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Volumn 1793, Issue 6, 2009, Pages 993-1007

Binding of S100 proteins to RAGE: An update

Author keywords

RAGE; S100; Surface plasmon resonance

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; CALCIUM BINDING PROTEIN; CALCYCLIN; CALGRANULIN A; IMMUNOGLOBULIN; PROTEIN S 100; PROTEIN S100A1; PROTEIN S100A11; PROTEIN S100A12; PROTEIN S100A13; PROTEIN S100A2; PROTEIN S100A5; PROTEIN S100B; PROTEIN S100P; PSORIASIN; UNCLASSIFIED DRUG;

EID: 67349265963     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.11.016     Document Type: Review
Times cited : (416)

References (357)
  • 1
    • 0036580943 scopus 로고    scopus 로고
    • S100 proteins: structure, functions and pathology
    • Heizmann C.W., Fritz G., and Schäfer B.W. S100 proteins: structure, functions and pathology. Front Biosci. 7 (2002) d1356-68
    • (2002) Front Biosci. , vol.7
    • Heizmann, C.W.1    Fritz, G.2    Schäfer, B.W.3
  • 2
    • 0142229704 scopus 로고    scopus 로고
    • Intracellular and extracellular roles of S100 proteins
    • Donato R. Intracellular and extracellular roles of S100 proteins. Microsc. Res. Tech. 60 (2003) 540-551
    • (2003) Microsc. Res. Tech. , vol.60 , pp. 540-551
    • Donato, R.1
  • 4
    • 67349199049 scopus 로고    scopus 로고
    • E. Leclerc, E. Stürchler and C.W. Heizmann. in (Mikoshiba, ed.) Handbook of Neurochemistry and Molecular Neurobiology, Springer, New York in press.
    • E. Leclerc, E. Stürchler and C.W. Heizmann. in (Mikoshiba, ed.) Handbook of Neurochemistry and Molecular Neurobiology, Springer, New York in press.
  • 7
    • 40749099385 scopus 로고    scopus 로고
    • Calcium, troponin, calmodulin, S100 proteins: from myocardial basics to new therapeutic strategies
    • Schaub M.C., and Heizmann C.W. Calcium, troponin, calmodulin, S100 proteins: from myocardial basics to new therapeutic strategies. Biochem. Biophys. Res. Commun. 369 (2008) 247-264
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 247-264
    • Schaub, M.C.1    Heizmann, C.W.2
  • 8
    • 0242304100 scopus 로고    scopus 로고
    • Molecular mechanisms of S100-target protein interactions
    • Zimmer D.B., Wright Sadosky P., and Weber D.J. Molecular mechanisms of S100-target protein interactions. Microsc. Res. Tech. 60 (2003) 552-559
    • (2003) Microsc. Res. Tech. , vol.60 , pp. 552-559
    • Zimmer, D.B.1    Wright Sadosky, P.2    Weber, D.J.3
  • 9
    • 1642336086 scopus 로고    scopus 로고
    • Messerschmidt A., Bode W., and Cygler M. (Eds), Wiley, Chichester
    • Fritz G., and Heizmann C.W. In: Messerschmidt A., Bode W., and Cygler M. (Eds). Handbook of Metalloproteins Vol. 3 (2004), Wiley, Chichester 529-540
    • (2004) Handbook of Metalloproteins , vol.3 , pp. 529-540
    • Fritz, G.1    Heizmann, C.W.2
  • 11
    • 33744782044 scopus 로고    scopus 로고
    • Calcium-dependent and -independent interactions of the S100 protein family
    • Santamaria-Kisiel L., Rintala-Dempsey A.C., and Shaw G.S. Calcium-dependent and -independent interactions of the S100 protein family. Biochem. J. 396 (2006) 201-214
    • (2006) Biochem. J. , vol.396 , pp. 201-214
    • Santamaria-Kisiel, L.1    Rintala-Dempsey, A.C.2    Shaw, G.S.3
  • 17
    • 0034705690 scopus 로고    scopus 로고
    • Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system.
    • Tarabykina S. Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system. FEBS Lett. 475 (2000) 187-191
    • (2000) FEBS Lett. , vol.475 , pp. 187-191
    • Tarabykina, S.1
  • 18
    • 0029090604 scopus 로고
    • The myeloic related protein MRO8/14 (27E10 antigen)-usefulness as a potential marker for disease activity in ulcerative colitis and putative biological function
    • Lugering N., Stoll R., Schmid K.W., Kucharzik T., Stein H., Burmeister G., Sorg C., and Domschke W. The myeloic related protein MRO8/14 (27E10 antigen)-usefulness as a potential marker for disease activity in ulcerative colitis and putative biological function. Eur. J. Clin. Invest. 25 (1995) 659-664
    • (1995) Eur. J. Clin. Invest. , vol.25 , pp. 659-664
    • Lugering, N.1    Stoll, R.2    Schmid, K.W.3    Kucharzik, T.4    Stein, H.5    Burmeister, G.6    Sorg, C.7    Domschke, W.8
  • 21
    • 33744813581 scopus 로고    scopus 로고
    • Calcium-dependent tetramer formation of S100A8 and S100A9 is essential for biological activity
    • Leukert N., Vogl T., Strupat K., Reichelt R., Sorg C., and Roth J. Calcium-dependent tetramer formation of S100A8 and S100A9 is essential for biological activity. J. Mol. Biol. 359 (2006) 961-972
    • (2006) J. Mol. Biol. , vol.359 , pp. 961-972
    • Leukert, N.1    Vogl, T.2    Strupat, K.3    Reichelt, R.4    Sorg, C.5    Roth, J.6
  • 24
    • 33947510205 scopus 로고    scopus 로고
    • Hexameric calgranulin C (S100A12) binds to the receptor for advanced glycated end products (RAGE) using symmetric hydrophobic target-binding patches
    • Xie J., Burz D.S., He W., Bronstein I.B., Lednev I., and Shekhtman A. Hexameric calgranulin C (S100A12) binds to the receptor for advanced glycated end products (RAGE) using symmetric hydrophobic target-binding patches. J. Biol. Chem. 282 (2007) 4218-4231
    • (2007) J. Biol. Chem. , vol.282 , pp. 4218-4231
    • Xie, J.1    Burz, D.S.2    He, W.3    Bronstein, I.B.4    Lednev, I.5    Shekhtman, A.6
  • 27
    • 34249827565 scopus 로고    scopus 로고
    • S100B protein is released from rat neonatal neurons, astrocytes, and microglia by in vitro trauma and anti-S100 increases trauma-induced delayed neuronal injury and negates the protective effect of exogenous S100B on neurons
    • Ellis E.F., Willoughby K.A., Sparks S.A., and Chen T. S100B protein is released from rat neonatal neurons, astrocytes, and microglia by in vitro trauma and anti-S100 increases trauma-induced delayed neuronal injury and negates the protective effect of exogenous S100B on neurons. J. Neurochem. 101 (2007) 1463-1470
    • (2007) J. Neurochem. , vol.101 , pp. 1463-1470
    • Ellis, E.F.1    Willoughby, K.A.2    Sparks, S.A.3    Chen, T.4
  • 28
    • 0035903170 scopus 로고    scopus 로고
    • 2+ levels regulate the alternative cell density-dependent secretion of S100B in human glioblastoma cells
    • 2+ levels regulate the alternative cell density-dependent secretion of S100B in human glioblastoma cells. J. Biol. Chem. 276 (2001) 30819-30826
    • (2001) J. Biol. Chem. , vol.276 , pp. 30819-30826
    • Davey, G.E.1    Murmann, P.2    Heizmann, C.W.3
  • 29
    • 49649090145 scopus 로고    scopus 로고
    • RAGE recycles at the plasma membrane in S100B secretory vesicles and promotes Schwann cells morphological changes
    • Perrone L., Peluso G., and Melone M.A. RAGE recycles at the plasma membrane in S100B secretory vesicles and promotes Schwann cells morphological changes. J. Cell. Physiol. 217 (2008) 60-71
    • (2008) J. Cell. Physiol. , vol.217 , pp. 60-71
    • Perrone, L.1    Peluso, G.2    Melone, M.A.3
  • 31
    • 0030898101 scopus 로고    scopus 로고
    • Myeloid-related protein (MRP) 8 and MRP14, calcium-binding 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., and Sorg C. Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway. J. Biol. Chem. 272 (1997) 9496-9502
    • (1997) J. Biol. Chem. , vol.272 , pp. 9496-9502
    • Rammes, A.1    Roth, J.2    Goebeler, M.3    Klempt, M.4    Hartmann, M.5    Sorg, C.6
  • 32
    • 0033998727 scopus 로고    scopus 로고
    • Calcium-dependent secretion in human neutrophils: a proteomic approach
    • Boussac M., and Garin J. Calcium-dependent secretion in human neutrophils: a proteomic approach. Electrophoresis 21 (2000) 665-672
    • (2000) Electrophoresis , vol.21 , pp. 665-672
    • Boussac, M.1    Garin, J.2
  • 33
    • 33645129229 scopus 로고    scopus 로고
    • Parietal endoderm secreted S100A4 promotes early cardiomyogenesis in embryoid bodies
    • Stary M., Schneider M., Sheikh S.P., and Weitzer G. Parietal endoderm secreted S100A4 promotes early cardiomyogenesis in embryoid bodies. Biochem. Biophys. Res. Commun. 343 (2006) 555-563
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 555-563
    • Stary, M.1    Schneider, M.2    Sheikh, S.P.3    Weitzer, G.4
  • 36
    • 35748967902 scopus 로고    scopus 로고
    • S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains
    • Leclerc E., Fritz G., Weibel M., Heizmann C.W., and Galichet A. S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains. J. Biol. Chem. 282 (2007) 31317-31331
    • (2007) J. Biol. Chem. , vol.282 , pp. 31317-31331
    • Leclerc, E.1    Fritz, G.2    Weibel, M.3    Heizmann, C.W.4    Galichet, A.5
  • 39
    • 27644454639 scopus 로고    scopus 로고
    • Total chemical synthesis of human psoriasin by native chemical ligation
