메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

α-enolase, a multifunctional protein: Its role on pathophysiological situations

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ENOLASE; DESMIN; INTERLEUKIN 8; PLASMINOGEN; ENOLASE;

EID: 84869025512     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2012/156795     Document Type: Review
Times cited : (319)

References (142)
  • 1
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional α-enolase: Its role in diseases
    • Pancholi V., Multifunctional α -enolase: its role in diseases. Cellular and Molecular Life Sciences 2001 58 7 902 920 2-s2.0-0034947535 (Pubitemid 32652817)
    • (2001) Cellular and Molecular Life Sciences , vol.58 , Issue.7 , pp. 902-920
    • Pancholi, V.1
  • 3
    • 0018103888 scopus 로고
    • Functional properties of neuronal and glial isoenzymes of brain enolase
    • Marangos P. J., Parma A. M., Goodwin F. K., Functional properties of neuronal and glial isoenzymes of brain enolase. Journal of Neurochemistry 1978 31 3 727 732 2-s2.0-0018103888 (Pubitemid 8401303)
    • (1978) Journal of Neurochemistry , vol.31 , Issue.3 , pp. 727-732
    • Marangos, P.J.1    Parma, A.M.2    Goodwin, F.K.3
  • 4
    • 0025372882 scopus 로고
    • The gene for the muscle-specific enolase is on the short arm of human chromosome 17
    • DOI 10.1016/0888-7543(90)90467-9
    • Feo S., Oliva D., Barbieri G., Xu W., Fried M., Giallongo A., The gene for the muscle-specific enolase is on the short arm of human chromosome 17. Genomics 1990 6 1 192 194 2-s2.0-0025372882 10.1016/0888-7543(90)90467-9 (Pubitemid 20172373)
    • (1990) Genomics , vol.6 , Issue.1 , pp. 192-194
    • Feo, S.1    Oliva, D.2    Barbieri, G.3    Xu, W.4    Fried, M.5    Giallongo, A.6
  • 5
    • 0038464170 scopus 로고
    • Molecular cloning and nucleotide sequence of a full-length cDNA for human α enolase
    • DOI 10.1073/pnas.83.18.6741
    • Giallongo A., Feo S., Moore R., Croce C. M., Showe L. C., Molecular cloning and nucleotide sequence of a full-length cDNA for human α enolase. Proceedings of the National Academy of Sciences of the United States of America 1986 83 18 6741 6745 2-s2.0-0038464170 (Pubitemid 16002309)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.18 , pp. 6741-6745
    • Giallongo, A.1    Feo, S.2    Moore, R.3
  • 6
    • 0017104529 scopus 로고
    • Enolase isoenzymes. III. Chromatographic and immunological characteristics of rat brain enolase
    • 2-s2.0-0017104529
    • Fletcher L., Rider C. C., Taylor C. B., Enolase isoenzymes. III. Chromatographic and immunological characteristics of rat brain enolase. Biochimica et Biophysica Acta 1976 452 1 245 252 2-s2.0-0017104529
    • (1976) Biochimica et Biophysica Acta , vol.452 , Issue.1 , pp. 245-252
    • Fletcher, L.1    Rider, C.C.2    Taylor, C.B.3
  • 7
    • 0020629120 scopus 로고
    • Immunoassay of human muscle enolase subunit in serum: A novel marker antigen for muscle diseases
    • Kato K., Okagawa Y., Suzuki F., Shimizu A., Mokuno K., Takahashi Y., Immunoassay of human muscle enolase subunit in serum: a novel marker antigen for muscle diseases. Clinica Chimica Acta 1983 131 1-2 75 85 2-s2.0-0020629120 (Pubitemid 13105536)
    • (1983) Clinica Chimica Acta , vol.131 , Issue.1-2 , pp. 75-85
    • Kato, K.1    Okagawa, Y.2    Suzuki, F.3
  • 8
    • 0024289934 scopus 로고
    • Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor
    • 2-s2.0-0024289934
    • Lebioda L., Stec B., Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Nature 1988 333 6174 683 686 2-s2.0-0024289934
    • (1988) Nature , vol.333 , Issue.6174 , pp. 683-686
    • Lebioda, L.1    Stec, B.2
  • 9
    • 0030827288 scopus 로고    scopus 로고
    • Mechanism of enolase: The crystal structure of asymmetric dimer enolase- 2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
    • DOI 10.1021/bi9712450
    • Zhang E., Brewer J. M., Minor W., Carreira L. A., Lebioda L., Mechanism of enolase: the crystal structure of asymmetric dimer enolase- 2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution. Biochemistry 1997 36 41 12526 12534 2-s2.0-0030827288 10.1021/bi9712450 (Pubitemid 27446676)
    • (1997) Biochemistry , vol.36 , Issue.41 , pp. 12526-12534
    • Zhang, E.1    Brewer, J.M.2    Minor, W.3    Carreira, L.A.4    Lebioda, L.5
  • 10
    • 45749150355 scopus 로고    scopus 로고
    • Structure of human α-enolase (hENO1), a multifunctional glycolytic enzyme
    • DOI 10.1107/S0907444908008561, PII S0907444908008561
    • Kang H. J., Jung S. K., Kim S. J., Chung S. J., Structure of human α -enolase (hENO1), a multifunctional glycolytic enzyme. Acta Crystallographica D 2008 64 6 651 657 2-s2.0-45749150355 10.1107/ S0907444908008561 (Pubitemid 351872066)
    • (2008) Acta Crystallographica Section D: Biological Crystallography , vol.64 , Issue.6 , pp. 651-657
    • Kang, H.J.1    Jung, S.-K.2    Kim, S.J.3    Chung, S.J.4
  • 11
    • 0020490759 scopus 로고
    • Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes
    • 2-s2.0-0020490759
    • McAlister L., Holland M. J., Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes. Journal of Biological Chemistry 1982 257 12 7181 7188 2-s2.0-0020490759
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.12 , pp. 7181-7188
    • McAlister, L.1    Holland, M.J.2
  • 12
    • 0020575745 scopus 로고
    • Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. The primary structure of a third yeast glyceraldehyde-3-phosphate dehydrogenase gene
    • Holland J. P., Labieniec L., Swimmer C., Holland M. J., Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. The primary structure of a third yeast glyceraldehyde-3-phosphate dehydrogenase gene. Journal of Biological Chemistry 1983 258 8 5291 5299 2-s2.0-0020575745 (Pubitemid 13096423)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.8 , pp. 5291-5299
    • Holland, J.P.1    Labieniec, L.2    Swimmer, C.3    Holland, M.J.4
  • 14
    • 0034604055 scopus 로고    scopus 로고
    • ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: Relationship with Myc promoter-binding protein 1 (MBP-1)
    • DOI 10.1016/S0014-5793(00)01494-0, PII S0014579300014940
    • Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A., ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Letters 2000 473 1 47 52 2-s2.0-0034604055 10.1016/S0014-5793(00)01494-0 (Pubitemid 30235183)
    • (2000) FEBS Letters , vol.473 , Issue.1 , pp. 47-52
    • Feo, S.1    Arcuri, D.2    Piddini, E.3    Passantino, R.4    Giallongo, A.5
  • 15
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: Identification of α -enolase as a candidate plasminogen receptor
    • 2-s2.0-0025819231
    • Miles L. A., Dahlberg C. M., Plescia J., Felez J., Kato K., Plow E. F., Role of cell-surface lysines in plasminogen binding to cells: identification of α -enolase as a candidate plasminogen receptor. Biochemistry 1991 30 6 1682 1691 2-s2.0-0025819231
    • (1991) Biochemistry , vol.30 , Issue.6 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5    Plow, E.F.6
  • 16
    • 0027948296 scopus 로고
    • Plasminogen binds specifically to α-enolase on rat neuronal plasma membrane
    • Nakajima K., Hamanoue M., Takemoto N., Hattori T., Kato K., Kohsaka S., Plasminogen binds specifically to α -enolase on rat neuronal plasma membrane. Journal of Neurochemistry 1994 63 6 2048 2057 2-s2.0-0027948296 (Pubitemid 24369977)
    • (1994) Journal of Neurochemistry , vol.63 , Issue.6 , pp. 2048-2057
