메뉴 건너뛰기




Volumn 2011, Issue , 2011, Pages

Protein Profiling of human nonpigmented ciliary epithelium cell secretome: The differentiation factors characterization for retinal ganglion cell line

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; N METHYL DEXTRO ASPARTIC ACID; NEUROPEPTIDE; PROTEIN; PROTEOME; SIGNAL PEPTIDE;

EID: 80053578716     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2011/901329     Document Type: Article
Times cited : (7)

References (87)
  • 1
    • 44649172369 scopus 로고    scopus 로고
    • Endothelin-1 mediated regulation of extracellular matrix collagens in cells of human lamina cribrosa
    • Rao V. R., Krishnamoorthy R. R., Yorio T., Endothelin-1 mediated regulation of extracellular matrix collagens in cells of human lamina cribrosa Experimental Eye Research 2008 86 6 886 894
    • (2008) Experimental Eye Research , vol.86 , Issue.6 , pp. 886-894
    • Rao, V.R.1    Krishnamoorthy, R.R.2    Yorio, T.3
  • 2
    • 42749091665 scopus 로고    scopus 로고
    • Retinal ganglion cell neuroprotection in a rat model of glaucoma following brimonidine, latanoprost or combined treatments
    • Hernndez M., Urcola J. H., Vecino E., Retinal ganglion cell neuroprotection in a rat model of glaucoma following brimonidine, latanoprost or combined treatments Experimental Eye Research 2008 86 5 798 806
    • (2008) Experimental Eye Research , vol.86 , Issue.5 , pp. 798-806
    • Hernndez, M.1    Urcola, J.H.2    Vecino, E.3
  • 3
    • 33644655886 scopus 로고    scopus 로고
    • The number of people with glaucoma worldwide in 2010 and 2020
    • DOI 10.1136/bjo.2005.081224
    • Quigley H., Broman A. T., The number of people with glaucoma worldwide in 2010 and 2020 British Journal of Ophthalmology 2006 90 3 262 267 (Pubitemid 43325451)
    • (2006) British Journal of Ophthalmology , vol.90 , Issue.3 , pp. 262-267
    • Quigley, H.1    Broman, A.T.2
  • 4
    • 24644516739 scopus 로고    scopus 로고
    • Glaucoma: Macrocosm to microcosm. The Friedenwald Lecture
    • DOI 10.1167/iovs.04-1070
    • Quigley H. A., Glaucoma: macrocosm to microcosm the Friedenwald lecture Investigative Ophthalmology and Visual Science 2005 46 8 2663 2670 (Pubitemid 43086683)
    • (2005) Investigative Ophthalmology and Visual Science , vol.46 , Issue.8 , pp. 2663-2670
    • Quigley, H.A.1
  • 5
    • 0034063141 scopus 로고    scopus 로고
    • Retinal ganglion cell death in experimental glaucoma
    • DOI 10.1136/bjo.84.3.303
    • Morgan J. E., Uchida H., Caprioli J., Retinal ganglion cell death in experimental glaucoma British Journal of Ophthalmology 2000 84 3 303 310 (Pubitemid 30251688)
    • (2000) British Journal of Ophthalmology , vol.84 , Issue.3 , pp. 303-310
    • Morgan, J.E.1    Uchida, H.2    Caprioli, J.3
  • 7
    • 17044366269 scopus 로고    scopus 로고
    • Aquaporins as targets for drug discovery
    • Castle N. A., Aquaporins as targets for drug discovery Drug Discovery Today 2005 10 7 485 493
    • (2005) Drug Discovery Today , vol.10 , Issue.7 , pp. 485-493
    • Castle, N.A.1
  • 9
    • 0017551138 scopus 로고
    • Fluorescein angiographic defects of the optic disc in glaucoma
    • Schwartz B., Rieser J. C., Fishbein S. L., Fluorescein angiographic defects of the optic disc in glaucoma Archives of Ophthalmology 1977 95 11 1961 1974
    • (1977) Archives of Ophthalmology , vol.95 , Issue.11 , pp. 1961-1974
    • Schwartz, B.1    Rieser, J.C.2    Fishbein, S.L.3
  • 10
    • 0021237733 scopus 로고
    • Thy-1 antigen: A ganglion cell specific marker in rodent retina
    • DOI 10.1016/0306-4522(84)90195-7
    • Barnstable C. J., Drager U. C., Thy-1 antigen: a ganglion cell specific marker in rodent retina Neuroscience 1984 11 4 847 855 (Pubitemid 14111174)
    • (1984) Neuroscience , vol.11 , Issue.4 , pp. 847-855
    • Barnstable, C.J.1    Drager, U.C.2
  • 11
    • 0029588473 scopus 로고
    • Immune effector mechanisms required for protection to rabies virus
    • DOI 10.1006/viro.1995.0049
    • Xiang Z. Q., Knowles B. B., McCarrick J. W., Ertl H. C. J., Immune effector mechanisms required for protection to rabies virus Virology 1995 214 2 398 404 (Pubitemid 26027768)
    • (1995) Virology , vol.214 , Issue.2 , pp. 398-404