    • Li X., de Leeuw E., and Lu W. Total chemical synthesis of human psoriasin by native chemical ligation. Biochemistry 44 (2005) 14688-14694
    • (2005) Biochemistry , vol.44 , pp. 14688-14694
    • Li, X.1    de Leeuw, E.2    Lu, W.3
  • 40
    • 33947241444 scopus 로고    scopus 로고
    • S100A7 (Psoriasin)-mechanism of antibacterial action in wounds
    • Lee K.C., and Eckert R.L. S100A7 (Psoriasin)-mechanism of antibacterial action in wounds. J. Invest. Dermatol. 127 (2007) 945-957
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 945-957
    • Lee, K.C.1    Eckert, R.L.2
  • 41
    • 0033635831 scopus 로고    scopus 로고
    • RAGE: a multiligand receptor contributing to the cellular response in diabetic vasculopathy and inflammation
    • Schmidt A.M., Hofmann M., Taguchi A., Yan S.D., and Stern D.M. RAGE: a multiligand receptor contributing to the cellular response in diabetic vasculopathy and inflammation. Semin. Thromb. Hemost. 26 (2000) 485-493
    • (2000) Semin. Thromb. Hemost. , vol.26 , pp. 485-493
    • Schmidt, A.M.1    Hofmann, M.2    Taguchi, A.3    Yan, S.D.4    Stern, D.M.5
  • 42
    • 38349138516 scopus 로고    scopus 로고
    • RAGE: a single receptor for several ligands and different cellular responses: the case of certain S100 proteins
    • Donato R. RAGE: a single receptor for several ligands and different cellular responses: the case of certain S100 proteins. Curr. Mol. Med. 7 (2007) 711-724
    • (2007) Curr. Mol. Med. , vol.7 , pp. 711-724
    • Donato, R.1
  • 43
    • 0026650438 scopus 로고
    • Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface
    • Schmidt A.M., Vianna M., Gerlach M., Brett J., Ryan J., Kao J., Esposito C., Hegarty H., Hurley W., Clauss M., et al. Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface. J. Biol. Chem. 267 (1992) 14987-14997
    • (1992) J. Biol. Chem. , vol.267 , pp. 14987-14997
    • Schmidt, A.M.1    Vianna, M.2    Gerlach, M.3    Brett, J.4    Ryan, J.5    Kao, J.6    Esposito, C.7    Hegarty, H.8    Hurley, W.9    Clauss, M.10
  • 45
    • 0030899695 scopus 로고    scopus 로고
    • The First Immunoglobulin-like Neural Cell Adhesion Molecule (NCAM) Domain is involved in double-reciprocal Interaction with the Second Immunoglobulin-like NCAM Domain and in Heparin Binding
    • Kiselyov V.V., Berezin V., Maar T.E., Soroka V., Edvardsen K., Schousboe A., and Bock E. The First Immunoglobulin-like Neural Cell Adhesion Molecule (NCAM) Domain is involved in double-reciprocal Interaction with the Second Immunoglobulin-like NCAM Domain and in Heparin Binding. J. Biol. Chem. 272 (1997) 10125-10134
    • (1997) J. Biol. Chem. , vol.272 , pp. 10125-10134
    • Kiselyov, V.V.1    Berezin, V.2    Maar, T.E.3    Soroka, V.4    Edvardsen, K.5    Schousboe, A.6    Bock, E.7
  • 46
    • 0042620298 scopus 로고    scopus 로고
    • Membrane proteins with immunoglobulin-like domains-a master superfamily of interaction molecules
    • Barclay A.N. Membrane proteins with immunoglobulin-like domains-a master superfamily of interaction molecules. Semin. Immunol. 15 (2003) 215-223
    • (2003) Semin. Immunol. , vol.15 , pp. 215-223
    • Barclay, A.N.1
  • 48
    • 0034695098 scopus 로고    scopus 로고
    • The biology of the receptor for advanced glycation end products and its ligands
    • Schmidt A.M., Yan S.D., Yan S.F., and Stern D.M. The biology of the receptor for advanced glycation end products and its ligands. Biochim. Biophys. Acta 1498 (2000) 99-111
    • (2000) Biochim. Biophys. Acta , vol.1498 , pp. 99-111
    • Schmidt, A.M.1    Yan, S.D.2    Yan, S.F.3    Stern, D.M.4
  • 49
    • 55249118389 scopus 로고    scopus 로고
    • Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE)
    • Xie J., Reverdatto S., Frolov A., Hoffmann R., Burz D.S., and Shekhtman A. Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE). J. Biol. Chem. 283 (2008) 27255-27269
    • (2008) J. Biol. Chem. , vol.283 , pp. 27255-27269
    • Xie, J.1    Reverdatto, S.2    Frolov, A.3    Hoffmann, R.4    Burz, D.S.5    Shekhtman, A.6
  • 50
    • 0036320685 scopus 로고    scopus 로고
    • N -Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth
    • Srikrishna G., Huttunen H.J., Johansson L., Weigle B., Yamaguchi Y., Rauvala H., and Freeze H.H. N -Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth. J. Neurochem. 80 (2002) 998-1008
    • (2002) J. Neurochem. , vol.80 , pp. 998-1008
    • Srikrishna, G.1    Huttunen, H.J.2    Johansson, L.3    Weigle, B.4    Yamaguchi, Y.5    Rauvala, H.6    Freeze, H.H.7
  • 52
    • 0032500885 scopus 로고    scopus 로고
    • Sequencing of two alternatively spliced mRNAs corresponding to the extracellular domain of the rat receptor for advanced glycosylation end products (RAGE)
    • Giron M.D., Vargas A.M., Suarez M.D., and Salto R. Sequencing of two alternatively spliced mRNAs corresponding to the extracellular domain of the rat receptor for advanced glycosylation end products (RAGE). Biochem. Biophys. Res. Commun. 251 (1998) 230-234
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 230-234
    • Giron, M.D.1    Vargas, A.M.2    Suarez, M.D.3    Salto, R.4
  • 53
    • 0142122366 scopus 로고    scopus 로고
    • Tissue-specific expression patterns of the RAGE receptor and its soluble forms-a result of regulated alternative splicing?
    • Schlueter C., Hauke S., Flohr A.M., Rogalla P., and Bullerdiek J. Tissue-specific expression patterns of the RAGE receptor and its soluble forms-a result of regulated alternative splicing?. Biochim. Biophys. Acta 1630 (2003) 1-6
    • (2003) Biochim. Biophys. Acta , vol.1630 , pp. 1-6
    • Schlueter, C.1    Hauke, S.2    Flohr, A.M.3    Rogalla, P.4    Bullerdiek, J.5
  • 54
    • 0032741165 scopus 로고    scopus 로고
    • cDNA cloning of a novel secreted isoform of the human receptor for advanced glycation end products and characterization of cells co-expressing cell-surface scavenger receptors and Swedish mutant amyloid precursor protein
    • Malherbe P., Richards J.G., Gaillard H., Thompson A., Diener C., Schuler A., and Huber G. cDNA cloning of a novel secreted isoform of the human receptor for advanced glycation end products and characterization of cells co-expressing cell-surface scavenger receptors and Swedish mutant amyloid precursor protein. Brain Res. Mol. Brain Res. 71 (1999) 159-170
    • (1999) Brain Res. Mol. Brain Res. , vol.71 , pp. 159-170
    • Malherbe, P.1    Richards, J.G.2    Gaillard, H.3    Thompson, A.4    Diener, C.5    Schuler, A.6    Huber, G.7
  • 56
    • 0037444761 scopus 로고    scopus 로고
    • Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury
    • Yonekura H., Yamamoto Y., Sakurai S., Petrova R.G., Abedin M.J., Li H., Yasui K., Takeuchi M., Makita Z., Takasawa S., Okamoto H., Watanabe T., and Yamamoto H. Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury. Biochem. J. 370 (2003) 1097-1109
    • (2003) Biochem. J. , vol.370 , pp. 1097-1109
    • Yonekura, H.1    Yamamoto, Y.2    Sakurai, S.3    Petrova, R.G.4    Abedin, M.J.5    Li, H.6    Yasui, K.7    Takeuchi, M.8    Makita, Z.9    Takasawa, S.10    Okamoto, H.11    Watanabe, T.12    Yamamoto, H.13
  • 57
    • 1142273309 scopus 로고    scopus 로고
    • Expression of a novel secreted splice variant of the receptor for advanced glycation end products (RAGE) in human brain astrocytes and peripheral blood mononuclear cells
    • Park I.H., Yeon S.I., Youn J.H., Choi J.E., Sasaki N., Choi I.H., and Shin J.S. Expression of a novel secreted splice variant of the receptor for advanced glycation end products (RAGE) in human brain astrocytes and peripheral blood mononuclear cells. Mol. Immunol. 40 (2004) 1203-1211
    • (2004) Mol. Immunol. , vol.40 , pp. 1203-1211
    • Park, I.H.1    Yeon, S.I.2    Youn, J.H.3    Choi, J.E.4    Sasaki, N.5    Choi, I.H.6    Shin, J.S.7
  • 58
    • 26944494920 scopus 로고    scopus 로고
    • Evaluation of RAGE isoforms, ligands, and signaling in the brain
    • Ding Q., and Keller J.N. Evaluation of RAGE isoforms, ligands, and signaling in the brain. Biochim. Biophys. Acta 1746 (2005) 18-27
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 18-27
    • Ding, Q.1    Keller, J.N.2
  • 59
    • 8844263841 scopus 로고    scopus 로고
    • Splice variants of the receptor for advanced glycosylation end products (RAGE) in human brain
    • Ding Q., and Keller J.N. Splice variants of the receptor for advanced glycosylation end products (RAGE) in human brain. Neurosci. Lett. 373 (2005) 67-72
    • (2005) Neurosci. Lett. , vol.373 , pp. 67-72
    • Ding, Q.1    Keller, J.N.2
  • 60
    • 0027957087 scopus 로고
    • Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3
