메뉴 건너뛰기




Volumn 115, Issue 7, 2010, Pages 1319-1330

Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; LYSINE; PLASMINOGEN ACTIVATOR; PLG RKT; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG; UROKINASE RECEPTOR; COLONY STIMULATING FACTOR 1; DETERGENT; HOMEODOMAIN PROTEIN; MESSENGER RNA; PLASMINOGEN; PLG R(KT) PROTEIN, HUMAN; PLG-R(KT) PROTEIN, HUMAN; TRANSCRIPTION FACTOR HOXA9;

EID: 77949897126     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-11-188938     Document Type: Article
Times cited : (124)

References (78)
  • 1
    • 0022404962 scopus 로고
    • Plasminogen activation and regulation of pericellular proteolysis
    • Saksela O. Plasminogen activation and regulation of pericellular proteolysis. Biochim Biophys Acta. 1985(1):823:35-65.
    • (1985) Biochim Biophys Acta , vol.1 , Issue.823 , pp. 35-65
    • Saksela, O.1
  • 2
    • 0023741644 scopus 로고
    • Protease receptors on cell surfaces: New mechanistic formulas applied to an old problem
    • Testa JE, Quigley JP. Protease receptors on cell surfaces: new mechanistic formulas applied to an old problem. J Natl Cancer Inst. 1988;80(10):712-713.
    • (1988) J Natl Cancer Inst , vol.80 , Issue.10 , pp. 712-713
    • Testa, J.E.1    Quigley, J.P.2
  • 3
    • 0032521250 scopus 로고    scopus 로고
    • Plasminogen deficiency differentially affects recruitment of inflammatory cell populations in mice
    • Ploplis VA, French EL, Carmeliet P, Collen D, Plow EF. Plasminogen deficiency differentially affects recruitment of inflammatory cell populations in mice. Blood. 1998;91(6):2005-2009.
    • (1998) Blood , vol.91 , Issue.6 , pp. 2005-2009
    • Ploplis, V.A.1    French, E.L.2    Carmeliet, P.3    Collen, D.4    Plow, E.F.5
  • 4
    • 0033375846 scopus 로고    scopus 로고
    • A role of plasminogen in atherosclerosis and restenosis models in mice
    • Plow EF, Ploplis VA, Busuttil S, Carmeliet P, Collen D. A role of plasminogen in atherosclerosis and restenosis models in mice. Thromb Haemost. 1999;82(suppl 1):4-7.
    • (1999) Thromb Haemost , vol.82 , Issue.SUPPL. 1 , pp. 4-7
    • Plow, E.F.1    Ploplis, V.A.2    Busuttil, S.3    Carmeliet, P.4    Collen, D.5
  • 5
    • 3242710053 scopus 로고    scopus 로고
    • A central role for plasminogen in the inflammatory response to biomaterials
    • Busuttil SJ, Ploplis VA, Castellino FJ, et al. A central role for plasminogen in the inflammatory response to biomaterials. J Thromb Haemost. 2004;2(10):1798-1805.
    • (2004) J Thromb Haemost , vol.2 , Issue.10 , pp. 1798-1805
    • Busuttil, S.J.1    Ploplis, V.A.2    Castellino, F.J.3
  • 6
    • 36348985036 scopus 로고    scopus 로고
    • Histone H2B as a functionally important plasminogen receptor on macrophages
    • Das R, Burke T, Plow EF. Histone H2B as a functionally important plasminogen receptor on macrophages. Blood. 2007;110(10):3763-3772.
    • (2007) Blood , vol.110 , Issue.10 , pp. 3763-3772
    • Das, R.1    Burke, T.2    Plow, E.F.3
  • 7
    • 0033739699 scopus 로고    scopus 로고
    • Lactational competence and involution of the mouse mammary gland require plasminogen
    • Lund LR, Bjorn SF, Sternlicht MD, et al. Lactational competence and involution of the mouse mammary gland require plasminogen. Development. 2000;127(20):4481-4492.
    • (2000) Development , vol.127 , Issue.20 , pp. 4481-4492
    • Lund, L.R.1    Bjorn, S.F.2    Sternlicht, M.D.3
  • 8
    • 0030007064 scopus 로고    scopus 로고
    • Impaired wound healing in mice with a disrupted plasminogen gene
    • Romer J, Bugge TH, Pyke C, et al. Impaired wound healing in mice with a disrupted plasminogen gene. Nat Med. 1996;2(3):287-292.