    • Xiang, Z.Q.1    Knowles, B.B.2    McCarrick, J.W.3    Ertl, H.C.J.4
  • 12
    • 0037473953 scopus 로고    scopus 로고
    • Protective effect of nilvadipine against glutamate neurotoxicity in purified retinal ganglion cells
    • DOI 10.1016/S0006-8993(02)03951-3, PII S0006899302039513
    • Otori Y., Kusaka S., Kawasaki A., Morimura H., Miki A., Tano Y., Protective effect of nilvadipine against glutamate neurotoxicity in purified retinal ganglion cells Brain Research 2003 961 2 213 219 (Pubitemid 36071582)
    • (2003) Brain Research , vol.961 , Issue.2 , pp. 213-219
    • Otori, Y.1    Kusaka, S.2    Kawasaki, A.3    Morimura, H.4    Miki, A.5    Tano, Y.6
  • 13
    • 0033056139 scopus 로고    scopus 로고
    • Differential gene expression in the human ciliary epithelium
    • DOI 10.1016/S1350-9462(98)00026-3, PII S1350946298000263
    • Coca-Prados M., Escribano J., Ortego J., Differential gene expression in the human ciliary epithelium Progress in Retinal and Eye Research 1999 18 3 403 429 (Pubitemid 29092614)
    • (1999) Progress in Retinal and Eye Research , vol.18 , Issue.3 , pp. 403-429
    • Coca-Prados, M.1    Escribano, J.2    Ortego, J.3
  • 14
    • 0028874426 scopus 로고
    • Isolation and characterization of cell-specific cDNA clones from a subtractive library of the ocular ciliary body of a single normal human donor: Transcription and synthesis of plasma proteins
    • Escribano J., Ortego J., Coca-Prados M., Isolation and characterization of cell-specific cDNA clones from a subtractive library of the ocular ciliary body of a single normal human donor: transcription and synthesis of plasma proteins Journal of Biochemistry 1995 118 5 921 931
    • (1995) Journal of Biochemistry , vol.118 , Issue.5 , pp. 921-931
    • Escribano, J.1    Ortego, J.2    Coca-Prados, M.3
  • 15
    • 0030800670 scopus 로고    scopus 로고
    • Molecular characterization and differential gene induction of the neuroendocrine-specific genes neurotensin, neurotensin receptor, PC1, PC2, and 7B2 in the human ocular ciliary epithelium
    • Ortego J., Coca-Prados M., Molecular characterization and differential gene induction of the neuroendocrine-specific genes neurotensin, neurotensin receptor, PC1, PC2, and 7B2 in the human ocular ciliary epithelium Journal of Neurochemistry 1997 69 5 1829 1839 (Pubitemid 27452727)
    • (1997) Journal of Neurochemistry , vol.69 , Issue.5 , pp. 1829-1839
    • Ortego, J.1    Coca-Prados, M.2
  • 17
    • 16344363037 scopus 로고    scopus 로고
    • Proteomic analysis of human pleural effusion
    • Tyan Y. C., Wu H. Y., Su W. C., Chen P. W., Liao P. C., Proteomic analysis of human pleural effusion Proteomics 2005 5 4 1062 1074
    • (2005) Proteomics , vol.5 , Issue.4 , pp. 1062-1074
    • Tyan, Y.C.1    Wu, H.Y.2    Su, W.C.3    Chen, P.W.4    Liao, P.C.5
  • 18
    • 23944498611 scopus 로고    scopus 로고
    • Proteomic profiling of human pleural effusion using two-dimensional nano liquid chromatography tandem mass spectrometry
    • Tyan Y. C., Wu H. Y., Lai W. W., Su W. C., Liao P. C., Proteomic profiling of human pleural effusion using two-dimensional nano liquid chromatography tandem mass spectrometry Journal of Proteome Research 2005 4 4 1274 1286
    • (2005) Journal of Proteome Research , vol.4 , Issue.4 , pp. 1274-1286
    • Tyan, Y.C.1    Wu, H.Y.2    Lai, W.W.3    Su, W.C.4    Liao, P.C.5
  • 19
    • 0034602654 scopus 로고    scopus 로고
    • Analysis of receptor signaling pathways by mass spectrometry: Identification of Vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors
    • DOI 10.1073/pnas.97.1.179
    • Pandey A., Podtelejnikov A. V., Blagoev B., Bustelo X. R., Mann M., Lodish H. F., Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors Proceedings of the National Academy of Sciences of the United States of America 2000 97 1 179 184 (Pubitemid 30055804)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.1 , pp. 179-184
    • Pandey, A.1    Podtelejnikov, A.V.2    Blagoev, B.3    Bustelo, X.R.4    Mann, M.5    Lodish, H.F.6
  • 21
    • 0043122944 scopus 로고    scopus 로고
    • ExPASy: The proteomics server for in-depth protein knowledge and analysis
    • DOI 10.1093/nar/gkg563