    • Sugaya K., Fukagawa T., Matsumoto K., Mita K., Takahashi E., Ando A., Inoko H., and Ikemura T. Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3. Genomics 23 (1994) 408-419
    • (1994) Genomics , vol.23 , pp. 408-419
    • Sugaya, K.1    Fukagawa, T.2    Matsumoto, K.3    Mita, K.4    Takahashi, E.5    Ando, A.6    Inoko, H.7    Ikemura, T.8
  • 62
    • 54049108485 scopus 로고    scopus 로고
    • A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10)
    • Raucci A., Cugusi S., Antonelli A., Barabino S.M., Monti L., Bierhaus A., Reiss K., Saftig P., and Bianchi M.E. A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10). FASEB J. 22 10 (2008) 3716-3727
    • (2008) FASEB J. , vol.22 , Issue.10 , pp. 3716-3727
    • Raucci, A.1    Cugusi, S.2    Antonelli, A.3    Barabino, S.M.4    Monti, L.5    Bierhaus, A.6    Reiss, K.7    Saftig, P.8    Bianchi, M.E.9
  • 63
    • 50849094595 scopus 로고    scopus 로고
    • Implication of receptor for advanced glycation end product (RAGE) in pulmonary health and pathophysiology
    • Mukherjee T.K., Mukhopadhyay S., and Hoidal J.R. Implication of receptor for advanced glycation end product (RAGE) in pulmonary health and pathophysiology. Respir. Physiol. Neurobiol. 162 3 (2008) 210-215
    • (2008) Respir. Physiol. Neurobiol. , vol.162 , Issue.3 , pp. 210-215
    • Mukherjee, T.K.1    Mukhopadhyay, S.2    Hoidal, J.R.3
  • 65
    • 0028851635 scopus 로고
    • The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system
    • Hori O., Brett J., Slattery T., Cao R., Zhang J., Chen J.X., Nagashima M., Lundh E.R., Vijay S., Nitecki D., et al. The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system. J. Biol. Chem. 270 (1995) 25752-25761
    • (1995) J. Biol. Chem. , vol.270 , pp. 25752-25761
    • Hori, O.1    Brett, J.2    Slattery, T.3    Cao, R.4    Zhang, J.5    Chen, J.X.6    Nagashima, M.7    Lundh, E.R.8    Vijay, S.9    Nitecki, D.10
  • 67
    • 33646082729 scopus 로고    scopus 로고
    • Expression and purification of recombinant human receptor for advanced glycation endproducts in Escherichia coli
    • Wilton R., Yousef M.A., Saxena P., Szpunar M., and Stevens F.J. Expression and purification of recombinant human receptor for advanced glycation endproducts in Escherichia coli. Protein Expression Purif. 47 (2006) 25-35
    • (2006) Protein Expression Purif. , vol.47 , pp. 25-35
    • Wilton, R.1    Yousef, M.A.2    Saxena, P.3    Szpunar, M.4    Stevens, F.J.5
  • 68
    • 0342646984 scopus 로고    scopus 로고
    • Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor kB (NF-kB) activation
    • Sousa M.M., Yan S.D., Stern D., and Saraiva M.J. Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor kB (NF-kB) activation. Lab. Invest. 80 (2000) 1101-1110
    • (2000) Lab. Invest. , vol.80 , pp. 1101-1110
    • Sousa, M.M.1    Yan, S.D.2    Stern, D.3    Saraiva, M.J.4
  • 71
    • 26444478269 scopus 로고    scopus 로고
    • Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation
    • Ramasamy R., Vannucci S.J., Yan S.S., Herold K., Yan S.F., and Schmidt A.M. Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation. Glycobiology 15 (2005) 16R-28R
    • (2005) Glycobiology , vol.15
    • Ramasamy, R.1    Vannucci, S.J.2    Yan, S.S.3    Herold, K.4    Yan, S.F.5    Schmidt, A.M.6
  • 72
    • 0029088742 scopus 로고
    • Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes
    • Schmidt A.M., Hori O., Chen J.X., Li J.F., Crandall J., Zhang J., Cao R., Yan S.D., Brett J., and Stern D. Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes. J. Clin. Invest. 96 (1995) 1395-1403
    • (1995) J. Clin. Invest. , vol.96 , pp. 1395-1403
    • Schmidt, A.M.1    Hori, O.2    Chen, J.X.3    Li, J.F.4    Crandall, J.5    Zhang, J.6    Cao, R.7    Yan, S.D.8    Brett, J.9    Stern, D.10
  • 73
    • 1642336325 scopus 로고    scopus 로고
    • Advanced glycation end products induce tubular epithelial-myofibroblast transition through the RAGE-ERK1/2 MAP kinase signaling pathway
    • Li J.H., Wang W., Huang X.R., Oldfield M., Schmidt A.M., Cooper M.E., and Lan H.Y. Advanced glycation end products induce tubular epithelial-myofibroblast transition through the RAGE-ERK1/2 MAP kinase signaling pathway. Am. J. Pathol. 164 (2004) 1389-1397
    • (2004) Am. J. Pathol. , vol.164 , pp. 1389-1397
    • Li, J.H.1    Wang, W.2    Huang, X.R.3    Oldfield, M.4    Schmidt, A.M.5    Cooper, M.E.6    Lan, H.Y.7
  • 74
    • 0037133280 scopus 로고    scopus 로고
    • Advanced glycation end products activate endothelium through signal-transduction receptor RAGE: a mechanism for amplification of inflammatory responses
    • Basta G., Lazzerini G., Massaro M., Simoncini T., Tanganelli P., Fu C., Kislinger T., Stern D.M., Schmidt A.M., and De Caterina R. Advanced glycation end products activate endothelium through signal-transduction receptor RAGE: a mechanism for amplification of inflammatory responses. Circulation 105 (2002) 816-822
    • (2002) Circulation , vol.105 , pp. 816-822
    • Basta, G.1    Lazzerini, G.2    Massaro, M.3    Simoncini, T.4    Tanganelli, P.5    Fu, C.6    Kislinger, T.7    Stern, D.M.8    Schmidt, A.M.9    De Caterina, R.10
  • 75
    • 4043145689 scopus 로고    scopus 로고
    • Protein glycation: a firm link to endothelial cell dysfunction
    • Wautier J.L., and Schmidt A.M. Protein glycation: a firm link to endothelial cell dysfunction. Circ. Res. 95 (2004) 233-238
    • (2004) Circ. Res. , vol.95 , pp. 233-238
    • Wautier, J.L.1    Schmidt, A.M.2
  • 76
    • 34948829109 scopus 로고    scopus 로고
    • Arguing for the motion: yes, RAGE is a receptor for advanced glycation endproducts
    • Ramasamy R., Yan S.F., and Schmidt A.M. Arguing for the motion: yes, RAGE is a receptor for advanced glycation endproducts. Mol. Nutr. Food Res. 51 (2007) 1111-1115
    • (2007) Mol. Nutr. Food Res. , vol.51 , pp. 1111-1115
    • Ramasamy, R.1    Yan, S.F.2    Schmidt, A.M.3
  • 77
    • 0030763201 scopus 로고    scopus 로고
    • Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl)lysine in human tissues in diabetes and aging
    • Schleicher E.D., Wagner E., and Nerlich A.G. Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl)lysine in human tissues in diabetes and aging. J. Clin. Invest. 99 (1997) 457-468
    • (1997) J. Clin. Invest. , vol.99 , pp. 457-468
    • Schleicher, E.D.1    Wagner, E.2    Nerlich, A.G.3
  • 78
    • 0029665694 scopus 로고    scopus 로고
    • N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction
    • Ikeda K., Higashi T., Sano H., Jinnouchi Y., Yoshida M., Araki T., Ueda S., and Horiuchi S. N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction. Biochemistry 35 (1996) 8075-8083
    • (1996) Biochemistry , vol.35 , pp. 8075-8083
    • Ikeda, K.1    Higashi, T.2    Sano, H.3    Jinnouchi, Y.4    Yoshida, M.5    Araki, T.6    Ueda, S.7    Horiuchi, S.8
  • 79
    • 0028979597 scopus 로고
    • N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins
    • Reddy S., Bichler J., Wells-Knecht K.J., Thorpe S.R., and Baynes J.W. N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. Biochemistry 34 (1995) 10872-10878
    • (1995) Biochemistry , vol.34 , pp. 10872-10878
    • Reddy, S.1    Bichler, J.2    Wells-Knecht, K.J.3    Thorpe, S.R.4    Baynes, J.W.5
  • 80
    • 0033615356 scopus 로고    scopus 로고
    • N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression
    • Kislinger T., Fu C., Huber B., Qu W., Taguchi A., Du Yan S., Hofmann M., Yan S.F., Pischetsrieder M., Stern D., and Schmidt A.M. N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression. J. Biol. Chem. 274 (1999) 31740-31749
    • (1999) J. Biol. Chem. , vol.274 , pp. 31740-31749
    • Kislinger, T.1    Fu, C.2    Huber, B.3    Qu, W.4    Taguchi, A.5    Du Yan, S.6    Hofmann, M.7    Yan, S.F.8    Pischetsrieder, M.9    Stern, D.10    Schmidt, A.M.11
  • 81
    • 33846260239 scopus 로고    scopus 로고
    • Mesothelial RAGE activation by AGEs enhances VEGF release and potentiates capillary tube formation
    • Boulanger E., Grossin N., Wautier M.P., Taamma R., and Wautier J.L. Mesothelial RAGE activation by AGEs enhances VEGF release and potentiates capillary tube formation. Kidney Int. 71 (2007) 126-133
    • (2007) Kidney Int. , vol.71 , pp. 126-133
    • Boulanger, E.1    Grossin, N.2    Wautier, M.P.3    Taamma, R.4    Wautier, J.L.5
  • 83
    • 2942628078 scopus 로고    scopus 로고
    • Binding of receptor for advanced glycation end products (RAGE) ligands is not sufficient to induce inflammatory signals: lack of activity of endotoxin-free albumin-derived advanced glycation end products (AGEs)
    • Valencia J.V., Mone M., Koehne C., Rediske J., and Hughes T.E. Binding of receptor for advanced glycation end products (RAGE) ligands is not sufficient to induce inflammatory signals: lack of activity of endotoxin-free albumin-derived advanced glycation end products (AGEs). Diabetologia 47 (2004) 844-852