    • (1996) Nat Med , vol.2 , Issue.3 , pp. 287-292
    • Romer, J.1    Bugge, T.H.2    Pyke, C.3
  • 9
    • 0033881033 scopus 로고    scopus 로고
    • Disruption of the plasminogen gene in mice abolishes wound healing after myocardial infarction
    • Creemers E, Cleutjens J, Smits J, et al. Disruption of the plasminogen gene in mice abolishes wound healing after myocardial infarction. Am J Pathol. 2000;156(6):1865-1873.
    • (2000) Am J Pathol , vol.156 , Issue.6 , pp. 1865-1873
    • Creemers, E.1    Cleutjens, J.2    Smits, J.3
  • 10
    • 0031972273 scopus 로고    scopus 로고
    • Increased plasminogen binding is associated with metastatic breast cancer cells: Differential expression of plasminogen binding proteins
    • Ranson M, Andronicos NM, O'Mullane MJ, Baker MS. Increased plasminogen binding is associated with metastatic breast cancer cells: differential expression of plasminogen binding proteins. Br J Cancer. 1998;77(10):1586-1597.
    • (1998) Br J Cancer , vol.77 , Issue.10 , pp. 1586-1597
    • Ranson, M.1    Andronicos, N.M.2    O'Mullane, M.J.3    Baker, M.S.4
  • 11
    • 0141993055 scopus 로고    scopus 로고
    • Plasminogen supports tumor growth through a fibrinogendependent mechanism linked to vascular patency
    • Palumbo JS, Talmage KE, Liu H, et al. Plasminogen supports tumor growth through a fibrinogendependent mechanism linked to vascular patency. Blood. 2003;102(8):2819-2827.
    • (2003) Blood , vol.102 , Issue.8 , pp. 2819-2827
    • Palumbo, J.S.1    Talmage, K.E.2    Liu, H.3
  • 12
    • 9644276729 scopus 로고    scopus 로고
    • Angiostatin directly inhibits human prostate tumor cell invasion by blocking plasminogen binding to its cellular receptor, CD26
    • Gonzalez-Gronow M, Grenett HE, Gawdi G, Pizzo SV. Angiostatin directly inhibits human prostate tumor cell invasion by blocking plasminogen binding to its cellular receptor, CD26. Exp Cell Res. 2005;303(1):22-31.
    • (2005) Exp Cell Res , vol.303 , Issue.1 , pp. 22-31
    • Gonzalez-Gronow, M.1    Grenett, H.E.2    Gawdi, G.3    Pizzo, S.V.4
  • 13
    • 0142061003 scopus 로고    scopus 로고
    • Plasmin generation dependent on alpha-enolase-type plasminogen receptor is required for myogenesis
    • López-Alemany R, Suelves M, Munoz-Canoves P. Plasmin generation dependent on alpha-enolase-type plasminogen receptor is required for myogenesis. Thromb Haemost. 2003;90(4):724-733.
    • (2003) Thromb Haemost , vol.90 , Issue.4 , pp. 724-733
    • López-Alemany, R.1    Suelves, M.2    Munoz-Canoves, P.3
  • 14
    • 0035816635 scopus 로고    scopus 로고
    • Proteolytic cleavage of chromogranin a (CgA) by plasmin: Selective liberation of a specific bioactive CgA fragment that regulates catecholamine release
    • Jiang Q, Taupenot L, Mahata SK, et al. Proteolytic cleavage of chromogranin A (CgA) by plasmin: selective liberation of a specific bioactive CgA fragment that regulates catecholamine release. J Biol Chem. 2001;276(27):25022-25029.
    • (2001) J Biol Chem , vol.276 , Issue.27 , pp. 25022-25029
    • Jiang, Q.1    Taupenot, L.2    Mahata, S.K.3
  • 15
    • 0037024540 scopus 로고    scopus 로고
    • The local chromaffin cell plasminogen/plasmin system and the regulation of catecholamine secretion
    • Jiang Q, Yasothornsrikul S, Taupenot L, Miles LA, Parmer RJ. The local chromaffin cell plasminogen/plasmin system and the regulation of catecholamine secretion. Ann N Y Acad Sci. 2002;971:445-449.
    • (2002) Ann N Y Acad Sci , vol.971 , pp. 445-449
    • Jiang, Q.1    Yasothornsrikul, S.2    Taupenot, L.3    Miles, L.A.4    Parmer, R.J.5
  • 16
    • 0035966011 scopus 로고    scopus 로고
    • Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation
    • Jacovina AT, Zhong F, Khazanova E, et al. Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation. J Biol Chem. 2001;276(52):49350-49358.