    • Nakajima, K.1    Hamanoue, M.2    Takemoto, N.3    Hattori, T.4    Kato, K.5    Kohsaka, S.6
  • 17
    • 0027403372 scopus 로고
    • Isolation of a novel 45 kDa plasminogen receptor from human endothelial cells
    • DOI 10.1016/0049-3848(93)90044-O
    • Dudani A. K., Cummings C., Hashemi S., Ganz P. R., Isolation of a novel 45 kDa plasminogen receptor from human endothelial cells. Thrombosis Research 1993 69 2 185 196 2-s2.0-0027403372 10.1016/0049-3848(93)90044-O (Pubitemid 23068243)
    • (1993) Thrombosis Research , vol.69 , Issue.2 , pp. 185-196
    • Dudani, A.K.1    Cummings, C.2    Hashemi, S.3    Ganz, P.R.4
  • 18
    • 0028839088 scopus 로고
    • The role of an enolase-related molecule in plasminogen binding to cells
    • 2-s2.0-0028839088 10.1111/j.1432-1033.1995.tb20403.x
    • Redlitz A., Fowler B. J., Plow E. F., Miles L. A., The role of an enolase-related molecule in plasminogen binding to cells. European Journal of Biochemistry 1995 227 1-2 407 415 2-s2.0-0028839088 10.1111/j.1432-1033.1995. tb20403.x
    • (1995) European Journal of Biochemistry , vol.227 , Issue.1-2 , pp. 407-415
    • Redlitz, A.1    Fowler, B.J.2    Plow, E.F.3    Miles, L.A.4
  • 19
    • 0033680465 scopus 로고    scopus 로고
    • Antibodies to streptococcal surface enolase react with human α -enolase: Implications in poststreptococcal sequelae
    • 2-s2.0-0033680465 10.1086/317604
    • Fontan P. A., Pancholi V., Nociari M. M., Fischetti V. A., Antibodies to streptococcal surface enolase react with human α -enolase: implications in poststreptococcal sequelae. Journal of Infectious Diseases 2000 182 6 1712 1721 2-s2.0-0033680465 10.1086/317604
    • (2000) Journal of Infectious Diseases , vol.182 , Issue.6 , pp. 1712-1721
    • Fontan, P.A.1    Pancholi, V.2    Nociari, M.M.3    Fischetti, V.A.4
  • 20
    • 0025945872 scopus 로고
    • Neuronal survival factor from bovine brain is identical to neuron-specific enolase
    • Takei N., Kondo J., Nagaike K., Ohsawa K., Kato K., Kohsaka S., Neuronal survival factor from bovine brain is identical to neuron-specific enolase. Journal of Neurochemistry 1991 57 4 1178 1184 2-s2.0-0025945872 (Pubitemid 21922739)
    • (1991) Journal of Neurochemistry , vol.57 , Issue.4 , pp. 1178-1184
    • Takei, N.1    Kondo, J.2    Nagaike, K.3    Ohsawa, K.4    Kato, K.5    Kohsaka, S.6
  • 21
    • 0021984720 scopus 로고
    • Yeast heat-shock protein of M(r) 48,000 is an isoprotein of enolase
    • DOI 10.1038/315688a0
    • Iida H., Yahara I., Yeast heat-shock protein of M(r) 48,000 is an isoprotein of enolase. Nature 1985 315 6021 688 690 2-s2.0-0021984720 (Pubitemid 15232887)
    • (1985) Nature , vol.315 , Issue.6021 , pp. 688-690
    • Iida, H.1    Yahara, I.2
  • 22
    • 0028856318 scopus 로고
    • Non-neuronal enolase is an endothelial hypoxic stress protein
    • 2-s2.0-0028856318 10.1074/jbc.270.46.27752
    • Aaronson R. M., Graven K. K., Tucci M., McDonald R. J., Farber H. W., Non-neuronal enolase is an endothelial hypoxic stress protein. Journal of Biological Chemistry 1995 270 46 27752 27757 2-s2.0-0028856318 10.1074/jbc.270.46.27752
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.46 , pp. 27752-27757
    • Aaronson, R.M.1    Graven, K.K.2    Tucci, M.3    McDonald, R.J.4    Farber, H.W.5
  • 23
    • 0026609068 scopus 로고
    • Investigation of lens glycolytic enzymes: Species distribution and interaction with supramolecular order
    • 2-s2.0-0026609068
    • Mathur R. L., Reddy M. C., Yee S., Imbesi R., Groth-Vasselli B., Farnsworth P. N., Investigation of lens glycolytic enzymes: species distribution and interaction with supramolecular order. Experimental Eye Research 1992 54 2 253 260 2-s2.0-0026609068
    • (1992) Experimental Eye Research , vol.54 , Issue.2 , pp. 253-260
    • Mathur, R.L.1    Reddy, M.C.2    Yee, S.3    Imbesi, R.4    Groth-Vasselli, B.5    Farnsworth, P.N.6
  • 25
    • 0026693656 scopus 로고
    • Enolase is present at the centrosome of HeLa cells
    • 2-s2.0-0026693656 10.1016/0014-4827(92)90099-T
    • Johnstone S. A., Waisman D. M., Rattner J. B., Enolase is present at the centrosome of HeLa cells. Experimental Cell Research 1992 202 2 458 463 2-s2.0-0026693656 10.1016/0014-4827(92)90099-T
    • (1992) Experimental Cell Research , vol.202 , Issue.2 , pp. 458-463
    • Johnstone, S.A.1    Waisman, D.M.2    Rattner, J.B.3
  • 26
    • 0030908790 scopus 로고    scopus 로고
    • Biochemical characterization of the mouse muscle-specific enolase: Developmental changes in electrophoretic variants and selective binding to other proteins
    • Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J. D., Gros F., Lazar M., Keller A., Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins. Biochemical Journal 1997 323 3 791 800 2-s2.0-0030908790 (Pubitemid 27202351)
    • (1997) Biochemical Journal , vol.323 , Issue.3 , pp. 791-800
    • Merkulova, T.1    Lucas, M.2    Jabet, C.3    Lamande, N.4    Rouzeau, J.-D.5    Gros, F.6    Lazar, M.7    Keller, A.8
  • 27
    • 0034009502 scopus 로고    scopus 로고
    • Structural analysis of α-enolase: Mapping the functional domains involved in down-regulation of the c-myc protooncogene
    • DOI 10.1074/jbc.275.8.5958
    • Subramanian A., Miller D. M., Structural analysis of α -enolase: mapping the functional domains involved in down-regulation of the c-myc protooncogene. Journal of Biological Chemistry 2000 275 8 5958 5965 2-s2.0-0034009502 10.1074/jbc.275.8.5958 (Pubitemid 30115245)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , pp. 5958-5965
    • Subramanian, A.1    Miller, D.M.2
  • 28
    • 0033843657 scopus 로고    scopus 로고
    • Tumor markers in neuroendocrine tumors
    • Eriksson B., Öberg K., Stridsberg M., Tumor markers in neuroendocrine tumors. Digestion 2000 62 supplement 1 33 38 2-s2.0-0033843657 (Pubitemid 30665937)
    • (2000) Digestion , vol.62 , Issue.SUPPL. 1 , pp. 33-38
    • Eriksson, B.1    Oberg, K.2    Stridsberg, M.3
  • 29
    • 0028942282 scopus 로고
    • Clinical tumour markers in lung cancer
    • 2-s2.0-0028942282
    • Niklinski J., Furman M., Clinical tumour markers in lung cancer. European Journal of Cancer Prevention 1995 4 2 129 138 2-s2.0-0028942282
    • (1995) European Journal of Cancer Prevention , vol.4 , Issue.2 , pp. 129-138
    • Niklinski, J.1    Furman, M.2
  • 31
    • 0028236442 scopus 로고
    • Serum neurone-specific enolase and other neuroendocrine markers in lung cancer
    • DOI 10.1016/0959-8049(94)90519-3
    • Ledermann J. A., Serum neurone-specific enolase and other neuroendocrine markers in lung cancer. European Journal of Cancer A 1994 30 5 574 576 2-s2.0-0028236442 10.1016/0959-8049(94)90519-3 (Pubitemid 24164234)
    • (1994) European Journal of Cancer Part A: General Topics , vol.30 , Issue.5 , pp. 574-576
    • Ledermann, J.A.1
  • 32
    • 17844380283 scopus 로고    scopus 로고
    • Overexpression of alpha enolase in hepatitis C virus-related hepatocellular carcinoma: Association with tumor progression as determined by proteomic analysis
    • DOI 10.1002/pmic.200401022
    • Takashima M., Kuramitsu Y., Yokoyama Y., Iizuka N., Fujimoto M., Nishisaka T., Okita K., Oka M., Nakamura K., Overexpression of alpha enolase in hepatitis C virus-related hepatocellular carcinoma: association with tumor progression as determined by proteomic analysis. Proteomics 2005 5 6 1686 1692 2-s2.0-17844380283 10.1002/pmic.200401022 (Pubitemid 40593274)
    • (2005) Proteomics , vol.5 , Issue.6 , pp. 1686-1692
