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Volumn 39, Issue 4, 2013, Pages 338-346

Annexin A2 system in human biology: Cell surface and beyond

Author keywords

annexin A2; fibrinolysis; inflammation; S100A2 protein p11

Indexed keywords

ANNEXIN A2 ANTIBODY; INFLAMMASOME; LIPOCORTIN 2; OXYGEN; PLASMIN; PROTEIN; PROTEIN ANTIBODY; PROTEIN S100A10; SEROTONIN RECEPTOR; SODIUM CHANNEL; TAU PROTEIN; TETRAMER; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG;

EID: 84878306011     PISSN: 00946176     EISSN: 10989064     Source Type: Journal    
DOI: 10.1055/s-0033-1334143     Document Type: Article
Times cited : (88)

References (129)
  • 2
    • 0033118303 scopus 로고    scopus 로고
    • "Annexinopathieso"-a new class of diseases
    • Rand J. H. "Annexinopathieso"-a new class of diseases. N Engl J Med: 1999; 340 13 1035 1036
    • (1999) N Engl J Med , vol.340 , Issue.13 , pp. 1035-1036
    • Rand, J.H.1
  • 3
    • 0034695094 scopus 로고    scopus 로고
    • The annexinopathies: A new category of diseases
    • Rand J. H. The annexinopathies: a new category of diseases. Biochim Biophys Acta: 2000; 1498 2-3 169 173
    • (2000) Biochim Biophys Acta , vol.1498 , Issue.23 , pp. 169-173
    • Rand, J.H.1
  • 6
    • 77950191136 scopus 로고    scopus 로고
    • Annexins as disease modifiers
    • Fatimathas L., Moss S. E. Annexins as disease modifiers. Histol Histopathol: 2010; 25 4 527 532
    • (2010) Histol Histopathol , vol.25 , Issue.4 , pp. 527-532
    • Fatimathas, L.1    Moss, S.E.2
  • 8
    • 84869059089 scopus 로고    scopus 로고
    • The annexin A2/S100A10 system in health and disease: Emerging paradigms
    • Hedhli N., Falcone D. J., Huang B., et al. The annexin A2/S100A10 system in health and disease: emerging paradigms. J Biomed Biotechnol: 2012; 2012 406273
    • (2012) J Biomed Biotechnol , vol.2012 , pp. 406273
    • Hedhli, N.1    Falcone, D.J.2    Huang, B.3
  • 10
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke V., Moss S. E. Annexins: from structure to function. Physiol Rev: 2002; 82 2 331 371 (Pubitemid 34654456)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 11
    • 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., Colella C., Melli M. Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication. Gene: 1990; 95 2 243 251
    • (1990) Gene , vol.95 , Issue.2 , pp. 243-251
    • Spano, F.1    Raugei, G.2    Palla, E.3    Colella, C.4    Melli, M.5
  • 12
    • 0028844290 scopus 로고
    • Annexin II tetramer: Structure and function
    • Waisman D. M. Annexin II tetramer: structure and function. Mol Cell Biochem: 1995; 149-150 301 322
    • (1995) Mol Cell Biochem , vol.149-150 , pp. 301-322
    • Waisman, D.M.1
  • 13
    • 36349028713 scopus 로고    scopus 로고
    • S100A10/p11: Family, friends, and functions
    • J Physiol
    • Rescher U., Gerke V. S100A10/p11: Family, friends, and functions. Pflugers Arch Eur J Physiol: 2007; 455 575 582
    • (2007) Pflugers Arch Eur , vol.455 , pp. 575-582
    • Rescher, U.1    Gerke, V.2
  • 14
    • 0034995073 scopus 로고    scopus 로고
    • S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • DOI 10.1016/S1357-2725(01)00046-2, PII S1357272501000462
    • Donato R. S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int J Biochem Cell Biol: 2001; 33 7 637 668 (Pubitemid 32520962)
    • (2001) International Journal of Biochemistry and Cell Biology , vol.33 , Issue.7 , pp. 637-668
    • Donato, R.1
  • 16
    • 4143100481 scopus 로고    scopus 로고
    • Rab3D and annexin A2 play a role in regulated of vWF, but not tPA, from endothelial cells
    • DOI 10.1038/sj.emboj.7600319
    • Knop M., Aareskjold E., Bode G., Gerke V. Rab3D and annexin A2 play a role in regulated secretion of vWF, but not tPA, from endothelial cells. EMBO J: 2004; 23 15 2982 2992 (Pubitemid 39093592)
    • (2004) EMBO Journal , vol.23 , Issue.15 , pp. 2982-2992
    • Knop, M.1    Aareskjold, E.2    Bode, G.3    Gerke, V.4
  • 17
    • 77954711973 scopus 로고    scopus 로고
    • S100A10-mediated translocation of annexin-A2 to SNARE proteins in adrenergic chromaffin cells undergoing exocytosis
    • Umbrecht-Jenck E., Demais V., Calco V., Bailly Y., Bader M. F., Chasserot-Golaz S. S100A10-mediated translocation of annexin-A2 to SNARE proteins in adrenergic chromaffin cells undergoing exocytosis. Traffic: 2010; 11 7 958 971
    • (2010) Traffic , vol.11 , Issue.7 , pp. 958-971
    • Umbrecht-Jenck, E.1    Demais, V.2    Calco, V.3    Bailly, Y.4    Bader, M.F.5    Chasserot-Golaz, S.6
  • 19
    • 0344012479 scopus 로고    scopus 로고
    • The Annexin 2/S100A10 Complex Controls the Distribution of Transferrin Receptor-containing Recycling Endosomes
    • DOI 10.1091/mbc.E03-06-0387
    • Zobiack N., Rescher U., Ludwig C., Zeuschner D., Gerke V. The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes. Mol Biol Cell: 2003; 14 12 4896 4908 (Pubitemid 37484805)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.12 , pp. 4896-4908
    • Zobiack, N.1    Rescher, U.2    Ludwig, C.3    Zeuschner, D.4    Gerke, V.5
  • 20
    • 0034789106 scopus 로고    scopus 로고
    • Control of the nuclear-cytoplasmic partitioning of annexin II by a nuclear export signal and by p11 binding
