메뉴 건너뛰기




Volumn 8, Issue 4, 2009, Pages 318-328

Apoptosis-inducing activity of the S100A8/A9 heterodimer

Author keywords

Apoptosis; Calprotectin; S100A8 A9; Zinc

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; ANTIINFLAMMATORY AGENT; CALGRANULIN A; CALGRANULIN B; CASPASE 10; CASPASE 3; CASPASE 7; CASPASE 8; CASPASE 9; CYTOCHROME C; DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEIN; DEATH RECEPTOR 3; DEATH RECEPTOR 4; DEATH RECEPTOR 5; FAS ANTIGEN; GRANZYME B; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY GB3.1; PENTETIC ACID; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 10; PROTEIN BCL 2; PROTEIN BID; QUINOLINE 3 CARBOXAMIDE DERIVATIVE; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SERINE PROTEINASE OMI; STAT3 PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR 1; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 73649114605     PISSN: 18715230     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152309789838993     Document Type: Review
Times cited : (3)

References (94)
  • 1
    • 0032435515 scopus 로고    scopus 로고
    • Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9)
    • Kerkhoff, C.; Klempt, M., Sorg, C. Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). Biochim. Biophys. Acta, 1998, 1448(2), 200-11.
    • (1998) Biochim. Biophys. Acta , vol.1448 , Issue.2 , pp. 200-211
    • Kerkhoff, C.1    Klempt, M.2    Sorg, C.3
  • 2
    • 0030612692 scopus 로고    scopus 로고
    • The heterodimer of the Ca2+-binding proteins MRP8 and MRP14 binds to arachidonic acid
    • Klempt, M.; H. Melkonyan; W. Nacken; D. Wiesmann; U. Holtkemper, and C. Sorg. The heterodimer of the Ca2+-binding proteins MRP8 and MRP14 binds to arachidonic acid. FEBS Lett., 1997, 408(1), 81-4.
    • (1997) FEBS Lett , vol.408 , Issue.1 , pp. 81-84
    • Klempt, M.1    Melkonyan, H.2    Nacken, W.3    Wiesmann, D.4    Holtkemper, U.5    Sorg, C.6
  • 3
    • 0030898101 scopus 로고    scopus 로고
    • Myeloid-related protein (MRP) 8 and MRP14, calciumbinding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway
    • Rammes, A.; Roth J.; Goebeler, M.; Klempt, M.; Hartmann M., Sorg, C. Myeloid-related protein (MRP) 8 and MRP14, calciumbinding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway. J. Biol. Chem., 1997, 272(14), 9496-9502.
    • (1997) J. Biol. Chem , vol.272 , Issue.14 , pp. 9496-9502
    • Rammes, A.1    Roth, J.2    Goebeler, M.3    Klempt, M.4    Hartmann, M.5    Sorg, C.6
  • 4
    • 0030614513 scopus 로고    scopus 로고
    • Growthinhibitory and apoptosis-inducing activities of calprotectin derived from inflammatory exudate cells on normal fibroblasts: Regulation by metal ions
    • Yui, S.; Mikami, M.; Tsurumaki, K.; Yamazaki, M. Growthinhibitory and apoptosis-inducing activities of calprotectin derived from inflammatory exudate cells on normal fibroblasts: regulation by metal ions. J. Leukoc. Biol., 1997, 6(1), 50-57.
    • (1997) J. Leukoc. Biol , vol.6 , Issue.1 , pp. 50-57
    • Yui, S.1    Mikami, M.2    Tsurumaki, K.3    Yamazaki, M.4
  • 5
    • 58049163436 scopus 로고    scopus 로고
    • Subversion of antimicrobial calprotectin (S100A8/S100A9 complex) in the cytoplasm of TR146 epithelial cells after invasion by Listeria monocytogenes
    • Zaia, A.A.; Sappington, K.J.; Nisapakultorn, K.; Chazin, W.J.; Dietrich, E.A.; Ross, K.F., Herzberg, M.C. Subversion of antimicrobial calprotectin (S100A8/S100A9 complex) in the cytoplasm of TR146 epithelial cells after invasion by Listeria monocytogenes. Mucosal Immunol., 2009, 2(1), 43-53.
    • (2009) Mucosal Immunol , vol.2 , Issue.1 , pp. 43-53
    • Zaia, A.A.1    Sappington, K.J.2    Nisapakultorn, K.3    Chazin, W.J.4    Dietrich, E.A.5    Ross, K.F.6    Herzberg, M.C.7
  • 7
    • 67649208478 scopus 로고    scopus 로고
    • The endogenous Toll-like receptor 4 agonist S100A8/S100A9 (calprotectin) as innate amplifier of infection, autoimmunity, and cancer
    • Ehrchen, J.M.; Sunderkotter, C.; Foell, D.; Vogl, T.; Roth, J. The endogenous Toll-like receptor 4 agonist S100A8/S100A9 (calprotectin) as innate amplifier of infection, autoimmunity, and cancer. J. Leukoc. Biol., 2009, 86(3), 557-563.