    • Takashima, M.1    Kuramitsu, Y.2    Yokoyama, Y.3    Iizuka, N.4    Fujimoto, M.5    Nishisaka, T.6    Okita, K.7    Oka, M.8    Nakamura, K.9
  • 33
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • DOI 10.1016/S0968-0004(98)01335-8, PII S0968000498013358
    • Jeffery C. J., Moonlighting proteins. Trends in Biochemical Sciences 1999 24 1 8 11 2-s2.0-0033048066 10.1016/S0968-0004(98)01335-8 (Pubitemid 29074455)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.1 , pp. 8-11
    • Jeffery, C.J.1
  • 34
    • 0031970686 scopus 로고    scopus 로고
    • Multifunctional lens crystallins and corneal enzymes: More than meets the eye
    • 2-s2.0-0031970686
    • Piatigorsky J., Multifunctional lens crystallins and corneal enzymes: more than meets the eye. Annals of the New York Academy of Sciences 1998 842 7 15 2-s2.0-0031970686
    • (1998) Annals of the New York Academy of Sciences , vol.842 , pp. 7-15
    • Piatigorsky, J.1
  • 36
    • 0022001189 scopus 로고
    • Binding and activation of plasminogen on the platelet surface
    • Miles L. A., Plow E. F., Binding and activation of plasminogen on the platelet surface. Journal of Biological Chemistry 1985 260 7 4303 4311 2-s2.0-0022001189 (Pubitemid 15091978)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.7 , pp. 4303-4311
    • Miles, L.A.1    Plow, E.F.2
  • 37
    • 0022978141 scopus 로고
    • Binding of plasminogen to cultured human endothelial cells
    • Hajjar K. A., Harpel P. C., Jaffe E. A., Nachman R. L., Binding of plasminogen to cultured human endothelial cells. Journal of Biological Chemistry 1986 261 25 11656 11662 2-s2.0-0022978141 (Pubitemid 17206086)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.25 , pp. 11656-11662
    • Hajjar, K.A.1    Harpel, P.C.2    Jaffe, E.A.3    Nachman, R.L.4
  • 38
    • 0023025270 scopus 로고
    • The plasminogen system and cell surfaces: Evidence for plasminogen and urokinase receptors on the same cell type
    • DOI 10.1083/jcb.103.6.2411
    • Plow E. F., Freaney D. E., Plescia J., Miles L. A., The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type. Journal of Cell Biology 1986 103 6 2411 2420 2-s2.0-0023025270 (Pubitemid 17216665)
    • (1986) Journal of Cell Biology , vol.103 , Issue.I6 , pp. 2411-2420
    • Plow, E.F.1    Freaney, D.E.2    Plescia, J.3    Miles, L.A.4
  • 39
    • 0023624310 scopus 로고
    • Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells
    • Miles L. A., Plow E. F., Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells. Thrombosis and Haemostasis 1987 58 3 936 942 2-s2.0-0023624310 (Pubitemid 18020467)
    • (1987) Thrombosis and Haemostasis , vol.58 , Issue.3 , pp. 936-942
    • Miles, L.A.1    Plow, E.F.2
  • 40
    • 0036906177 scopus 로고    scopus 로고
    • UPAR: A versatile signalling orchestrator
    • DOI 10.1038/nrm977
    • Blasi F., Carmeliet P., uPAR: a versatile signalling orchestrator. Nature Reviews Molecular Cell Biology 2002 3 12 932 943 2-s2.0-0036906177 10.1038/nrm977 (Pubitemid 35477371)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.12 , pp. 932-943
    • Blasi, F.1    Carmeliet, P.2
  • 41
    • 0033824172 scopus 로고    scopus 로고
    • Urokinase receptor and integrin partnership: Coordination of signaling for cell adhesion, migration and growth
    • 2-s2.0-0033824172 10.1016/S0955-0674(00)00140-X
    • Ossowski L., Aguirre-Ghiso J. A., Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth. Current Opinion in Cell Biology 2000 12 5 613 620 2-s2.0-0033824172 10.1016/S0955-0674(00)00140-X
    • (2000) Current Opinion in Cell Biology , vol.12 , Issue.5 , pp. 613-620
    • Ossowski, L.1    Aguirre-Ghiso, J.A.2
  • 42
    • 0028133563 scopus 로고
    • Purification of the plasmin receptor from human carcinoma cells and comparison to α-enolase
    • DOI 10.1016/0049-3848(94)90252-6
    • Lopez-Alemany R., Correc P., Camoin L., Burtin P., Purification of the plasmin receptor from human carcinoma cells and comparison to α -enolase. Thrombosis Research 1994 75 4 371 381 2-s2.0-0028133563 10.1016/0049-3848(94) 90252-6 (Pubitemid 24265070)
    • (1994) Thrombosis Research , vol.75 , Issue.4 , pp. 371-381
    • Lopez-Alemany, R.1    Correc, P.2    Camoin, L.3    Burtin, P.4
  • 43
    • 0028023538 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II
    • 2-s2.0-0028023538
    • Hajjar K. A., Jacovina A. T., Chacko J., An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II. Journal of Biological Chemistry 1994 269 33 21191 21197 2-s2.0-0028023538
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.33 , pp. 21191-21197
    • Hajjar, K.A.1    Jacovina, A.T.2    Chacko, J.3
  • 44
    • 0032374094 scopus 로고    scopus 로고
    • The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation
    • DOI 10.1021/bi981713l
    • Kassam G., Le B. H., Choi K. S., Kang H. M., Fitzpatrick S. L., Louie P., Waisman D. M., The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry 1998 37 48 16958 16966 2-s2.0-0032374094 10.1021/bi981713l (Pubitemid 28566773)
    • (1998) Biochemistry , vol.37 , Issue.48 , pp. 16958-16966
    • Kassam, G.1    Le, B.-H.2    Choi, K.-S.3    Kang, H.-M.4    Fitzpatrick, S.L.5    Louie, P.6    Waisman, D.M.7
  • 45
    • 33747093008 scopus 로고    scopus 로고
    • Identification of histone H2B as a regulated plasminogen receptor
    • DOI 10.1021/bi060756w
    • Herren T., Burke T. A., Das R., Plow E. F., Identification of histone H2B as a regulated plasminogen receptor. Biochemistry 2006 45 31 9463 9474 2-s2.0-33747093008 10.1021/bi060756w (Pubitemid 44223250)
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9463-9474
    • Herren, T.1    Burke, T.A.2    Das, R.3    Plow, E.F.4
  • 46
    • 36348985036 scopus 로고    scopus 로고
    • Histone H2B as a functionally important plasminogen receptor on macrophages
    • DOI 10.1182/blood-2007-03-079392
    • Das R., Burke T., Plow E. F., Histone H2B as a functionally important plasminogen receptor on macrophages. Blood 2007 110 10 3763 3772 2-s2.0-36348985036 10.1182/blood-2007-03-079392 (Pubitemid 350159647)
    • (2007) Blood , vol.110 , Issue.10 , pp. 3763-3772
    • Das, R.1    Burke, T.2    Plow, E.F.3
  • 47
    • 0029817448 scopus 로고    scopus 로고
    • Endothelial cell surface actin serves as a binding site for plasminogen, tissue plasminogen activator and lipoprotein(a)
    • Dudani A. K., Ganz P. R., Endothelial cell surface actin serves as a binding site for plasminogen, tissue plasminogen activator and lipoprotein(a). British Journal of Haematology 1996 95 1 168 178 2-s2.0-0029817448 (Pubitemid 26340247)
    • (1996) British Journal of Haematology , vol.95 , Issue.1 , pp. 168-178
    • Dudani, A.K.1    Ganz, P.R.2
  • 48
    • 0025833080 scopus 로고
    • Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen
    • Kanalas J. J., Makker S. P., Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen. Journal of Biological Chemistry 1991 266 17 10825 10829 2-s2.0-0025833080 (Pubitemid 21906879)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.17 , pp. 10825-10829
    • Kanalas, J.J.1    Makker, S.P.2
  • 49
    • 0029795405 scopus 로고    scopus 로고
    • Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell- associated plasminogen by tissue-type plasminogen activator
    • DOI 10.1074/jbc.271.41.25684
    • Hembrough T. A., Li L., Gonias S. L., Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell- associated plasminogen by tissue-type plasminogen activator. Journal of Biological Chemistry 1996 271 41 25684 25691 2-s2.0-0029795405 10.1074/jbc.271.41.25684 (Pubitemid 26337950)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.41 , pp. 25684-25691