    • Eberhard D. A., Karns L. R., VandenBerg S. R., Creutz C. E. Control of the nuclear-cytoplasmic partitioning of annexin II by a nuclear export signal and by p11 binding. J Cell Sci: 2001; 114 Pt 17 3155 3166 (Pubitemid 32910470)
    • (2001) Journal of Cell Science , vol.114 , Issue.17 , pp. 3155-3166
    • Eberhard, D.A.1    Karns, L.R.2    VandenBerg, S.R.3    Creutz, C.E.4
  • 21
    • 84863924021 scopus 로고    scopus 로고
    • Multiple roles of annexin A2 in post-transcriptional regulation of gene expression
    • Vedeler A., Hollås H., Grindheim A. K., Raddum A. M. Multiple roles of annexin A2 in post-transcriptional regulation of gene expression. Curr Protein Pept Sci: 2012; 13 4 401 412
    • (2012) Curr Protein Pept Sci , vol.13 , Issue.4 , pp. 401-412
    • Vedeler, A.1    Hollås, H.2    Grindheim, A.K.3    Raddum, A.M.4
  • 22
    • 84858312078 scopus 로고    scopus 로고
    • Annexin A2 at the interface of actin and membrane dynamics: A focus on its roles in endocytosis and cell polarization
    • Grieve A. G., Moss S. E., Hayes M. J. Annexin A2 at the interface of actin and membrane dynamics: a focus on its roles in endocytosis and cell polarization. Int J Cell Biol: 2012; 2012 852430
    • (2012) Int J Cell Biol , vol.2012 , pp. 852430
    • Grieve, A.G.1    Moss, S.E.2    Hayes, M.J.3
  • 23
    • 79957955929 scopus 로고    scopus 로고
    • The annexin A2 system and vascular homeostasis
    • Flood E. C., Hajjar K. A. The annexin A2 system and vascular homeostasis. Vascul Pharmacol: 2011; 54 3-6 59 67
    • (2011) Vascul Pharmacol , vol.54 , Issue.36 , pp. 59-67
    • Flood, E.C.1    Hajjar, K.A.2
  • 24
    • 77149148713 scopus 로고    scopus 로고
    • The endothelial cell annexin A2 system and vascular fibrinolysis
    • Dassah M., Deora A. B., He K., Hajjar K. A. The endothelial cell annexin A2 system and vascular fibrinolysis. Gen Physiol Biophys: 2009; 28 Spec No Focus F20 F28
    • (2009) Gen Physiol Biophys , vol.28 SPEC NO FOCUS
    • Dassah, M.1    Deora, A.B.2    He, K.3    Hajjar, K.A.4
  • 26
    • 18444386848 scopus 로고    scopus 로고
    • Molecular mechanisms of fibrinolysis
    • DOI 10.1111/j.1365-2141.2005.05444.x
    • Cesarman-Maus G., Hajjar K. A. Molecular mechanisms of fibrinolysis. Br J Haematol: 2005; 129 3 307 321 (Pubitemid 40646889)
    • (2005) British Journal of Haematology , vol.129 , Issue.3 , pp. 307-321
    • Cesarman-Maus, G.1    Hajjar, K.A.2
  • 27
    • 84878296880 scopus 로고    scopus 로고
    • Orkin S.H. Nathan D.G. Ginsburg D. Look A.T. Fisher D.E. Lux S.E. eds. Nathan and Oski's Hematology of Infancy and Childhood. 7th ed Philadelphia Saunders Elsevier
    • Hajjar K. A. The molecular basis of fibrinolysis. In: Orkin S. H., Nathan D. G., Ginsburg D., Look A. T., Fisher D. E., Lux S. E., eds. Nathan and Oski's Hematology of Infancy and Childhood. 7th ed. Philadelphia Saunders Elsevier: 2009; 1425 1447
    • (2009) The Molecular Basis of Fibrinolysis , pp. 1425-1447
    • Hajjar, K.A.1
  • 28
    • 84878288623 scopus 로고    scopus 로고
    • Kaushansky K. Lichtman M.A. Beutler E. Kipps T.J. Seligsohn U. Prchal J.T. eds. Williams Hematology. 8th ed New York McGraw-Hill
    • Hajjar K. A., Ruan J. Fibrinolysis and thrombolysis. In: Kaushansky K., Lichtman M. A., Beutler E., Kipps T. J., Seligsohn U., Prchal J. T., eds. Williams Hematology. 8th ed. New York McGraw-Hill: 2010; 2219 2246
    • (2010) Fibrinolysis and Thrombolysis , pp. 2219-2246
    • Hajjar, K.A.1    Ruan, J.2
  • 29
    • 80052187639 scopus 로고    scopus 로고
    • Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2
    • Valapala M., Vishwanatha J. K. Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2. J Biol Chem: 2011; 286 35 30911 30925
    • (2011) J Biol Chem , vol.286 , Issue.35 , pp. 30911-30925
    • Valapala, M.1    Vishwanatha, J.K.2
  • 30
    • 0036351802 scopus 로고    scopus 로고
    • Annexin 2 "secretion" accompanying exocytosis of chromaffin cells: Possible mechanisms of annexin release
    • DOI 10.1006/excr.2002.5512
    • Faure A. V., Migné C., Devilliers G., Ayala-Sanmartin J. Annexin 2 "secretiono" accompanying exocytosis of chromaffin cells: possible mechanisms of annexin release. Exp Cell Res: 2002; 276 1 79 89 (Pubitemid 34948353)
    • (2002) Experimental Cell Research , vol.276 , Issue.1 , pp. 79-89
    • Faure, A.-V.1    Migne, C.2    Devilliers, G.3    Ayala-Sanmartin, J.4
  • 31
    • 0347481133 scopus 로고    scopus 로고
    • "Nonclassical" Secretion of Annexin A2 to the Lumenal Side of the Enterocyte Brush Border Membrane
    • DOI 10.1021/bi0355239
    • Danielsen E. M., van Deurs B., Hansen G. H. "Nonclassicalo" secretion of annexin A2 to the lumenal side of the enterocyte brush border membrane. Biochemistry: 2003; 42 49 14670 14676 (Pubitemid 37532014)
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14670-14676
    • Danielsen, E.M.1    Van Deurs, B.2    Hansen, G.H.3
  • 32
    • 39749084641 scopus 로고    scopus 로고
    • Active Caspase-1 Is a Regulator of Unconventional Protein Secretion
    • DOI 10.1016/j.cell.2007.12.040, PII S0092867408001116
    • Keller M., Rüegg A., Werner S., Beer H. D. Active caspase-1 is a regulator of unconventional protein secretion. Cell: 2008; 132 5 818 831 (Pubitemid 351312798)
    • (2008) Cell , vol.132 , Issue.5 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.-D.4
  • 33
    • 0037821650 scopus 로고    scopus 로고
    • Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2
    • DOI 10.1242/jcs.00434
    • Peterson E. A., Sutherland M. R., Nesheim M. E., Pryzdial E. L. Thrombin induces endothelial cell-surface exposure of the plasminogen receptor annexin 2. J Cell Sci: 2003; 116 Pt 12 2399 2408 (Pubitemid 36790122)
    • (2003) Journal of Cell Science , vol.116 , Issue.12 , pp. 2399-2408
    • Peterson, E.A.1    Sutherland, M.R.2    Nesheim, M.E.3    Pryzdial, E.L.G.4
  • 34
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface
    • DOI 10.1074/jbc.M408078200
    • Deora A. B., Kreitzer G., Jacovina A. T., Hajjar K. A. An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface. J Biol Chem: 2004; 279 42 43411 43418 (Pubitemid 39390640)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 35
    • 80052684642 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 drives annexin A2 system-mediated perivascular fibrin clearance in oxygen-induced retinopathy in mice
    • Huang B., Deora A. B., He K. L., et al. Hypoxia-inducible factor-1 drives annexin A2 system-mediated perivascular fibrin clearance in oxygen-induced retinopathy in mice. Blood: 2011; 118 10 2918 2929
    • (2011) Blood , vol.118 , Issue.10 , pp. 2918-2929
    • Huang, B.1    Deora, A.B.2    He, K.L.3
  • 36
    • 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: 1980; 21 3 829 836 (Pubitemid 10022891)
    • (1980) Cell , vol.21 , Issue.3 , pp. 829-836
    • Erikson, E.1    Erikson, R.L.2
  • 37
    • 50349088997 scopus 로고    scopus 로고
    • Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11
    • He K. L., Deora A. B., Xiong H., et al. Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11. J Biol Chem: 2008; 283 28 19192 19200
    • (2008) J Biol Chem , vol.283 , Issue.28 , pp. 19192-19200
    • He, K.L.1    Deora, A.B.2    Xiong, H.3
  • 38
    • 79955382971 scopus 로고    scopus 로고
    • Feedback regulation of endothelial cell surface plasmin generation by PKC-dependent phosphorylation of annexin A2
    • He K. L., Sui G., Xiong H., et al. Feedback regulation of endothelial cell surface plasmin generation by PKC-dependent phosphorylation of annexin A2. J Biol Chem: 2011; 286 17 15428 15439
    • (2011) J Biol Chem , vol.286 , Issue.17 , pp. 15428-15439
    • He, K.L.1    Sui, G.2    Xiong, H.3
  • 39
    • 0030580041 scopus 로고    scopus 로고
    • Mapping of a regulatory important site for protein kinase C phosphorylation in the N-terminal domain of annexin II
    • DOI 10.1016/0167-4889(96)00101-2
    • Jost M., Gerke V. Mapping of a regulatory important site for protein kinase C phosphorylation in the N-terminal domain of annexin II. Biochim Biophys Acta: 1996; 1313 3 283 289 (Pubitemid 26342960)
    • (1996) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1313 , Issue.3 , pp. 283-289
    • Jost, M.1    Gerke, V.2
  • 40
    • 0028023538 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II
    • Hajjar K. A., Jacovina A. T., Chacko J. An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II. J Biol Chem: 1994; 269 33 21191 21197
    • (1994) J Biol Chem , vol.269 , Issue.33 , pp. 21191-21197
    • Hajjar, K.A.1    Jacovina, A.T.2    Chacko, J.3
  • 41
    • 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
    • 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. J Biol Chem: 1994; 269 33 21198 21203
    • (1994) J Biol Chem , vol.269 , Issue.33 , pp. 21198-21203
    • Cesarman, G.M.1    Guevara, C.A.2    Hajjar, K.A.3
  • 43
    • 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 (Pubitemid 350159647)
    • (2007) Blood , vol.110 , Issue.10 , pp. 3763-3772
    • Das, R.1    Burke, T.2    Plow, E.F.3
  • 45
    • 0029788890 scopus 로고    scopus 로고
    • Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2
    • DOI 10.1074/jbc.271.35.21652
    • Hajjar K. A., Guevara C. A., Lev E., Dowling K., Chacko J. Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2. J Biol Chem: 1996; 271 35 21652 21659 (Pubitemid 26293036)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.35 , pp. 21652-21659
    • Hajjar, K.A.1    Guevara, C.A.2    Lev, E.3    Dowling, K.4    Chacko, J.5
  • 48
    • 70449428712 scopus 로고    scopus 로고
    • Homocysteine inhibits neoangiogenesis in mice through blockade of annexin A2-dependent fibrinolysis
    • Jacovina A. T., Deora A. B., Ling Q., et al. Homocysteine inhibits neoangiogenesis in mice through blockade of annexin A2-dependent fibrinolysis. J Clin Invest: 2009; 119 11 3384 3394
    • (2009) J Clin Invest , vol.119 , Issue.11 , pp. 3384-3394
    • Jacovina, A.T.1    Deora, A.B.2    Ling, Q.3
  • 49
    • 0032771346 scopus 로고    scopus 로고
    • Homocysteine metabolism
    • DOI 10.1146/annurev.nutr.19.1.217
    • Selhub J. Homocysteine metabolism. Annu Rev Nutr: 1999; 19 217 246 (Pubitemid 29380603)
    • (1999) Annual Review of Nutrition , vol.19 , pp. 217-246
    • Selhub, J.1
  • 50
    • 55549115068 scopus 로고    scopus 로고
    • Homocysteine level and coronary heart disease incidence: A systematic review and meta-analysis
    • Humphrey L. L., Fu R., Rogers K., Freeman M., Helfand M. Homocysteine level and coronary heart disease incidence: a systematic review and meta-analysis. Mayo Clin Proc: 2008; 83 11 1203 1212
    • (2008) Mayo Clin Proc , vol.83 , Issue.11 , pp. 1203-1212