    • Gasteiger E., Gattiker A., Hoogland C., Ivanyi I., Appel R. D., Bairoch A., ExPASy: the proteomics server for in-depth protein knowledge and analysis Nucleic Acids Research 2003 31 13 3784 3788 (Pubitemid 37442246)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3784-3788
    • Gasteiger, E.1    Gattiker, A.2    Hoogland, C.3    Ivanyi, I.4    Appel, R.D.5    Bairoch, A.6
  • 22
    • 77950641486 scopus 로고    scopus 로고
    • Workflow comparison for label-free, quantitative secretome proteomics for cancer biomarker discovery: Method evaluation, differential analysis, and verification in serum
    • Piersma S. R., Fiedler U., Span S., Lingnau A., Pham T. V., Hoffmann S., Kubbutat M. H. G., Jiménez C. R., Workflow comparison for label-free, quantitative secretome proteomics for cancer biomarker discovery: method evaluation, differential analysis, and verification in serum Journal of Proteome Research 2010 9 4 1913 1922
    • (2010) Journal of Proteome Research , vol.9 , Issue.4 , pp. 1913-1922
    • Piersma, S.R.1    Fiedler, U.2    Span, S.3    Lingnau, A.4    Pham, T.V.5    Hoffmann, S.6    Kubbutat, M.H.G.7    Jiménez, C.R.8
  • 23
    • 77957755656 scopus 로고    scopus 로고
    • Secretome proteomics for discovery of cancer biomarkers
    • Makridakis M., Vlahou A., Secretome proteomics for discovery of cancer biomarkers Journal of Proteomics 2010 73 12 2291 2305
    • (2010) Journal of Proteomics , vol.73 , Issue.12 , pp. 2291-2305
    • Makridakis, M.1    Vlahou, A.2
  • 24
    • 34247133868 scopus 로고    scopus 로고
    • Approaches to the study of the cell secretome
    • DOI 10.1586/14789450.4.2.239
    • Hathout Y., Approaches to the study of the cell secretome Expert Review of Proteomics 2007 4 2 239 248 (Pubitemid 46588459)
    • (2007) Expert Review of Proteomics , vol.4 , Issue.2 , pp. 239-248
    • Hathout, Y.1
  • 29
    • 0033564455 scopus 로고    scopus 로고
    • POU domain factor Brn-3b is essential for retinal ganglion cell differentiation and survival but not for initial cell fate specification
    • DOI 10.1006/dbio.1999.9280
    • Gan L., Wang S. W., Huang Z., Klein W. H., POU domain factor Brn-3b is essential for retinal ganglion cell differentiation and survival but not for initial cell fate specification Developmental Biology 1999 210 2 469 480 (Pubitemid 29283017)
    • (1999) Developmental Biology , vol.210 , Issue.2 , pp. 469-480
    • Gan, L.1    Wang, S.W.2    Huang, Z.3    Klein, W.H.4
  • 30
    • 0842346312 scopus 로고    scopus 로고
    • A gene regulatory hierarchy for retinal ganglion cell specification and differentiation
    • DOI 10.1016/j.semcdb.2003.09.009
    • Mu X., Klein W. H., A gene regulatory hierarchy for retinal ganglion cell specification and differentiation Seminars in Cell and Developmental Biology 2004 15 1 115 123 (Pubitemid 38177375)
    • (2004) Seminars in Cell and Developmental Biology , vol.15 , Issue.1 , pp. 115-123
    • Mu, X.1    Klein, W.H.2
  • 31
    • 0942287072 scopus 로고    scopus 로고
    • Proteogenomic mapping as a complementary method to perform genome annotation
    • DOI 10.1002/pmic.200300511
    • Jaffe J. D., Berg H. C., Church G. M., Proteogenomic mapping as a complementary method to perform genome annotation Proteomics 2004 4 1 59 77 (Pubitemid 38140875)
    • (2004) Proteomics , vol.4 , Issue.1 , pp. 59-77
    • Jaffe, J.D.1    Berg, H.C.2    Church, G.M.3
  • 32
    • 28444454083 scopus 로고    scopus 로고
    • 1-DE MS and 2-D LC-MS analysis of the mouse bronchoalveolar lavage proteome
    • DOI 10.1002/pmic.200500052
    • Guo Y., Ma S. F., Grigoryev D., Van Eyk J., Garcia J. G. N., 1-DE MS and 2-D LC-MS analysis of the mouse bronchoalveolar lavage proteome Proteomics 2005 5 17 4608 4624 (Pubitemid 41739938)
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4608-4624
    • Guo, Y.1    Ma, S.F.2    Grigoryev, D.3    Van Eyk, J.4    Garcia, J.G.N.5
  • 33
    • 0028867216 scopus 로고
    • Differential modulation of integrin receptors and extracellular matrix laminin by transforming growth factor- 1 in rat alveolar epithelial cells
    • Kumar N. M., Sigurdson S. L., Sheppard D., Lwebuga-Mukasa J. S., Differential modulation of integrin receptors and extracellular matrix laminin by transforming growth factor- 1 in rat alveolar epithelial cells Experimental Cell Research 1995 221 2 385 394
