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Volumn 9, Issue 5, 1999, Pages 128-138

Annexin II: A mediator of the plasmin/plasminogen activator system

Author keywords

[No Author keywords available]

Indexed keywords

ANNEXIN; HOMOCYSTEINE; LIPOPROTEIN A; PLASMIN; PLASMINOGEN ACTIVATOR; TISSUE PLASMINOGEN ACTIVATOR;

EID: 0033407492     PISSN: 10501738     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1050-1738(99)00020-1     Document Type: Review
Times cited : (146)

References (107)
  • 1
    • 0024390672 scopus 로고
    • A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells
    • Ali S.M., Geisow M.J., Burgoyne R.D. A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature. 340:1989;313-315.
    • (1989) Nature , vol.340 , pp. 313-315
    • Ali, S.M.1    Geisow, M.J.2    Burgoyne, R.D.3
  • 2
    • 0021320736 scopus 로고
    • Interaction of plasmin with endothelial cells
    • Bauer P.I., Machovich R., Buki K.G.et al. Interaction of plasmin with endothelial cells. Biochem J. 218:1984;119-124.
    • (1984) Biochem J , vol.218 , pp. 119-124
    • Bauer, P.I.1    MacHovich, R.2    Buki, K.G.3
  • 3
    • 0030966570 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Benz J., Hofmann A. Annexins. from structure to function Biol Chem. 378:1997;177-183.
    • (1997) Biol Chem , vol.378 , pp. 177-183
    • Benz, J.1    Hofmann, A.2
  • 4
    • 0029817743 scopus 로고    scopus 로고
    • Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion
    • Bold S., Ohlin M., Garten W.et al. Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion. J Gen Virol. 77:1996;2297-2302.
    • (1996) J Gen Virol , vol.77 , pp. 2297-2302
    • Bold, S.1    Ohlin, M.2    Garten, W.3
  • 5
    • 1842338654 scopus 로고    scopus 로고
    • Modification of apolipoprotein(a) lysine binding site reduces atherosclerosis in transgenic mice
    • Boonmark N.W., Lou X.J., Schwartz K.et al. Modification of apolipoprotein(a) lysine binding site reduces atherosclerosis in transgenic mice. J Clin Invest. 100:1997;558-564.
    • (1997) J Clin Invest , vol.100 , pp. 558-564
    • Boonmark, N.W.1    Lou, X.J.2    Schwartz, K.3
  • 6
    • 0029066299 scopus 로고
    • A quantitative assessment of plasma homocysteine as a risk factor for vascular disease
    • Boushey C.J., Beresford S.A.A., Omenn G.S.et al. A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. JAMA. 274:1995;1049-1057.
    • (1995) JAMA , vol.274 , pp. 1049-1057
    • Boushey, C.J.1    Beresford, S.A.A.2    Omenn, G.S.3
  • 7
    • 0025766346 scopus 로고
    • Characterization of the tyrosine phosphorylation of calpactin I (annexin II) induced by platelet-derived growth factor
    • Brambilla R., Zippel R., Sturani E.et al. Characterization of the tyrosine phosphorylation of calpactin I (annexin II) induced by platelet-derived growth factor. Biochem J. 278:1991;447-452.
    • (1991) Biochem J , vol.278 , pp. 447-452
    • Brambilla, R.1    Zippel, R.2    Sturani, E.3
  • 8
    • 0029887641 scopus 로고    scopus 로고
    • The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein
    • Burger A., Berendes R., Liemann S.et al. The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein. J Mol Biol. 257:1996;839-847.
    • (1996) J Mol Biol , vol.257 , pp. 839-847
    • Burger, A.1    Berendes, R.2    Liemann, S.3
  • 9
    • 52449149626 scopus 로고
    • Developmental regulation of tyrosine kinase substrate p36 (calpactin heavy chain) in rat cerebellum
    • Burgoyne R.D., Cambray-Deakin M.A., Norman K.M. Developmental regulation of tyrosine kinase substrate p36 (calpactin heavy chain) in rat cerebellum. J Mol Neurosci. 1:1989;47-54.
    • (1989) J Mol Neurosci , vol.1 , pp. 47-54
    • Burgoyne, R.D.1    Cambray-Deakin, M.A.2    Norman, K.M.3
  • 10
    • 0023001104 scopus 로고
    • The tyrosine phosphorylation substrate p36 is developmentally regulated in embryonic avian limb and is induced in cell culture
    • Carter C.V., Howlett A.R., Martin G.S.et al. The tyrosine phosphorylation substrate p36 is developmentally regulated in embryonic avian limb and is induced in cell culture. J Cell Biol. 103:1986;2017-2024.
    • (1986) J Cell Biol , vol.103 , pp. 2017-2024
    • Carter, C.V.1    Howlett, A.R.2    Martin, G.S.3
  • 11
    • 0028129557 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator: II. Annexin II-mediated enhancement of tPA-dependent plasminogen activation
    • Cesarman G.M., Guevara C.A., Hajjar K.A. An endothelial cell receptor for plasminogen/tissue plasminogen activator. II. Annexin II-mediated enhancement of tPA-dependent plasminogen activation J Biol Chem. 269:1994;21198-21203.
    • (1994) J Biol Chem , vol.269 , pp. 21198-21203
    • Cesarman, G.M.1    Guevara, C.A.2    Hajjar, K.A.3
  • 12
    • 0032512432 scopus 로고    scopus 로고
    • Annexin II tetramer inhibits plasmin-dependent fibrinolysis
    • Choi K.S., Ghuman J., Kassam G.et al. Annexin II tetramer inhibits plasmin-dependent fibrinolysis. Biochemistry. 37:1998;648-655.