    • (2004) Diabetologia , vol.47 , pp. 844-852
    • Valencia, J.V.1    Mone, M.2    Koehne, C.3    Rediske, J.4    Hughes, T.E.5
  • 85
    • 43049127240 scopus 로고    scopus 로고
    • V domain of RAGE interacts with AGEs on prostate carcinoma cells
    • Uetz-von Allmen E., Koch M., Fritz G., and Legler D. V domain of RAGE interacts with AGEs on prostate carcinoma cells. Prostate 68 (2008) 748-758
    • (2008) Prostate , vol.68 , pp. 748-758
    • Uetz-von Allmen, E.1    Koch, M.2    Fritz, G.3    Legler, D.4
  • 88
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear protein HMG1
    • Bianchi M.E., Beltrame M., and Paonessa G. Specific recognition of cruciform DNA by nuclear protein HMG1. Science 243 (1989) 1056-1059
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 89
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal
    • Lotze M.T., and Tracey K.J. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat. Rev., Immunol. 5 (2005) 331-342
    • (2005) Nat. Rev., Immunol. , vol.5 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 90
    • 0036510750 scopus 로고    scopus 로고
    • HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter
    • Stros M., Ozaki T., Bacikova A., Kageyama H., and Nakagawara A. HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter. J. Biol. Chem. 277 (2002) 7157-7164
    • (2002) J. Biol. Chem. , vol.277 , pp. 7157-7164
    • Stros, M.1    Ozaki, T.2    Bacikova, A.3    Kageyama, H.4    Nakagawara, A.5
  • 91
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • Scaffidi P., Misteli T., and Bianchi M.E. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 418 (2002) 191-195
    • (2002) Nature , vol.418 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 96
    • 41049117932 scopus 로고    scopus 로고
    • Convergence and amplification of toll-like receptor (TLR) and receptor for advanced glycation end products (RAGE) signaling pathways via high mobility group B1 (HMGB1)
    • van Beijnum J.R., Buurman W.A., and Griffioen A.W. Convergence and amplification of toll-like receptor (TLR) and receptor for advanced glycation end products (RAGE) signaling pathways via high mobility group B1 (HMGB1). Angiogenesis 11 (2008) 91-99
    • (2008) Angiogenesis , vol.11 , pp. 91-99
    • van Beijnum, J.R.1    Buurman, W.A.2    Griffioen, A.W.3
  • 97
    • 1542285224 scopus 로고    scopus 로고
    • Amphoterin as an extracellular regulator of cell motility: from discovery to disease
    • Huttunen H.J., and Rauvala H. Amphoterin as an extracellular regulator of cell motility: from discovery to disease. J. Intern. Med. 255 (2004) 351-366
    • (2004) J. Intern. Med. , vol.255 , pp. 351-366
    • Huttunen, H.J.1    Rauvala, H.2
  • 100
    • 0000920292 scopus 로고    scopus 로고
    • Amyloid-beta peptide-receptor for advanced glycation endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: a proinflammatory pathway in Alzheimer disease
    • Du Yan S., Zhu H., Fu J., Yan S.F., Roher A., Tourtellotte W.W., Rajavashisth T., Chen X., Godman G.C., Stern D., and Schmidt A.M. Amyloid-beta peptide-receptor for advanced glycation endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: a proinflammatory pathway in Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 5296-5301
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5296-5301
    • Du Yan, S.1    Zhu, H.2    Fu, J.3    Yan, S.F.4    Roher, A.5    Tourtellotte, W.W.6    Rajavashisth, T.7    Chen, X.8    Godman, G.C.9    Stern, D.10    Schmidt, A.M.11
  • 102
    • 45549097081 scopus 로고    scopus 로고
    • Site-specific blockade of RAGE-Vd prevents amyloid-beta oligomer neurotoxicity
    • Stürchler E., Galichet A., Weibel M., Leclerc E., and Heizmann C.W. Site-specific blockade of RAGE-Vd prevents amyloid-beta oligomer neurotoxicity. J. Neurosci. 28 (2008) 5149-5158
    • (2008) J. Neurosci. , vol.28 , pp. 5149-5158
    • Stürchler, E.1    Galichet, A.2    Weibel, M.3    Leclerc, E.4    Heizmann, C.W.5
  • 104
    • 0013844612 scopus 로고
    • A soluble protein characteristic of the nervous system
    • Moore B.W. A soluble protein characteristic of the nervous system. Biochem. Biophys. Res. Commun. 19 (1965) 739-744
    • (1965) Biochem. Biophys. Res. Commun. , vol.19 , pp. 739-744
    • Moore, B.W.1
  • 105
    • 0023499458 scopus 로고
    • Secretion of S-100 from rat C6 glioma cells
    • Van Eldik L.J., and Zimmer D.B. Secretion of S-100 from rat C6 glioma cells. Brain Res. 436 (1987) 367-370
    • (1987) Brain Res. , vol.436 , pp. 367-370
    • Van Eldik, L.J.1    Zimmer, D.B.2
  • 106
    • 0034672543 scopus 로고    scopus 로고
    • Immunocontent and secretion of S100B in astrocyte cultures from different brain regions in relation to morphology
    • Pinto S.S., Gottfried C., Mendez A., Goncalves D., Karl J., Goncalves C.A., Wofchuk S., and Rodnight R. Immunocontent and secretion of S100B in astrocyte cultures from different brain regions in relation to morphology. FEBS Lett. 486 (2000) 203-207
    • (2000) FEBS Lett. , vol.486 , pp. 203-207
    • Pinto, S.S.1    Gottfried, C.2    Mendez, A.3    Goncalves, D.4    Karl, J.5    Goncalves, C.A.6    Wofchuk, S.7    Rodnight, R.8
  • 108
    • 0022973592 scopus 로고
    • Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein
    • Baudier J., Glasser N., and Gerard D. Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein. J. Biol. Chem. 261 (1986) 8192-8203
    • (1986) J. Biol. Chem. , vol.261 , pp. 8192-8203
    • Baudier, J.1    Glasser, N.2    Gerard, D.3
  • 109
    • 0030819491 scopus 로고    scopus 로고
    • Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage
    • Nishikawa T., Lee I.S., Shiraishi N., Ishikawa T., Ohta Y., and Nishikimi M. Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage. J. Biol. Chem. 272 (1997) 23037-23041
    • (1997) J. Biol. Chem. , vol.272 , pp. 23037-23041
    • Nishikawa, T.1    Lee, I.S.2    Shiraishi, N.3    Ishikawa, T.4    Ohta, Y.5    Nishikimi, M.6
  • 111
    • 0030587521 scopus 로고    scopus 로고
    • The solution structure of the bovine S100B protein dimer in the calcium-free state
    • Kilby P.M., Van Eldik L.J., and Roberts G.C. The solution structure of the bovine S100B protein dimer in the calcium-free state. Structure 4 (1996) 1041-1052
    • (1996) Structure , vol.4 , pp. 1041-1052
    • Kilby, P.M.1    Van Eldik, L.J.2    Roberts, G.C.3
  • 112
    • 0032478114 scopus 로고    scopus 로고
    • Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy
    • Drohat A.C., Baldisseri D.M., Rustandi R.R., and Weber D.J. Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy. Biochemistry 37 (1998) 2729-2740
    • (1998) Biochemistry , vol.37 , pp. 2729-2740
    • Drohat, A.C.1    Baldisseri, D.M.2    Rustandi, R.R.3    Weber, D.J.4
  • 113
    • 0032520233 scopus 로고    scopus 로고
    • A novel mode of target recognition suggested by the 2.0 Å structure of holo S100B from bovine brain
    • Matsumura H., Shiba T., Inoue T., Harada S., and Kai Y. A novel mode of target recognition suggested by the 2.0 Å structure of holo S100B from bovine brain. Structure 6 (1998) 233-241
    • (1998) Structure , vol.6 , pp. 233-241
    • Matsumura, H.1    Shiba, T.2    Inoue, T.3    Harada, S.4    Kai, Y.5
  • 114
    • 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., and Shaw G.S. A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure 6 (1998) 211-222
    • (1998) Structure , vol.6 , pp. 211-222
    • Smith, S.P.1    Shaw, G.S.2
  • 115
    • 0033945124 scopus 로고    scopus 로고
    • Structure of the negative regulatory domain of p53 bound to S100B(betabeta)
    • Rustandi R.R., Baldisseri D.M., and Weber D.J. Structure of the negative regulatory domain of p53 bound to S100B(betabeta). Nat. Struct. Biol. 7 (2000) 570-574
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 570-574
    • Rustandi, R.R.1    Baldisseri, D.M.2    Weber, D.J.3
  • 116
    • 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., and Chazin W.J. Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase. Biochemistry 42 (2003) 14416-14426
    • (2003) Biochemistry , vol.42 , pp. 14416-14426
    • Bhattacharya, S.1    Large, E.2    Heizmann, C.W.3    Hemmings, B.4    Chazin, W.J.5
  • 119
    • 0032968036 scopus 로고    scopus 로고
    • S100B protein detection in serum is a significant prognostic factor in metastatic melanoma
    • Hauschild A., Engel G., Brenner W., Glaser R., Monig H., Henze E., and Christophers E. S100B protein detection in serum is a significant prognostic factor in metastatic melanoma. Oncology 56 (1999) 338-344