    • (2001) J Biol Chem , vol.276 , Issue.52 , pp. 49350-49358
    • Jacovina, A.T.1    Zhong, F.2    Khazanova, E.3
  • 17
    • 77950379579 scopus 로고    scopus 로고
    • Role of the plasminogen activation system in hippocampal neuritogenesis
    • Bai H, Dehmelt L, Halpain S, et al. Role of the plasminogen activation system in hippocampal neuritogenesis. J Thromb Haemost. 2006;4(supp 1):146.
    • (2006) J Thromb Haemost , vol.4 , Issue.SUPPL. 1 , pp. 146
    • Bai, H.1    Dehmelt, L.2    Halpain, S.3
  • 18
    • 0022001189 scopus 로고
    • Binding and activation of plasminogen on the platelet surface
    • Miles LA, Plow EF. Binding and activation of plasminogen on the platelet surface. J Biol Chem. 1985;260(7):4303-4311.
    • (1985) J Biol Chem , vol.260 , Issue.7 , pp. 4303-4311
    • Miles, L.A.1    Plow, E.F.2
  • 19
    • 0022483249 scopus 로고
    • Activation of plasminogen by tissue plasminoagen activator on normal and thrombasthenic platelets: Effects on surface proteins and platelet aggregation
    • Stricker RB, Wong D, Tak Shiu D, Reyes PT, Shuman MA. Activation of plasminogen by tissue plasminoagen activator on normal and thrombasthenic platelets: effects on surface proteins and platelet aggregation. Blood. 1986;68(1):275-280.
    • (1986) Blood , vol.68 , Issue.1 , pp. 275-280
    • Stricker, R.B.1    Wong, D.2    Tak Shiu, D.3    Reyes, P.T.4    Shuman, M.A.5
  • 20
    • 0022978141 scopus 로고
    • Binding of plasminogen to cultured human endothelial cells
    • Hajjar KA, Harpel PC, Jaffe EA, Nachman RL. Binding of plasminogen to cultured human endothelial cells. J Biol Chem. 1986;261(25):11656-11662.
    • (1986) J Biol Chem , vol.261 , Issue.25 , pp. 11656-11662
    • Hajjar, K.A.1    Harpel, P.C.2    Jaffe, E.A.3    Nachman, R.L.4
  • 21
    • 0025883277 scopus 로고
    • Plasminogen activation by receptor-bound urokinase: A kinetic study with both cell-associated and isolated receptor
    • Ellis V, Behrendt N, Dano K. Plasminogen activation by receptor-bound urokinase: a kinetic study with both cell-associated and isolated receptor. J Biol Chem. 1991;266(19):12752-12758.
    • (1991) J Biol Chem , vol.266 , Issue.19 , pp. 12752-12758
    • Ellis, V.1    Behrendt, N.2    Dano, K.3
  • 22
    • 0024399984 scopus 로고
    • Plasminogen binding to rat hepatocytes in primary culture and to thin slices of rat liver
    • Gonias SL, Braud LL, Geary WA, VandenBerg SR. Plasminogen binding to rat hepatocytes in primary culture and to thin slices of rat liver. Blood. 1989;74(2):729-736.
    • (1989) Blood , vol.74 , Issue.2 , pp. 729-736
    • Gonias, S.L.1    Braud, L.L.2    Geary, W.A.3    Vandenberg, S.R.4
  • 23
    • 0027935492 scopus 로고
    • Regulation of plasminogen activation by human U937 promonocytic cells
    • Duval-Jobe C, Parmely MJ. Regulation of plasminogen activation by human U937 promonocytic cells. J Biol Chem. 1994;269(33):21353-21357.
    • (1994) J Biol Chem , vol.269 , Issue.33 , pp. 21353-21357
    • Duval-Jobe, C.1    Parmely, M.J.2
  • 24
    • 0029805471 scopus 로고    scopus 로고
    • Characterization of cellular binding sites and interactive regions within reactants required for enhancement of plasminogen activation by tPA on the surface of leukocytic cells
    • Félez J, Miles LA, Fabregas P, et al. Characterization of cellular binding sites and interactive regions within reactants required for enhancement of plasminogen activation by tPA on the surface of leukocytic cells. Thromb Haemost. 1996;76(4):577-584.