    • (1998) Biochemistry , vol.37 , pp. 648-655
    • Choi, K.S.1    Ghuman, J.2    Kassam, G.3
  • 13
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung C.Y., Erickson H.P. Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J Cell Biol. 126:1994;539-548.
    • (1994) J Cell Biol , vol.126 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 14
    • 0030003154 scopus 로고    scopus 로고
    • Mitogenesis, cell migration and loss of focal adhesion induced by tenascin-C interacting with its cell surface receptor, annexin II
    • Chung C.Y., Murphy-Ullrich J.E., Erickson H.P. Mitogenesis, cell migration and loss of focal adhesion induced by tenascin-C interacting with its cell surface receptor, annexin II. Mol Biol Cell. 7:1996;883-892.
    • (1996) Mol Biol Cell , vol.7 , pp. 883-892
    • Chung, C.Y.1    Murphy-Ullrich, J.E.2    Erickson, H.P.3
  • 15
    • 0029556991 scopus 로고
    • Annexins in plant cells
    • Clark G.B., Roux S.J. Annexins in plant cells. Plant Physiol. 109:1995;1133-1139.
    • (1995) Plant Physiol , vol.109 , pp. 1133-1139
    • Clark, G.B.1    Roux, S.J.2
  • 17
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz C.E. The annexins and exocytosis. Science. 258:1992;924-931.
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 18
    • 0023800570 scopus 로고
    • +-binding protein p68 a novel member of a protein family
    • [published erratum appears in EMBO J 1988;7:1914]
    • +-binding protein p68 a novel member of a protein family. EMBO J. 7:1988;21-27. [published erratum appears in EMBO J 1988;7:1914].
    • (1988) EMBO J , vol.7 , pp. 21-27
    • Crompton, M.R.1    Owens, R.J.2    Totty, N.F.3
  • 19
    • 0027457754 scopus 로고
    • Annexin II is a major component of fusogenic endosomal vesicles
    • Emans N., Gorvel J.P., Walter C.et al. Annexin II is a major component of fusogenic endosomal vesicles. J Cell Biol. 120:1993;1357-1369.
    • (1993) J Cell Biol , vol.120 , pp. 1357-1369
    • Emans, N.1    Gorvel, J.P.2    Walter, C.3
  • 20
    • 0018945601 scopus 로고
    • Identification of a cellular protein substrate phosphorylated by the avian sarcoma virus-transforming gene product
    • Erikson E., Erikson R.L. Identification of a cellular protein substrate phosphorylated by the avian sarcoma virus-transforming gene product. Cell. 21:1980;829-836.
    • (1980) Cell , vol.21 , pp. 829-836
    • Erikson, E.1    Erikson, R.L.2
  • 21
    • 0030047497 scopus 로고    scopus 로고
    • The high-resolution crystal structure of human annexin III shows subtle differences with annexin V
    • Favier-Perron B., Lewit-Bentley A., Russo-Marie F. The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry. 35:1996;1740-1744.
    • (1996) Biochemistry , vol.35 , pp. 1740-1744
    • Favier-Perron, B.1    Lewit-Bentley, A.2    Russo-Marie, F.3
  • 23
    • 0029049553 scopus 로고
    • A candidate genetic risk factor for vascular disease: A common mutation in methylenetetrahydrofolate reductase
    • Frosst P., Blom H.J., Milos R.et al. A candidate genetic risk factor for vascular disease. a common mutation in methylenetetrahydrofolate reductase Nat Genet. 10:1995;111-113.
    • (1995) Nat Genet , vol.10 , pp. 111-113
    • Frosst, P.1    Blom, H.J.2    Milos, R.3
  • 24
    • 0011829734 scopus 로고
    • Evolutionary conservation and three-dimensional folding of the tyrosine kinase substrate annexin II
    • In Moss SE, ed. London, Portland Press
    • Gerke V: 1992. Evolutionary conservation and three-dimensional folding of the tyrosine kinase substrate annexin II. In Moss SE, ed. The Annexins. London, Portland Press, pp. 47-59.
    • (1992) The Annexins , pp. 47-59
    • Gerke, V.1
  • 25
    • 0021943945 scopus 로고
    • Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein I related to the cellular 36-kDa target of Rous sarcoma virus tyrosine kinase
    • Gerke V., Weber K. Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein I related to the cellular 36-kDa target of Rous sarcoma virus tyrosine kinase. J Biol Chem. 260:1985;1688-1695.
    • (1985) J Biol Chem , vol.260 , pp. 1688-1695
    • Gerke, V.1    Weber, K.2
  • 26
    • 0022928659 scopus 로고
    • ++ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core
    • ++ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core. J Biol Chem. 261:1986;7247-7252.
    • (1986) J Biol Chem , vol.261 , pp. 7247-7252
    • Glenney, J.R.1
  • 27
    • 0022996716 scopus 로고
    • Association of the S-100-related calpactin I light chain with the NH2-terminal tail of the 36-kDa heavy chain
    • Glenney J.R., Boudreau M., Galyean R.et al. Association of the S-100-related calpactin I light chain with the NH2-terminal tail of the 36-kDa heavy chain. J Biol Chem. 261:1986;10,485-10,488.
    • (1986) J Biol Chem , vol.261 , pp. 10
    • Glenney, J.R.1    Boudreau, M.2    Galyean, R.3
  • 28
    • 0024498468 scopus 로고
    • Further characterization of the cellular plasminogen binding site: Evidence that plasminogen 2 and lipoprotein a compete for the same site
    • Gonzales-Gronow M., Edelberg J.M., Pizzo S.V. Further characterization of the cellular plasminogen binding site. evidence that plasminogen 2 and lipoprotein a compete for the same site Biochemistry. 28:1989;2374-2377.