    • Humphrey, L.L.1    Fu, R.2    Rogers, K.3    Freeman, M.4    Helfand, M.5
  • 51
    • 33645796222 scopus 로고    scopus 로고
    • Homocysteine lowering and cardiovascular events after acute myocardial infarction
    • NORVIT Trial Investigators
    • Bonaa K. H., Njolstad I., Ueland P. M., et al. NORVIT Trial Investigators Homocysteine lowering and cardiovascular events after acute myocardial infarction. N Engl J Med: 2006; 354 15 1578 1588
    • (2006) N Engl J Med , vol.354 , Issue.15 , pp. 1578-1588
    • Bonaa, K.H.1    Njolstad, I.2    Ueland, P.M.3
  • 52
    • 0027288252 scopus 로고
    • Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor
    • Hajjar K. A. Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor. J Clin Invest: 1993; 91 6 2873 2879 (Pubitemid 23182548)
    • (1993) Journal of Clinical Investigation , vol.91 , Issue.6 , pp. 2873-2879
    • Hajjar, K.A.1
  • 53
    • 37349042862 scopus 로고    scopus 로고
    • Genes, endothelial function and cerebral small vessel disease in man
    • DOI 10.1113/expphysiol.2007.038752
    • Markus H. S. Genes, endothelial function and cerebral small vessel disease in man. Exp Physiol: 2008; 93 1 121 127 (Pubitemid 350293974)
    • (2008) Experimental Physiology , vol.93 , Issue.1 , pp. 121-127
    • Markus, H.S.1
  • 54
    • 33745672761 scopus 로고    scopus 로고
    • Hyperhomocysteinemia is associated with volumetric white matter change in patients with small vessel disease
    • DOI 10.1007/s00415-005-0022-x
    • Wong A., Mok V., Fan Y. H., Lam W. WM, Liang K. S., Wong K. S. Hyperhomocysteinemia is associated with volumetric white matter change in patients with small vessel disease. J Neurol: 2006; 253 4 441 447 (Pubitemid 43965608)
    • (2006) Journal of Neurology , vol.253 , Issue.4 , pp. 441-447
    • Wong, A.1    Mok, V.2    Fan, Y.H.3    Lam, W.W.M.4    Liang, K.S.5    Wong, K.S.6
  • 55
    • 77953229376 scopus 로고    scopus 로고
    • Annexin A2 combined with low-dose tPA improves thrombolytic therapy in a rat model of focal embolic stroke
    • Zhu H., Fan X., Yu Z., et al. Annexin A2 combined with low-dose tPA improves thrombolytic therapy in a rat model of focal embolic stroke. J Cereb Blood Flow Metab: 2010; 30 6 1137 1146
    • (2010) J Cereb Blood Flow Metab , vol.30 , Issue.6 , pp. 1137-1146
    • Zhu, H.1    Fan, X.2    Yu, Z.3
  • 57
    • 79954610203 scopus 로고    scopus 로고
    • Visualization of clot lysis in a rat embolic stroke model: Application to comparative lytic efficacy
    • Walvick R. P., Bråtane B. T., Henninger N., et al. Visualization of clot lysis in a rat embolic stroke model: application to comparative lytic efficacy. Stroke: 2011; 42 4 1110 1115
    • (2011) Stroke , vol.42 , Issue.4 , pp. 1110-1115
    • Walvick, R.P.1    Bråtane, B.T.2    Henninger, N.3
  • 59
    • 77957979815 scopus 로고    scopus 로고
    • Annexin A2: A tissue plasminogen activator amplifier for thrombolytic stroke therapy
    • Fan X., Yu Z., Liu J., et al. Annexin A2: a tissue plasminogen activator amplifier for thrombolytic stroke therapy. Stroke: 2010; 41 10, Suppl S54 S58
    • (2010) Stroke , vol.41 , Issue.10 SUPPL.
    • Fan, X.1    Yu, Z.2    Liu, J.3
  • 60
    • 0345824713 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator induces opening of the blood-brain barrier via the LDL receptor-related protein
    • DOI 10.1172/JCI200319212
    • Yepes M., Sandkvist M., Moore E. G., Bugge T. H., Strickland D. K., Lawrence D. A. Tissue-type plasminogen activator induces opening of the blood-brain barrier via the LDL receptor-related protein. J Clin Invest: 2003; 112 10 1533 1540 (Pubitemid 38056279)
    • (2003) Journal of Clinical Investigation , vol.112 , Issue.10 , pp. 1533-1540
    • Yepes, M.1    Sandkvist, M.2    Moore, E.G.3    Bugge, T.H.4    Strickland, D.K.5    Lawrence, D.A.6
  • 61
    • 7644227043 scopus 로고    scopus 로고
    • Mechanisms of hemorrhagic transformation after tissue plasminogen activator reperfusion therapy for ischemic stroke
    • DOI 10.1161/01.STR.0000143219.16695.af
    • Wang X., Tsuji K., Lee S. R., et al. Mechanisms of hemorrhagic transformation after tissue plasminogen activator reperfusion therapy for ischemic stroke. Stroke: 2004; 35 11 01 2726 2730 (Pubitemid 39458380)
    • (2004) Stroke , vol.35 , Issue.11 SUPPL. 1 , pp. 2726-2730
    • Wang, X.1    Tsuji, K.2    Lee, S.-R.3    Ning, M.4    Furie, K.L.5    Buchan, A.M.6    Lo, E.H.7
  • 63
    • 59649101650 scopus 로고    scopus 로고
    • Annexin A2: Biology and relevance to the antiphospholipid syndrome
    • Cockrell E., Espinola R. G., McCrae K. R. Annexin A2: biology and relevance to the antiphospholipid syndrome. Lupus: 2008; 17 10 943 951
    • (2008) Lupus , vol.17 , Issue.10 , pp. 943-951
    • Cockrell, E.1    Espinola, R.G.2    McCrae, K.R.3
  • 66
    • 79960013939 scopus 로고    scopus 로고
    • Anti-annexin II antibody is associated with thrombosis and/or pregnancy morbidity in antiphospholipid syndrome and systemic lupus erythematosus with thrombosis
    • Ao W., Zheng H., Chen X. W., Shen Y., Yang C. D. Anti-annexin II antibody is associated with thrombosis and/or pregnancy morbidity in antiphospholipid syndrome and systemic lupus erythematosus with thrombosis. Rheumatol Int: 2011; 31 7 865 869
    • (2011) Rheumatol Int , vol.31 , Issue.7 , pp. 865-869