    • (1995) Experimental Cell Research , vol.221 , Issue.2 , pp. 385-394
    • Kumar, N.M.1    Sigurdson, S.L.2    Sheppard, D.3    Lwebuga-Mukasa, J.S.4
  • 36
    • 0028314882 scopus 로고
    • Modulation of thrombospondin expression during differentiation of embryonal carcinoma cells
    • Liska D. J., Hawkins R., Wikstrom K., Bornstein P., Modulation of thrombospondin expression during differentiation of embryonal carcinoma cells Journal of Cellular Physiology 1994 158 3 495 505 (Pubitemid 24094431)
    • (1994) Journal of Cellular Physiology , vol.158 , Issue.3 , pp. 495-505
    • Liska, D.J.1    Hawkins, R.2    Wikstrom, K.3    Bornstein, P.4
  • 37
    • 0028325423 scopus 로고
    • Modulation of thrombospondin receptor expression during HL-60 cell differentiation
    • Suchard S. J., Mansfield P. J., Dixit V. M., Modulation of thrombospondin receptor expression during HL-60 cell differentiation Journal of Immunology 1994 152 2 877 888 (Pubitemid 24072993)
    • (1994) Journal of Immunology , vol.152 , Issue.2 , pp. 877-888
    • Suchard, S.J.1    Mansfield, P.J.2    Dixit, V.M.3
  • 38
    • 0026650892 scopus 로고
    • Differentiation-controlled synthesis and binding of thrombospondin to granulosa cells
    • Dreyfus M., Dardik R., Suh B. S., Amsterdam A., Lahav J., Differentiation-controlled synthesis and binding of thrombospondin to granulosa cells Endocrinology 1992 130 5 2565 2570
    • (1992) Endocrinology , vol.130 , Issue.5 , pp. 2565-2570
    • Dreyfus, M.1    Dardik, R.2    Suh, B.S.3    Amsterdam, A.4    Lahav, J.5
  • 39
    • 0024245150 scopus 로고
    • Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo
    • DOI 10.1083/jcb.107.6.2737
    • O'Shea K. S., Dixit V. M., Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo Journal of Cell Biology 1988 107 6 2737 2748 (Pubitemid 19019408)
    • (1988) Journal of Cell Biology , vol.107 , Issue.6 , pp. 2737-2748
    • O'Shea, K.S.1    Dixit, V.M.2
  • 40
    • 49649084238 scopus 로고    scopus 로고
    • TSP-1 secreted by one marrow stroma cells contributes to retinal ganglion cell neurite outgrowth and survival
    • Yu K., Ge J., Summers J. B., Li F., Liu X., Ma P., Kaminski J., Zhuang J., TSP-1 secreted by one marrow stroma cells contributes to retinal ganglion cell neurite outgrowth and survival PLoS One 2008 3 6 1 11
    • (2008) PLoS One , vol.3 , Issue.6 , pp. 1-11
    • Yu, K.1    Ge, J.2    Summers, J.B.3    Li, F.4    Liu, X.5    Ma, P.6    Kaminski, J.7    Zhuang, J.8
  • 41
    • 0030062183 scopus 로고    scopus 로고
    • Association of thrombospondin-1 with osteogenic differentiation of retinal pericytes in vitro
    • Canfield A. E., Sutton A. B., Hoyland J. A., Schor A. M., Association of thrombospondin-1 with osteogenic differentiation of retinal pericytes in vitro Journal of Cell Science 1996 109 2 343 353 (Pubitemid 26057117)
    • (1996) Journal of Cell Science , vol.109 , Issue.2 , pp. 343-353
    • Canfield, A.E.1    Sutton, A.B.2    Hoyland, J.A.3    Schor, A.M.4
  • 42
    • 72449157009 scopus 로고    scopus 로고
    • Thrombospondin-2 and SPARC/osteonectin are critical regulators of bone remodeling
    • Delany A. M., Hankenson K. D., Thrombospondin-2 and SPARC/osteonectin are critical regulators of bone remodeling Journal of Cell Communication and Signaling 2009 3 3-4 227 238
    • (2009) Journal of Cell Communication and Signaling , vol.3 , Issue.34 , pp. 227-238
    • Delany, A.M.1    Hankenson, K.D.2
  • 44
    • 35548971113 scopus 로고    scopus 로고
    • Galectin 3-binding protein is a potential contaminant of recombinantly produced factor IX
    • DOI 10.1111/j.1365-2516.2007.01525.x
    • Blostein M., Cuerquis J., Galipeau J., Galectin 3-binding protein is a potential contaminant of recombinantly produced factor IX Haemophilia 2007 13 6 701 706 (Pubitemid 350018259)
    • (2007) Haemophilia , vol.13 , Issue.6 , pp. 701-706
    • Blostein, M.1    Cuerquis, J.2    Galipeau, J.3
  • 45
    • 33847339730 scopus 로고    scopus 로고
    • Combination of abundant protein depletion and Multi-Lectin Affinity Chromatography (M-LAC) for plasma protein biomarker discovery
    • DOI 10.1021/pr060413k