    • (1989) Biochemistry , vol.28 , pp. 2374-2377
    • Gonzales-Gronow, M.1    Edelberg, J.M.2    Pizzo, S.V.3
  • 29
    • 0021362113 scopus 로고
    • The 46,000-dalton tyrosine kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues
    • Gould K.L., Cooper J.A., Hunter T. The 46,000-dalton tyrosine kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues. J Cell Biol. 98:1984;487-497.
    • (1984) J Cell Biol , vol.98 , pp. 487-497
    • Gould, K.L.1    Cooper, J.A.2    Hunter, T.3
  • 30
    • 0022755882 scopus 로고
    • The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo
    • Gould K.L., Woodgett J.R., Isacke C.M.et al. The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo. Mol Cell Biol. 6:1986;2738-2744.
    • (1986) Mol Cell Biol , vol.6 , pp. 2738-2744
    • Gould, K.L.1    Woodgett, J.R.2    Isacke, C.M.3
  • 32
    • 1842331509 scopus 로고    scopus 로고
    • Plasma homocysteine as a risk factor for vascular disease: The European Concerted Action Project
    • Graham I.M., Daly L.E., Refsum H.M.et al. Plasma homocysteine as a risk factor for vascular disease. the European Concerted Action Project JAMA. 277:1997;1775-1781.
    • (1997) JAMA , vol.277 , pp. 1775-1781
    • Graham, I.M.1    Daly, L.E.2    Refsum, H.M.3
  • 33
    • 0027989926 scopus 로고
    • Activation of transforming growth factor-beta is inhibited in transgenic apolipoprotein(a) mice
    • Grainger D.J., Kemp P.R., Liu A.C.et al. Activation of transforming growth factor-beta is inhibited in transgenic apolipoprotein(a) mice. Nature. 370:1994;460-462.
    • (1994) Nature , vol.370 , pp. 460-462
    • Grainger, D.J.1    Kemp, P.R.2    Liu, A.C.3
  • 34
    • 0021332781 scopus 로고
    • Changes in the distribution of the 34-kdalton tyrosine kinase substrate during differentiation and maturation of chicken tissues
    • Greenberg M.E., Brackenbury R., Edelman G.M. Changes in the distribution of the 34-kdalton tyrosine kinase substrate during differentiation and maturation of chicken tissues. J Cell Biol. 98:1984;473-486.
    • (1984) J Cell Biol , vol.98 , pp. 473-486
    • Greenberg, M.E.1    Brackenbury, R.2    Edelman, G.M.3
  • 35
    • 0025880945 scopus 로고
    • The endothelial cell tissue plasminogen activator receptor: Specific interaction with plasminogen
    • Hajjar K.A. The endothelial cell tissue plasminogen activator receptor. specific interaction with plasminogen J Biol Chem. 266:1991;21,962-21,970.
    • (1991) J Biol Chem , vol.266 , pp. 21
    • Hajjar, K.A.1
  • 36
    • 0027288252 scopus 로고
    • Homocysteine-induced modulation of tissue plasminogen activator to its endothelial cell membrane receptor
    • Hajjar K.A. Homocysteine-induced modulation of tissue plasminogen activator to its endothelial cell membrane receptor. J Clin Invest. 91:1993;2873-2879.
    • (1993) J Clin Invest , vol.91 , pp. 2873-2879
    • Hajjar, K.A.1
  • 37
    • 0001737647 scopus 로고    scopus 로고
    • The molecular basis of fibrinolysis
    • In Nathan DG, Orkin SH, eds. Philadelphia: WB Saunders
    • Hajjar KA: 1998. The molecular basis of fibrinolysis. In Nathan DG, Orkin SH, eds. Hematology of Infancy and Childhood. Philadelphia: WB Saunders, pp. 1557-1573.
    • (1998) Hematology of Infancy and Childhood , pp. 1557-1573
    • Hajjar, K.A.1
  • 38
    • 0025363927 scopus 로고
    • Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase
    • Hajjar K.A., Hamel N.M. Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase. J Biol Chem. 265:1990;2908-2916.
    • (1990) J Biol Chem , vol.265 , pp. 2908-2916
    • Hajjar, K.A.1    Hamel, N.M.2
  • 39
    • 0032185702 scopus 로고    scopus 로고
    • Modulation of annexin II by homocysteine: Implications for atherothrombosis
    • Hajjar K.A., Jacovina A.T. Modulation of annexin II by homocysteine. implications for atherothrombosis J Invest Med. 46:1998;1-6.
    • (1998) J Invest Med , vol.46 , pp. 1-6
    • Hajjar, K.A.1    Jacovina, A.T.2
  • 40
    • 0024245005 scopus 로고
    • Endothelial cell-mediated conversion of glu-plasminogen to lys-plasminogen: Further evidence for assembly of the fibrinolytic system on the endothelial cell surface
    • Hajjar K.A., Nachman R.L. Endothelial cell-mediated conversion of glu-plasminogen to lys-plasminogen. further evidence for assembly of the fibrinolytic system on the endothelial cell surface J Clin Invest. 82:1988;1769-1778.
    • (1988) J Clin Invest , vol.82 , pp. 1769-1778
    • Hajjar, K.A.1    Nachman, R.L.2
  • 41
    • 0029964212 scopus 로고    scopus 로고
    • The role of lipoprotein(a) in atherogenesis and thrombosis
    • Hajjar K.A., Nachman R.L. The role of lipoprotein(a) in atherogenesis and thrombosis. Ann Rev Med. 47:1996;423-442.