    • (2009) J. Leukoc. Biol , vol.86 , Issue.3 , pp. 557-563
    • Ehrchen, J.M.1    Sunderkotter, C.2    Foell, D.3    Vogl, T.4    Roth, J.5
  • 8
    • 0347726938 scopus 로고    scopus 로고
    • Calprotectin (S100A8/S100A9), an inflammatory protein complex from neutrophils with a broad apoptosis-inducing activity
    • Yui, S.; Nakatani, Y.; Mikami, M. Calprotectin (S100A8/S100A9), an inflammatory protein complex from neutrophils with a broad apoptosis-inducing activity. Biol. Pharm. Bull., 2003, 26(6), 753-760.
    • (2003) Biol. Pharm. Bull , vol.26 , Issue.6 , pp. 753-760
    • Yui, S.1    Nakatani, Y.2    Mikami, M.3
  • 9
    • 3042740431 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by S100A8/ A9 in colon cancer cell lines: The role of ROS and the effect of metal ions
    • Ghavami, S.; Kerkhoff, C.; Los, M.; Hashemi, M.; Sorg, C.; Karami-Tehrani, F. Mechanism of apoptosis induced by S100A8/ A9 in colon cancer cell lines: the role of ROS and the effect of metal ions. J. Leukoc. Biol., 2004, 76(1), 169-175.
    • (2004) J. Leukoc. Biol , vol.76 , Issue.1 , pp. 169-175
    • Ghavami, S.1    Kerkhoff, C.2    Los, M.3    Hashemi, M.4    Sorg, C.5    Karami-Tehrani, F.6
  • 11
    • 38349077454 scopus 로고    scopus 로고
    • Evaluation of growth inhibitory and apoptosis inducing activity of human calprotectin on the human gastric cell line (AGS)
    • Zali, H.; Rezaei-Tavirani, M.; Kariminia, A.; Yousefi, R.; Shokrgozar, M.A. Evaluation of growth inhibitory and apoptosis inducing activity of human calprotectin on the human gastric cell line (AGS). Iran Biomed. J., 2008, 12(1), 7-14.
    • (2008) Iran Biomed. J , vol.12 , Issue.1 , pp. 7-14
    • Zali, H.1    Rezaei-Tavirani, M.2    Kariminia, A.3    Yousefi, R.4    Shokrgozar, M.A.5
  • 12
    • 0029583965 scopus 로고
    • Induction of apoptotic cell death in mouse lymphoma and human leukemia cell lines by a calcium-binding protein complex, calprotectin, derived from inflammatory peritoneal exudate cells
    • Yui, S.; Mikami, M.; Yamazaki, M. Induction of apoptotic cell death in mouse lymphoma and human leukemia cell lines by a calcium-binding protein complex, calprotectin, derived from inflammatory peritoneal exudate cells. J. Leukoc. Biol., 1995, 58(6), 650-658.
    • (1995) J. Leukoc. Biol , vol.58 , Issue.6 , pp. 650-658
    • Yui, S.1    Mikami, M.2    Yamazaki, M.3
  • 13
    • 27644494779 scopus 로고    scopus 로고
    • Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity
    • Nakatani, Y.; Yamazaki, M.; Chazin, W.J.; Yui, S. Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity. Mediators Inflamm., 2005, 2005(5), 280-292.
    • (2005) Mediators Inflamm , vol.2005 , Issue.5 , pp. 280-292
    • Nakatani, Y.1    Yamazaki, M.2    Chazin, W.J.3    Yui, S.4
  • 14
    • 0035999163 scopus 로고    scopus 로고
    • Implication of extracellular zinc exclusion by recombinant human calprotectin (MRP8 and MRP14) from target cells in its apoptosisinducing activity
    • Yui, S.; Nakatani, Y.; Hunter, M.J.; Chazin, W.J.; Yamazaki, M. Implication of extracellular zinc exclusion by recombinant human calprotectin (MRP8 and MRP14) from target cells in its apoptosisinducing activity. Mediators Inflamm, 2002, 11(3), 165-172.
    • (2002) Mediators Inflamm , vol.11 , Issue.3 , pp. 165-172
    • Yui, S.1    Nakatani, Y.2    Hunter, M.J.3    Chazin, W.J.4    Yamazaki, M.5
  • 15
    • 22944473642 scopus 로고    scopus 로고
    • Hashemi, M.; Kroczak, T.J. Apoptosis and autoimmune disease. Curr. Med. Chem. - Anti-Inflamm. Anti-Allergy Agents, 2005, 4, 429-437.
    • Hashemi, M.; Kroczak, T.J. Apoptosis and autoimmune disease. Curr. Med. Chem. - Anti-Inflamm. Anti-Allergy Agents, 2005, 4, 429-437.
  • 17
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen, G.S.; Dixit, V.M. Caspases: intracellular signaling by proteolysis. Cell, 1997, 91(4), 443-446.
    • (1997) Cell , vol.91 , Issue.4 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 18
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N.A.; Lazebnik, Y. Caspases: enemies within. Science, 1998, 281(5381), 1312-1316.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 19
    • 34250308322 scopus 로고    scopus 로고
    • Elmore, S. Apoptosis: a review of programmed cell death. Toxicol. Pathol., 2007, 35(4), 495-516.
    • Elmore, S. Apoptosis: a review of programmed cell death. Toxicol. Pathol., 2007, 35(4), 495-516.