    • Plavina T., Wakshull E., Hancock W. S., Hincapie M., Combination of abundant protein depletion and multi-lectin affinity chromatography (M-LAC) for plasma protein biomarker discovery Journal of Proteome Research 2007 6 2 662 671 (Pubitemid 46340170)
    • (2007) Journal of Proteome Research , vol.6 , Issue.2 , pp. 662-671
    • Plavina, T.1    Wakshull, E.2    Hancock, W.S.3    Hincapie, M.4
  • 46
    • 0028923421 scopus 로고
    • The gene (LGALS3BP) encoding the serum protein 90K, associated with cancer and infection by the human immunodeficiency virus, maps at 17q25
    • Calabrese G., Sures I., Pompetti F., Natoli G., Palka G., Iacobelli S., The gene (LGALS3BP) encoding the serum protein 90K, associated with cancer and infection by the human immunodeficiency virus, maps at 17q25 Cytogenetics and Cell Genetics 1995 69 3-4 223 225
    • (1995) Cytogenetics and Cell Genetics , vol.69 , Issue.34 , pp. 223-225
    • Calabrese, G.1    Sures, I.2    Pompetti, F.3    Natoli, G.4    Palka, G.5    Iacobelli, S.6
  • 47
    • 0027229657 scopus 로고
    • Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain
    • Koths K., Taylor E., Halenbeck R., Casipit C., Wang A., Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain Journal of Biological Chemistry 1993 268 19 14245 14249 (Pubitemid 23195548)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.19 , pp. 14245-14249
    • Koths, K.1    Taylor, E.2    Halenbeck, R.3    Casipit, C.4    Wang, A.5
  • 48
    • 49649091570 scopus 로고    scopus 로고
    • Identification of galectin-3-binding protein as a factor secreted by tumor cells that stimulates interleukin-6 expression in the bone marrow stroma
    • Fukaya Y., Shimada H., Wang L. C., Zandi E., DeClerck Y. A., Identification of galectin-3-binding protein as a factor secreted by tumor cells that stimulates interleukin-6 expression in the bone marrow stroma Journal of Biological Chemistry 2008 283 27 18573 18581
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.27 , pp. 18573-18581
    • Fukaya, Y.1    Shimada, H.2    Wang, L.C.3    Zandi, E.4    Declerck, Y.A.5
  • 49
    • 0030745381 scopus 로고    scopus 로고
    • A goldfish Notch-3 homologue is expressed in neurogenic regions of embryonic, adult, and regenerating brain and retina
    • DOI 10.1002/(SICI)1520-6408(1997)20:3<208::AID-DVG4>3.0.CO;2-B
    • Sullivan S. A., Barthel L. K., Largent B. L., Raymond P. A., A goldfish Notch-3 homologue is expressed in neurogenic regions of embryonic, adult and regenerating brain and retina Developmental Genetics 1997 20 3 208 223 (Pubitemid 27284083)
    • (1997) Developmental Genetics , vol.20 , Issue.3 , pp. 208-223
    • Sullivan, S.A.1    Barthel, L.K.2    Largent, B.L.3    Raymond, P.A.4
  • 51
    • 0030273134 scopus 로고    scopus 로고
    • Expression of the Notch 3 intracellular domain in mouse central nervous system progenitor cells is lethal and leads to disturbed neural tube development
    • DOI 10.1016/0925-4773(96)00589-8, PII S0925477396005898
    • Lardelli M., Williams R., Mitsiadis T., Lendahl U., Expression of the Notch 3 intracellular domain in mouse central nervous system progenitor cells is lethal and leads to disturbed neural tube development Mechanisms of Development 1996 59 2 177 190 (Pubitemid 26379338)
    • (1996) Mechanisms of Development , vol.59 , Issue.2 , pp. 177-190
    • Lardelli, M.1    Williams, R.2    Mitsiadis, T.3    Lendahl, U.4
  • 53
    • 0034918750 scopus 로고    scopus 로고
    • Human follistatin-related protein: A structural homologue of follistatin with nuclear localization
    • DOI 10.1210/en.142.8.3426
    • Tortoriello D. V., Sidis Y., Holtzman D. A., Holmes W. E., Schneyer A. L., Human follistatin-related protein: a structural homologue of follistatin with nuclear localization Endocrinology 2001 142 8 3426 3434 (Pubitemid 32681749)
    • (2001) Endocrinology , vol.142 , Issue.8 , pp. 3426-3434
    • Tortoriello, D.V.1    Sidis, Y.2    Holtzman, D.A.3    Holmes, W.E.4    Schneyer, A.L.5
  • 54
    • 0036850778 scopus 로고    scopus 로고
    • 2 in cultured granulosa-luteal cells
    • Liu J., Vnttinen T., Hydén-Granskog C., Voutilainen R., Regulation of follistatin-related gene (FLRG) expression by protein kinase C and prostaglandin E(2) in cultured granulosa-luteal cells Molecular Human Reproduction 2002 8 11 992 997 (Pubitemid 35331803)