    • (1996) Ann Rev Med , vol.47 , pp. 423-442
    • Hajjar, K.A.1    Nachman, R.L.2
  • 42
    • 0022978141 scopus 로고
    • Binding of plasminogen to cultured human endothelial cells
    • Hajjar K.A., Harpel P.C., Jaffe E.A.et al. Binding of plasminogen to cultured human endothelial cells. J Biol Chem. 261:1986;11,656-11,662.
    • (1986) J Biol Chem , vol.261 , pp. 11
    • Hajjar, K.A.1    Harpel, P.C.2    Jaffe, E.A.3
  • 43
    • 0023515489 scopus 로고
    • Binding of tissue plasminogen activator to cultured human endothelial cells
    • Hajjar K.A., Hamel N.M., Harpel P.C.et al. Binding of tissue plasminogen activator to cultured human endothelial cells. J Clin Invest. 80:1987;1712-1719.
    • (1987) J Clin Invest , vol.80 , pp. 1712-1719
    • Hajjar, K.A.1    Hamel, N.M.2    Harpel, P.C.3
  • 44
    • 0024539832 scopus 로고
    • Lipoprotein(a) modulation of endothelial cell surface fibrinolysis and its potential role in atherosclerosis
    • Hajjar K.A., Gavish D., Breslow J.et al. Lipoprotein(a) modulation of endothelial cell surface fibrinolysis and its potential role in atherosclerosis. Nature. 339:1989;303-305.
    • (1989) Nature , vol.339 , pp. 303-305
    • Hajjar, K.A.1    Gavish, D.2    Breslow, J.3
  • 45
    • 0028023538 scopus 로고
    • An endothelial cell receptor for plasminogen and tissue plasminogen activator: I. Identity with annexin II
    • Hajjar K.A., Jacovina A.T., Chacko J. An endothelial cell receptor for plasminogen and tissue plasminogen activator. I. Identity with annexin II J Biol Chem. 269:1994;21,191-21,197.
    • (1994) J Biol Chem , vol.269 , pp. 21
    • Hajjar, K.A.1    Jacovina, A.T.2    Chacko, J.3
  • 46
    • 0029788890 scopus 로고    scopus 로고
    • Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface: Essential role of endonexin repeat 2
    • Hajjar K.A., Guevara C.A., Lev E.et al. Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. essential role of endonexin repeat 2 J Biol Chem. 271:1996;21,652-21,659.
    • (1996) J Biol Chem , vol.271 , pp. 21
    • Hajjar, K.A.1    Guevara, C.A.2    Lev, E.3
  • 47
    • 0032540276 scopus 로고    scopus 로고
    • Tissue plasminogen activator binding to the annexin II tail domain: Direct modulation by homocysteine
    • Hajjar K.A., Mauri L., Jacovina A.T.et al. Tissue plasminogen activator binding to the annexin II tail domain. direct modulation by homocysteine J Biol Chem. 273:1998;9987-9993.
    • (1998) J Biol Chem , vol.273 , pp. 9987-9993
    • Hajjar, K.A.1    Mauri, L.2    Jacovina, A.T.3
  • 48
    • 0028955068 scopus 로고
    • The annexins: Specific markers of midline structures and sensory neurons in the developing murine central nervous system
    • Hamre K.M., Chepenik K.P., Goldowitz D. The annexins. specific markers of midline structures and sensory neurons in the developing murine central nervous system J Comp Neurol. 352:1995;421-435.
    • (1995) J Comp Neurol , vol.352 , pp. 421-435
    • Hamre, K.M.1    Chepenik, K.P.2    Goldowitz, D.3
  • 49
    • 0029913002 scopus 로고    scopus 로고
    • Annexin IV is a marker of roof and floor plate development in the murine CNS
    • Hamre K.M., Keller-Peck C.R., Campbell R.M.et al. Annexin IV is a marker of roof and floor plate development in the murine CNS. J Comp Neurol. 368:1996;527-537.
    • (1996) J Comp Neurol , vol.368 , pp. 527-537
    • Hamre, K.M.1    Keller-Peck, C.R.2    Campbell, R.M.3
  • 50
    • 0022517061 scopus 로고
    • Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60 v-src and of the epidermal growth factor receptor/kinase
    • Huang K., Wallner B.P., Mattaliano R.J.et al. Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60 v-src and of the epidermal growth factor receptor/kinase. Cell. 46:1986;191-199.
    • (1986) Cell , vol.46 , pp. 191-199
    • Huang, K.1    Wallner, B.P.2    Mattaliano, R.J.3
  • 51
    • 0026575572 scopus 로고
    • Crystal and molecular structure of human annexin V after refinement: Implications for structure, membrane binding and ion channel formation of the annexin family of proteins
    • Huber R., Berendes R., Burger A.et al. Crystal and molecular structure of human annexin V after refinement. implications for structure, membrane binding and ion channel formation of the annexin family of proteins J Mol Biol. 223:1992;683-704.
    • (1992) J Mol Biol , vol.223 , pp. 683-704
    • Huber, R.1    Berendes, R.2    Burger, A.3
  • 52
    • 0023937186 scopus 로고
    • Chromosomal localization of the genes for lipocortin I and lipocortin II
    • Huebner K., Cannizzaro L.A., Frey A.Z.et al. Chromosomal localization of the genes for lipocortin I and lipocortin II. Oncogene Res. 2:1988;299-310.