  • 20
    • 26444560960 scopus 로고    scopus 로고
    • Caspases: Pharmacological manipulation of cell death
    • Lavrik, I.N.; Golks, A.; Krammer, P.H. Caspases: pharmacological manipulation of cell death. J. Clin. Invest., 2005, 115(10), 2665-2672.
    • (2005) J. Clin. Invest , vol.115 , Issue.10 , pp. 2665-2672
    • Lavrik, I.N.1    Golks, A.2    Krammer, P.H.3
  • 21
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin, M.P.; Goncharov, T.M.; Goltsev, Y.V.; Wallach, D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell, 1996, 85(6), 803-815.
    • (1996) Cell , vol.85 , Issue.6 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 22
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel, F.C.; Hellbardt, S.; Behrmann, I.; Germer, M.; Pawlita, M.; Krammer, P.H.; Peter, M.E. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J., 1995, 14(22), 5579-5588.
    • (1995) EMBO J , vol.14 , Issue.22 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6    Peter, M.E.7
  • 23
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi, A.; Dixit, V.M. Death receptors: signaling and modulation. Science, 1998, 281(5381), 1305-1308.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 24
    • 0032555716 scopus 로고    scopus 로고
    • Luo, X.; Budihardjo, I.; Zou, H.; Slaughter, C.; Wang, X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell, 1998, 94(4), 481-490.
    • Luo, X.; Budihardjo, I.; Zou, H.; Slaughter, C.; Wang, X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell, 1998, 94(4), 481-490.
  • 25
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li, H.; H. Zhu; C.J. Xu, and J. Yuan. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell, 1998, 94(4), 491-501.
    • (1998) Cell , vol.94 , Issue.4 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 26
    • 33846396238 scopus 로고    scopus 로고
    • Cytotoxic effects of intra and extracellular zinc chelation on human breast cancer cells
    • Hashemi, M.; Ghavami, S.; Eshraghi, M.; Booy, E.P.; Los, M. Cytotoxic effects of intra and extracellular zinc chelation on human breast cancer cells. Eur. J. Pharmacol., 2007, 557(1), 9-19.
    • (2007) Eur. J. Pharmacol , vol.557 , Issue.1 , pp. 9-19
    • Hashemi, M.1    Ghavami, S.2    Eshraghi, M.3    Booy, E.P.4    Los, M.5
  • 27
    • 27144519159 scopus 로고    scopus 로고
    • Adenosine and deoxyadenosine induces apoptosis in oestrogen receptor-positive and -negative human breast cancer cells via the intrinsic pathway
    • Hashemi, M.; Karami-Tehrani, F.; Ghavami, S.; Maddika, S.; Los, M. Adenosine and deoxyadenosine induces apoptosis in oestrogen receptor-positive and -negative human breast cancer cells via the intrinsic pathway. Cell Prolif., 2005, 38(5), 269-285.
    • (2005) Cell Prolif , vol.38 , Issue.5 , pp. 269-285
    • Hashemi, M.1    Karami-Tehrani, F.2    Ghavami, S.3    Maddika, S.4    Los, M.5
  • 28
    • 33747884339 scopus 로고    scopus 로고
    • DNA damage-induced cell death by apoptosis
    • Roos, W.P.; Kaina, B. DNA damage-induced cell death by apoptosis. Trends Mol. Med., 2006, 12(9), 440-450.
    • (2006) Trends Mol. Med , vol.12 , Issue.9 , pp. 440-450
    • Roos, W.P.1    Kaina, B.2
  • 30
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk, J.E.; Green, D.R. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol., 2008, 18(4), 157-164.
    • (2008) Trends Cell Biol , vol.18 , Issue.4 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 31
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle, R.J.; Strasser, A. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol., 2008, 9(1), 47-59.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , Issue.1 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 32
    • 0032504574 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: The role of cytochrome c
    • Cai, J.; Yang, J., Jones, D.P. Mitochondrial control of apoptosis: the role of cytochrome c. Biochim. Biophys. Acta, 1998, 1366(1-2), 139-149.
    • (1998) Biochim. Biophys. Acta , vol.1366 , Issue.1-2 , pp. 139-149
    • Cai, J.1    Yang, J.2    Jones, D.P.3
  • 33
    • 34347272654 scopus 로고    scopus 로고
    • Regulation of caspase-9 activity by differential binding to the apoptosome complex
    • Saikumar, P.; Mikhailova, M.; Pandeswara, S.L. Regulation of caspase-9 activity by differential binding to the apoptosome complex. Front Biosci., 2007, 12, 3343-3354.
    • (2007) Front Biosci , vol.12 , pp. 3343-3354
    • Saikumar, P.1    Mikhailova, M.2    Pandeswara, S.L.3
  • 35
    • 0036792475 scopus 로고    scopus 로고
    • The role of mitochondrial factors in apoptosis: A Russian roulette with more than one bullet
    • van Loo, G.; Saelens, X.; van Gurp, M.; MacFarlane, M.; Martin, S.J.; Vandenabeele, P. The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet. Cell Death Differ., 2002, 9(10), 1031-1042.