    • (1996) Thromb Haemost , vol.76 , Issue.4 , pp. 577-584
    • Félez, J.1    Miles, L.A.2    Fabregas, P.3
  • 25
    • 0023025270 scopus 로고
    • The plasminogen system and cell surfaces: Evidence for plasminogen and urokinase receptors on the same cell type
    • Plow EF, Freaney DE, Plescia J, Miles LA. The plasminogen system and cell surfaces: Evidence for plasminogen and urokinase receptors on the same cell type. J Cell Biol. 1986;103(6 pt 1):2411-2420.
    • (1986) J Cell Biol , vol.103 , Issue.6 PART 1 , pp. 2411-2420
    • Plow, E.F.1    Freaney, D.E.2    Plescia, J.3    Miles, L.A.4
  • 27
    • 17244363565 scopus 로고    scopus 로고
    • Plasminogen receptors: The sine qua non of cell surface plasminogen activation
    • Miles LA, Hawley SB, Baik N, et al. Plasminogen receptors: the sine qua non of cell surface plasminogen activation. Front Biosci. 2005;10:1754-1762.
    • (2005) Front Biosci , vol.10 , pp. 1754-1762
    • Miles, L.A.1    Hawley, S.B.2    Baik, N.3
  • 28
    • 0025611638 scopus 로고
    • Plasminogen receptors in the mediation of pericellular proteolysis
    • Plow EF, Miles LA. Plasminogen receptors in the mediation of pericellular proteolysis. Cell Differ Dev. 1990;32(2):293-298.
    • (1990) Cell Differ Dev , vol.32 , Issue.2 , pp. 293-298
    • Plow, E.F.1    Miles, L.A.2
  • 29
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-Enolase as a candidate plasminogen receptor
    • Miles LA, Dahlberg CM, Plescia J, et al. Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-Enolase as a candidate plasminogen receptor. Biochemistry. 1991;30:1(6)682-1691.
    • (1991) Biochemistry , vol.30 , Issue.1-6 , pp. 682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3
  • 30
    • 0036843274 scopus 로고    scopus 로고
    • In vivo regulation of plasminogen function by plasma carboxypeptidase B
    • Swaisgood CM, Schmitt D, Eaton D, Plow EF. In vivo regulation of plasminogen function by plasma carboxypeptidase B. J Clin Invest. 2002;110(9):1275-1282.
    • (2002) J Clin Invest , vol.110 , Issue.9 , pp. 1275-1282
    • Swaisgood, C.M.1    Schmitt, D.2    Eaton, D.3    Plow, E.F.4
  • 31
    • 0028839088 scopus 로고
    • The role of an enolase-related molecule in plasminogen binding to cells
    • Redlitz A, Fowler BJ, Plow EF, Miles LA. The role of an enolase-related molecule in plasminogen binding to cells. Eur J Biochem. 1995;227(1-2):407-415.
    • (1995) Eur J Biochem , vol.227 , Issue.1-2 , pp. 407-415
    • Redlitz, A.1    Fowler, B.J.2    Plow, E.F.3    Miles, L.A.4
  • 32
    • 0035808318 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a
    • Hawley SB, Tamura T, Miles LA. Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a. J Biol Chem. 2001;276(1):179-186.
    • (2001) J Biol Chem , vol.276 , Issue.1 , pp. 179-186
    • Hawley, S.B.1    Tamura, T.2    Miles, L.A.3
  • 33
    • 33747093008 scopus 로고    scopus 로고
    • Identification of histone H2B as a regulated plasminogen receptor
    • Herren T, Burke TA, Das R, Plow EF. Identification of histone H2B as a regulated plasminogen receptor. Biochemistry. 2006;45(31):9463-9474.
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9463-9474
    • Herren, T.1    Burke, T.A.2    Das, R.3    Plow, E.F.4
  • 34
    • 0035253824 scopus 로고    scopus 로고
    • Plasminogen-mediated matrix invasion and degradation by macrophages is dependent on surface expression of annexin II
    • Falcone DJ, Borth W, Khan KM, Hajjar KA. Plasminogen-mediated matrix invasion and degradation by macrophages is dependent on surface expression of annexin II. Blood. 2001;97(3):777-784.
    • (2001) Blood , vol.97 , Issue.3 , pp. 777-784
    • Falcone, D.J.1    Borth, W.2    Khan, K.M.3    Hajjar, K.A.4
  • 35
    • 3843144977 scopus 로고    scopus 로고
    • Regulation of monocyte migration by amphoterin (HMGB1)
    • Rouhiainen A, Kuja-Panula J, Wilkman E, et al. Regulation of monocyte migration by amphoterin (HMGB1). Blood. 2004;104(4):1174-1182.