    • (2002) Molecular Human Reproduction , vol.8 , Issue.11 , pp. 992-997
    • Liu, J.1    Vanttinen, T.2    Hyden-Granskog, C.3    Voutilainen, R.4
  • 55
    • 11044233758 scopus 로고    scopus 로고
    • Follistatin-related protein gene (FRP) is expressed in the synovial tissues of rheumatoid arthritis, but its polymorphisms are not associated with genetic susceptibility
    • Ehara Y., Sakurai D., Tsuchiya N., Nakano K., Tanaka Y., Yamaguchi A., Tokunaga K., Follistatin-related protein gene (FRP) is expressed in the synovial tissues of rheumatoid arthritis, but its polymorphisms are not associated with genetic susceptibility Clinical and Experimental Rheumatology 2004 22 6 707 712 (Pubitemid 40045532)
    • (2004) Clinical and Experimental Rheumatology , vol.22 , Issue.6 , pp. 707-712
    • Ehara, Y.1    Sakurai, D.2    Tsuchiya, N.3    Nakano, K.4    Tanaka, Y.5    Yamaguchi, A.6    Tokunaga, K.7
  • 56
    • 0035234139 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: At the crossroads of cell-matrix communication
    • Brekken R. A., Sage E. H., SPARC, a matricellular protein: at the crossroads of cell-matrix communication Matrix Biology 2001 19 8 815 827
    • (2001) Matrix Biology , vol.19 , Issue.8 , pp. 815-827
    • Brekken, R.A.1    Sage, E.H.2
  • 57
    • 0035022957 scopus 로고    scopus 로고
    • SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury
    • Bradshaw A. D., Sage E. H., SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury Journal of Clinical Investigation 2001 107 9 1049 1054 (Pubitemid 32422898)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.9 , pp. 1049-1054
    • Bradshaw, A.D.1    Sage, E.H.2
  • 59
    • 20444493997 scopus 로고    scopus 로고
    • Secreted protein acidic and rich in cysteine produced by human melanoma cells modulates polymorphonuclear leukocyte recruitment and antitumor cytotoxic capacity
    • DOI 10.1158/0008-5472.CAN-04-1102
    • Alvarez M. J., Prada F., Salvatierra E., Bravo A. I., Lutzky V. P., Carbone C., Pitossi F. J., Chuluyan H. E., Podhajcer O. L., Secreted protein acidic and rich in cysteine produced by human melanoma cells modulates polymorphonuclear leukocyte recruitment and antitumor cytotoxic capacity Cancer Research 2005 65 12 5123 5132 (Pubitemid 40827321)
    • (2005) Cancer Research , vol.65 , Issue.12 , pp. 5123-5132
    • Alvarez, M.J.1    Prada, F.2    Salvatierra, E.3    Bravo, A.I.4    Lutzky, V.P.5    Carbone, C.6    Pitossi, F.J.7    Chuluyan, H.E.8    Podhajcer, O.L.9
  • 62
    • 34547565424 scopus 로고    scopus 로고
    • 83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2
    • DOI 10.1074/jbc.M610330200
    • Lee W., Choi K. S., Riddell J., Ip C., Ghosh D., Park J. H., Park Y. M., Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2 Journal of Biological Chemistry 2007 282 30 22011 22022 (Pubitemid 47195750)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.30 , pp. 22011-22022
    • Lee, W.1    Choi, K.-S.2    Riddell, J.3    Ip, C.4    Ghosh, D.5    Park, J.-H.6    Park, Y.-M.7
  • 64
    • 0035233637 scopus 로고    scopus 로고
    • Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down Syndrome
    • Kim S. H., Fountoulakis M., Cairns N., Lubec G., Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down Syndrome Journal of Neural Transmission, Supplement 2001 61 223 235 (Pubitemid 38085085)
    • (2001) Journal of Neural Transmission, Supplement , Issue.61 , pp. 223-235
    • Kim, S.H.1    Fountoulakis, M.2    Cairns, N.3    Lubec, G.4
  • 65
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • DOI 10.1038/40418
    • Lappalainen P., Drubin D. G., Cofilin promotes rapid actin filament turnover in vivo Nature 1997 388 6637 78 82 (Pubitemid 27283892)
    • (1997) Nature , vol.388 , Issue.6637 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 66
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • DOI 10.1083/jcb.138.4.771
    • McGough A., Pope B., Chiu W., Weeds A., Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function Journal of Cell Biology 1997 138 4 771 781 (Pubitemid 27365041)
    • (1997) Journal of Cell Biology , vol.138 , Issue.4 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 67