    • Hembrough, T.A.1    Li, L.2    Gonias, S.L.3
  • 50
    • 0031041077 scopus 로고    scopus 로고
    • Acceleration of plasminogen activation by tissue plasminogen activator on surface-bound histidine-proline-rich glycoprotein
    • DOI 10.1074/jbc.272.9.5718
    • Borza D. B., Morgan W. T., Acceleration of plasminogen activation by tissue plasminogen activator on surface-bound histidine-proline-rich glycoprotein. Journal of Biological Chemistry 1997 272 9 5718 5726 2-s2.0-0031041077 10.1074/jbc.272.9.5718 (Pubitemid 27102400)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.9 , pp. 5718-5726
    • Borza, D.-B.1    Morgan, W.T.2
  • 51
    • 0029799009 scopus 로고    scopus 로고
    • The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase
    • Winram S. B., Lottenberg R., The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase. Microbiology 1996 142 8 2311 2320 2-s2.0-0029799009 (Pubitemid 26288107)
    • (1996) Microbiology , vol.142 , Issue.8 , pp. 2311-2320
    • Winram, S.B.1    Lottenberg, R.2
  • 52
    • 77949897126 scopus 로고    scopus 로고
    • Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation
    • 2-s2.0-77949897126 10.1182/blood-2008-11-188938
    • Andronicos N. M., Chen E. I., Baik N., Bai H., Parmer C. M., Kiosses W. B., Kamps M. P., Yates J. R., Parmer R. J., Miles L. A., Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation. Blood 2010 115 7 1319 1330 2-s2.0-77949897126 10.1182/blood-2008-11- 188938
    • (2010) Blood , vol.115 , Issue.7 , pp. 1319-1330
    • Andronicos, N.M.1    Chen, E.I.2    Baik, N.3    Bai, H.4    Parmer, C.M.5    Kiosses, W.B.6    Kamps, M.P.7    Yates, J.R.8    Parmer, R.J.9    Miles, L.A.10
  • 53
    • 0031735770 scopus 로고    scopus 로고
    • Plasminogen binding to cell surfaces
    • Felez J., Plasminogen binding to cell surfaces. Fibrinolysis and Proteolysis 1998 12 4 183 189 2-s2.0-0031735770 (Pubitemid 28539225)
    • (1998) Fibrinolysis and Proteolysis , vol.12 , Issue.4 , pp. 183-189
    • Felez, J.1
  • 55
    • 0033153103 scopus 로고    scopus 로고
    • Characterization of cell-associated plasminogen activation catalyzed by urokinase-type plasminogen activator, but independent of urokinase receptor (uPAR, CD87)
    • Longstaff C., Merton R. E., Fabregas P., Felez J., Characterization of cell-associated plasminogen activation catalyzed by urokinase-type plasminogen activator, but independent of urokinase receptor (uPAR, CD87). Blood 1999 93 11 3839 3846 2-s2.0-0033153103 (Pubitemid 29249831)
    • (1999) Blood , vol.93 , Issue.11 , pp. 3839-3846
    • Longstaff, C.1    Merton, R.E.2    Fabregas, P.3    Felez, J.4
  • 56
    • 0033617285 scopus 로고    scopus 로고
    • Regulation of tissue plasminogen activator activity by cells: Domains responsible for binding and mechanism of stimulation
    • DOI 10.1074/jbc.274.18.12414
    • Sinniger V., Mertont R. E., Fabregas P., Felez J., Longstaff C., Regulation of tissue plasminogen activator activity by cells: domains responsible for binding and mechanism of stimulation. Journal of Biological Chemistry 1999 274 18 12414 12422 2-s2.0-0033617285 10.1074/jbc.274.18.12414 (Pubitemid 29215472)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.18 , pp. 12414-12422
    • Sinniger, V.1    Mertont, R.E.2    Fabregas, P.3    Felez, J.4    Longstaff, C.5
  • 57
    • 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 L. A., Fábregas P., Jardí M., Plow E. F., Lijnen R. H., Characterization of cellular binding sites and interactive regions within reactants required for enhancement of plasminogen activation by tPA on the surface of leukocytic cells. Thrombosis and Haemostasis 1996 76 4 577 584 2-s2.0-0029805471 (Pubitemid 26372014)
    • (1996) Thrombosis and Haemostasis , vol.76 , Issue.4 , pp. 577-584
    • Felez, J.1    Miles, L.A.2    Fabregas, P.3    Jardi, M.4    Plow, E.F.5    Lijnen, R.H.6
  • 59
    • 67049088421 scopus 로고    scopus 로고
    • Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung
    • 2-s2.0-67049088421 10.1182/blood-2008-08-170837
    • Wygrecka M., Marsh L. M., Morty R. E., Henneke I., Guenther A., Lohmeyer J., Markart P., Preissner K. T., Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung. Blood 2009 113 22 5588 5598 2-s2.0-67049088421 10.1182/blood-2008-08-170837
    • (2009) Blood , vol.113 , Issue.22 , pp. 5588-5598
    • Wygrecka, M.1    Marsh, L.M.2    Morty, R.E.3    Henneke, I.4    Guenther, A.5    Lohmeyer, J.6    Markart, P.7    Preissner, K.T.8
  • 60
    • 0025868410 scopus 로고
    • The efficiency of the uncleaved secretion signal in the plasminogen activator inhibitor type 2 protein can be enhanced by point mutations that increase its hydrophobicity
    • von Heijne G., Liljestrom P., Mikus P., Andersson H., Ny T., The efficiency of the uncleaved secretion signal in the plasminogen activator inhibitor type 2 protein can be enhanced by point mutations that increase its hydrophobicity. Journal of Biological Chemistry 1991 266 23 15240 15243 2-s2.0-0025868410 (Pubitemid 21907640)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.23 , pp. 15240-15243
    • Von Heijne, G.1    Liljestrom, P.2    Mikus, P.3    Andersson, H.4    Ny, T.5
  • 61
    • 0027397616 scopus 로고
    • Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an α-enolase isoform
    • Bottalico L. A., Kendrick N. C., Keller A., Li Y., Tabas I., Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an α -enolase isoform. Arteriosclerosis and Thrombosis 1993 13 2 264 275 2-s2.0-0027397616 (Pubitemid 23056800)
    • (1993) Arteriosclerosis and Thrombosis , vol.13 , Issue.2 , pp. 264-275
    • Bottalico, L.A.1    Kendrick, N.C.2    Keller, A.3    Li, Y.4    Tabas, I.5
  • 62
    • 0021254544 scopus 로고
    • Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinase in vivo and in vitro
    • Cooper J. A., Esch F. S., Taylor S. S., Hunter T., Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinase in vivo and in vitro. Journal of Biological Chemistry 1984 259 12 7835 7841 2-s2.0-0021254544 (Pubitemid 14081202)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.12 , pp. 7835-7841
    • Cooper, J.A.1    Esch, F.S.2    Taylor, S.S.3    Hunter, T.4
  • 64
    • 0037089235 scopus 로고    scopus 로고
    • Plasmin activity is required for myogenesis in vitro and skeletal muscle regeneration in vivo
    • DOI 10.1182/blood.V99.8.2835
    • Suelves M., López-Alemany R., Lluís F., Aniorte G., Serrano E., Parra M., Carmeliet P., Muñoz-Cánoves P., Plasmin activity is required for myogenesis in vitro and skeletal muscle regeneration in vivo. Blood 2002 99 8 2835 2844 2-s2.0-0037089235 10.1182/blood.V99.8.2835 (Pubitemid 34525372)
    • (2002) Blood , vol.99 , Issue.8 , pp. 2835-2844
    • Suelves, M.1    Lopez-Alemany, R.2    Lluis, F.3    Aniorte, G.4    Serrano, E.5    Parra, M.6    Carmeliet, P.7    Munoz-Canoves, P.8
  • 67
    • 0035137484 scopus 로고    scopus 로고
    • Cell invasion is affected by differential expression of urokinase plasminogen activator/urokinase plasminogen activator receptor system in muscle satellite cells from normal and dystrophic patients
    • Fibbi G., Barletta E., Dini G., Del Rosso A., Pucci M., Cerletti M., Del Rosso M., Cell invasion is affected by differential expression of urokinase plasminogen activator/urokinase plasminogen activator receptor system in muscle satellite cells from normal and dystrophic patients. Laboratory Investigation 2001 81 1 27 39 2-s2.0-0035137484 (Pubitemid 32108637)