    • Ao, W.1    Zheng, H.2    Chen, X.W.3    Shen, Y.4    Yang, C.D.5
  • 67
    • 79251640440 scopus 로고    scopus 로고
    • Autoantibodies against the fibrinolytic receptor, annexin A2, in cerebral venous thrombosis
    • Cesarman-Maus G., Cantú-Brito C., Barinagarrementeria F., et al. Autoantibodies against the fibrinolytic receptor, annexin A2, in cerebral venous thrombosis. Stroke: 2011; 42 2 501 503
    • (2011) Stroke , vol.42 , Issue.2 , pp. 501-503
    • Cesarman-Maus, G.1    Cantú-Brito, C.2    Barinagarrementeria, F.3
  • 68
    • 84865685933 scopus 로고    scopus 로고
    • Antibodies against the N-terminal domain of annexin A2 in antiphospholipid syndrome
    • Salle V., Mazière J. C., Brulé A., et al. Antibodies against the N-terminal domain of annexin A2 in antiphospholipid syndrome. Eur J Intern Med: 2012; 23 7 665 668
    • (2012) Eur J Intern Med , vol.23 , Issue.7 , pp. 665-668
    • Salle, V.1    Mazière, J.C.2    Brulé, A.3
  • 69
    • 46749138272 scopus 로고    scopus 로고
    • Anti-annexin II antibodies in systemic autoimmune diseases and antiphospholipid syndrome
    • Salle V., Mazière J. C., Smail A., et al. Anti-annexin II antibodies in systemic autoimmune diseases and antiphospholipid syndrome. J Clin Immunol: 2008; 28 4 291 297
    • (2008) J Clin Immunol , vol.28 , Issue.4 , pp. 291-297
    • Salle, V.1    Mazière, J.C.2    Smail, A.3
  • 70
    • 79960013939 scopus 로고    scopus 로고
    • Anti-annexin II antibody is associated with thrombosis and/or pregnancy morbidity in antiphospholipid syndrome and systemic lupus erythematosus with thrombosis
    • Ao W., Zheng H., Chen X. W., Shen Y., Yang C. D. Anti-annexin II antibody is associated with thrombosis and/or pregnancy morbidity in antiphospholipid syndrome and systemic lupus erythematosus with thrombosis. Rheumatol Int: 2011; 31 7 865 869
    • (2011) Rheumatol Int , vol.31 , Issue.7 , pp. 865-869
    • Ao, W.1    Zheng, H.2    Chen, X.W.3    Shen, Y.4    Yang, C.D.5
  • 71
    • 78149305875 scopus 로고    scopus 로고
    • Anti-dsDNA antibodies bind to mesangial annexin II in lupus nephritis
    • Yung S., Cheung K. F., Zhang Q. Y., Chan T. M. Anti-dsDNA antibodies bind to mesangial annexin II in lupus nephritis. J Am Soc Nephrol: 2010; 21 11 1912 1927
    • (2010) J Am Soc Nephrol , vol.21 , Issue.11 , pp. 1912-1927
    • Yung, S.1    Cheung, K.F.2    Zhang, Q.Y.3    Chan, T.M.4
  • 72
    • 77249085573 scopus 로고    scopus 로고
    • Impaired fibrinolysis in the antiphospholipid syndrome
    • Krone K. A., Allen K. L., McCrae K. R. Impaired fibrinolysis in the antiphospholipid syndrome. Curr Rheumatol Rep: 2010; 12 1 53 57
    • (2010) Curr Rheumatol Rep , vol.12 , Issue.1 , pp. 53-57
    • Krone, K.A.1    Allen, K.L.2    McCrae, K.R.3
  • 73
    • 29544447720 scopus 로고    scopus 로고
    • Preventing stroke in sickle cell anemia
    • DOI 10.1056/NEJMp058274
    • Platt O. S. Preventing stroke in sickle cell anemia. N Engl J Med: 2005; 353 26 2743 2745 (Pubitemid 43016813)
    • (2005) New England Journal of Medicine , vol.353 , Issue.26 , pp. 2743-2745
    • Platt, O.S.1
  • 74
    • 16844366938 scopus 로고    scopus 로고
    • Genetic dissection and prognostic modeling of overt stroke in sickle cell anemia
    • Sebastiani P., Ramoni M. F., Nolan V., Baldwin C. T., Steinberg M. H. Genetic dissection and prognostic modeling of overt stroke in sickle cell anemia. Nat Genet: 2005; 37 4 435 440
    • (2005) Nat Genet , vol.37 , Issue.4 , pp. 435-440
    • Sebastiani, P.1    Ramoni, M.F.2    Nolan, V.3    Baldwin, C.T.4    Steinberg, M.H.5
  • 75
    • 79959278268 scopus 로고    scopus 로고
    • Genetic predictors for stroke in children with sickle cell anemia
    • Flanagan J. M., Frohlich D. M., Howard T. A., et al. Genetic predictors for stroke in children with sickle cell anemia. Blood: 2011; 117 24 6681 6684
    • (2011) Blood , vol.117 , Issue.24 , pp. 6681-6684
    • Flanagan, J.M.1    Frohlich, D.M.2    Howard, T.A.3
  • 77
    • 47049113837 scopus 로고    scopus 로고
    • Identification of genetic polymorphisms associated with risk for pulmonary hypertension in sickle cell disease
    • Ashley-Koch A. E., Elliott L., Kail M. E., et al. Identification of genetic polymorphisms associated with risk for pulmonary hypertension in sickle cell disease. Blood: 2008; 111 12 5721 5726
    • (2008) Blood , vol.111 , Issue.12 , pp. 5721-5726
    • Ashley-Koch, A.E.1    Elliott, L.2    Kail, M.E.3
  • 80
    • 79958720444 scopus 로고    scopus 로고
    • The expression of annexin II and its role in the fibrinolytic activity in acute promyelocytic leukemia
    • Liu Y., Wang Z., Jiang M., et al. The expression of annexin II and its role in the fibrinolytic activity in acute promyelocytic leukemia. Leuk Res: 2011; 35 7 879 884
    • (2011) Leuk Res , vol.35 , Issue.7 , pp. 879-884
    • Liu, Y.1    Wang, Z.2    Jiang, M.3
  • 82
    • 84863582642 scopus 로고    scopus 로고
    • Methionine-induced hyperhomocysteinemia reverts fibrinolytic pathway activation in a murine model of acute promyelocytic leukemia
    • Jácomo R. H., Santana-Lemos B. A., Lima A. SG., et al. Methionine-induced hyperhomocysteinemia reverts fibrinolytic pathway activation in a murine model of acute promyelocytic leukemia. Blood: 2012; 120 1 207 213
    • (2012) Blood , vol.120 , Issue.1 , pp. 207-213