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima J., Toshima J. Y., Amano T., Yang N., Narumiya S., Mizuno K., Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation Molecular Biology of the Cell 2001 12 4 1131 1145 (Pubitemid 33052004)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 68
    • 0344131934 scopus 로고    scopus 로고
    • Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-σ (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas
    • DOI 10.1002/(SICI)1522-2683(19991001)20:14<2952::AID-ELPS2952>3.0. CO;2-H
    • Sinha P., Hutter G., Kottgen E., Dietel M., Schadendorf D., Lage H., Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-sigma (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas Electrophoresis 1999 20 2952 2960 (Pubitemid 29517227)
    • (1999) Electrophoresis , vol.20 , Issue.14 , pp. 2952-2960
    • Sinha, P.1    Hutter, G.2    Kottgen, E.3    Dletel, M.4    Schadendorf, D.5    Lage, H.6
  • 70
    • 0028004565 scopus 로고
    • Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development
    • DOI 10.1016/0092-8674(94)90199-6
    • Haugwitz M., Noegel A. A., Karakesisoglou J., Schleicher M., Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development Cell 1994 79 2 303 314 (Pubitemid 24324920)
    • (1994) Cell , vol.79 , Issue.2 , pp. 303-314
    • Haugwitz, M.1    Noegel, A.A.2    Karakesisoglou, J.3    Schleicher, M.4
  • 71
    • 0028212157 scopus 로고
    • Profilin mutations disrupt multiple actin-dependent processes during Drosophila development
    • Verheyen E. M., Cooley L., Profilin mutations disrupt multiple actin-dependent processes during Drosophila development Development 1994 120 4 717 728 (Pubitemid 24111539)
    • (1994) Development , vol.120 , Issue.4 , pp. 717-728
    • Verheyen, E.M.1    Cooley, L.2
  • 72
    • 34250822246 scopus 로고    scopus 로고
    • SELDI-TOF-MS ProteinChip array profiling of T-cell clones propagated in long-term culture identifies human profilin-1 as a potential bio-marker of immunosenescence
    • Mazzatti D. J., Pawelec G., Longdin R., Powell J. R., Forsey R. J., SELDI-TOF-MS ProteinChip array profiling of T-cell clones propagated in long-term culture identifies human profilin-1 as a potential bio-marker of immunosenescence Proteome Science 2007 5, article 7 1 13
    • (2007) Proteome Science , vol.57 , pp. 1-13
    • Mazzatti, D.J.1    Pawelec, G.2    Longdin, R.3    Powell, J.R.4    Forsey, R.J.5
  • 73
    • 36148972452 scopus 로고    scopus 로고
    • Profilin-1 is a negative regulator of mammary carcinoma aggressiveness
    • DOI 10.1038/sj.bjc.6604038, PII 6604038
    • Zou L., Jaramillo M., Whaley D., Wells A., Panchapakesa V., Das T., Roy P., Profilin-1 is a negative regulator of mammary carcinoma aggressiveness British Journal of Cancer 2007 97 10 1361 1371 (Pubitemid 350114790)
    • (2007) British Journal of Cancer , vol.97 , Issue.10 , pp. 1361-1371
    • Zou, L.1    Jaramillo, M.2    Whaley, D.3    Wells, A.4    Panchapakesa, V.5    Das, T.6    Roy, P.7
  • 76
    • 1842367267 scopus 로고    scopus 로고
    • Differential expression of galectin-1 and galectin-3 during first trimester human embryogenesis
    • DOI 10.1002/(SICI)1097-0177(199708)209:4<399::AID-AJA7>3.0.CO;2-D
    • Van Den Brle F. A., Fernandez P. L., Buicu C., Liu F. U. T., Jackers P., Lambotte R., Castronovo V., Differential expression of galectin-1 and galectin-3 during first trimester human embryogenesis Developmental Dynamics 1997 209 4 399 405 (Pubitemid 27328466)
    • (1997) Developmental Dynamics , vol.209 , Issue.4 , pp. 399-405
    • Van Den Brule, F.A.1    Fernandez, P.L.2    Buicu, C.3    Liu, F.U.-T.4    Jackers, P.5    Lambotte, R.6    Castronovo, V.7
  • 77
    • 18044374479 scopus 로고    scopus 로고
    • Galectin-1 as a potential cancer target
    • DOI 10.1038/sj.bjc.6602493
    • Rabinovich G. A., Galectin-1 as a potential cancer target British Journal of Cancer 2005 92 7 1188 1192 (Pubitemid 40604390)
    • (2005) British Journal of Cancer , vol.92 , Issue.7 , pp. 1188-1192
    • Rabinovich, G.A.1
  • 78
    • 34250686672 scopus 로고    scopus 로고
    • Perinatal diagnosis of malignant hyperthermia susceptibility [12]