    • (1988) Oncogene Res , vol.2 , pp. 299-310
    • Huebner, K.1    Cannizzaro, L.A.2    Frey, A.Z.3
  • 53
    • 0022753927 scopus 로고
    • Modulation of p36 phosphorylation in human cells: Studies using anti-p36 monoclonal antibodies
    • Isacke C.M., Trowbridge I.S., Hunter T. Modulation of p36 phosphorylation in human cells. studies using anti-p36 monoclonal antibodies Mol Cell Biol. 6:1986;2745-2751.
    • (1986) Mol Cell Biol , vol.6 , pp. 2745-2751
    • Isacke, C.M.1    Trowbridge, I.S.2    Hunter, T.3
  • 54
    • 0026075259 scopus 로고
    • Xenopus annexin II (calpactin II) heavy chain has a distinct amino terminus
    • Izant J.G., Bryson L.J. Xenopus annexin II (calpactin II) heavy chain has a distinct amino terminus. J Biol Chem. 266:1991;18,560-18,566.
    • (1991) J Biol Chem , vol.266 , pp. 18
    • Izant, J.G.1    Bryson, L.J.2
  • 55
    • 0025855150 scopus 로고
    • The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase α
    • Jindahl H.K., Chaney W.G., Anderson C.W.et al. The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase α J Biol Chem. 266:1991;5169-5176.
    • (1991) J Biol Chem , vol.266 , pp. 5169-5176
    • Jindahl, H.K.1    Chaney, W.G.2    Anderson, C.W.3
  • 56
    • 0024062670 scopus 로고
    • P36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphipathic helix
    • Johnsson N., Marriott G., Weber K. p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphipathic helix. EMBO J. 7:1988;2435-2442.
    • (1988) EMBO J , vol.7 , pp. 2435-2442
    • Johnsson, N.1    Marriott, G.2    Weber, K.3
  • 59
    • 21844489253 scopus 로고
    • Annexins: Novel calcium-dependent regulators of membrane function
    • Kaetzel M.A., Dedman J.R. Annexins. novel calcium-dependent regulators of membrane function News in Physiol Sci. 10:1995;171-176.
    • (1995) News in Physiol Sci , vol.10 , pp. 171-176
    • Kaetzel, M.A.1    Dedman, J.R.2
  • 60
    • 0023708269 scopus 로고
    • Lipocortins 1 and 2 as substrates for the insulin receptor kinase in rat liver
    • Karasik A., Pepinsky R.B., Shoelson S.E.et al. Lipocortins 1 and 2 as substrates for the insulin receptor kinase in rat liver. J Biol Chem. 263:1988;11,862-11,867.
    • (1988) J Biol Chem , vol.263 , pp. 11
    • Karasik, A.1    Pepinsky, R.B.2    Shoelson, S.E.3
  • 61
    • 0032549029 scopus 로고    scopus 로고
    • The role of annexin II tetramer in the activation of plasminogen
    • a
    • Kassam G., Choi K.S., Ghuman J.et al. The role of annexin II tetramer in the activation of plasminogen. J Biol Chem. 273:1998;4790-4799. a.
    • (1998) J Biol Chem , vol.273 , pp. 4790-4799
    • Kassam, G.1    Choi, K.S.2    Ghuman, J.3
  • 62
    • 0032374094 scopus 로고    scopus 로고
    • The p11 subunit of the annexin II tetramer plays a key role in the stimulation of tPA-dependent plasminogen activation
    • b
    • Kassam G., Le B.H., Choi K.S.et al. The p11 subunit of the annexin II tetramer plays a key role in the stimulation of tPA-dependent plasminogen activation. Biochemistry. 37:1998;16,958-16,966. b.
    • (1998) Biochemistry , vol.37 , pp. 16
    • Kassam, G.1    Le, B.H.2    Choi, K.S.3
  • 63
    • 0028001103 scopus 로고
    • Molecular basis of phenotype expression in homocystinuria
    • Kraus J.P. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 17:1994;383-390.
    • (1994) J Inherit Metab Dis , vol.17 , pp. 383-390
    • Kraus, J.P.1
  • 64
    • 0029813535 scopus 로고    scopus 로고
    • Surface annexin II on placental membranes of the fetomaternal interface
    • Kristoffersen E.K., Matre R. Surface annexin II on placental membranes of the fetomaternal interface. Am J Reprod Immunol. 36:1996;141-149.
    • (1996) Am J Reprod Immunol , vol.36 , pp. 141-149
    • Kristoffersen, E.K.1    Matre, R.2
  • 65
    • 0026677342 scopus 로고
    • Atherogenesis in transgenic mice expressing human apolipoprotein(a)
    • Lawn R.M., Wade D.P., Hammer R.E.et al. Atherogenesis in transgenic mice expressing human apolipoprotein(a). Nature. 360:1992;670-672.
    • (1992) Nature , vol.360 , pp. 670-672
    • Lawn, R.M.1    Wade, D.P.2    Hammer, R.E.3
  • 66
    • 0027076458 scopus 로고
    • Differential expression of two forms of annexin 3 in human neutrophils and monocytes and along their differentiation
    • Le Cabec V., Russo-Marie F., Maridonneau-Parini I. Differential expression of two forms of annexin 3 in human neutrophils and monocytes and along their differentiation. Biochem Biophys Res Commun. 189:1992;1471-1476.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1471-1476
    • Le Cabec, V.1    Russo-Marie, F.2    Maridonneau-Parini, I.3
  • 67
    • 0029644245 scopus 로고
    • Annexins: A novel family of calcium- And membrane-binding proteins in search of a function
    • Liemann S., Lewit-Bentley A. Annexins. a novel family of calcium- and membrane-binding proteins in search of a function Structure. 3:1995;233-237.