    • Jácomo, R.H.1    Santana-Lemos, B.A.2    Lima, A.S.3
  • 84
    • 79955548255 scopus 로고    scopus 로고
    • A competitive hexapeptide inhibitor of annexin A2 prevents hypoxia-induced angiogenic events
    • Valapala M., Thamake S. I., Vishwanatha J. K. A competitive hexapeptide inhibitor of annexin A2 prevents hypoxia-induced angiogenic events. J Cell Sci: 2011; 124 Pt 9 1453 1464
    • (2011) J Cell Sci , vol.124 , Issue.PART 9 , pp. 1453-1464
    • Valapala, M.1    Thamake, S.I.2    Vishwanatha, J.K.3
  • 85
    • 67650067208 scopus 로고    scopus 로고
    • Vascular endothelial growth factor upregulates expression of annexin A2 in vitro and in a mouse model of ischemic retinopathy
    • Zhao S., Huang L., Wu J., Zhang Y., Pan D., Liu X. Vascular endothelial growth factor upregulates expression of annexin A2 in vitro and in a mouse model of ischemic retinopathy. Mol Vis: 2009; 15 1231 1242
    • (2009) Mol Vis , vol.15 , pp. 1231-1242
    • Zhao, S.1    Huang, L.2    Wu, J.3    Zhang, Y.4    Pan, D.5    Liu, X.6
  • 86
    • 58349095562 scopus 로고    scopus 로고
    • Comprehensive gene-expression profile in murine oxygen-induced retinopathy
    • Sato T., Kusaka S., Hashida N., Saishin Y., Fujikado T., Tano Y. Comprehensive gene-expression profile in murine oxygen-induced retinopathy. Br J Ophthalmol: 2009; 93 1 96 103
    • (2009) Br J Ophthalmol , vol.93 , Issue.1 , pp. 96-103
    • Sato, T.1    Kusaka, S.2    Hashida, N.3    Saishin, Y.4    Fujikado, T.5    Tano, Y.6
  • 87
    • 77949828830 scopus 로고    scopus 로고
    • Annexin A2 promotes choroidal neovascularization by increasing vascular endothelial growth factor expression in a rat model of argon laser coagulation-induced choroidal neovascularization
    • Zhao S. H., Pan D. Y., Zhang Y., Wu J. H., Liu X., Xu Y. Annexin A2 promotes choroidal neovascularization by increasing vascular endothelial growth factor expression in a rat model of argon laser coagulation-induced choroidal neovascularization. Chin Med J (Engl): 2010; 123 6 713 721
    • (2010) Chin Med J (Engl) , vol.123 , Issue.6 , pp. 713-721
    • Zhao, S.H.1    Pan, D.Y.2    Zhang, Y.3    Wu, J.H.4    Liu, X.5    Xu, Y.6
  • 88
    • 77957738254 scopus 로고    scopus 로고
    • Agents that bind annexin A2 suppress ocular neovascularization
    • Lima e Silva R., Shen J., Gong Y. Y., et al. Agents that bind annexin A2 suppress ocular neovascularization. J Cell Physiol: 2010; 225 3 855 864
    • (2010) J Cell Physiol , vol.225 , Issue.3 , pp. 855-864
    • Lima Silva, E.R.1    Shen, J.2    Gong, Y.Y.3
  • 89
    • 0041737535 scopus 로고    scopus 로고
    • Molecular mechanisms of glioma invasiveness: The role of proteases
    • Rao J. S. Molecular mechanisms of glioma invasiveness: the role of proteases. Nat Rev Cancer: 2003; 3 7 489 501 (Pubitemid 37328837)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.7 , pp. 489-501
    • Rao, J.S.1
  • 90
    • 0037344085 scopus 로고    scopus 로고
    • The role of the plasminogen activation cascade in glioma cell invasion: A review
    • DOI 10.1016/S0967-5868(02)00328-4
    • Tsatas D., Kaye A. H. The role of the plasminogen activation cascade in glioma cell invasion: a review. J Clin Neurosci: 2003; 10 2 139 145 (Pubitemid 36358356)
    • (2003) Journal of Clinical Neuroscience , vol.10 , Issue.2 , pp. 139-145
    • Tsatas, D.1    Kaye, A.H.2
  • 91
    • 84878294552 scopus 로고    scopus 로고
    • Proteomics-based analysis of invasion-related proteins in malignant gliomas
    • Epub ahead of print
    • Maruo T., Ichikawa T., Kanzaki H., et al. Proteomics-based analysis of invasion-related proteins in malignant gliomas. Neuropathology: 2012;; Epub ahead of print
    • (2012) Neuropathology
    • Maruo, T.1    Ichikawa, T.2    Kanzaki, H.3
  • 92
    • 14744296225 scopus 로고    scopus 로고
    • Proteomic characterization of harvested pseudopodia with differential gel electrophoresis and specific antibodies
    • DOI 10.1038/labinvest.3700239
    • Beckner M. E., Chen X., An J., Day B. W., Pollack I. F. Proteomic characterization of harvested pseudopodia with differential gel electrophoresis and specific antibodies. Lab Invest: 2005; 85 3 316 327 (Pubitemid 40333149)
    • (2005) Laboratory Investigation , vol.85 , Issue.3 , pp. 316-327
    • Beckner, M.E.1    Chen, X.2    An, J.3    Day, B.W.4    Pollack, I.F.5
  • 93
    • 80053655299 scopus 로고    scopus 로고
    • Annexin A2 promotes tumor progression in glioma cells
    • Zhai H., Acharya S., Gravanis I., et al. Annexin A2 promotes tumor progression in glioma cells. J Neurosci: 2011; 31 40 14346 14360
    • (2011) J Neurosci , vol.31 , Issue.40 , pp. 14346-14360
    • Zhai, H.1    Acharya, S.2    Gravanis, I.3
  • 94
    • 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., Rosenblum M., Israel M. A. Developmental regulation of annexin II (lipocortin 2) in human brain and expression in high grade glioma. Cancer Res: 1992; 52 24 6871 6876 (Pubitemid 23006292)
    • (1992) Cancer Research , vol.52 , Issue.24 , pp. 6871-6876
    • Reeves, S.A.1    Chavez-Kappel, C.2    Davis, R.3    Rosenblum, M.4    Israel, M.A.5
  • 96
    • 0028633553 scopus 로고
    • Annexin II marks astrocytic brain tumors of high histologic grade