    • (2001) Laboratory Investigation , vol.81 , Issue.1 , pp. 27-39
    • Fibbi, G.1    Barletta, E.2    Dini, G.3    Del Rosso, A.4    Pucci, M.5    Cerletti, M.6    Del Rosso, M.7
  • 68
    • 0028842013 scopus 로고
    • Regulation of the myoblast-specific expression of the human β -enolase gene
    • 2-s2.0-0028842013 10.1074/jbc.270.6.2535
    • Taylor J. M., Davies J. D., Peterson C. A., Regulation of the myoblast-specific expression of the human β -enolase gene. Journal of Biological Chemistry 1995 270 6 2535 2540 2-s2.0-0028842013 10.1074/jbc.270.6. 2535
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.6 , pp. 2535-2540
    • Taylor, J.M.1    Davies, J.D.2    Peterson, C.A.3
  • 71
    • 0033921682 scopus 로고    scopus 로고
    • Differential modulation of α, β and γ enolase isoforms in regenerating mouse skeletal muscle
    • DOI 10.1046/j.1432-1327.2000.01408.x
    • Merkulova T., Dehaupas M., Nevers M. C., Créminon C., Alameddine H., Keller A., Differential modulation of α β and γ enolase isoforms in regenerating mouse skeletal muscle. European Journal of Biochemistry 2000 267 12 3735 3743 2-s2.0-0033921682 10.1046/j.1432-1327.2000.01408.x (Pubitemid 30423036)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.12 , pp. 3735-3743
    • Merkulova, T.1    Dehaupas, M.2    Nevers, M.-C.3    Creminon, C.4    Alameddine, H.5    Keller, A.6
  • 72
    • 0142061003 scopus 로고    scopus 로고
    • Plasmin generation dependent on α-enolase-type plasminogen receptor is required for myogenesis
    • López-Alemany R., Suelves M., Muñoz-Cánoves P., Plasmin generation dependent on α -enolase-type plasminogen receptor is required for myogenesis. Thrombosis and Haemostasis 2003 90 4 724 733 2-s2.0-0142061003 (Pubitemid 37287642)
    • (2003) Thrombosis and Haemostasis , vol.90 , Issue.4 , pp. 724-733
    • Lopez-Alemany, R.1    Suelves, M.2    Munoz-Canoves, P.3
  • 73
    • 34548396678 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator receptor is not required for skeletal muscle inflammation or regeneration
    • DOI 10.1152/ajpregu.00132.2007
    • Bryer S. C., Koh T. J., The urokinase-type plasminogen activator receptor is not required for skeletal muscle inflammation or regeneration. American Journal of Physiology 2007 293 3 R1152 R1158 2-s2.0-34548396678 10.1152/ajpregu.00132.2007 (Pubitemid 47358936)
    • (2007) American Journal of Physiology - Regulatory Integrative and Comparative Physiology , vol.293 , Issue.3
    • Bryer, S.C.1    Koh, T.J.2
  • 75
    • 67649422687 scopus 로고    scopus 로고
    • Differential expression of α -enolase in the normal and pathological cardiac growth
    • 2-s2.0-67649422687 10.1016/j.yexmp.2009.05.002
    • Zhu L. A., Fang N. Y., Gao P. J., Jin X., Wang H. Y., Differential expression of α -enolase in the normal and pathological cardiac growth. Experimental and Molecular Pathology 2009 87 1 27 31 2-s2.0-67649422687 10.1016/j.yexmp.2009.05.002
    • (2009) Experimental and Molecular Pathology , vol.87 , Issue.1 , pp. 27-31
    • Zhu, L.A.1    Fang, N.Y.2    Gao, P.J.3    Jin, X.4    Wang, H.Y.5
  • 76
    • 9644266707 scopus 로고    scopus 로고
    • ERK1/2 regulates intracellular ATP levels through α-enolase expression in cardiomyocytes exposed to ischemic hypoxia and reoxygenation
    • DOI 10.1074/jbc.M402299200
    • Mizukami Y., Iwamatsu A., Aki T., Kimura M., Nakamura K., Nao T., Okusa T., Matsuzaki M., Yoshida K. I., Kobayashi S., ERK1/2 regulates intracellular ATP levels through α -enolase expression in cardiomyocytes exposed to ischemic hypoxia and reoxygenation. Journal of Biological Chemistry 2004 279 48 50120 50131 2-s2.0-9644266707 10.1074/jbc.M402299200 (Pubitemid 39577824)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 50120-50131
    • Mizukami, Y.1    Iwamatsu, A.2    Aki, T.3    Kimura, M.4    Nakamura, K.5    Nao, T.6    Okusa, T.7    Matsuzaki, M.8    Yoshida, K.-I.9    Kobayashi, S.10
  • 77
    • 0030936680 scopus 로고    scopus 로고
    • Progress in myocardial damage detection: New biochemical markers for clinicians
    • Mair J., Progress in myocardial damage detection: new biochemical markers for clinicians. Critical Reviews in Clinical Laboratory Sciences 1997 34 1 1 66 2-s2.0-0030936680 (Pubitemid 27129513)
    • (1997) Critical Reviews in Clinical Laboratory Sciences , vol.34 , Issue.1 , pp. 1-66
    • Mair, J.1
  • 83
    • 0029120866 scopus 로고
    • Gene expression in a swine model of right ventricular hypertrophy: Intercellular adhesion molecule, vascular endothelial growth factor and plasminogen activators are upregulated during pressure overload
    • 2-s2.0-0029120866 10.1006/jmcc.1995.0135
    • Carroll S. M., Nimmo L. E., Knoepfler P. S., White F. C., Bloor C. M., Gene expression in a swine model of right ventricular hypertrophy: intercellular adhesion molecule, vascular endothelial growth factor and plasminogen activators are upregulated during pressure overload. Journal of Molecular and Cellular Cardiology 1995 27 7 1427 1441 2-s2.0-0029120866 10.1006/jmcc.1995.0135
    • (1995) Journal of Molecular and Cellular Cardiology , vol.27 , Issue.7 , pp. 1427-1441
    • Carroll, S.M.1    Nimmo, L.E.2    Knoepfler, P.S.3    White, F.C.4    Bloor, C.M.5
  • 84
    • 0037205320 scopus 로고    scopus 로고
    • Cardiomyocyte cell cycle regulation
    • DOI 10.1161/01.RES.0000020201.44772.67
    • Pasumarthi K. B. S., Field L. J., Cardiomyocyte cell cycle regulation. Circulation Research 2002 90 10 1044 1054 2-s2.0-0037205320 10.1161/01.RES. 0000020201.44772.67 (Pubitemid 34627902)
    • (2002) Circulation Research , vol.90 , Issue.10 , pp. 1044-1054
    • Pasumarthi, K.B.S.1    Field, L.J.2
  • 87
    • 22144488826 scopus 로고    scopus 로고
    • Functional hierarchy of plasminogen kringles 1 and 4 in fibrinolysis and plasmin-induced cell detachment and apoptosis
    • DOI 10.1111/j.1742-4658.2005.04754.x
    • Ho-Tin-Noé B., Rojas G., Vranckx R., Lijnen H. R., Anglés-Cano E., Functional hierarchy of plasminogen kringles 1 and 4 in fibrinolysis and plasmin-induced cell detachment and apoptosis. FEBS Journal 2005 272 13 3387 3400 2-s2.0-22144488826 10.1111/j.1742-4658.2005.04754.x (Pubitemid 40979309)
    • (2005) FEBS Journal , vol.272 , Issue.13 , pp. 3387-3400
    • Ho-Tin-Noe, B.1    Rojas, G.2    Vranckx, R.3    Lijnen, H.R.4    Angles-Cano, E.5
  • 92
    • 0031838606 scopus 로고    scopus 로고
    • Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus
    • DOI 10.1002/1529-0131(199807)41:7<1241::AID-ART15>3.0.CO;2-H
    • Herrmann M., Voll R. E., Zoller O. M., Hagenhofer M., Ponner B. B., Kalden J. R., Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus. Arthritis and Rheumatism 1998 41 1241 1250 (Pubitemid 28313427)
    • (1998) Arthritis and Rheumatism , vol.41 , Issue.7 , pp. 1241-1250
    • Herrmann, M.1    Voll, R.E.2    Zoller, O.M.3    Hagenhofer, M.4    Ponner, B.B.5    Kalden, J.R.6
  • 94
    • 36849033963 scopus 로고    scopus 로고
    • TAM receptors are pleiotropic inhibitors of the innate immune response
    • DOI 10.1016/j.cell.2007.10.034, PII S0092867407013529
    • Rothlin C. V., Ghosh S., Zuniga E. I., Oldstone M. B. A., Lemke G., TAM receptors are pleiotropic inhibitors of the innate immune response. Cell 2007 131 6 1124 1136 2-s2.0-36849033963 10.1016/j.cell.2007.10.034 (Pubitemid 350235020)
    • (2007) Cell , vol.131 , Issue.6 , pp. 1124-1136