    • (1995) Structure , vol.3 , pp. 233-237
    • Liemann, S.1    Lewit-Bentley, A.2
  • 68
    • 0025148799 scopus 로고
    • Lipoprotein(a), a unique risk factor for atherothrombotic disease
    • Loscalzo J. Lipoprotein(a), a unique risk factor for atherothrombotic disease. Arteriosclerosis. 10:1990;672-679.
    • (1990) Arteriosclerosis , vol.10 , pp. 672-679
    • Loscalzo, J.1
  • 69
    • 0024517357 scopus 로고
    • Developmental regulation of calcium-binding proteins (calelectrins and calpactin I) in mammary glands
    • Lozano J.J., Silberstein G.B., Hwang S.I.et al. Developmental regulation of calcium-binding proteins (calelectrins and calpactin I) in mammary glands. J Cell Physiol. 138:1989;503-510.
    • (1989) J Cell Physiol , vol.138 , pp. 503-510
    • Lozano, J.J.1    Silberstein, G.B.2    Hwang, S.I.3
  • 70
    • 0028846237 scopus 로고
    • Crystal structure of the annexin XII hexamer and implications for bilayer insertion
    • Luecke H., Chang B.T., Mailliard W.S.et al. Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature. 378:1995;512-515.
    • (1995) Nature , vol.378 , pp. 512-515
    • Luecke, H.1    Chang, B.T.2    Mailliard, W.S.3
  • 71
    • 0025904861 scopus 로고
    • Alternative splicing of human synexin mRNA in brain, cardiac, and skeletal muscle alters the unique N-terminal domain
    • Magendzo K., Shirvan A., Cultraro C.et al. Alternative splicing of human synexin mRNA in brain, cardiac, and skeletal muscle alters the unique N-terminal domain. J Biol Chem. 266:1991;3228-3232.
    • (1991) J Biol Chem , vol.266 , pp. 3228-3232
    • Magendzo, K.1    Shirvan, A.2    Cultraro, C.3
  • 72
    • 0024516466 scopus 로고
    • The EGF receptor kinase substrate p35 in the floor plate of the embryonic rat CNS
    • McKanna J.A., Cohen S. The EGF receptor kinase substrate p35 in the floor plate of the embryonic rat CNS. Science. 243:1989;1477-1479.
    • (1989) Science , vol.243 , pp. 1477-1479
    • McKanna, J.A.1    Cohen, S.2
  • 73
    • 0023636242 scopus 로고
    • CDNA sequence of human apolipoprotein(a) is homologous to plasminogen
    • McLean J.W., Tomlinson J.E., Kuang W.J.et al. cDNA sequence of human apolipoprotein(a) is homologous to plasminogen. Nature. 330:1987;132-137.
    • (1987) Nature , vol.330 , pp. 132-137
    • McLean, J.W.1    Tomlinson, J.E.2    Kuang, W.J.3
  • 74
    • 0033119584 scopus 로고    scopus 로고
    • Annexin II and bleeding in acute promyelocytic leukemia
    • Menell J.S., Cesarman G.M., Jacovina A.T.et al. Annexin II and bleeding in acute promyelocytic leukemia. N Engl J Med. 340:1999;994-1004.
    • (1999) N Engl J Med , vol.340 , pp. 994-1004
    • Menell, J.S.1    Cesarman, G.M.2    Jacovina, A.T.3
  • 75
    • 0024554547 scopus 로고
    • A potential basis for the thrombotic risks associated with lipoprotein(a)
    • Miles L.A., Fless G.M., Levin E.G.et al. A potential basis for the thrombotic risks associated with lipoprotein(a). Nature. 339:1989;301-303.
    • (1989) Nature , vol.339 , pp. 301-303
    • Miles, L.A.1    Fless, G.M.2    Levin, E.G.3
  • 77
    • 0028879868 scopus 로고
    • Annexins taken to task
    • Moss S.E. Annexins taken to task. Nature. 378:1995;446-447.
    • (1995) Nature , vol.378 , pp. 446-447
    • Moss, S.E.1
  • 79
    • 0021894152 scopus 로고
    • The natural history of homocystinuria due to cystathionine b-synthase deficiency
    • Mudd H., Skovby F., Levy H.L.et al. The natural history of homocystinuria due to cystathionine b-synthase deficiency. Am J Hum Genet. 37:1985;1-31.
    • (1985) Am J Hum Genet , vol.37 , pp. 1-31
    • Mudd, H.1    Skovby, F.2    Levy, H.L.3
  • 80
    • 0000167774 scopus 로고
    • Disorders of transsulfuration
    • In Scriver CR, Beaudet AL, Sly WS, et al., eds. New York, McGraw-Hill
    • Mudd H, Levy HL, Skovby F, et al.: 1995. Disorders of transsulfuration. In Scriver CR, Beaudet AL, Sly WS, et al., eds. The Metabolic and Molecular Basis of Inherited Disease. New York, McGraw-Hill, pp. 1279-1327.
    • (1995) The Metabolic and Molecular Basis of Inherited Disease , pp. 1279-1327
    • Mudd, H.1    Levy, H.L.2    Skovby, F.3
  • 81
    • 0024549533 scopus 로고
    • Crystallization of p68 on lipid monolayers and as three-dimensional single crystals
    • Newman R., Tucker A., Ferguson C.et al. Crystallization of p68 on lipid monolayers and as three-dimensional single crystals. J Mol Biol. 206:1989;213-219.
    • (1989) J Mol Biol , vol.206 , pp. 213-219
    • Newman, R.1    Tucker, A.2    Ferguson, C.3
  • 82
    • 1842370239 scopus 로고    scopus 로고
    • Plasma homocysteine levels and mortality in patients with coronary artery disease
    • Nygard O., Nordrehaug J.E., Refsum H.et al. Plasma homocysteine levels and mortality in patients with coronary artery disease. N Engl J Med. 337:1997;230-236.