    • Roseman B. J., Bollen A., Hsu J., Lamborn K., Israel M. A. Annexin II marks astrocytic brain tumors of high histologic grade. Oncol Res: 1994; 6 12 561 567
    • (1994) Oncol Res , vol.6 , Issue.12 , pp. 561-567
    • Roseman, B.J.1    Bollen, A.2    Hsu, J.3    Lamborn, K.4    Israel, M.A.5
  • 97
    • 84155176820 scopus 로고    scopus 로고
    • Antibody-directed neutralization of annexin II (ANX II) inhibits neoangiogenesis and human breast tumor growth in a xenograft model
    • Sharma M., Blackman M. R., Sharma M. C. Antibody-directed neutralization of annexin II (ANX II) inhibits neoangiogenesis and human breast tumor growth in a xenograft model. Exp Mol Pathol: 2012; 92 1 175 184
    • (2012) Exp Mol Pathol , vol.92 , Issue.1 , pp. 175-184
    • Sharma, M.1    Blackman, M.R.2    Sharma, M.C.3
  • 98
    • 33750812269 scopus 로고    scopus 로고
    • Angiogenesis-associated protein annexin II in breast cancer: Selective expression in invasive breast cancer and contribution to tumor invasion and progression
    • DOI 10.1016/j.yexmp.2006.03.003, PII S0014480006000256
    • Sharma M. R., Koltowski L., Ownbey R. T., Tuszynski G. P., Sharma M. C. Angiogenesis-associated protein annexin II in breast cancer: selective expression in invasive breast cancer and contribution to tumor invasion and progression. Exp Mol Pathol: 2006; 81 2 146 156 (Pubitemid 44715786)
    • (2006) Experimental and Molecular Pathology , vol.81 , Issue.2 , pp. 146-156
    • Sharma, M.R.1    Koltowski, L.2    Ownbey, R.T.3    Tuszynski, G.P.4    Sharma, M.C.5
  • 99
    • 77950628360 scopus 로고    scopus 로고
    • Breast cancer cell surface annexin II induces cell migration and neoangiogenesis via tPA dependent plasmin generation
    • Sharma M., Ownbey R. T., Sharma M. C. Breast cancer cell surface annexin II induces cell migration and neoangiogenesis via tPA dependent plasmin generation. Exp Mol Pathol: 2010; 88 2 278 286
    • (2010) Exp Mol Pathol , vol.88 , Issue.2 , pp. 278-286
    • Sharma, M.1    Ownbey, R.T.2    Sharma, M.C.3
  • 100
    • 80155192757 scopus 로고    scopus 로고
    • Plasmingen receptor S100A10 is essential for the migration of tumor-promoting macrophages into tumor sites
    • Phipps K. D., Surette A. P., O'Connell P. A., Waisman D. M. Plasmingen receptor S100A10 is essential for the migration of tumor-promoting macrophages into tumor sites. Cancer Res: 2011; 7 6676 6683
    • (2011) Cancer Res , vol.7 , pp. 6676-6683
    • Phipps, K.D.1    Surette, A.P.2    O'Connell, P.A.3    Waisman, D.M.4
  • 101
    • 77449113227 scopus 로고    scopus 로고
    • Annexin A2 tetramer activates human and murine macrophages through TLR4
    • Swisher J. FA, Burton N., Bacot S. M., Vogel S. N., Feldman G. M. Annexin A2 tetramer activates human and murine macrophages through TLR4. Blood: 2010; 115 3 549 558
    • (2010) Blood , vol.115 , Issue.3 , pp. 549-558
    • Swisher, J.F.1    Burton, N.2    Bacot, S.M.3    Vogel, S.N.4    Feldman, G.M.5
  • 102
    • 85117738754 scopus 로고    scopus 로고
    • Clinical and prognostic role of annexin A2 in multiple myleoma
    • Seckinger A., Meissner T., Moreaux J., et al. Clinical and prognostic role of annexin A2 in multiple myleoma. Blood: 2012; 120 10871094
    • (2012) Blood , vol.120 , pp. 10871094
    • Seckinger, A.1    Meissner, T.2    Moreaux, J.3
  • 104
    • 70350569248 scopus 로고    scopus 로고
    • Overexpression of Annexin II affects the proliferation, apoptosis, invasion and production of proangiogenic factors in multiple myeloma
    • Bao H., Jiang M., Zhu M., Sheng F., Ruan J., Ruan C. Overexpression of Annexin II affects the proliferation, apoptosis, invasion and production of proangiogenic factors in multiple myeloma. Int J Hematol: 2009; 90 2 177 185
    • (2009) Int J Hematol , vol.90 , Issue.2 , pp. 177-185
    • Bao, H.1    Jiang, M.2    Zhu, M.3    Sheng, F.4    Ruan, J.5    Ruan, C.6
  • 105
    • 84857616177 scopus 로고    scopus 로고
    • Annexin II interactions with the annexin II receptor enhance multiple myeloma cell adhesion and growth in the bone marrow microenvironment
    • D'Souza S., Kurihara N., Shiozawa Y., et al. Annexin II interactions with the annexin II receptor enhance multiple myeloma cell adhesion and growth in the bone marrow microenvironment. Blood: 2012; 119 8 1888 1896
    • (2012) Blood , vol.119 , Issue.8 , pp. 1888-1896
    • D'Souza, S.1    Kurihara, N.2    Shiozawa, Y.3
  • 106
    • 53949112969 scopus 로고    scopus 로고
    • Annexin II/annexin II receptor axis regulates adhesion, migration, homing, and growth of prostate cancer
    • Shiozawa Y., Havens A. M., Jung Y., et al. Annexin II/annexin II receptor axis regulates adhesion, migration, homing, and growth of prostate cancer. J Cell Biochem: 2008; 105 2 370 380
    • (2008) J Cell Biochem , vol.105 , Issue.2 , pp. 370-380
    • Shiozawa, Y.1    Havens, A.M.2    Jung, Y.3
  • 107
    • 33846968447 scopus 로고    scopus 로고
    • P11 (S100A10)-an inducible adaptor protein that modulates neuronal functions
    • Svenningsson P., Greengard P. p11 (S100A10)-an inducible adaptor protein that modulates neuronal functions. Curr Opin Pharmacol: 2007; 7 1 27 32
    • (2007) Curr Opin Pharmacol , vol.7 , Issue.1 , pp. 27-32
    • Svenningsson, P.1    Greengard, P.2
  • 109
    • 77958529521 scopus 로고    scopus 로고
    • Reversal of depressed behaviors in mice by p11 gene therapy in the nucleus accumbens