    • (2002) Cell Death Differ , vol.9 , Issue.10 , pp. 1031-1042
    • van Loo, G.1    Saelens, X.2    van Gurp, M.3    MacFarlane, M.4    Martin, S.J.5    Vandenabeele, P.6
  • 36
    • 5644259587 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins: Translating basic knowledge into clinical practice
    • Schimmer, A.D. Inhibitor of apoptosis proteins: translating basic knowledge into clinical practice. Cancer Res., 2004, 64(20), 7183-7190.
    • (2004) Cancer Res , vol.64 , Issue.20 , pp. 7183-7190
    • Schimmer, A.D.1
  • 37
    • 4344691959 scopus 로고    scopus 로고
    • Shiozaki, E.N.; Shi, Y. Caspases, IAPs and Smac/DIABLO: mechanisms from structural biology. Trends Biochem. Sci., 2004, 29(9), 486-494.
    • Shiozaki, E.N.; Shi, Y. Caspases, IAPs and Smac/DIABLO: mechanisms from structural biology. Trends Biochem. Sci., 2004, 29(9), 486-494.
  • 38
    • 22944472086 scopus 로고    scopus 로고
    • Kerkhoff, C.; Ghavami, S. Induction of apoptotic cell death in tumor cells by S100A8/A9 released from inflammatory cells upon cellular activation. Curr. Med. Chem-Anti-Inflamm. Anti-Allergy Agents, 2005, 4(4), 383-391.
    • Kerkhoff, C.; Ghavami, S. Induction of apoptotic cell death in tumor cells by S100A8/A9 released from inflammatory cells upon cellular activation. Curr. Med. Chem-Anti-Inflamm. Anti-Allergy Agents, 2005, 4(4), 383-391.
  • 39
    • 0036479102 scopus 로고    scopus 로고
    • The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells
    • Robinson, M.J.; Tessier, P.; Poulsom, R.; Hogg, N. The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells. J. Biol. Chem., 2002, 277(5), 3658-3665.
    • (2002) J. Biol. Chem , vol.277 , Issue.5 , pp. 3658-3665
    • Robinson, M.J.1    Tessier, P.2    Poulsom, R.3    Hogg, N.4
  • 40
    • 0036200968 scopus 로고    scopus 로고
    • S100A8, S100A9 and the S100A8/A9 heterodimer complex specifically bind to human endothelial cells: Identification and characterization of ligands for the myeloid-related proteins S100A9 and S100A8/A9 on human dermal microvascular endothelial cell line-1 cells
    • Eue, I.; Konig, S.; Pior, J.; Sorg, C. S100A8, S100A9 and the S100A8/A9 heterodimer complex specifically bind to human endothelial cells: identification and characterization of ligands for the myeloid-related proteins S100A9 and S100A8/A9 on human dermal microvascular endothelial cell line-1 cells. Int. Immunol., 2002, 14(3), 287-297.
    • (2002) Int. Immunol , vol.14 , Issue.3 , pp. 287-297
    • Eue, I.1    Konig, S.2    Pior, J.3    Sorg, C.4
  • 41
    • 0030959556 scopus 로고    scopus 로고
    • A heterocomplex formed by the calcium-binding proteins MRP8 (S100A8) and MRP14 (S100A9) binds unsaturated fatty acids with high affinity
    • Siegenthaler, G.; Roulin, K.; Chatellard-Gruaz, D.; Hotz, R.; Saurat, J.H.; Hellman, U.; Hagens, G. A heterocomplex formed by the calcium-binding proteins MRP8 (S100A8) and MRP14 (S100A9) binds unsaturated fatty acids with high affinity. J. Biol. Chem., 1997, 272(14), 9371-9377.
    • (1997) J. Biol. Chem , vol.272 , Issue.14 , pp. 9371-9377
    • Siegenthaler, G.1    Roulin, K.2    Chatellard-Gruaz, D.3    Hotz, R.4    Saurat, J.H.5    Hellman, U.6    Hagens, G.7
  • 42
    • 0035830423 scopus 로고    scopus 로고
    • Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells
    • Kerkhoff, C.; Sorg, C.; Tandon, N.N.; Nacken, W. Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells. Biochemistry, 2001, 40(1), 241-248.
    • (2001) Biochemistry , vol.40 , Issue.1 , pp. 241-248
    • Kerkhoff, C.1    Sorg, C.2    Tandon, N.N.3    Nacken, W.4
  • 43
    • 28344438623 scopus 로고    scopus 로고
    • S100A8 and S100A9 activate MAP kinase and NF-kappaB signaling pathways and trigger translocation of RAGE in human prostate cancer cells
    • Hermani, A.; Servi, B. De.; Medunjanin, S.; Tessier, P.A.; Mayer, D. S100A8 and S100A9 activate MAP kinase and NF-kappaB signaling pathways and trigger translocation of RAGE in human prostate cancer cells. Exp. Cell Res., 2006, 312(2), 184-197.
    • (2006) Exp. Cell Res , vol.312 , Issue.2 , pp. 184-197
    • Hermani, A.1    Servi, B.D.2    Medunjanin, S.3    Tessier, P.A.4    Mayer, D.5
  • 45
    • 57149103758 scopus 로고    scopus 로고
    • RAGE: A biomarker for acute lung injury
    • Griffiths, M.J.; McAuley, D.F. RAGE: a biomarker for acute lung injury. Thorax, 2008, 63(12), 1034-1036.