    • (2004) Blood , vol.104 , Issue.4 , pp. 1174-1182
    • Rouhiainen, A.1    Kuja-Panula, J.2    Wilkman, E.3
  • 36
    • 0032521473 scopus 로고    scopus 로고
    • Tissue factor regulates plasminogen binding and activation
    • Fan ZQ, Larson PJ, Bognacki J, et al. Tissue factor regulates plasminogen binding and activation. Blood. 1998;91(6):1987-1998.
    • (1998) Blood , vol.91 , Issue.6 , pp. 1987-1998
    • Fan, Z.Q.1    Larson, P.J.2    Bognacki, J.3
  • 37
    • 2342433057 scopus 로고    scopus 로고
    • Integrin alphaMbeta2 orchestrates and accelerates plasminogen activation and fibrinolysis by neutrophils
    • Pluskota E, Soloviev DA, Bdeir K, Cines DB, Plow EF. Integrin alphaMbeta2 orchestrates and accelerates plasminogen activation and fibrinolysis by neutrophils. J Biol Chem. 2004;279(17):18063-18072.
    • (2004) J Biol Chem , vol.279 , Issue.17 , pp. 18063-18072
    • Pluskota, E.1    Soloviev, D.A.2    Bdeir, K.3    Cines, D.B.4    Plow, E.F.5
  • 38
    • 0014932863 scopus 로고
    • Plasminogen: Purification from human plasma by affinity chromatography
    • Deutsch DG, Mertz ET. Plasminogen: purification from human plasma by affinity chromatography. Science. 1970;170(962):1995-1996.
    • (1970) Science , vol.170 , Issue.962 , pp. 1995-1996
    • Deutsch, D.G.1    Mertz, E.T.2
  • 39
    • 0033797198 scopus 로고    scopus 로고
    • Processing of chromogranin a by plasmin provides a novel mechanism for regulating catecholamine secretioin
    • Parmer RJ, Mahata M, Gong Y, et al. Processing of chromogranin A by plasmin provides a novel mechanism for regulating catecholamine secretioin. J Clin Invest. 2000;106(7):907-915.
    • (2000) J Clin Invest , vol.106 , Issue.7 , pp. 907-915
    • Parmer, R.J.1    Mahata, M.2    Gong, Y.3
  • 40
    • 0022973444 scopus 로고
    • Topography of the high-affinity lysine binding site of plasminogen as defined with a specific antibody probe
    • Miles LA, Plow EF. Topography of the high-affinity lysine binding site of plasminogen as defined with a specific antibody probe. Biochemistry. 1986;25(22):6926-6933.
    • (1986) Biochemistry , vol.25 , Issue.22 , pp. 6926-6933
    • Miles, L.A.1    Plow, E.F.2
  • 41
    • 33847777650 scopus 로고    scopus 로고
    • Quantitative expansion of ES cell-derived myeloid progenitors capable of differentiating into macrophages
    • Odegaard JI, Vats D, Zhang L, et al. Quantitative expansion of ES cell-derived myeloid progenitors capable of differentiating into macrophages. J Leukoc Biol. 2007;81(3):711-719.
    • (2007) J Leukoc Biol , vol.81 , Issue.3 , pp. 711-719
    • Odegaard, J.I.1    Vats, D.2    Zhang, L.3
  • 42
    • 33845612415 scopus 로고    scopus 로고
    • Cell-surface actin binds plasminogen and modulates neurotransmitter release from catecholaminergic cells
    • Miles LA, Andronicos NM, Baik N, Parmer RJ. Cell-surface actin binds plasminogen and modulates neurotransmitter release from catecholaminergic cells. J Neurosci. 2006;26(50):13017-13024.
    • (2006) J Neurosci , vol.26 , Issue.50 , pp. 13017-13024
    • Miles, L.A.1    Andronicos, N.M.2    Baik, N.3    Parmer, R.J.4
  • 43
    • 0033678175 scopus 로고    scopus 로고
    • Discriminating between cell surface and intracellular plasminogen-binding proteins: Heterogeneity in profibrinolytic plasminogen-binding proteins on monocytoid cells
    • Hawley SB, Green MA, Miles LA. Discriminating between cell surface and intracellular plasminogen-binding proteins: heterogeneity in profibrinolytic plasminogen-binding proteins on monocytoid cells. Thromb Haemost. 2000;84(5):882-890.