    • Rothlin, C.V.1    Ghosh, S.2    Zuniga, E.I.3    Oldstone, M.B.A.4    Lemke, G.5
  • 95
    • 77956904529 scopus 로고    scopus 로고
    • Mechanisms of failed apoptotic cell clearance by phagocyte subsets in cardiovascular disease
    • 2-s2.0-77956904529 10.1007/s10495-010-0516-6
    • Thorp E. B., Mechanisms of failed apoptotic cell clearance by phagocyte subsets in cardiovascular disease. Apoptosis 2010 15 9 1124 1136 2-s2.0-77956904529 10.1007/s10495-010-0516-6
    • (2010) Apoptosis , vol.15 , Issue.9 , pp. 1124-1136
    • Thorp, E.B.1
  • 96
    • 0031814996 scopus 로고    scopus 로고
    • Loss of cell viability dramatically elevates cell surface plasminogen binding and activation
    • DOI 10.1006/excr.1998.4067
    • O'Mullane M. J., Baker M. S., Loss of cell viability dramatically elevates cell surface plasminogen binding and activation. Experimental Cell Research 1998 242 1 153 164 2-s2.0-0031814996 10.1006/excr.1998.4067 (Pubitemid 28366531)
    • (1998) Experimental Cell Research , vol.242 , Issue.1 , pp. 153-164
    • O'Mullane, M.J.1    Baker, M.S.2
  • 97
    • 0028129557 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator (t-PA). II. Annexin II-mediated enhancement of t-PA-dependent plasminogen activation
    • 2-s2.0-0028129557
    • Cesarman G. M., Guevara C. A., Hajjar K. A., An endothelial cell receptor for plasminogen/tissue plasminogen activator (t-PA). II. Annexin II-mediated enhancement of t-PA-dependent plasminogen activation. Journal of Biological Chemistry 1994 269 33 21198 21203 2-s2.0-0028129557
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.33 , pp. 21198-21203
    • Cesarman, G.M.1    Guevara, C.A.2    Hajjar, K.A.3
  • 100
    • 33751402104 scopus 로고    scopus 로고
    • Protein pattern difference in the colon cancer cell lines examined by two-dimensional differential in-gel electrophoresis and mass spectrometry
    • DOI 10.1007/s00595-006-3301-y
    • Katayama M., Nakano H., Ishiuchi A., Wu W., Oshima R., Sakurai J., Nishikawa H., Yamaguchi S., Otsubo T., Protein pattern difference in the colon cancer cell lines examined by two-dimensional differential in-gel electrophoresis and mass spectrometry. Surgery Today 2006 36 12 1085 1093 2-s2.0-33751402104 10.1007/s00595-006-3301-y (Pubitemid 44819452)
    • (2006) Surgery Today , vol.36 , Issue.12 , pp. 1085-1093
    • Katayama, M.1    Nakano, H.2    Ishiuchi, A.3    Wu, W.4    Oshima, R.5    Sakurai, J.6    Nishikawa, H.7    Yamaguchi, S.8    Otsubo, T.9
  • 101
    • 79952830765 scopus 로고    scopus 로고
    • α -enolase: A promising therapeutic and diagnostic tumor target
    • 2-s2.0-79952830765 10.1111/j.1742-4658.2011.08025.x
    • Capello M., Ferri-Borgogno S., Cappello P., Novelli F., α -enolase: a promising therapeutic and diagnostic tumor target. FEBS Journal 2011 278 7 1064 1074 2-s2.0-79952830765 10.1111/j.1742-4658.2011.08025.x
    • (2011) FEBS Journal , vol.278 , Issue.7 , pp. 1064-1074
    • Capello, M.1    Ferri-Borgogno, S.2    Cappello, P.3    Novelli, F.4
  • 102
    • 52249100151 scopus 로고    scopus 로고
    • Constructing disease-specific gene networks using pair-wise relevance metric: Application to colon cancer identifies interleukin 8, desmin and enolase 1 as the central elements
    • 2-s2.0-52249100151 10.1186/1752-0509-2-72
    • Jiang W., Li X., Rao S., Wang L., Du L., Li C., Wu C., Wang H., Wang Y., Yang B., Constructing disease-specific gene networks using pair-wise relevance metric: application to colon cancer identifies interleukin 8, desmin and enolase 1 as the central elements. BMC Systems Biology 2008 2, article 72 2-s2.0-52249100151 10.1186/1752-0509-2-72
    • (2008) BMC Systems Biology , vol.272
    • Jiang, W.1    Li, X.2    Rao, S.3    Wang, L.4    Du, L.5    Li, C.6    Wu, C.7    Wang, H.8    Wang, Y.9    Yang, B.10
  • 103
    • 84855939630 scopus 로고    scopus 로고
    • RNAi-mediated knockdown of alpha-enolase increases the sensitivity of tumor cells to antitubulin chemotherapeutics
    • Georges E., Bonneau A. M., Prinos P., RNAi-mediated knockdown of alpha-enolase increases the sensitivity of tumor cells to antitubulin chemotherapeutics. International Journal of Biochemistry and Molecular Biology 2011 2 303 308
    • (2011) International Journal of Biochemistry and Molecular Biology , vol.2 , pp. 303-308
    • Georges, E.1    Bonneau, A.M.2    Prinos, P.3
  • 105
    • 77952584341 scopus 로고    scopus 로고
    • ENO1, a potential prognostic head and neck cancer marker, promotes transformation partly via chemokine CCL20 induction
    • 2-s2.0-77952584341 10.1016/j.ejca.2010.03.018
    • Tsai S. T., Chien I. H., Shen W. H., Kuo Y. Z., Jin Y. T., Wong T. Y., Hsiao J. R., Wang H. P., Shih N. Y., Wu L. W., ENO1, a potential prognostic head and neck cancer marker, promotes transformation partly via chemokine CCL20 induction. European Journal of Cancer 2010 46 9 1712 1723 2-s2.0-77952584341 10.1016/j.ejca.2010.03.018
    • (2010) European Journal of Cancer , vol.46 , Issue.9 , pp. 1712-1723
    • Tsai, S.T.1    Chien, I.H.2    Shen, W.H.3    Kuo, Y.Z.4    Jin, Y.T.5    Wong, T.Y.6    Hsiao, J.R.7    Wang, H.P.8    Shih, N.Y.9    Wu, L.W.10
  • 106
    • 33847400593 scopus 로고    scopus 로고
    • Metabolic catastrophe as a means to cancer cell death
    • DOI 10.1242/jcs.03349
    • Jin S., DiPaola R. S., Mathew R., White E., Metabolic catastrophe as a means to cancer cell death. Journal of Cell Science 2007 120 3 379 383 2-s2.0-33847400593 10.1242/jcs.03349 (Pubitemid 46332501)
    • (2007) Journal of Cell Science , vol.120 , Issue.3 , pp. 379-383
    • Jin, S.1    DiPaola, R.S.2    Mathew, R.3    White, E.4
  • 107
    • 0037309763 scopus 로고    scopus 로고
    • Expression of MIP-3α/CCL20, a macrophage inflammatory protein in oral squamous cell carcinoma
    • DOI 10.1016/S0003-9969(02)00167-X
    • Abiko Y., Nishimura M., Kusano K., Nakashima K., Okumura K., Arakawa T., Takuma T., Mizoguchi I., Kaku T., Expression of MIP-3 α /CCL20, a macrophage inflammatory protein in oral squamous cell carcinoma. Archives of Oral Biology 2003 48 2 171 175 2-s2.0-0037309763 10.1016/S0003-9969(02)00167-X (Pubitemid 36453669)
    • (2003) Archives of Oral Biology , vol.48 , Issue.2 , pp. 171-175
    • Abiko, Y.1    Nishimura, M.2    Kusano, K.3    Nakashima, K.4    Okumura, K.5    Arakawa, T.6    Takuma, T.7    Mizoguchi, I.8    Kaku, T.9
  • 108
    • 77954565511 scopus 로고    scopus 로고
    • Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells
    • 2-s2.0-77954565511 10.1021/pr901109w
    • Zhou W., Capello M., Fredolini C., Piemonti L., Liotta L. A., Novelli F., Petricoin E. F., Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells. Journal of Proteome Research 2010 9 6 2929 2936 2-s2.0-77954565511 10.1021/pr901109w
    • (2010) Journal of Proteome Research , vol.9 , Issue.6 , pp. 2929-2936
    • Zhou, W.1    Capello, M.2    Fredolini, C.3    Piemonti, L.4    Liotta, L.A.5    Novelli, F.6    Petricoin, E.F.7
  • 110
    • 29544438797 scopus 로고    scopus 로고
    • Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies
    • DOI 10.1002/pmic.200500042
    • Iwabata H., Yoshida M., Komatsu Y., Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies. Proteomics 2005 5 18 4653 4664 2-s2.0-29544438797 10.1002/pmic.200500042 (Pubitemid 43016886)
    • (2005) Proteomics , vol.5 , Issue.18 , pp. 4653-4664
    • Iwabata, H.1    Yoshida, M.2    Komatsu, Y.3
  • 111
    • 77249139132 scopus 로고    scopus 로고
    • Oxidative and nitrative modifications of α -enolase in cardiac proteins from diabetic rats