    • (1999) Oncology , vol.56 , pp. 338-344
    • Hauschild, A.1    Engel, G.2    Brenner, W.3    Glaser, R.4    Monig, H.5    Henze, E.6    Christophers, E.7
  • 120
    • 85047691446 scopus 로고    scopus 로고
    • Harm avoidance, anxiety, and response to novelty in the adolescent S-100beta transgenic mouse: role of serotonin and relevance to Down syndrome
    • Bell K., Shokrian D., Potenzieri C., and Whitaker-Azmitia P.M. Harm avoidance, anxiety, and response to novelty in the adolescent S-100beta transgenic mouse: role of serotonin and relevance to Down syndrome. Neuropsychopharmacology 28 (2003) 1810-1816
    • (2003) Neuropsychopharmacology , vol.28 , pp. 1810-1816
    • Bell, K.1    Shokrian, D.2    Potenzieri, C.3    Whitaker-Azmitia, P.M.4
  • 121
    • 0037087213 scopus 로고    scopus 로고
    • Normal development of serotonergic neurons in mice lacking S100B
    • Nishiyama H., Takemura M., Takeda T., and Itohara S. Normal development of serotonergic neurons in mice lacking S100B. Neurosci. Lett. 321 (2002) 49-52
    • (2002) Neurosci. Lett. , vol.321 , pp. 49-52
    • Nishiyama, H.1    Takemura, M.2    Takeda, T.3    Itohara, S.4
  • 123
    • 0034660044 scopus 로고    scopus 로고
    • Enhanced calcium transients in glial cells in neonatal cerebellar cultures derived from S100B null mice
    • Xiong Z., O'Hanlon D., Becker L.E., Roder J., MacDonald J.F., and Marks A. Enhanced calcium transients in glial cells in neonatal cerebellar cultures derived from S100B null mice. Exp. Cell Res. 257 (2000) 281-289
    • (2000) Exp. Cell Res. , vol.257 , pp. 281-289
    • Xiong, Z.1    O'Hanlon, D.2    Becker, L.E.3    Roder, J.4    MacDonald, J.F.5    Marks, A.6
  • 124
    • 0029266133 scopus 로고
    • Abnormal exploratory behavior in transgenic mice carrying multiple copies of the human gene for S100 beta
    • Gerlai R., and Roder J. Abnormal exploratory behavior in transgenic mice carrying multiple copies of the human gene for S100 beta. J. Psychiatry. Neurosci. 20 (1995) 105-112
    • (1995) J. Psychiatry. Neurosci. , vol.20 , pp. 105-112
    • Gerlai, R.1    Roder, J.2
  • 125
    • 0030237082 scopus 로고    scopus 로고
    • Spatial and nonspatial learning in mice: effects of S100 beta overexpression and age
    • Gerlai R., and Roder J. Spatial and nonspatial learning in mice: effects of S100 beta overexpression and age. Neurobiol. Learn. Mem. 66 (1996) 143-154
    • (1996) Neurobiol. Learn. Mem. , vol.66 , pp. 143-154
    • Gerlai, R.1    Roder, J.2
  • 126
    • 0035704553 scopus 로고    scopus 로고
    • Learning and memory in S100-beta transgenic mice: an analysis of impaired and preserved function
    • Winocur G., Roder J., and Lobaugh N. Learning and memory in S100-beta transgenic mice: an analysis of impaired and preserved function. Neurobiol. Learn. Mem. 75 (2001) 230-243
    • (2001) Neurobiol. Learn. Mem. , vol.75 , pp. 230-243
    • Winocur, G.1    Roder, J.2    Lobaugh, N.3
  • 127
    • 0034704068 scopus 로고    scopus 로고
    • Coregulation of neurite outgrowth and cell survival by amphoterin and S100 proteins through receptor for advanced glycation end products (RAGE) activation
    • Huttunen H.J., Kuja-Panula J., Sorci G., Agneletti A.L., Donato R., and Rauvala H. Coregulation of neurite outgrowth and cell survival by amphoterin and S100 proteins through receptor for advanced glycation end products (RAGE) activation. J. Biol. Chem. 275 (2000) 40096-40105
    • (2000) J. Biol. Chem. , vol.275 , pp. 40096-40105
    • Huttunen, H.J.1    Kuja-Panula, J.2    Sorci, G.3    Agneletti, A.L.4    Donato, R.5    Rauvala, H.6
  • 128
    • 4143053661 scopus 로고    scopus 로고
    • S100B potently activates p65/c-Rel transcriptional complexes in hippocampal neurons: clinical implications for the role of S100B in excitotoxic brain injury
    • Kögel D., Peters M., König H.G., Hashémi S.M.A., Bui N.T., Arolt V., Rothermundt M., and Prehn J.H.M. S100B potently activates p65/c-Rel transcriptional complexes in hippocampal neurons: clinical implications for the role of S100B in excitotoxic brain injury. Neuroscience 127 (2004) 913-920
    • (2004) Neuroscience , vol.127 , pp. 913-920
    • Kögel, D.1    Peters, M.2    König, H.G.3    Hashémi, S.M.A.4    Bui, N.T.5    Arolt, V.6    Rothermundt, M.7    Prehn, J.H.M.8
  • 129
    • 33645312665 scopus 로고    scopus 로고
    • S100B protects LAN-5 neuroblastoma cells against Abeta amyloid-induced neurotoxicity via RAGE engagement at low doses but increases Abeta amyloid neurotoxicity at high doses
    • Businaro R., Leone S., Fabrizi C., Sorci G., Donato R., Lauro G.M., and Fumagalli L. S100B protects LAN-5 neuroblastoma cells against Abeta amyloid-induced neurotoxicity via RAGE engagement at low doses but increases Abeta amyloid neurotoxicity at high doses. J. Neurosci. Res. 83 (2006) 897-906
    • (2006) J. Neurosci. Res. , vol.83 , pp. 897-906
    • Businaro, R.1    Leone, S.2    Fabrizi, C.3    Sorci, G.4    Donato, R.5    Lauro, G.M.6    Fumagalli, L.7
  • 130
    • 36148959724 scopus 로고    scopus 로고
    • Cell cycle related signaling in Neuro2a cells proceeds via the receptor for advanced glycation end products
    • Schmidt A., Kuhla B., Bigl K., Munch G., and Arendt T. Cell cycle related signaling in Neuro2a cells proceeds via the receptor for advanced glycation end products. J. Neural Transm. 114 (2007) 1413-1424
    • (2007) J. Neural Transm. , vol.114 , pp. 1413-1424
    • Schmidt, A.1    Kuhla, B.2    Bigl, K.3    Munch, G.4    Arendt, T.5
  • 131
    • 33846460101 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products activation injures primary sensory neurons via oxidative stress
    • Vincent A.M., Perrone L., Sullivan K.A., Backus C., Sastry A.M., Lastoskie C., and Feldman E.L. Receptor for advanced glycation end products activation injures primary sensory neurons via oxidative stress. Endocrinology 148 (2007) 548-558
    • (2007) Endocrinology , vol.148 , pp. 548-558
    • Vincent, A.M.1    Perrone, L.2    Sullivan, K.A.3    Backus, C.4    Sastry, A.M.5    Lastoskie, C.6    Feldman, E.L.7
  • 133
    • 10044230497 scopus 로고    scopus 로고
    • S100B-stimulated NO production by BV-2 microglia is independent of RAGE transducing activity but dependent on RAGE extracellular domain
    • Adami C., Bianchi R., Pula G., and Donato R. S100B-stimulated NO production by BV-2 microglia is independent of RAGE transducing activity but dependent on RAGE extracellular domain. Biochim. Biophys. Acta 1742 (2004) 169-177
    • (2004) Biochim. Biophys. Acta , vol.1742 , pp. 169-177
    • Adami, C.1    Bianchi, R.2    Pula, G.3    Donato, R.4
  • 134
    • 33845885123 scopus 로고    scopus 로고
    • S100B binding to RAGE in microglia stimulates COX-2 expression
    • Bianchi R., Adami C., Giambanco I., and Donato R. S100B binding to RAGE in microglia stimulates COX-2 expression. J. Leukocyte Biol. 81 (2007) 108-118
    • (2007) J. Leukocyte Biol. , vol.81 , pp. 108-118
    • Bianchi, R.1    Adami, C.2    Giambanco, I.3    Donato, R.4
  • 135
    • 67349085636 scopus 로고    scopus 로고
    • S100B/RAGE-dependent activation of microglia via NF-kappaB and AP-1 Co-regulation of COX-2 expression by S100B, IL-1beta and TNF-alpha
    • [Electronic publication ahead of print]
    • Bianchi R., Giambanco I., and Donato R. S100B/RAGE-dependent activation of microglia via NF-kappaB and AP-1 Co-regulation of COX-2 expression by S100B, IL-1beta and TNF-alpha. Neurobiol. Aging (2008) [Electronic publication ahead of print]
    • (2008) Neurobiol. Aging
    • Bianchi, R.1    Giambanco, I.2    Donato, R.3
  • 136
    • 0042317299 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase-2 expression in monocytes by ligation of the receptor for advanced glycation end products
    • Shanmugam N., Kim Y.S., Lanting L., and Natarajan R. Regulation of cyclooxygenase-2 expression in monocytes by ligation of the receptor for advanced glycation end products. J. Biol. Chem. 278 (2003) 34834-34844
    • (2003) J. Biol. Chem. , vol.278 , pp. 34834-34844
    • Shanmugam, N.1    Kim, Y.S.2    Lanting, L.3    Natarajan, R.4
  • 138
    • 33846029512 scopus 로고    scopus 로고
    • Interferon-gamma-inducible protein (IP)-10 mRNA stabilized by RNA-binding proteins in monocytes treated with S100B
    • Shanmugam N., Ransohoff R.M., and Natarajan R. Interferon-gamma-inducible protein (IP)-10 mRNA stabilized by RNA-binding proteins in monocytes treated with S100B. J. Biol. Chem. 281 (2006) 31212-31221
    • (2006) J. Biol. Chem. , vol.281 , pp. 31212-31221
    • Shanmugam, N.1    Ransohoff, R.M.2    Natarajan, R.3
  • 139
    • 12844266704 scopus 로고    scopus 로고
    • Chronic vascular inflammation in patients with type 2 diabetes: endothelial biopsy and RT-PCR analysis