    • (2000) Thromb Haemost , vol.84 , Issue.5 , pp. 882-890
    • Hawley, S.B.1    Green, M.A.2    Miles, L.A.3
  • 44
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormick AL, Yates JRI. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom. 1994;5(6):976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , Issue.6 , pp. 976-989
    • Eng, J.K.1    McCormick, A.L.2    Yates, J.R.I.3
  • 45
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link AJ, Eng J, Schieltz DM, et al. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol. 1999;17(7):676-682.
    • (1999) Nat Biotechnol , vol.17 , Issue.7 , pp. 676-682
    • Link, A.J.1    Eng, J.2    Schieltz, D.M.3
  • 46
    • 0027298080 scopus 로고
    • Two-dimensional separations of peptides and proteins by comprehensive liquid chromatography-capillary electrophoresis
    • Larmann JP Jr, Lemmo AV, Moore AW Jr, Jorgenson JW. Two-dimensional separations of peptides and proteins by comprehensive liquid chromatography-capillary electrophoresis. Electrophoresis. 1993;14(5-6):439-447.
    • (1993) Electrophoresis , vol.14 , Issue.5-6 , pp. 439-447
    • Larmann Jr., J.P.1    Lemmo, A.V.2    Moore Jr., A.W.3    Jorgenson, J.W.4
  • 47
    • 0031184405 scopus 로고    scopus 로고
    • Two-dimensional SEC/RPLC coupled to mass spectrometry for the analysis of peptides
    • Opiteck GJ, Jorgenson JW. Two-dimensional SEC/RPLC coupled to mass spectrometry for the analysis of peptides. Anal Chem. 1997;69(13):2283-2291.
    • (1997) Anal Chem , vol.69 , Issue.13 , pp. 2283-2291
    • Opiteck, G.J.1    Jorgenson, J.W.2
  • 48
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters DA, Washburn MP, Yates JR III. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem. 2001;73(23):5683-5690.
    • (2001) Anal Chem , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 49
    • 24744455665 scopus 로고    scopus 로고
    • Automatic quality assessment of peptide tandem mass spectra
    • Bern M, Goldberg D, McDonald WH, Yates JR III. Automatic quality assessment of peptide tandem mass spectra. Bioinformatics. 2004;20(suppl 1):I49-I54.
    • (2004) Bioinformatics , vol.20 , Issue.SUPPL. 1
    • Bern, M.1    Goldberg, D.2    McDonald, W.H.3    Yates III, J.R.4
  • 50
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J Proteome Res. 2003;2(1):43-50.
    • (2003) J Proteome Res , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 51
    • 77950435999 scopus 로고    scopus 로고
    • International Protein Index (IPI). Accessed December 1
    • European Bioinformatics Institute. International Protein Index (IPI). http://www.ebi.ac.uk/IPI/IPIhelp.html. Accessed December 1, 2006.
    • (2006)
  • 52
    • 0031814022 scopus 로고    scopus 로고
    • Database searching using mass spectrometry data
    • Yates JR III. Database searching using mass spectrometry data. Electrophoresis. 1998;19(6):893-900.
    • (1998) Electrophoresis , vol.19 , Issue.6 , pp. 893-900
    • Yates III, J.R.1
  • 53
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates JR III. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res. 2002;1(1):21-26.
    • (2002) J Proteome Res , vol.1 , Issue.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 54
    • 0034007381 scopus 로고    scopus 로고
    • Elevated matrix metalloprotease and angiostatin levels in integrin alpha 1 knockout mice cause reduced tumor vascularization
    • Pozzi A, Moberg PE, Miles LA, et al. Elevated matrix metalloprotease and angiostatin levels in integrin alpha 1 knockout mice cause reduced tumor vascularization. Proc Natl Acad Sci U S A. 2000;97(5):2202-2207.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.5 , pp. 2202-2207
    • Pozzi, A.1    Moberg, P.E.2    Miles, L.A.3
  • 55
    • 0023624310 scopus 로고
    • Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells
    • Miles LA, Plow EF. Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells. Thromb Haemost. 1987;58(3):936-942.
    • (1987) Thromb Haemost , vol.58 , Issue.3 , pp. 936-942
    • Miles, L.A.1    Plow, E.F.2
  • 56
    • 33645318751 scopus 로고    scopus 로고
    • Quantitative production of macrophages or neutrophils ex vivo using conditional Hoxb8
    • Wang GG, Calvo KR, Pasillas MP, et al. Quantitative production of macrophages or neutrophils ex vivo using conditional Hoxb8. Nat Methods. 2006;3(4):287-293.