    • (1997) N Engl J Med , vol.337 , pp. 230-236
    • Nygard, O.1    Nordrehaug, J.E.2    Refsum, H.3
  • 83
    • 0028951047 scopus 로고
    • Antifibrinolytic activity of apolipoprotein(a) in vivo: Human apolipoprotein(a) transgenic mice are resistant to tissue plasminogen activator-mediated thrombolysis
    • Palabrica T.M., Liu A.C., Aronovitz M.J.et al. Antifibrinolytic activity of apolipoprotein(a) in vivo. human apolipoprotein(a) transgenic mice are resistant to tissue plasminogen activator-mediated thrombolysis Nature Med. 1:1995;256-259.
    • (1995) Nature Med , vol.1 , pp. 256-259
    • Palabrica, T.M.1    Liu, A.C.2    Aronovitz, M.J.3
  • 84
    • 0018959961 scopus 로고
    • Transformation by Rous sarcoma virus: A cellular substrate for transformation-specific protein phosphorylation contains phosphotyrosine
    • Radke K., Gilmore T., Martin G.S. Transformation by Rous sarcoma virus. a cellular substrate for transformation-specific protein phosphorylation contains phosphotyrosine Cell. 21:1980;821-828.
    • (1980) Cell , vol.21 , pp. 821-828
    • Radke, K.1    Gilmore, T.2    Martin, G.S.3
  • 85
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biologic role for a gene family of multifunctional calcium- And phospholipid-binding proeins
    • Raynal P., Pollard H.B. Annexins. the problem of assessing the biologic role for a gene family of multifunctional calcium- and phospholipid-binding proeins Biochim Biophys Acta. 1197:1994;63-93.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 86
    • 0027092615 scopus 로고
    • Developmental regulation of annexin II (lipocortin 2) in human brain and expression in high grade glioma
    • Reeves S.A., Chavez-Kappel C., Davis R.et al. Developmental regulation of annexin II (lipocortin 2) in human brain and expression in high grade glioma. Cancer Res. 52:1992;6871-6876.
    • (1992) Cancer Res , vol.52 , pp. 6871-6876
    • Reeves, S.A.1    Chavez-Kappel, C.2    Davis, R.3
  • 87
    • 0031958860 scopus 로고    scopus 로고
    • Homocysteine and cardiovascular disease
    • Refsum H., Ueland P.M., Nygard O.et al. Homocysteine and cardiovascular disease. Ann Rev Med. 49:1998;31-62.
    • (1998) Ann Rev Med , vol.49 , pp. 31-62
    • Refsum, H.1    Ueland, P.M.2    Nygard, O.3
  • 88
    • 0027456952 scopus 로고
    • Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells
    • Roth D., Morgan A., Burgoyne R.D. Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. FEBS Lett. 320:1993;207-210.
    • (1993) FEBS Lett , vol.320 , pp. 207-210
    • Roth, D.1    Morgan, A.2    Burgoyne, R.D.3
  • 89
    • 0025311925 scopus 로고
    • Lipoprotein(a) heterogeneity and biologic relevance
    • Scanu A.M., Fless G.M. Lipoprotein(a) heterogeneity and biologic relevance. J Clin Invest. 85:1990;1709-1715.
    • (1990) J Clin Invest , vol.85 , pp. 1709-1715
    • Scanu, A.M.1    Fless, G.M.2
  • 90
    • 0028966321 scopus 로고
    • Association between plasma homocysteine concentrations and extracranial carotid-artery stenosis
    • Selhub J., Jacques P.F., Bostom A.G.et al. Association between plasma homocysteine concentrations and extracranial carotid-artery stenosis. N Engl J Med. 332:1995;286-291.
    • (1995) N Engl J Med , vol.332 , pp. 286-291
    • Selhub, J.1    Jacques, P.F.2    Bostom, A.G.3
  • 92
    • 0025224832 scopus 로고
    • Characterization of the human lipocortin-2-encoding multigene family: Its structure suggests the existence of a short amino acid unit undergoing duplication
    • Spano F., Raugei G., Palla E.et al. Characterization of the human lipocortin-2-encoding multigene family. its structure suggests the existence of a short amino acid unit undergoing duplication Gene. 95:1990;243-251.
    • (1990) Gene , vol.95 , pp. 243-251
    • Spano, F.1    Raugei, G.2    Palla, E.3
  • 93
    • 0028944244 scopus 로고
    • The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae
    • Stahl A., Mueller B.M. The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae. J Cell Biol. 129:1995;335-344.
    • (1995) J Cell Biol , vol.129 , pp. 335-344
    • Stahl, A.1    Mueller, B.M.2
  • 94
    • 0021956465 scopus 로고
    • Phosphorylation of a chromaffin granule-binding protein by protein kinase C
    • Summers T.A., Creutz C.E. Phosphorylation of a chromaffin granule-binding protein by protein kinase C. J Biol Chem. 260:1985;2437-2443.
    • (1985) J Biol Chem , vol.260 , pp. 2437-2443
    • Summers, T.A.1    Creutz, C.E.2
  • 95
    • 0028233432 scopus 로고
    • Annexin structure and membrane interactions: A molecular perspective
    • Swairjo M.A., Seaton B.A. Annexin structure and membrane interactions. a molecular perspective Ann Rev Biophys Biomol Struct. 23:1994;193-213.