    • Feng L., Matsumoto C., Schwartz A., Schmidt A.M., Stern D.M., and Pile-Spellman J. Chronic vascular inflammation in patients with type 2 diabetes: endothelial biopsy and RT-PCR analysis. Diabetes Care 28 (2005) 379-384
    • (2005) Diabetes Care , vol.28 , pp. 379-384
    • Feng, L.1    Matsumoto, C.2    Schwartz, A.3    Schmidt, A.M.4    Stern, D.M.5    Pile-Spellman, J.6
  • 140
    • 0041319299 scopus 로고    scopus 로고
    • S100B-RAGE-mediated augmentation of angiotensin II-induced activation of JAK2 in vascular smooth muscle cells is dependent on PLD2
    • Shaw S.S., Schmidt A.M., Banes A.K., Wang X., Stern D.M., and Marrero M.B. S100B-RAGE-mediated augmentation of angiotensin II-induced activation of JAK2 in vascular smooth muscle cells is dependent on PLD2. Diabetes 52 (2003) 2381-2388
    • (2003) Diabetes , vol.52 , pp. 2381-2388
    • Shaw, S.S.1    Schmidt, A.M.2    Banes, A.K.3    Wang, X.4    Stern, D.M.5    Marrero, M.B.6
  • 141
    • 33744958085 scopus 로고    scopus 로고
    • Key role of Src kinase in S100B-induced activation of the receptor for advanced glycation end products in vascular smooth muscle cells
    • Reddy M.A., Li S.L., Sahar S., Kim Y.S., Xu Z.G., Lanting L., and Natarajan R. Key role of Src kinase in S100B-induced activation of the receptor for advanced glycation end products in vascular smooth muscle cells. J. Biol. Chem. 281 (2006) 13685-13693
    • (2006) J. Biol. Chem. , vol.281 , pp. 13685-13693
    • Reddy, M.A.1    Li, S.L.2    Sahar, S.3    Kim, Y.S.4    Xu, Z.G.5    Lanting, L.6    Natarajan, R.7
  • 142
    • 0038788905 scopus 로고    scopus 로고
    • S100B inhibits myogenic differentiation and myotube formation in a RAGE-independent manner
    • Sorci G., Riuzzi F., Agneletti A.L., Marchetti C., and Donato R. S100B inhibits myogenic differentiation and myotube formation in a RAGE-independent manner. Mol. Cell. Biol. 23 (2003) 4870-4881
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4870-4881
    • Sorci, G.1    Riuzzi, F.2    Agneletti, A.L.3    Marchetti, C.4    Donato, R.5
  • 143
    • 1842421190 scopus 로고    scopus 로고
    • S100B causes apoptosis in a myoblast cell line in a RAGE-independent manner
    • Sorci G., Riuzzi F., Agneletti A.L., Marchetti C., and Donato R. S100B causes apoptosis in a myoblast cell line in a RAGE-independent manner. J. Cell. Physiol. 199 (2004) 274-283
    • (2004) J. Cell. Physiol. , vol.199 , pp. 274-283
    • Sorci, G.1    Riuzzi, F.2    Agneletti, A.L.3    Marchetti, C.4    Donato, R.5
  • 144
    • 34250171731 scopus 로고    scopus 로고
    • The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units
    • Dattilo B.M., Fritz G., Leclerc E., Kooi C.W., Heizmann C.W., and Chazin W.J. The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units. Biochemistry 46 (2007) 6957-6970
    • (2007) Biochemistry , vol.46 , pp. 6957-6970
    • Dattilo, B.M.1    Fritz, G.2    Leclerc, E.3    Kooi, C.W.4    Heizmann, C.W.5    Chazin, W.J.6
  • 145
    • 0028892477 scopus 로고
    • Effects of receptor dimerization on the interaction between the class I major histocompatibility complex-related Fc receptor and IgG
    • Raghavan M., Wang Y., and Bjorkman P.J. Effects of receptor dimerization on the interaction between the class I major histocompatibility complex-related Fc receptor and IgG. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 11200-11204
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11200-11204
    • Raghavan, M.1    Wang, Y.2    Bjorkman, P.J.3
  • 146
    • 30644464166 scopus 로고    scopus 로고
    • S100-mediated signal transduction in the nervous system and neurological diseases
    • Zimmer D.B., Chaplin J., Baldwin A., and Rast M. S100-mediated signal transduction in the nervous system and neurological diseases. Cell. Mol. Biol. 51 (2005) 201-214
    • (2005) Cell. Mol. Biol. , vol.51 , pp. 201-214
    • Zimmer, D.B.1    Chaplin, J.2    Baldwin, A.3    Rast, M.4
  • 151
    • 34249882040 scopus 로고    scopus 로고
    • S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance
    • Most P., Remppis A., Pleger S.T., Katus H.A., and Koch W.J. S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance. Am. J. Physiol. Regul. Integr. Comp. Physiol. 293 (2007) R568-577
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.293
    • Most, P.1    Remppis, A.2    Pleger, S.T.3    Katus, H.A.4    Koch, W.J.5
  • 154
    • 0025877670 scopus 로고
    • Positive selection of candidate tumor-suppressor genes by subtractive hybridization
    • Lee S.W., Tomasetto C., and Sager R. Positive selection of candidate tumor-suppressor genes by subtractive hybridization. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 2825-2829
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 2825-2829
    • Lee, S.W.1    Tomasetto, C.2    Sager, R.3
  • 155
    • 0031870090 scopus 로고    scopus 로고
    • Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium
    • Mandinova A., Atar D., Schafer B.W., Spiess M., Aebi U., and Heizmann C.W. Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium. J. Cell. Sci. 111 Pt. 14 (1998) 2043-2054
    • (1998) J. Cell. Sci. , vol.111 , Issue.PART 14 , pp. 2043-2054
    • Mandinova, A.1    Atar, D.2    Schafer, B.W.3    Spiess, M.4    Aebi, U.5    Heizmann, C.W.6
  • 156
    • 0024593613 scopus 로고
    • Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution
    • Glenney Jr. J.R., Kindy M.S., and Zokas L. Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution. J. Cell Biol. 108 (1989) 569-578
    • (1989) J. Cell Biol. , vol.108 , pp. 569-578
    • Glenney Jr., J.R.1    Kindy, M.S.2    Zokas, L.3
  • 157
    • 0036445630 scopus 로고    scopus 로고
    • Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes
    • Zhang T., Woods T.L., and Elder J.T. Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes. J. Invest. Dermatol. 119 (2002) 1196-1201
    • (2002) J. Invest. Dermatol. , vol.119 , pp. 1196-1201
    • Zhang, T.1    Woods, T.L.2    Elder, J.T.3
  • 158
    • 41949135835 scopus 로고    scopus 로고
    • Crystal structure of Ca2+ -free S100A2 at 1.6-A resolution
    • Koch M., Diez J., and Fritz G. Crystal structure of Ca2+ -free S100A2 at 1.6-A resolution. J. Mol. Biol. 378 (2008) 931-940
    • (2008) J. Mol. Biol. , vol.378 , pp. 931-940
    • Koch, M.1    Diez, J.2    Fritz, G.3
  • 159
    • 0030767388 scopus 로고    scopus 로고
    • Differential expression patterns of S100A2, S100A4 and S100A6 during progression of human malignant melanoma
    • Maelandsmo G.M., Florenes V.A., Mellingsaeter T., Hovig E., Kerbel R.S., and Fodstad O. Differential expression patterns of S100A2, S100A4 and S100A6 during progression of human malignant melanoma. Int. J. Cancer 74 (1997) 464-469
    • (1997) Int. J. Cancer , vol.74 , pp. 464-469
    • Maelandsmo, G.M.1    Florenes, V.A.2    Mellingsaeter, T.3    Hovig, E.4    Kerbel, R.S.5    Fodstad, O.6
  • 160
    • 0037208581 scopus 로고    scopus 로고
    • Differential expression of S100A2 and S100A4 during progression of human prostate adenocarcinoma
    • Gupta S., Hussain T., MacLennan G.T., Fu P., Patel J., and Mukhtar H. Differential expression of S100A2 and S100A4 during progression of human prostate adenocarcinoma. J. Clin. Oncol. 21 (2003) 106-112
    • (2003) J. Clin. Oncol. , vol.21 , pp. 106-112
    • Gupta, S.1    Hussain, T.2    MacLennan, G.T.3    Fu, P.4    Patel, J.5    Mukhtar, H.6
  • 161
    • 33644684254 scopus 로고    scopus 로고
    • S100A2 expression as a predictive marker for late cervical metastasis in stage I and II invasive squamous cell carcinoma of the oral cavity
    • Suzuki F., Oridate N., Homma A., Nakamaru Y., Nagahashi T., Yagi K., Yamaguchi S., Furuta Y., and Fukuda S. S100A2 expression as a predictive marker for late cervical metastasis in stage I and II invasive squamous cell carcinoma of the oral cavity. Oncol. Rep. 14 (2005) 1493-1498
    • (2005) Oncol. Rep. , vol.14 , pp. 1493-1498
    • Suzuki, F.1    Oridate, N.2    Homma, A.3    Nakamaru, Y.4    Nagahashi, T.5    Yagi, K.6    Yamaguchi, S.7    Furuta, Y.8    Fukuda, S.9
  • 162
    • 0035503058 scopus 로고    scopus 로고
    • Diminished expression of S100A2, a putative tumor suppressor, at early stage of human lung carcinogenesis
    • Feng G., Xu X., Youssef E.M., and Lotan R. Diminished expression of S100A2, a putative tumor suppressor, at early stage of human lung carcinogenesis. Cancer Res. 61 (2001) 7999-8004
    • (2001) Cancer Res. , vol.61 , pp. 7999-8004
    • Feng, G.1    Xu, X.2    Youssef, E.M.3    Lotan, R.4
  • 163
    • 0026607123 scopus 로고
    • Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment
    • Lee S.W., Tomasetto C., Swisshelm K., Keyomarsi K., and Sager R. Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 2504-2508