    • (2006) Nat Methods , vol.3 , Issue.4 , pp. 287-293
    • Wang, G.G.1    Calvo, K.R.2    Pasillas, M.P.3
  • 57
    • 0016809359 scopus 로고
    • Molecular biology of human plasminogen, II: Metabolism in physiological and some pathophysiological conditions in man
    • Collen D, Verstraete M. Molecular biology of human plasminogen, II: metabolism in physiological and some pathophysiological conditions in man. Thromb Diath Haemorrh Suppl. 1975;34(2):403-408.
    • (1975) Thromb Diath Haemorrh Suppl , vol.34 , Issue.2 , pp. 403-408
    • Collen, D.1    Verstraete, M.2
  • 58
    • 0027515051 scopus 로고
    • Competition between plasminogen and tissue plasminogen activator for cellular binding sites
    • Felez J, Chanquias CJ, Fabregas P, Plow EF, Miles LA. Competition between plasminogen and tissue plasminogen activator for cellular binding sites. Blood. 1993;82(8):2433-2441.
    • (1993) Blood , vol.82 , Issue.8 , pp. 2433-2441
    • Felez, J.1    Chanquias, C.J.2    Fabregas, P.3    Plow, E.F.4    Miles, L.A.5
  • 59
    • 77950441333 scopus 로고    scopus 로고
    • Basic Local Alignment Search Tool (BLAST). Accessed December 1
    • National Center for Biotechnology Information. Basic Local Alignment Search Tool (BLAST). http://www.ncbi.nlm.nih.gov/blast/Blast.cgi. Accessed December 1, 2006.
    • (2006)
  • 60
    • 77950438069 scopus 로고    scopus 로고
    • Wellcome Trust Sanger. Accessed June 11
    • Wellcome Trust Sanger. Ensembl. http://www.ensembl.org. Accessed June 11, 2009.
    • (2009)
  • 61
    • 77950389209 scopus 로고    scopus 로고
    • Single Nucleotide Polymorphism. Accessed March 8
    • National Center for Biotechnology Information. Single Nucleotide Polymorphism. http://www.ncbi.nlm.nih.gov/projects/SNP. Accessed March 8, 2009.
    • (2009)
  • 62
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnády GE, Simon I. Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J Mol Biol. 1998;283(2):489-506.
    • (1998) J Mol Biol , vol.283 , Issue.2 , pp. 489-506
    • Tusnády, G.E.1    Simon, I.2
  • 63
    • 41949125627 scopus 로고    scopus 로고
    • Contribution of positively charged flanking residues to the insertion of transmembrane helices into the endoplasmic reticulum
    • Lerch-Bader M, Lundin C, Kim H, Nilsson I, von Heijne G. Contribution of positively charged flanking residues to the insertion of transmembrane helices into the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2008;105(11):4127- 4132.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.11 , pp. 4127-4132
    • Lerch-Bader, M.1    Lundin, C.2    Kim, H.3    Nilsson, I.4    Von Heijne, G.5
  • 64
    • 77950375944 scopus 로고    scopus 로고
    • Accessed March 8, 2009
    • SPLIT 4.0 Server. http://split.pmfst.hr/split/4. Accessed March 8, 2009.
    • SPLIT 4.0 Server
  • 65
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature. 1989;341(6241):456-458.
    • (1989) Nature , vol.341 , Issue.6241 , pp. 456-458
    • Von Heijne, G.1
  • 66
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem. 1981;256(4):1604-1607.
    • (1981) J Biol Chem , vol.256 , Issue.4 , pp. 1604-1607
    • Bordier, C.1
  • 67
    • 0024597669 scopus 로고
    • Characterization of the cellular binding site for the urokinase-type plasminogen activator
    • Estreicher A, Wohlwend A, Belin D, Scleuning W-D, Vassalli JD. Characterization of the cellular binding site for the urokinase-type plasminogen activator. J Biol Chem. 1989;264(2):1180-1189.
    • (1989) J Biol Chem , vol.264 , Issue.2 , pp. 1180-1189
    • Estreicher, A.1    Wohlwend, A.2    Belin, D.3    Scleuning, W.-D.4    Vassalli, J.D.5
  • 69
    • 0023515489 scopus 로고
    • Binding of tissue plasminogen activator to cultured human endothelial cells
    • Hajjar KA, Hamel NM, Harpel PC, Nachman RL. Binding of tissue plasminogen activator to cultured human endothelial cells. J Clin Invest. 1987;80(6):1712-1719.
