A. TGF-beta superfamily expression and actions in the endometrium and placenta Reproduction 2006, 132 (2) 217-32
    • (2006) Reproduction , vol.132 , Issue.2 , pp. 217-32
    • Jones, R.L.1    Stoikos, C.2    Findlay, J.K.3    Salamonsen, L.A.4
  • 51
    • 44449125724 scopus 로고    scopus 로고
    • A distinct cohort of the TGFbeta superfamily members expressed in human endometrium regulate decidualization
    • Stoikos, C. J.; Harrison, C. A.; Salamonsen, L. A.; Dimitriadis, E. A distinct cohort of the TGFbeta superfamily members expressed in human endometrium regulate decidualization Hum. Reprod. 2008, 23 (6) 1447-56
    • (2008) Hum. Reprod. , vol.23 , Issue.6 , pp. 1447-56
    • Stoikos, C.J.1    Harrison, C.A.2    Salamonsen, L.A.3    Dimitriadis, E.4
  • 53
    • 0035092334 scopus 로고    scopus 로고
    • Characterization of a rat uterine cell line, U(III) cells: Prolactin (PRL) expression and endogenous regulation of PRL-dependent genes; Estrogen receptor beta, alpha(2)-macroglobulin, and decidual PRL involving the Jak2 and Stat5 pathway
    • Prigent-Tessier, A.; Barkai, U.; Tessier, C.; Cohen, H.; Gibori, G. Characterization of a rat uterine cell line, U(III) cells: prolactin (PRL) expression and endogenous regulation of PRL-dependent genes; estrogen receptor beta, alpha(2)-macroglobulin, and decidual PRL involving the Jak2 and Stat5 pathway Endocrinology 2001, 142 (3) 1242-50
    • (2001) Endocrinology , vol.142 , Issue.3 , pp. 1242-50
    • Prigent-Tessier, A.1    Barkai, U.2    Tessier, C.3    Cohen, H.4    Gibori, G.5
  • 54
    • 0034871776 scopus 로고    scopus 로고
    • PRL antiapoptotic effect in the rat decidua involves the PI3K/protein kinase B-mediated inhibition of caspase-3 activity
    • Tessier, C.; Prigent-Tessier, A.; Ferguson-Gottschall, S.; Gu, Y.; Gibori, G. PRL antiapoptotic effect in the rat decidua involves the PI3K/protein kinase B-mediated inhibition of caspase-3 activity Endocrinology 2001, 142 (9) 4086-94
    • (2001) Endocrinology , vol.142 , Issue.9 , pp. 4086-94
    • Tessier, C.1    Prigent-Tessier, A.2    Ferguson-Gottschall, S.3    Gu, Y.4    Gibori, G.5
  • 55
    • 33645806978 scopus 로고    scopus 로고
    • Cyclic and characteristic expression of phosphorylated Akt in human endometrium and decidual cells in vivo and in vitro
    • Toyofuku, A.; Hara, T.; Taguchi, T.; Katsura, Y.; Ohama, K.; Kudo, Y. Cyclic and characteristic expression of phosphorylated Akt in human endometrium and decidual cells in vivo and in vitro Hum. Reprod. 2006, 21 (5) 1122-8
    • (2006) Hum. Reprod. , vol.21 , Issue.5 , pp. 1122-8
    • Toyofuku, A.1    Hara, T.2    Taguchi, T.3    Katsura, Y.4    Ohama, K.5    Kudo, Y.6


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