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 2504-2508
    • Lee, S.W.1    Tomasetto, C.2    Swisshelm, K.3    Keyomarsi, K.4    Sager, R.5
  • 164
    • 17444365831 scopus 로고    scopus 로고
    • S100A2 overexpression is frequently observed in esophageal squamous cell carcinoma
    • Imazawa M., Hibi K., Fujitake S., Kodera Y., Ito K., Akiyama S., and Nakao A. S100A2 overexpression is frequently observed in esophageal squamous cell carcinoma. Anticancer Res. 25 (2005) 1247-1250
    • (2005) Anticancer Res. , vol.25 , pp. 1247-1250
    • Imazawa, M.1    Hibi, K.2    Fujitake, S.3    Kodera, Y.4    Ito, K.5    Akiyama, S.6    Nakao, A.7
  • 165
    • 7944233764 scopus 로고    scopus 로고
    • S100A2 is strongly expressed in airway basal cells, preneoplastic bronchial lesions and primary non-small cell lung carcinomas
    • Smith S.L., Gugger M., Hoban P., Ratschiller D., Watson S.G., Field J.K., Betticher D.C., and Heighway J. S100A2 is strongly expressed in airway basal cells, preneoplastic bronchial lesions and primary non-small cell lung carcinomas. Br. J. Cancer 91 (2004) 1515-1524
    • (2004) Br. J. Cancer , vol.91 , pp. 1515-1524
    • Smith, S.L.1    Gugger, M.2    Hoban, P.3    Ratschiller, D.4    Watson, S.G.5    Field, J.K.6    Betticher, D.C.7    Heighway, J.8
  • 168
    • 23844505646 scopus 로고    scopus 로고
    • The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity
    • Mueller A., Schäfer B.W., Ferrari S., Weibel M., Makek M., Hochli M., and Heizmann C.W. The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity. J. Biol. Chem. 280 (2005) 29186-29193
    • (2005) J. Biol. Chem. , vol.280 , pp. 29186-29193
    • Mueller, A.1    Schäfer, B.W.2    Ferrari, S.3    Weibel, M.4    Makek, M.5    Hochli, M.6    Heizmann, C.W.7
  • 171
    • 57649136391 scopus 로고    scopus 로고
    • Interactions of S100A2 and S100A6 with the tetratricopeptide repeat proteins, Hsp90/Hsp70-organizing protein and kinesin-light chain
    • Shimamoto S., Takata M., Tokuda M., Oohira F., Tokumitsu H., and Kobayashi R. Interactions of S100A2 and S100A6 with the tetratricopeptide repeat proteins, Hsp90/Hsp70-organizing protein and kinesin-light chain. J. Biol. Chem. 283 (2008) 28246-28258
    • (2008) J. Biol. Chem. , vol.283 , pp. 28246-28258
    • Shimamoto, S.1    Takata, M.2    Tokuda, M.3    Oohira, F.4    Tokumitsu, H.5    Kobayashi, R.6
  • 174
    • 21244446530 scopus 로고    scopus 로고
    • The metastasis associated protein S100A4: role in tumour progression and metastasis
    • Helfman D.M., Kim E.J., Lukanidin E., and Grigorian M. The metastasis associated protein S100A4: role in tumour progression and metastasis. Br. J. Cancer 92 (2005) 1955-1958
    • (2005) Br. J. Cancer , vol.92 , pp. 1955-1958
    • Helfman, D.M.1    Kim, E.J.2    Lukanidin, E.3    Grigorian, M.4
  • 176
    • 0034698974 scopus 로고    scopus 로고
    • Metastasis-associated mts1 (S100A4) protein in the developing and adult central nervous system
    • Åberg F., and Kozlova E.N. Metastasis-associated mts1 (S100A4) protein in the developing and adult central nervous system. J. Comp. Neurol. 424 (2000) 269-282
    • (2000) J. Comp. Neurol. , vol.424 , pp. 269-282
    • Åberg, F.1    Kozlova, E.N.2
  • 177
    • 0033199468 scopus 로고    scopus 로고
    • Metastasis-associated mts1 (S100A4) protein is selectively expressed in white matter astrocytes and is up-regulated after peripheral nerve or dorsal root injury
    • Kozlova E.N., and Lukanidin E. Metastasis-associated mts1 (S100A4) protein is selectively expressed in white matter astrocytes and is up-regulated after peripheral nerve or dorsal root injury. Glia 27 (1999) 249-258
    • (1999) Glia , vol.27 , pp. 249-258
    • Kozlova, E.N.1    Lukanidin, E.2
  • 178
    • 0037085716 scopus 로고    scopus 로고
    • Mts1 protein expression in the central nervous system after injury
    • Kozlova E.N., and Lukanidin E. Mts1 protein expression in the central nervous system after injury. Glia 37 (2002) 337-348
    • (2002) Glia , vol.37 , pp. 337-348
    • Kozlova, E.N.1    Lukanidin, E.2
  • 180
    • 52049083050 scopus 로고    scopus 로고
    • Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form
    • Pathuri P., Vogeley L., and Luecke H. Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form. J. Mol. Biol. 383 (2008) 62-77
    • (2008) J. Mol. Biol. , vol.383 , pp. 62-77
    • Pathuri, P.1    Vogeley, L.2    Luecke, H.3
  • 181
    • 43549125729 scopus 로고    scopus 로고
    • Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4
    • Gingras A.R., Basran J., Prescott A., Kriajevska M., Bagshaw C.R., and Barsukov I.L. Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4. FEBS Lett. 582 (2008) 1651-1656
    • (2008) FEBS Lett. , vol.582 , pp. 1651-1656
    • Gingras, A.R.1    Basran, J.2    Prescott, A.3    Kriajevska, M.4    Bagshaw, C.R.5    Barsukov, I.L.6
  • 184
    • 0043032436 scopus 로고    scopus 로고
    • Characterization of the metastasis-associated protein, S100A4. Roles of calcium binding and dimerization in cellular localization and interaction with myosin
    • Kim E.J., and Helfman D.M. Characterization of the metastasis-associated protein, S100A4. Roles of calcium binding and dimerization in cellular localization and interaction with myosin. J. Biol. Chem. 278 (2003) 30063-30073
    • (2003) J. Biol. Chem. , vol.278 , pp. 30063-30073
    • Kim, E.J.1    Helfman, D.M.2
  • 185
    • 0028329819 scopus 로고
    • Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin
    • Takenaga K., Nakamura Y., Sakiyama S., Hasegawa Y., Sato K., and Endo H. Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin. J. Cell Biol. 124 (1994) 757-768
    • (1994) J. Cell Biol. , vol.124 , pp. 757-768
    • Takenaga, K.1    Nakamura, Y.2    Sakiyama, S.3    Hasegawa, Y.4    Sato, K.5    Endo, H.6
  • 186
    • 0028808337 scopus 로고
    • Expression of Mts1, a metastasis-associated gene, increases motility but not invasion of a nonmetastatic mouse mammary adenocarcinoma cell line
    • Ford H.L., Salim M.M., Chakravarty R., Aluiddin V., and Zain S.B. Expression of Mts1, a metastasis-associated gene, increases motility but not invasion of a nonmetastatic mouse mammary adenocarcinoma cell line. Oncogene 11 (1995) 2067-2075
    • (1995) Oncogene , vol.11 , pp. 2067-2075
    • Ford, H.L.1    Salim, M.M.2    Chakravarty, R.3    Aluiddin, V.4    Zain, S.B.5
  • 187
    • 33744931917 scopus 로고    scopus 로고
    • The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA
    • Li Z.H., and Bresnick A.R. The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA. Cancer Res. 66 (2006) 5173-5180
    • (2006) Cancer Res. , vol.66 , pp. 5173-5180
    • Li, Z.H.1    Bresnick, A.R.2
  • 188
    • 0344198168 scopus 로고    scopus 로고
    • Mts1 regulates the assembly of nonmuscle myosin-IIA
    • Li Z.H., Spektor A., Varlamova O., and Bresnick A.R. Mts1 regulates the assembly of nonmuscle myosin-IIA. Biochemistry 42 (2003) 14258-14266
    • (2003) Biochemistry , vol.42 , pp. 14258-14266
    • Li, Z.H.1    Spektor, A.2    Varlamova, O.3    Bresnick, A.R.4
  • 190
    • 0033568527 scopus 로고    scopus 로고
    • S100A4 involvement in metastasis: deregulation of matrix metalloproteinases and tissue inhibitors of matrix metalloproteinases in osteosarcoma cells transfected with an anti-S100A4 ribozyme
    • Bjornland K., Winberg J.O., Odegaard O.T., Hovig E., Loennechen T., Aasen A.O., Fodstad O., and Maelandsmo G.M. S100A4 involvement in metastasis: deregulation of matrix metalloproteinases and tissue inhibitors of matrix metalloproteinases in osteosarcoma cells transfected with an anti-S100A4 ribozyme. Cancer Res. 59 (1999) 4702-4708
    • (1999) Cancer Res. , vol.59 , pp. 4702-4708
    • Bjornland, K.1    Winberg, J.O.2    Odegaard, O.T.3    Hovig, E.4    Loennechen, T.5    Aasen, A.O.6    Fodstad, O.7    Maelandsmo, G.M.8
  • 191
    • 33749331604 scopus 로고    scopus 로고
    • Increase in production of matrix metalloproteinase 13 by human articular chondrocytes due to stimulation with S100A4: role of the receptor for advanced glycation end products
    • Yammani R.R., Carlson C.S., Bresnick A.R., and Loeser R.F. Increase in production of matrix metalloproteinase 13 by human articular chondrocytes due to stimulation with S100A4: role of the receptor for advanced glycation end products. Arthritis Rheum 54 (2006) 2901-2911
    • (2006) Arthritis Rheum , vol.54 , pp. 2901-2911
    • Yammani, R.R.1    Carlson, C.S.2    Bresnick, A.R.3    Loeser, R.F.4
  • 194
    • 0242335598 scopus 로고    scopus 로고
    • Differential expression of S100 proteins in the developing human hippocampus and temporal cortex