    • 2-s2.0-77249139132 10.1016/j.freeradbiomed.2010.01.010
    • Lu N., Zhang Y., Li H., Gao Z., Oxidative and nitrative modifications of α -enolase in cardiac proteins from diabetic rats. Free Radical Biology and Medicine 2010 48 7 873 881 2-s2.0-77249139132 10.1016/j.freeradbiomed.2010. 01.010
    • (2010) Free Radical Biology and Medicine , vol.48 , Issue.7 , pp. 873-881
    • Lu, N.1    Zhang, Y.2    Li, H.3    Gao, Z.4
  • 113
    • 80052711196 scopus 로고    scopus 로고
    • Oxidative stress-induced proteome alterations target different cellular pathways in human myoblasts
    • Baraibar M. A., Hyzewicz J., Rogowska-Wrzesinska A., Oxidative stress-induced proteome alterations target different cellular pathways in human myoblasts. Free Radical Biology and Medicine 2011 51 1522 1532
    • (2011) Free Radical Biology and Medicine , vol.51 , pp. 1522-1532
    • Baraibar, M.A.1    Hyzewicz, J.2    Rogowska-Wrzesinska, A.3
  • 116
    • 0033016168 scopus 로고    scopus 로고
    • Clinical applications of two-color telomeric fluorescence in situ hybridization for prenatal diagnosis: Identification of chromosomal translocation in five families with recurrent miscarriages or a child with multiple congenital anomalies
    • DOI 10.1007/s100380050115
    • Wakui K., Tanemura M., Suzumori K., Hidaka E., Ishikawa M., Kubota T., Fukushima Y., Clinical applications of two-color telomeric fluorescence in situ hybridization for prenatal diagnosis: identification of chromosomal translocation in five families with recurrent miscarriages or a child with multiple congenital anomalies. Journal of Human Genetics 1999 44 2 85 90 2-s2.0-0033016168 10.1007/s100380050115 (Pubitemid 29146929)
    • (1999) Journal of Human Genetics , vol.44 , Issue.2 , pp. 85-90
    • Wakui, K.1    Tanemura, M.2    Suzumori, K.3    Hidaka, E.4    Ishikawa, M.5    Kubota, T.6    Fukushima, Y.7
  • 117
    • 0036095626 scopus 로고    scopus 로고
    • Presence of autoantibodies to the glycolytic enzyme α-enolase in sera from patients with early rheumatoid arthritis
    • DOI 10.1002/art.10252
    • Saulot V., Vittecoq O., Charlionet R., Fardellone P., Lange C., Marvin L., Machour N., Le Loët X., Gilbert D., Tron F., Presence of autoantibodies to the glycolytic enzyme α -enolase in sera from patients with early rheumatoid arthritis. Arthritis and Rheumatism 2002 46 5 1196 1201 2-s2.0-0036095626 10.1002/art.10252 (Pubitemid 34525825)
    • (2002) Arthritis and Rheumatism , vol.46 , Issue.5 , pp. 1196-1201
    • Saulot, V.1    Vittecoq, O.2    Charlionet, R.3    Fardellone, P.4    Lange, C.5    Marvin, L.6    Machour, N.7    Le Loet, X.8    Gilbert, D.9    Tron, F.10
  • 118
    • 73249145617 scopus 로고    scopus 로고
    • Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis
    • 2-s2.0-73249145617 10.1111/j.0105-2896.2009.00850.x
    • Wegner N., Lundberg K., Kinloch A., Fisher B., Malmström V., Feldmann M., Venables P. J., Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis. Immunological Reviews 2010 233 1 34 54 2-s2.0-73249145617 10.1111/j.0105-2896.2009.00850.x
    • (2010) Immunological Reviews , vol.233 , Issue.1 , pp. 34-54
    • Wegner, N.1    Lundberg, K.2    Kinloch, A.3    Fisher, B.4    Malmström, V.5    Feldmann, M.6    Venables, P.J.7
  • 119
    • 79961132978 scopus 로고    scopus 로고
    • Glycolysis and rheumatoid arthritis
    • 2-s2.0-79961132978 10.1111/j.1756-185X.2011.01598.x
    • Chang X., Wei C., Glycolysis and rheumatoid arthritis. International Journal of Rheumatic Diseases 2011 14 3 217 222 2-s2.0-79961132978 10.1111/j.1756-185X.2011.01598.x
    • (2011) International Journal of Rheumatic Diseases , vol.14 , Issue.3 , pp. 217-222
    • Chang, X.1    Wei, C.2
  • 120
    • 0035966011 scopus 로고    scopus 로고
    • Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation
    • 2-s2.0-0035966011 10.1074/jbc.M106289200
    • Jacovina A. T., Zhong F., Khazanova E., Lev E., Deora A. B., Hajjar K. A., Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation. Journal of Biological Chemistry 2001 276 52 49350 49358 2-s2.0-0035966011 10.1074/jbc.M106289200
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.52 , pp. 49350-49358
    • Jacovina, A.T.1    Zhong, F.2    Khazanova, E.3    Lev, E.4    Deora, A.B.5    Hajjar, K.A.6
  • 121
    • 67349238285 scopus 로고    scopus 로고
    • Cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase and impairs survival and neuritogenesis of neuronal cells
    • 2-s2.0-67349238285 10.1016/j.biocel.2009.02.019
    • Obermajer N., Doljak B., Jamnik P., Fonović U. P., Kos J., Cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase and impairs survival and neuritogenesis of neuronal cells. International Journal of Biochemistry and Cell Biology 2009 41 8-9 1685 1696 2-s2.0-67349238285 10.1016/j.biocel.2009.02.019
    • (2009) International Journal of Biochemistry and Cell Biology , vol.41 , Issue.8-9 , pp. 1685-1696
    • Obermajer, N.1    Doljak, B.2    Jamnik, P.3    Fonović, U.P.4    Kos, J.5
  • 122
    • 70350129134 scopus 로고    scopus 로고
    • Multifunctional roles of enolase in Alzheimer's disease brain: Beyond altered glucose metabolism
    • 2-s2.0-70350129134 10.1111/j.1471-4159.2009.06397.x
    • Butterfield D. A., Lange M. L. B., Multifunctional roles of enolase in Alzheimer's disease brain: beyond altered glucose metabolism. Journal of
    • (2009) Journal of Neurochemistry , vol.111 , Issue.4 , pp. 915-933
    • Butterfield, D.A.1    Lange, M.L.B.2
  • 123
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, α -enolase and heat shock cognate 71
    • 2-s2.0-0036733145 10.1046/j.1471-4159.2002.01103.x
    • Castegna A., Aksenov M., Thongboonkerd V., Klein J. B., Pierce W. M., Booze R., Markesbery W. R., Butterfield D. A., Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, α -enolase and heat shock cognate 71. Journal of Neurochemistry 2002 82 6 1524 1532 2-s2.0-0036733145 10.1046/j.1471-4159.2002.01103.x
    • (2002) Journal of Neurochemistry , vol.82 , Issue.6 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 124
    • 61849168093 scopus 로고    scopus 로고
    • Proteomics-determined differences in the concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with alzheimer's disease and mild cognitive impairment: Implications for progression of AD
    • 2-s2.0-61849168093 10.1021/pr800667a
    • Owen J. B., Domenico F. D., Suitana R., Perluigi M., Cini C., Pierce W. M., Butterfield D. A., Proteomics-determined differences in the concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with alzheimer's disease and mild cognitive impairment: implications for progression of AD. Journal of Proteome Research 2009 8 2 471 482 2-s2.0-61849168093 10.1021/pr800667a
    • (2009) Journal of Proteome Research , vol.8 , Issue.2 , pp. 471-482
    • Owen, J.B.1    Domenico, F.D.2    Suitana, R.3    Perluigi, M.4    Cini, C.5    Pierce, W.M.6    Butterfield, D.A.7
  • 125
    • 34248223082 scopus 로고    scopus 로고
    • An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach
    • DOI 10.1002/jnr.21275
    • Newman S. F., Sultana R., Perluigi M., Coccia R., Cai J., Pierce W. M., Klein J. B., Turner D. M., Butterfield D. A., An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach. Journal of Neuroscience Research 2007 85 7 1506 1514 2-s2.0-34248223082 10.1002/jnr.21275 (Pubitemid 46724394)
    • (2007) Journal of Neuroscience Research , vol.85 , Issue.7 , pp. 1506-1514