    • (2008) Thorax , vol.63 , Issue.12 , pp. 1034-1036
    • Griffiths, M.J.1    McAuley, D.F.2
  • 46
    • 66949157648 scopus 로고    scopus 로고
    • RAGE: A novel biological and genetic marker for vascular disease
    • Kalea, A.Z.; Schmidt, A.M.; Hudson, B.I. RAGE: a novel biological and genetic marker for vascular disease. Clin. Sci. (Lond)., 2009, 116(8), 621-637.
    • (2009) Clin. Sci. (Lond) , vol.116 , Issue.8 , pp. 621-637
    • Kalea, A.Z.1    Schmidt, A.M.2    Hudson, B.I.3
  • 48
    • 64749107607 scopus 로고    scopus 로고
    • (Receptor for Advanced Glycation Endproducts), RAGE ligands, and their role in cancer and inflammation
    • Sparvero, L.J. RAGE (Receptor for Advanced Glycation Endproducts), RAGE ligands, and their role in cancer and inflammation. J. Transl. Med., 2009, 7, 17.
    • (2009) J. Transl. Med , vol.7 , pp. 17
    • Sparvero, L.J.R.1
  • 49
    • 77949274469 scopus 로고    scopus 로고
    • S100A8/A9 induces autophagy and apoptosis via ROS mediated cross-talk between mitochondria and lysosomes and it involves BNIP3
    • In Press
    • Ghavami, S.; Eshraghi, M.; Chazin, W.J.; Klonisch, T.; Halayko, A.J.; Hashemi, M.; Kerkhoff, C.; Mcneill, K., Los, M. S100A8/A9 induces autophagy and apoptosis via ROS mediated cross-talk between mitochondria and lysosomes and it involves BNIP3. Cell Res., 2009, In Press.
    • (2009) Cell Res
    • Ghavami, S.1    Eshraghi, M.2    Chazin, W.J.3    Klonisch, T.4    Halayko, A.J.5    Hashemi, M.6    Kerkhoff, C.7    Mcneill, K.8    Los, M.9
  • 50
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger, R.H.; Nockolds, C.E. Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem., 1973, 248(9), 3313-3326.
    • (1973) J. Biol. Chem , vol.248 , Issue.9 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 51
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loophelix calcium-binding proteins
    • Strynadka, N.C.; James, M.N. Crystal structures of the helix-loophelix calcium-binding proteins. Annu. Rev. Biochem., 1989, 58, 951-998.
    • (1989) Annu. Rev. Biochem , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 53
    • 0032462546 scopus 로고    scopus 로고
    • Structures of EF-hand Ca(2+)-binding proteins: Diversity in the organization, packing and response to Ca2+ binding
    • Nelson, M.R.; Chazin, W.J. Structures of EF-hand Ca(2+)-binding proteins: diversity in the organization, packing and response to Ca2+ binding. Biometals, 1998, 11(4), 297-318.
    • (1998) Biometals , vol.11 , Issue.4 , pp. 297-318
    • Nelson, M.R.1    Chazin, W.J.2
  • 54
    • 0032520211 scopus 로고    scopus 로고
    • The three-dimensional structure of Ca(2+)-bound calcyclin: Implications for Ca(2+)-signal transduction by S100 proteins
    • Sastry, M.; Ketchem, R.R.; Crescenzi, O.; Weber, C.; Lubienski, M.J.; Hidaka, H.; Chazin, W.J. The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins. Structure, 1998, 6(2), 223-231.
    • (1998) Structure , vol.6 , Issue.2 , pp. 223-231
    • Sastry, M.1    Ketchem, R.R.2    Crescenzi, O.3    Weber, C.4    Lubienski, M.J.5    Hidaka, H.6    Chazin, W.J.7
  • 55
    • 0347481143 scopus 로고    scopus 로고
    • Structure of the Ca2+/S100B/NDR kinase peptide complex: Insights into S100 target specificity and activation of the kinase
    • Bhattacharya, S.; Large, E.; Heizmann, C.W.; Hemmings, B.; Chazin, W.J. Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase. Biochemistry, 2003, 42(49), 14416-14426.
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14416-14426
    • Bhattacharya, S.1    Large, E.2    Heizmann, C.W.3    Hemmings, B.4    Chazin, W.J.5
  • 56
    • 0036296180 scopus 로고    scopus 로고
    • A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin
    • Maler, L.; Sastry, M.; Chazin, W.J. A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin. J. Mol. Biol., 2002, 317(2), 279-290.
    • (2002) J. Mol. Biol , vol.317 , Issue.2 , pp. 279-290
    • Maler, L.1    Sastry, M.2    Chazin, W.J.3
  • 58
    • 0033945124 scopus 로고    scopus 로고
    • Structure of the negative regulatory domain of p53 bound to S100B(betabeta)
    • Rustandi, R.R.; Baldisseri, D.M.; Weber, D.J. Structure of the negative regulatory domain of p53 bound to S100B(betabeta). Nat. Struct. Biol., 2000, 7(7), 570-574.