    • (1994) Ann Rev Biophys Biomol Struct , vol.23 , pp. 193-213
    • Swairjo, M.A.1    Seaton, B.A.2
  • 96
    • 0026749991 scopus 로고
    • Alternatively spliced annexin XI transcripts encode proteins that differ near the amino terminus
    • Towle C.A., Weissbach L., Treadwell B.V. Alternatively spliced annexin XI transcripts encode proteins that differ near the amino terminus. Biochim Biophys Aca. 1131:1992;223-226.
    • (1992) Biochim Biophys Aca , vol.1131 , pp. 223-226
    • Towle, C.A.1    Weissbach, L.2    Treadwell, B.V.3
  • 97
    • 0026575176 scopus 로고
    • Butanol-extractable and detergent-solubilized cell surface components from murine large cell lymphoma cells associated with adhesion to organ microvessel endothelial cells
    • Tressler R.J., Nicolson G.L. Butanol-extractable and detergent-solubilized cell surface components from murine large cell lymphoma cells associated with adhesion to organ microvessel endothelial cells. J Cell Biochem. 48:1992;162-171.
    • (1992) J Cell Biochem , vol.48 , pp. 162-171
    • Tressler, R.J.1    Nicolson, G.L.2
  • 98
    • 0027436971 scopus 로고
    • Extracellular annexin is associated with divalent cation-dependent tumor cell adhesion of metastatic RAW 117 large-cell lymphoma cells
    • Tressler R.J., Updyke T.V., Yeatman T.J.et al. Extracellular annexin is associated with divalent cation-dependent tumor cell adhesion of metastatic RAW 117 large-cell lymphoma cells. J Cell Biochem. 53:1993;265-276.
    • (1993) J Cell Biochem , vol.53 , pp. 265-276
    • Tressler, R.J.1    Updyke, T.V.2    Yeatman, T.J.3
  • 99
    • 0024362630 scopus 로고
    • The mysteries of lipoprotein(a)
    • Utermann G. The mysteries of lipoprotein(a). Science. 246:1989;904-910.
    • (1989) Science , vol.246 , pp. 904-910
    • Utermann, G.1
  • 100
    • 0028844290 scopus 로고
    • Annexin II tetramer: Structure and function
    • Waisman D.M. Annexin II tetramer. structure and function Mol Bell Biochem. 149(150):1995;301-322.
    • (1995) Mol Bell Biochem , vol.149 , Issue.150 , pp. 301-322
    • Waisman, D.M.1
  • 101
    • 0023922701 scopus 로고
    • Linkage between the loci for the Lp(a) lipoprotein (Lp) and plasminogen (PLG)
    • Weitkamp L.R., Guttormsen S.A., Schultz J.S. Linkage between the loci for the Lp(a) lipoprotein (Lp) and plasminogen (PLG). Hum Genet. 79:1988;80-82.
    • (1988) Hum Genet , vol.79 , pp. 80-82
    • Weitkamp, L.R.1    Guttormsen, S.A.2    Schultz, J.S.3
  • 102
    • 0027419410 scopus 로고
    • Crystal structure of human annexin I at 2.5A resolution
    • Weng X., Luecke H., Song I.S.et al. Crystal structure of human annexin I at 2.5A resolution. Protein Sci. 2:1993;448-458.
    • (1993) Protein Sci , vol.2 , pp. 448-458
    • Weng, X.1    Luecke, H.2    Song, I.S.3
  • 103
    • 0028334377 scopus 로고
    • An endothelial cell-surface form of annexin II binds human cytomegalovirus
    • Wright J.F., Kurosky A., Wasi S. An endothelial cell-surface form of annexin II binds human cytomegalovirus. Biochem Biophys Res Commun. 198:1994;983-989.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 983-989
    • Wright, J.F.1    Kurosky, A.2    Wasi, S.3
  • 104
    • 0029043553 scopus 로고
    • Host cellular annexin II is associated with cytomegalovirus particles isolated from cultured human fibroblasts
    • Wright J.F., Kurosky A., Pryzdial E.L.G.et al. Host cellular annexin II is associated with cytomegalovirus particles isolated from cultured human fibroblasts. J Virol. 69:1995;4784-4791.
    • (1995) J Virol , vol.69 , pp. 4784-4791
    • Wright, J.F.1    Kurosky, A.2    Pryzdial, E.L.G.3
  • 105
    • 0027462446 scopus 로고
    • Expression of annexins on the surfaces of non-metastatic human and rodent tumor cells
    • Yeatman T.J., Updyke T.V., Kaetzel M.A.et al. Expression of annexins on the surfaces of non-metastatic human and rodent tumor cells. Clin Exp Metastasis. 11:1993;37-44.
    • (1993) Clin Exp Metastasis , vol.11 , pp. 37-44
    • Yeatman, T.J.1    Updyke, T.V.2    Kaetzel, M.A.3
  • 106
    • 0031973175 scopus 로고    scopus 로고
    • Structure of the trigonal crystal form of bovine annexin IV
    • Zanotti G., Malpeli G., Gliubich F.et al. Structure of the trigonal crystal form of bovine annexin IV. Biochem J. 329:1998;101-106.
    • (1998) Biochem J , vol.329 , pp. 101-106
    • Zanotti, G.1    Malpeli, G.2    Gliubich, F.3
  • 107
    • 0027396098 scopus 로고
    • Genomic organization and chromosomal localization of the mouse synexin gene
    • Zhang-Keck Z.Y., Burns A.L., Pollard H.B. Genomic organization and chromosomal localization of the mouse synexin gene. Biochem J. 289:1993;735-741.
    • (1993) Biochem J , vol.289 , pp. 735-741
    • Zhang-Keck, Z.Y.1    Burns, A.L.2    Pollard, H.B.3


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