    • Alexander B., Warner-Schmidt J. L., Eriksson T., et al. Reversal of depressed behaviors in mice by p11 gene therapy in the nucleus accumbens. Sci Transl Med: 2010; 2 54 54ra76
    • (2010) Sci Transl Med , vol.2 , Issue.54
    • Alexander, B.1    Warner-Schmidt, J.L.2    Eriksson, T.3
  • 110
    • 79952620806 scopus 로고    scopus 로고
    • P11 (S100A10) as a potential biomarker of psychiatric patients at risk of suicide
    • Zhang L., Su T. P., Choi K., et al. P11 (S100A10) as a potential biomarker of psychiatric patients at risk of suicide. J Psychiatr Res: 2011; 45 4 435 441
    • (2011) J Psychiatr Res , vol.45 , Issue.4 , pp. 435-441
    • Zhang, L.1    Su, T.P.2    Choi, K.3
  • 112
    • 79959343388 scopus 로고    scopus 로고
    • Antidepressant effects of selective serotonin reuptake inhibitors (SSRIs) are attenuated by antiinflammatory drugs in mice and humans
    • Warner-Schmidt J. L., Vanover K. E., Chen E. Y., Marshall J. J., Greengard P. Antidepressant effects of selective serotonin reuptake inhibitors (SSRIs) are attenuated by antiinflammatory drugs in mice and humans. Proc Natl Acad Sci USA: 2011; 108 22 9262 9267
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.22 , pp. 9262-9267
    • Warner-Schmidt, J.L.1    Vanover, K.E.2    Chen, E.Y.3    Marshall, J.J.4    Greengard, P.5
  • 113
    • 77958575621 scopus 로고    scopus 로고
    • P11 and gene therapy for severe psychiatric disorders: A practical goal
    • Chen G., Twyman R., Manji H. K. p11 and gene therapy for severe psychiatric disorders: a practical goal? Sci Transl Med: 2010; 2 54 54ps51
    • (2010) Sci Transl Med , vol.2 , Issue.54
    • Chen, G.1    Twyman, R.2    Manji, H.K.3
  • 114
    • 0037030729 scopus 로고    scopus 로고
    • Annexin II light chain regulates sensory neuron-specific sodium channel expression
    • DOI 10.1038/nature00781
    • Okuse K., Malik-Hall M., Baker M. D., et al. Annexin II light chain regulates sensory neuron-specific sodium channel expression. Nature: 2002; 417 6889 653 656 (Pubitemid 34614824)
    • (2002) Nature , vol.417 , Issue.6889 , pp. 653-656
    • Okuse, K.1    Malik-Hall, M.2    Baker, M.D.3    Poon, W.-Y.L.4    Kong, H.5    Chao, M.V.6    Wood, J.N.7
  • 115
    • 77149161067 scopus 로고    scopus 로고
    • Unique S100 target protein interactions
    • Rezvanpour A., Shaw G. S. Unique S100 target protein interactions. Gen Physiol Biophys: 2009; 28 Spec No Focus F39 F46
    • (2009) Gen Physiol Biophys , vol.28 SPEC NO FOCUS
    • Rezvanpour, A.1    Shaw, G.S.2
  • 117
    • 34447099071 scopus 로고    scopus 로고
    • Gene expression analysis of frontotemporal lobar degeneration of the motor neuron disease type with ubiquitinated inclusions
    • DOI 10.1007/s00401-007-0240-7
    • Mishra M., Paunesku T., Woloschak G. E., et al. Gene expression analysis of frontotemporal lobar degeneration of the motor neuron disease type with ubiquitinated inclusions. Acta Neuropathol: 2007; 114 1 81 94 (Pubitemid 47029063)
    • (2007) Acta Neuropathologica , vol.114 , Issue.1 , pp. 81-94
    • Mishra, M.1    Paunesku, T.2    Woloschak, G.E.3    Siddique, T.4    Zhu, L.5    Lin, S.6    Greco, K.7    Bigio, E.H.8
  • 118
    • 84856145841 scopus 로고    scopus 로고
    • Genetics of dementia
    • Paulson H. L., Igo I. Genetics of dementia. Semin Neurol: 2011; 31 5 449 460
    • (2011) Semin Neurol , vol.31 , Issue.5 , pp. 449-460
    • Paulson, H.L.1    Igo, I.2
  • 119
    • 79951873381 scopus 로고    scopus 로고
    • The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner
    • Gauthier-Kemper A., Weissmann C., Golovyashkina N., et al. The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner. J Cell Biol: 2011; 192 4 647 661
    • (2011) J Cell Biol , vol.192 , Issue.4 , pp. 647-661
    • Gauthier-Kemper, A.1    Weissmann, C.2    Golovyashkina, N.3
  • 123
    • 33746701373 scopus 로고    scopus 로고
    • Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies
    • Cagliani R., Magri F., Toscano A., et al. Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies. Hum Mutat: 2005; 26 3 283
    • (2005) Hum Mutat , vol.26 , Issue.3 , pp. 283
    • Cagliani, R.1    Magri, F.2    Toscano, A.3
  • 126
    • 70450222517 scopus 로고    scopus 로고
    • Endosomal damage and TLR2 mediated inflammasome activation by alkane particles in the generation of aseptic osteolysis
    • Maitra R., Clement C. C., Scharf B., et al. Endosomal damage and TLR2 mediated inflammasome activation by alkane particles in the generation of aseptic osteolysis. Mol Immunol: 2009; 47 2-3 175 184
    • (2009) Mol Immunol , vol.47 , Issue.23 , pp. 175-184
    • Maitra, R.1    Clement, C.C.2    Scharf, B.3
  • 127
    • 84859179165 scopus 로고    scopus 로고
    • Annexin A2 binds to endosomes following organelle destabilization by particulate wear debris
    • Scharf B., Clement C. C., Wu X. X., et al. Annexin A2 binds to endosomes following organelle destabilization by particulate wear debris. Nat Commun: 2012; 3 755 765
    • (2012) Nat Commun , vol.3 , pp. 755-765
    • Scharf, B.1    Clement, C.C.2    Wu, X.X.3
  • 129
    • 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., et al. The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry: 1998; 37 16958 16966 (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.