    • (2000) Nat. Struct. Biol , vol.7 , Issue.7 , pp. 570-574
    • Rustandi, R.R.1    Baldisseri, D.M.2    Weber, D.J.3
  • 59
    • 0032520214 scopus 로고    scopus 로고
    • A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form
    • Smith, S.P.; Shaw, G.S. A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure, 1998, 6(2), 211-222.
    • (1998) Structure , vol.6 , Issue.2 , pp. 211-222
    • Smith, S.P.1    Shaw, G.S.2
  • 60
    • 0033043122 scopus 로고    scopus 로고
    • Zinc-binding site of an S100 protein revealed:two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states
    • Brodersen, D.E.; Nyborg, J.; Kjeldgaard M. Zinc-binding site of an S100 protein revealed:two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states. Biochemistry, 1999, 38(6), 1695-1704.
    • (1999) Biochemistry , vol.38 , Issue.6 , pp. 1695-1704
    • Brodersen, D.E.1    Nyborg, J.2    Kjeldgaard, M.3
  • 62
    • 67651160306 scopus 로고    scopus 로고
    • The crystal structures of human S100A12 in apo form and in complex with zinc: New insights into S100A12 oligomerisation
    • Moroz, O.V.; Blagova, E.V.; Wilkinson, A.J.; Wilson, K.S.; Bronstein, I.B. The crystal structures of human S100A12 in apo form and in complex with zinc: new insights into S100A12 oligomerisation. J. Mol. Biol., 2009, 391(3), 536-551.
    • (2009) J. Mol. Biol , vol.391 , Issue.3 , pp. 536-551
    • Moroz, O.V.1    Blagova, E.V.2    Wilkinson, A.J.3    Wilson, K.S.4    Bronstein, I.B.5
  • 63
    • 17144423909 scopus 로고    scopus 로고
    • Solution structure of zinc- and calcium-bound rat S100B as determined by nuclear magnetic resonance spectroscopy
    • Wilder, P.T.; Varney, K.M.; Weiss, M.B.; Gitti, R.K., Weber, D.J. Solution structure of zinc- and calcium-bound rat S100B as determined by nuclear magnetic resonance spectroscopy. Biochemistry, 2005, 44(15), 5690-5702.
    • (2005) Biochemistry , vol.44 , Issue.15 , pp. 5690-5702
    • Wilder, P.T.1    Varney, K.M.2    Weiss, M.B.3    Gitti, R.K.4    Weber, D.J.5
  • 64
    • 34250164654 scopus 로고    scopus 로고
    • The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EF-hand proteins
    • Korndorfer, I.P.; Brueckner, F., Skerra, A. The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EF-hand proteins. J. Mol. Biol., 2007, 370(5), 887-898.
    • (2007) J. Mol. Biol , vol.370 , Issue.5 , pp. 887-898
    • Korndorfer, I.P.1    Brueckner, F.2    Skerra, A.3
  • 65
    • 0036924694 scopus 로고    scopus 로고
    • Evidence for the involvement of the unique C-tail of S100A9 in the binding of arachidonic acid to the heterocomplex S100A8/A9
    • Sopalla, C.; Leukert, N.; Sorg, C., Kerkhoff, C. Evidence for the involvement of the unique C-tail of S100A9 in the binding of arachidonic acid to the heterocomplex S100A8/A9. Biol. Chem., 2002, 383(12), 1895-1905.
    • (2002) Biol. Chem , vol.383 , Issue.12 , pp. 1895-1905
    • Sopalla, C.1    Leukert, N.2    Sorg, C.3    Kerkhoff, C.4
  • 66
    • 39349117867 scopus 로고    scopus 로고
    • Metal chelation and inhibition of bacterial growth in tissue abscesses
    • Corbin, B.D. Metal chelation and inhibition of bacterial growth in tissue abscesses. Science, 2008, 319(5865), 962-965.
    • (2008) Science , vol.319 , Issue.5865 , pp. 962-965
    • Corbin, B.D.1
  • 67
    • 0031892521 scopus 로고    scopus 로고
    • The human S100 protein MRP-14 is a novel activator of the beta 2 integrin Mac-1 on neutrophils
    • Newton, R.A., Hogg, N. The human S100 protein MRP-14 is a novel activator of the beta 2 integrin Mac-1 on neutrophils. J. Immunol., 1998, 160(3), 1427-1435.
    • (1998) J. Immunol , vol.160 , Issue.3 , pp. 1427-1435
    • Newton, R.A.1    Hogg, N.2
  • 68
    • 0035313549 scopus 로고    scopus 로고
    • Srikrishna, G.; Panneerselvam, K.; Westphal,V.; Abraham,V.; Varki, A.;reeze, H.H. Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells. J. Immunol., 2001, 166(7), 4678-4688.
    • Srikrishna, G.; Panneerselvam, K.; Westphal,V.; Abraham,V.; Varki, A.;reeze, H.H. Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells. J. Immunol., 2001, 166(7), 4678-4688.
  • 69
    • 0036479102 scopus 로고    scopus 로고
    • The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells
    • Robinson, M.J.; Tessier, P.; Poulsom, R., Hogg, N. The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells. J. Biol. Chem., 2002, 277(5), 3658-3665.