    • Stowell K., Pollock N., Langton E., Perinatal diagnosis of malignant hyperthermia susceptibility Anaesthesia and Intensive Care 2007 35 3 454 455 (Pubitemid 46938817)
    • (2007) Anaesthesia and Intensive Care , vol.35 , Issue.3 , pp. 454-455
    • Stowell, K.1    Pollock, N.2    Langton, E.3
  • 79
    • 0030766193 scopus 로고    scopus 로고
    • Concepts of tumor lectinology
    • Gabius H. J., Concepts of tumor lectinology Cancer Investigation 1997 15 5 454 464
    • (1997) Cancer Investigation , vol.15 , Issue.5 , pp. 454-464
    • Gabius, H.J.1
  • 80
    • 0038823600 scopus 로고    scopus 로고
    • Prognostic values of galectin-3 and the macrophage migration inhibitory factor (MIF) in human colorectal cancers
    • DOI 10.1097/01.MP.0000068235.45178.C1
    • Legendre H., Decaestecker C., Nagy N., Hendlisz A., Schring M. P., Salmon I., Gabius H. J., Pector J. C., Kiss R., Prognostic values of galectin-3 and the macrophage migration inhibitory factor (MIF) in human colorectal cancers Modern Pathology 2003 16 5 491 504 (Pubitemid 36618470)
    • (2003) Modern Pathology , vol.16 , Issue.5 , pp. 491-504
    • Legendre, H.1    Decaestecker, C.2    Nagy, N.3    Hendlisz, A.4    Schuring, M.-P.5    Salmon, I.6    Gabius, H.-J.7    Pector, J.-C.8    Kiss, R.9
  • 81
    • 18044396712 scopus 로고    scopus 로고
    • On the role of galectin-3 in cancer apoptosis
    • DOI 10.1007/s10495-005-0801-y
    • Nakahara S., Oka N., Raz A., On the role of galectin-3 in cancer apoptosis Apoptosis 2005 10 2 267 275 (Pubitemid 40603482)
    • (2005) Apoptosis , vol.10 , Issue.2 , pp. 267-275
    • Nakahara, S.1    Oka, N.2    Raz, A.3
  • 82
    • 0037081723 scopus 로고    scopus 로고
    • The effect of galectin-1 on the differentiation of fibroblasts and myoblasts in vitro
    • Goldring K., Jones G. E., Thiagarajah R., Watt D. J., The effect of galectin-1 on the differentiation of fibroblasts and myoblasts in vitro Journal of Cell Science 2002 115 2 355 366 (Pubitemid 34145185)
    • (2002) Journal of Cell Science , vol.115 , Issue.2 , pp. 355-366
    • Goldring, K.1    Jones, G.E.2    Thiagarajah, R.3    Watt, D.J.4
  • 83
    • 9944222484 scopus 로고    scopus 로고
    • Galectin-1 induces nuclear translocation of endonuclease G in caspase- and cytochrome c-independent T cell death
    • DOI 10.1038/sj.cdd.4401485
    • Hahn H. P., Pang M., He J., Hernandez J. D., Yang R. Y., Li L. Y., Wang X., Liu F. T., Baum L. G., Galectin-1 induces nuclear translocation of endonuclease G in caspase- and cytochrome c-independent T cell death Cell Death and Differentiation 2004 11 12 1277 1286 (Pubitemid 39591773)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.12 , pp. 1277-1286
    • Hahn, H.P.1    Pang, M.2    He, J.3    Hernandez, J.D.4    Yang, R.-Y.5    Li, L.Y.6    Wang, X.7    Liu, F.-T.8    Baum, L.G.9
  • 84
    • 0033071024 scopus 로고    scopus 로고
    • Induction of differentiation and apoptosis in the prostate cancer cell line LNCaP by sodium butyrate and galectin-1
    • Ellerhorst J., Nguyen T., Cooper D. N., Estrov Y., Lotan D., Lotan R., Induction of differentiation and apoptosis in the prostate cancer cell line LNCaP by sodium butyrate and galectin-1 International Journal of Oncology 1999 14 225 232
    • (1999) International Journal of Oncology , vol.14 , pp. 225-232
    • Ellerhorst, J.1    Nguyen, T.2    Cooper, D.N.3    Estrov, Y.4    Lotan, D.5    Lotan, R.6
  • 86
    • 0029077050 scopus 로고
    • Quantification of myotrophin from spontaneously hypertensive and normal rat hearts
    • Sil P., Mukherjee D., Sen S., Quantification of myotrophin from spontaneously hypertensive and normal rat hearts Circulation Research 1995 76 6 1020 1027
    • (1995) Circulation Research , vol.76 , Issue.6 , pp. 1020-1027
    • Sil, P.1    Mukherjee, D.2    Sen, S.3
  • 87
    • 0027507022 scopus 로고
    • Myotrophin induces early response genes and enhances cardiac gene expression
    • Mukherjee D. P., McTiernan C. F., Sen S., Myotrophin induces early response genes and enhances cardiac gene expression Hypertension 1993 21 2 142 148 (Pubitemid 23035066)
    • (1993) Hypertension , vol.21 , Issue.2 , pp. 142-148
    • Mukherjee, D.P.1    McTiernan, C.F.2    Sen, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.