    • Newman, S.F.1    Sultana, R.2    Perluigi, M.3    Coccia, R.4    Cai, J.5    Pierce, W.M.6    Klein, J.B.7    Turner, D.M.8    Butterfield, D.A.9
  • 126
    • 38449100242 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator stimulation of monocyte matrix metalloproteinase-1 production is mediated by plasmin-dependent signaling through annexin A2 and inhibited by inactive plasmin
    • 2-s2.0-38449100242
    • Zhang Y., Zhou Z. H., Bugge T. H., Wahl L. M., Urokinase-type plasminogen activator stimulation of monocyte matrix metalloproteinase-1 production is mediated by plasmin-dependent signaling through annexin A2 and inhibited by inactive plasmin. Journal of Immunology 2007 179 5 3297 3304 2-s2.0-38449100242
    • (2007) Journal of Immunology , vol.179 , Issue.5 , pp. 3297-3304
    • Zhang, Y.1    Zhou, Z.H.2    Bugge, T.H.3    Wahl, L.M.4
  • 127
    • 0035877968 scopus 로고    scopus 로고
    • Plasmin-induced expression of cytokines and tissue factor in human monocytes involves AP-1 and IKK β -mediated NF- κ B activation
    • 2-s2.0-0035877968 10.1182/blood.V97.12.3941
    • Syrovets T., Jendrach M., Rohwedder A., Schüle A., Simmet T., Plasmin-induced expression of cytokines and tissue factor in human monocytes involves AP-1 and IKK β -mediated NF- κ B activation. Blood 2001 97 12 3941 3950 2-s2.0-0035877968 10.1182/blood.V97.12.3941
    • (2001) Blood , vol.97 , Issue.12 , pp. 3941-3950
    • Syrovets, T.1    Jendrach, M.2    Rohwedder, A.3    Schüle, A.4    Simmet, T.5
  • 128
    • 0037031851 scopus 로고    scopus 로고
    • The serine protease plasmin triggers expression of MCP-1 and CD40 in human primary monocytes via activation of p38 MAPK and Janus kinase (JAK)/STAT signaling pathways
    • DOI 10.1074/jbc.M201941200
    • Burysek L., Syrovets T., Simmet T., The serine protease plasmin triggers expression of MCP-1 and CD40 in human primary monocytes via activation of p38 MAPK and Janus kinase (JAK)/STAT signaling pathways. Journal of Biological Chemistry 2002 277 36 33509 33517 2-s2.0-0037031851 10.1074/jbc.M201941200 (Pubitemid 34987557)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 33509-33517
    • Burysek, L.1    Syrovets, T.2    Simmet, T.3
  • 129
    • 34249335018 scopus 로고    scopus 로고
    • Plasmin triggers cytokine induction in human monocyte-derived macrophages
    • DOI 10.1161/ATVBAHA.107.142901
    • Li Q., Laumonnier Y., Syrovets T., Simmet T., Plasmin triggers cytokine induction in human monocyte-derived macrophages. Arteriosclerosis, Thrombosis, and Vascular Biology 2007 27 6 1383 1389 2-s2.0-34249335018 10.1161/ATVBAHA.107. 142901 (Pubitemid 46809429)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.6 , pp. 1383-1389
    • Li, Q.1    Laumonnier, Y.2    Syrovets, T.3    Simmet, T.4
  • 130
    • 0036739950 scopus 로고    scopus 로고
    • Plasmin induces Cyr61 gene expression in fibroblasts via protease-activated receptor-1 and p44/42 mitogen-activated protein kinase-dependent signaling pathway
    • 2-s2.0-0036739950 10.1161/01.ATV.0000030200.59331.3F
    • Pendurthi U. R., Ngyuen M., Andrade-Gordon P., Petersen L. C., Rao L. V. M., Plasmin induces Cyr61 gene expression in fibroblasts via protease-activated receptor-1 and p44/42 mitogen-activated protein kinase-dependent signaling pathway. Arteriosclerosis, Thrombosis, and Vascular Biology 2002 22 9 1421 1426 2-s2.0-0036739950 10.1161/01.ATV.0000030200.59331.3F
    • (2002) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.22 , Issue.9 , pp. 1421-1426
    • Pendurthi, U.R.1    Ngyuen, M.2    Andrade-Gordon, P.3    Petersen, L.C.4    Rao, L.V.M.5
  • 131
    • 20444497340 scopus 로고    scopus 로고
    • A novel mechanism of plasmin-induced mitogenesis in fibroblasts
    • DOI 10.1111/j.1538-7836.2004.01054.x
    • Mandal S. K., Rao L. V. M., Tran T. T. T., Pendurthi U. R., A novel mechanism of plasmin-induced mitogenesis in fibroblasts. Journal of Thrombosis and Haemostasis 2005 3 1 163 169 2-s2.0-20444497340 10.1111/j.1538-7836.2004. 01054.x (Pubitemid 41647129)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.1 , pp. 163-169
    • Mandal, S.K.1    Rao, L.V.M.2    Tran, T.T.T.3    Pendurthi, U.R.4
  • 134
    • 4444229880 scopus 로고    scopus 로고
    • 1
    • DOI 10.1074/jbc.M401372200
    • Majumdar M., Tarui T., Shi B., Akakura N., Ruf W., Takada Y., Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin α 9 β 1. Journal of Biological Chemistry 2004 279 36 37528 37534 2-s2.0-4444229880 10.1074/jbc.M401372200 (Pubitemid 39195465)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37528-37534
    • Majumdar, M.1    Tarui, T.2    Shi, B.3    Akakura, N.4    Ruf, W.5    Takada, Y.6
  • 135
    • 0037072784 scopus 로고    scopus 로고
    • Plasmin-induced migration of endothelial cells: A potential target for the anti-angiogenic action of angiostatin
    • 2-s2.0-0037072784 10.1074/jbc.M205514200
    • Tarui T., Majumdar M., Miles L. A., Ruf W., Takada Y., Plasmin-induced migration of endothelial cells: a potential target for the anti-angiogenic action of angiostatin. Journal of Biological Chemistry 2002 277 37 33564 33570 2-s2.0-0037072784 10.1074/jbc.M205514200
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.37 , pp. 33564-33570
    • Tarui, T.1    Majumdar, M.2    Miles, L.A.3    Ruf, W.4    Takada, Y.5
  • 136
    • 24344484078 scopus 로고    scopus 로고
    • Plasmin-induced smooth muscle cell proliferation requires epidermal growth factor activation through an extracellular pathway
    • DOI 10.1016/j.surg.2005.06.014, PII S0039606005003089
    • Roztocil E., Nicholl S. M., Galaria I. I., Davies M. G., Plasmin-induced smooth muscle cell proliferation requires epidermal growth factor activation through an extracellular pathway. Surgery 2005 138 2 180 186 2-s2.0-24344484078 10.1016/j.surg.2005.06.014 (Pubitemid 41253799)
    • (2005) Surgery , vol.138 , Issue.2 , pp. 180-186
    • Roztocil, E.1    Nicholl, S.M.2    Galaria, I.I.3    Davies, M.G.4
  • 137
    • 43549094212 scopus 로고    scopus 로고
    • Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins
    • DOI 10.1002/pmic.200700919
    • Petrak J., Ivanek R., Toman O., Cmejla R., Cmejlova J., Vyoral D., Zivny J., Vulpe C. D., Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins. Proteomics 2008 8 9 1744 1749 2-s2.0-43549094212 10.1002/pmic.200700919 (Pubitemid 351678270)
    • (2008) Proteomics , vol.8 , Issue.9 , pp. 1744-1749
    • Petrak, J.1    Ivanek, R.2    Toman, O.3    Cmejla, R.4    Cmejlova, J.5    Vyoral, D.6    Zivny, J.7    Vulpe, C.D.8
  • 140
    • 0037381176 scopus 로고    scopus 로고
    • Identification of rat targets of anti-soluble liver antigen autoantibodies by serologic proteome analysis
    • DOI 10.1373/49.4.634
    • Ballot E., Bruneel A., Labas V., Johanet C., Identification of rat targets of anti-soluble liver antigen autoantibodies by serologic proteome analysis. Clinical Chemistry 2003 49 4 634 643 2-s2.0-0037381176 10.1373/49.4.634 (Pubitemid 36379529)
    • (2003) Clinical Chemistry , vol.49 , Issue.4 , pp. 634-643
    • Ballot, E.1    Bruneel, A.2    Labas, V.3    Johanet, C.4
  • 142
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • DOI 10.1016/j.tibs.2005.01.005
    • Kim J. W., Dang C. V., Multifaceted roles of glycolytic enzymes. Trends in Biochemical Sciences 2005 30 3 142 150 2-s2.0-14744284637 10.1016/j.tibs.2005.01.005 (Pubitemid 40332530)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.3 , pp. 142-150
    • Kim, J.-W.1    Dang, C.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.