    • (2002) J. Biol. Chem , vol.277 , Issue.5 , pp. 3658-3665
    • Robinson, M.J.1    Tessier, P.2    Poulsom, R.3    Hogg, N.4
  • 70
    • 0031777737 scopus 로고    scopus 로고
    • Koike, T.; K. Kondo; T. Makita; K. Kajiyama; Yoshida,Y.; Morikawa, M. Intracellular localization of migration inhibitory factorrelated protein (MRP) and detection of cell surface MRP binding sites on human leukemia cell lines. J. Biochem., 1998, 123(6), 1079-1087.
    • Koike, T.; K. Kondo; T. Makita; K. Kajiyama; Yoshida,Y.; Morikawa, M. Intracellular localization of migration inhibitory factorrelated protein (MRP) and detection of cell surface MRP binding sites on human leukemia cell lines. J. Biochem., 1998, 123(6), 1079-1087.
  • 71
    • 34247490186 scopus 로고    scopus 로고
    • Mitochondria, oxidative stress and cell death
    • Ott, M.; Gogvadze,V.; Orrenius,S., Zhivotovsky,B. Mitochondria, oxidative stress and cell death. Apoptosis, 2007, 12(5), 913-22.
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 913-922
    • Ott, M.1    Gogvadze, V.2    Orrenius, S.3    Zhivotovsky, B.4
  • 73
    • 0029165212 scopus 로고
    • Inhibition of adenine nucleotide translocator by lipid peroxidation products
    • Chen, J.J.; Bertrand, H.; Yu. B.P. Inhibition of adenine nucleotide translocator by lipid peroxidation products. Free Radic. Biol. Med., 1995, 19(5), 583-590.
    • (1995) Free Radic. Biol. Med , vol.19 , Issue.5 , pp. 583-590
    • Chen, J.J.1    Bertrand, H.2    Yu, B.P.3
  • 74
    • 0031943314 scopus 로고    scopus 로고
    • Kinetical analysis of tumor cell death-inducing mechanism by polymorphonuclear leukocytederived calprotectin: Involvement of protein synthesis and generation of reactive oxygen species in target cells
    • Mikami, M.; Yamazaki, M., Yui, S. Kinetical analysis of tumor cell death-inducing mechanism by polymorphonuclear leukocytederived calprotectin: involvement of protein synthesis and generation of reactive oxygen species in target cells. Microbiol. Immunol., 1998, 42(3), 211-221.
    • (1998) Microbiol. Immunol , vol.42 , Issue.3 , pp. 211-221
    • Mikami, M.1    Yamazaki, M.2    Yui, S.3
  • 75
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami, N.; Marchetti, P.; Castedo, M.; Zanin, C.; Vayssiere, J.L.; Petit, P.X., Kroemer, G. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med., 1995, 181(5), 1661-1672.
    • (1995) J. Exp. Med , vol.181 , Issue.5 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssiere, J.L.5    Petit, P.X.6    Kroemer, G.7
  • 76
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai, A.; Bassik, M.C.; Walensky, L.D.; Sorcinelli, M.D; Weiler, S., Korsmeyer S.J. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell, 2002, 2(3), 183-192.
    • (2002) Cancer Cell , vol.2 , Issue.3 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 78
    • 20444486559 scopus 로고    scopus 로고
    • Oltersdorf, T.; Elmore, S.W.; Shoemaker, A.R.; Armstrong, R.C.; Augeri, D.J.; Belli, B.A.; Bruncko, M.; Deckwerth, T.L.; Dinges, J.; Hajduk, P.J.; Joseph, M.K.; Kitada, S.; Korsmeyer, S.J.; Kunzer, A.R.; Letai, A.; Li, C.; Mitten, M.J.; Nettesheim, D.G.; Ng, S.; Nimmer, P.M.; O'Connor, J.M.; Oleksijew, A.; Petros, A.M.; Reed, J.C.; Shen, W.; Tahir, S.K.; Thompson, C.B.; Tomaselli, K.J.; Wang, B.; Wendt, M.D.; Zhang, H.; Fesik, S.W.; Rosenberg, S.H. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature, 2005, 435(7042), 677-681.
    • Oltersdorf, T.; Elmore, S.W.; Shoemaker, A.R.; Armstrong, R.C.; Augeri, D.J.; Belli, B.A.; Bruncko, M.; Deckwerth, T.L.; Dinges, J.; Hajduk, P.J.; Joseph, M.K.; Kitada, S.; Korsmeyer, S.J.; Kunzer, A.R.; Letai, A.; Li, C.; Mitten, M.J.; Nettesheim, D.G.; Ng, S.; Nimmer, P.M.; O'Connor, J.M.; Oleksijew, A.; Petros, A.M.; Reed, J.C.; Shen, W.; Tahir, S.K.; Thompson, C.B.; Tomaselli, K.J.; Wang, B.; Wendt, M.D.; Zhang, H.; Fesik, S.W.; Rosenberg, S.H. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature, 2005, 435(7042), 677-681.
  • 79
    • 0034730884 scopus 로고    scopus 로고
    • Mitochondria: Execution central
    • Gottlieb, R.A. Mitochondria: execution central. FEBS Lett., 2000, 482(1-2), 6-12.
    • (2000) FEBS Lett , vol.482 , Issue.1-2 , pp. 6-12
    • Gottlieb, R.A.1
  • 81
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green, D., Kroemer, G. The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol., 1998, 8(7), 267-271.