    • (1987) J Clin Invest , vol.80 , Issue.6 , pp. 1712-1719
    • Hajjar, K.A.1    Hamel, N.M.2    Harpel, P.C.3    Nachman, R.L.4
  • 70
    • 0023737274 scopus 로고
    • The cell-binding domains of plasminogen and their function in plasma
    • Miles LA, Dahlberg CM, Plow EF. The cell-binding domains of plasminogen and their function in plasma. J Biol Chem. 1988;263(24):11928-11934.
    • (1988) J Biol Chem , vol.263 , Issue.24 , pp. 11928-11934
    • Miles, L.A.1    Dahlberg, C.M.2    Plow, E.F.3
  • 71
    • 0026091437 scopus 로고
    • Binding of tissue plasminogen activator to human monocytes and monocytoid cells
    • Felez J, Chanquia CJ, Levin EG, Miles LA, Plow EF. Binding of tissue plasminogen activator to human monocytes and monocytoid cells. Blood. 1991;78(4):2318-2327.
    • (1991) Blood , vol.78 , Issue.4 , pp. 2318-2327
    • Felez, J.1    Chanquia, C.J.2    Levin, E.G.3    Miles, L.A.4    Plow, E.F.5
  • 72
    • 0037007048 scopus 로고    scopus 로고
    • Large-scale analysis of the human and mouse transcriptomes
    • Su AI, Cooke MP, Ching KA, et al. Large-scale analysis of the human and mouse transcriptomes. Proc Natl Acad Sci U S A. 2002;99(7):4465-4470.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.7 , pp. 4465-4470
    • Su, A.I.1    Cooke, M.P.2    Ching, K.A.3
  • 73
    • 11144358198 scopus 로고    scopus 로고
    • A gene atlas of the mouse and human protein-encoding transcriptomes
    • Su AI, Wiltshire T, Batalov S, et al. A gene atlas of the mouse and human protein-encoding transcriptomes. Proc Natl Acad Sci U S A. 2004;101(16):6062- 6067.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.16 , pp. 6062-6067
    • Su, A.I.1    Wiltshire, T.2    Batalov, S.3
  • 74
    • 77950450935 scopus 로고    scopus 로고
    • Array Express Gene Expression ATLAS. Accessed August 19
    • European Bioinformatics Institute. Array Express Gene Expression ATLAS. http://www.ebi.ac.uk/gxa. Accessed August 19, 2009.
    • (2009)
  • 75
    • 0025163024 scopus 로고
    • The presence of plasmin receptors on three mammary carcinoma MCF-7 sublines
    • Correc P, Fondanèche M-C, Bracke M, Burtin P. The presence of plasmin receptors on three mammary carcinoma MCF-7 sublines. Int J Cancer. 1990;46(4):745-750.
    • (1990) Int J Cancer , vol.46 , Issue.4 , pp. 745-750
    • Correc, P.1    Fondanèche, M.-C.2    Bracke, M.3    Burtin, P.4
  • 76
    • 23744508957 scopus 로고    scopus 로고
    • Identification of novel mammalian growth regulatory factors by genome-scale quantitative image analysis
    • Harada JN, Bower KE, Orth AP, et al. Identification of novel mammalian growth regulatory factors by genome-scale quantitative image analysis. Genome Res. 2005;15(8):1136-1144.
    • (2005) Genome Res , vol.15 , Issue.8 , pp. 1136-1144
    • Harada, J.N.1    Bower, K.E.2    Orth, A.P.3
  • 77
    • 34147163862 scopus 로고    scopus 로고
    • Identification of a predictive gene expression signature of cervical lymph node metastasis in oral squamous cell carcinoma
    • Nguyen ST, Hasegawa S, Tsuda H, et al. Identification of a predictive gene expression signature of cervical lymph node metastasis in oral squamous cell carcinoma. Cancer Sci. 2007;98(5):740-746.
    • (2007) Cancer Sci , vol.98 , Issue.5 , pp. 740-746
    • Nguyen, S.T.1    Hasegawa, S.2    Tsuda, H.3
  • 78
    • 33744482011 scopus 로고    scopus 로고
    • Plasminogen inhibits TNFα-induced apoptosis in monocytes
    • Mitchell JW, Baik N, Castellino FJ, Miles LA. Plasminogen inhibits TNFα-induced apoptosis in monocytes. Blood. 2006;107(11):4383-4390.
    • (2006) Blood , vol.107 , Issue.11 , pp. 4383-4390
    • Mitchell, J.W.1    Baik, N.2    Castellino, F.J.3    Miles, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.