    • (1998) Trends Cell Biol , vol.8 , Issue.7 , pp. 267-271
    • Green, D.1    Kroemer, G.2
  • 82
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev., 2001, 15(22), 2922-2933.
    • (2001) Genes Dev , vol.15 , Issue.22 , pp. 2922-2933
    • Wang, X.1
  • 83
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer, G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat. Med., 1997, 3(6), 614-20.
    • (1997) Nat. Med , vol.3 , Issue.6 , pp. 614-620
    • Kroemer, G.1
  • 84
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri, K.F., Kroemer,G. Organelle-specific initiation of cell death pathways. Nat. Cell Biol., 2001, 3(11), E255-63.
    • (2001) Nat. Cell Biol , vol.3 , Issue.11
    • Ferri, K.F.1    Kroemer, G.2
  • 85
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial, N.N., Korsmeyer, S.J. Cell death: critical control points. Cell, 2004, 116(2), 205-219.
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 86
    • 27544471076 scopus 로고    scopus 로고
    • The mitochondrial death squad: Hardened killers or innocent bystanders?
    • Ekert, P.G., Vaux, D.L. The mitochondrial death squad: hardened killers or innocent bystanders? Curr. Opin. Cell Biol., 2005, 17(6), 626-630.
    • (2005) Curr. Opin. Cell Biol , vol.17 , Issue.6 , pp. 626-630
    • Ekert, P.G.1    Vaux, D.L.2
  • 87
    • 0034682695 scopus 로고    scopus 로고
    • Apoptosis. Mitochondria--the death signal integrators
    • Brenner, C., Kroemer, G. Apoptosis. Mitochondria--the death signal integrators. Science, 2000, 289(5482), 1150-1151.
    • (2000) Science , vol.289 , Issue.5482 , pp. 1150-1151
    • Brenner, C.1    Kroemer, G.2
  • 88
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D.R., Reed, J.C. Mitochondria and apoptosis. Science, 1998, 281(5381), 1309-1312.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 90
    • 53349125963 scopus 로고    scopus 로고
    • Proinflammatory S100 proteins regulate the accumulation of myeloid-derived suppressor cells
    • Sinha, P.; Okoro, C.; Foell, D.; Freeze, H.H.; Ostrand-Rosenberg, S., Srikrishna, G. Proinflammatory S100 proteins regulate the accumulation of myeloid-derived suppressor cells. J. Immunol., 2008, 181(7), 4666-4675.
    • (2008) J. Immunol , vol.181 , Issue.7 , pp. 4666-4675
    • Sinha, P.1    Okoro, C.2    Foell, D.3    Freeze, H.H.4    Ostrand-Rosenberg, S.5    Srikrishna, G.6
  • 91
    • 53349099219 scopus 로고    scopus 로고
    • Inhibition of dendritic cell differentiation and accumulation of myeloid-derived suppressor cells in cancer is regulated by S100A9 protein
    • Cheng, P.; Corzo, C.A.; Luetteke, N.; Yu, B.; Nagaraj, S.; Bui, M.M.; Ortiz, M.; Nacken, W.; Sorg, C.; Vogl, T.; Roth, J.; Gabrilovich, D.I. Inhibition of dendritic cell differentiation and accumulation of myeloid-derived suppressor cells in cancer is regulated by S100A9 protein. J. Exp. Med., 2008, 205(10), 2235-2249.
    • (2008) J. Exp. Med , vol.205 , Issue.10 , pp. 2235-2249
    • Cheng, P.1    Corzo, C.A.2    Luetteke, N.3    Yu, B.4    Nagaraj, S.5    Bui, M.M.6    Ortiz, M.7    Nacken, W.8    Sorg, C.9    Vogl, T.10    Roth, J.11    Gabrilovich, D.I.12
  • 93
    • 70149117029 scopus 로고    scopus 로고
    • A novel p53 target gene, S100A9, induces p53-dependent cellular apoptosis and mediates the p53 apoptosis pathway
    • Li, C.; Chen, H.; Ding, F.; Zhang, Y.; Luo, A.; Wang, M., Liu, Z. A novel p53 target gene, S100A9, induces p53-dependent cellular apoptosis and mediates the p53 apoptosis pathway. Biochem. J., 2009, 422(2), 363-372.
    • (2009) Biochem. J , vol.422 , Issue.2 , pp. 363-372
    • Li, C.1    Chen, H.2    Ding, F.3    Zhang, Y.4    Luo, A.5    Wang, M.6    Liu, Z.7
  • 94
    • 65949111512 scopus 로고    scopus 로고
    • Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3- carboxamides
    • Bjork, P.; Bjork, A.; Vogl, T.; Stenstrom, M.; Liberg, D.; Olsson, A.; Roth, J.; Ivars, F.; Leanderson, T. Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3- carboxamides. PLoS Biol., 2009, 7(4), e97.
    • (2009) PLoS Biol , vol.7 , Issue.4
    • Bjork, P.1    Bjork, A.2    Vogl, T.3    Stenstrom, M.4    Liberg, D.5    Olsson, A.6    Roth, J.7    Ivars, F.8    Leanderson, T.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.