    • Chan W.Y., Xia C.L., Dong D.C., Heizmann C.W., and Yew D.T. Differential expression of S100 proteins in the developing human hippocampus and temporal cortex. Microsc. Res. Tech. 60 (2003) 600-613
    • (2003) Microsc. Res. Tech. , vol.60 , pp. 600-613
    • Chan, W.Y.1    Xia, C.L.2    Dong, D.C.3    Heizmann, C.W.4    Yew, D.T.5
  • 198
    • 0024463849 scopus 로고
    • Calcium-binding protein from mouse Ehrlich ascites-tumour cells is homologous to human calcyclin
    • Kuznicki J., Filipek A., Hunziker P.E., Huber S., and Heizmann C.W. Calcium-binding protein from mouse Ehrlich ascites-tumour cells is homologous to human calcyclin. Biochem. J. 263 (1989) 951-956
    • (1989) Biochem. J. , vol.263 , pp. 951-956
    • Kuznicki, J.1    Filipek, A.2    Hunziker, P.E.3    Huber, S.4    Heizmann, C.W.5
  • 199
    • 0024448350 scopus 로고
    • Tissue specific distribution of calcyclin-10.5 kDa Ca2+-binding protein
    • Kuznicki J., Filipek A., Heimann P., Kaczmarek L., and Kaminska B. Tissue specific distribution of calcyclin-10.5 kDa Ca2+-binding protein. FEBS Lett. 254 (1989) 141-144
    • (1989) FEBS Lett. , vol.254 , pp. 141-144
    • Kuznicki, J.1    Filipek, A.2    Heimann, P.3    Kaczmarek, L.4    Kaminska, B.5
  • 200
    • 0033615527 scopus 로고    scopus 로고
    • Ca(2+)-dependent association of S100A6 (Calcyclin) with the plasma membrane and the nuclear envelope
    • Stradal T.B., and Gimona M. Ca(2+)-dependent association of S100A6 (Calcyclin) with the plasma membrane and the nuclear envelope. J. Biol. Chem. 274 (1999) 31593-31596
    • (1999) J. Biol. Chem. , vol.274 , pp. 31593-31596
    • Stradal, T.B.1    Gimona, M.2
  • 201
    • 0036674199 scopus 로고    scopus 로고
    • S100A13 and S100A6 exhibit distinct translocation pathways in endothelial cells
    • Hsieh H.L., Schafer B.W., Cox J.A., and Heizmann C.W. S100A13 and S100A6 exhibit distinct translocation pathways in endothelial cells. J. Cell. Sci. 115 (2002) 3149-3158
    • (2002) J. Cell. Sci. , vol.115 , pp. 3149-3158
    • Hsieh, H.L.1    Schafer, B.W.2    Cox, J.A.3    Heizmann, C.W.4
  • 203
    • 0025352960 scopus 로고
    • Calcyclin is a calcium and zinc binding protein
    • Filipek A., Heizmann C.W., and Kuznicki J. Calcyclin is a calcium and zinc binding protein. FEBS Lett. 264 (1990) 263-266
    • (1990) FEBS Lett. , vol.264 , pp. 263-266
    • Filipek, A.1    Heizmann, C.W.2    Kuznicki, J.3
  • 205
    • 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., and Chazin W.J. The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins. Structure 6 (1998) 223-231
    • (1998) Structure , vol.6 , 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
  • 206
    • 0036223488 scopus 로고    scopus 로고
    • Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution
    • Otterbein L.R., Kordowska J., Witte-Hoffmann C., Wang C.L., and Dominguez R. Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution. Structure 10 (2002) 557-567
    • (2002) Structure , vol.10 , pp. 557-567
    • Otterbein, L.R.1    Kordowska, J.2    Witte-Hoffmann, C.3    Wang, C.L.4    Dominguez, R.5
  • 208
    • 67349088905 scopus 로고    scopus 로고
    • Tumor expression of S100A6 correlates with survival of patients with stage I non-small-cell lung cancer
    • [Electronic publication ahead of print]
    • De Petris L., Orre L.M., Kanter L., Pernemalm M., Koyi H., Lewensohn R., and Lehtio J. Tumor expression of S100A6 correlates with survival of patients with stage I non-small-cell lung cancer. Lung Cancer (2008) [Electronic publication ahead of print]
    • (2008) Lung Cancer
    • De Petris, L.1    Orre, L.M.2    Kanter, L.3    Pernemalm, M.4    Koyi, H.5    Lewensohn, R.6    Lehtio, J.7
  • 212
    • 0034695026 scopus 로고    scopus 로고
    • S100A6, a calcium- and zinc-binding protein, is overexpressed in SOD1 mutant mice, a model for amyotrophic lateral sclerosis
    • Hoyaux D., Alao J., Fuchs J., Kiss R., Keller B., Heizmann C.W., Pochet R., and Frermann D. S100A6, a calcium- and zinc-binding protein, is overexpressed in SOD1 mutant mice, a model for amyotrophic lateral sclerosis. Biochim. Biophys. Acta 1498 (2000) 264-272
    • (2000) Biochim. Biophys. Acta , vol.1498 , pp. 264-272
    • Hoyaux, D.1    Alao, J.2    Fuchs, J.3    Kiss, R.4    Keller, B.5    Heizmann, C.W.6    Pochet, R.7    Frermann, D.8
  • 214
    • 0037047290 scopus 로고    scopus 로고
    • CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family
    • Filipek A., Jastrzebska B., Nowotny M., and Kuznicki J. CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family. J. Biol. Chem. 277 (2002) 28848-28852
    • (2002) J. Biol. Chem. , vol.277 , pp. 28848-28852
    • Filipek, A.1    Jastrzebska, B.2    Nowotny, M.3    Kuznicki, J.4
  • 216
    • 0028879992 scopus 로고
    • Interaction of calcyclin and its cyanogen bromide fragments with annexin II and glyceraldehyde 3-phosphate dehydrogenase
    • Filipek A., Wojda U., and Lesniak W. Interaction of calcyclin and its cyanogen bromide fragments with annexin II and glyceraldehyde 3-phosphate dehydrogenase. Int. J. Biochem. Cell. Biol. 27 (1995) 1123-1131
    • (1995) Int. J. Biochem. Cell. Biol. , vol.27 , pp. 1123-1131
    • Filipek, A.1    Wojda, U.2    Lesniak, W.3
  • 217
    • 0032513018 scopus 로고    scopus 로고
    • Regulation of calcyclin (S100A6) binding by alternative splicing in the N-terminal regulatory domain of annexin XI isoforms
    • Sudo T., and Hidaka H. Regulation of calcyclin (S100A6) binding by alternative splicing in the N-terminal regulatory domain of annexin XI isoforms. J. Biol. Chem. 273 (1998) 6351-6357
    • (1998) J. Biol. Chem. , vol.273 , pp. 6351-6357
    • Sudo, T.1    Hidaka, H.2
  • 219
    • 0027155323 scopus 로고
    • Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart
    • Zeng F.Y., Gerke V., and Gabius H.J. Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart. Int J. Biochem. 25 (1993) 1019-1027
    • (1993) Int J. Biochem. , vol.25 , pp. 1019-1027
    • Zeng, F.Y.1    Gerke, V.2    Gabius, H.J.3
  • 221
    • 0029823752 scopus 로고    scopus 로고
    • Expression and divalent cation binding properties of the novel chemotactic inflammatory protein psoriasin
    • Vorum H., Madsen P., Rasmussen H.H., Etzerodt M., Svendsen I., Celis J.E., and Honore B. Expression and divalent cation binding properties of the novel chemotactic inflammatory protein psoriasin. Electrophoresis 17 (1996) 1787-1796
    • (1996) Electrophoresis , vol.17 , pp. 1787-1796
    • Vorum, H.1    Madsen, P.2    Rasmussen, H.H.3    Etzerodt, M.4    Svendsen, I.5    Celis, J.E.6    Honore, B.7
  • 224
    • 34249652337 scopus 로고    scopus 로고
    • Identification and validation of S100A7 associated with lung squamous cell carcinoma metastasis to brain
    • Zhang H., Wang Y., Chen Y., Sun S., Li N., Lv D., Liu C., Huang L., He D., and Xiao X. Identification and validation of S100A7 associated with lung squamous cell carcinoma metastasis to brain. Lung Cancer 57 (2007) 37-45
    • (2007) Lung Cancer , vol.57 , pp. 37-45
    • Zhang, H.1    Wang, Y.2    Chen, Y.3    Sun, S.4    Li, N.5    Lv, D.6    Liu, C.7    Huang, L.8    He, D.9    Xiao, X.10
  • 226
    • 38049110002 scopus 로고    scopus 로고
    • S100A7 (Psoriasin), highly expressed in ductal carcinoma in situ (DCIS), is regulated by IFN-gamma in mammary epithelial cells
    • Petersson S., Bylander A., Yhr M., and Enerback C. S100A7 (Psoriasin), highly expressed in ductal carcinoma in situ (DCIS), is regulated by IFN-gamma in mammary epithelial cells. BMC Cancer 7 (2007) 205-214
    • (2007) BMC Cancer , vol.7 , pp. 205-214
    • Petersson, S.1    Bylander, A.2    Yhr, M.3    Enerback, C.4
  • 227
    • 0032907122 scopus 로고    scopus 로고
    • Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales
    • Hagens G., Roulin K., Hotz R., Saurat J.H., Hellman U., and Siegenthaler G. Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales. Mol. Cell. Biochem. 192 (1999) 123-128
    • (1999) Mol. Cell. Biochem. , vol.192 , pp. 123-128
    • Hagens, G.1    Roulin, K.2    Hotz, R.3    Saurat, J.H.4    Hellman, U.5    Siegenthaler, G.6
  • 228
    • 0041342091 scopus 로고    scopus 로고
    • S100A7 (psoriasin) interacts with epidermal fatty acid binding protein and localizes in focal adhesion-like structures in cultured keratinocytes
    • Ruse M., Broome A.M., and Eckert R.L. S100A7 (psoriasin) interacts with epidermal fatty acid binding protein and localizes in focal adhesion-like structures in cultured keratinocytes. J. Invest. Dermatol. 121 (2003) 132-141
    • (2003) J. Invest. Dermatol. , vol.121 , pp. 132-141
    • Ruse, M.1    Broome, A.M.2    Eckert, R.L.3
  • 229
    • 3042757574 scopus 로고    scopus 로고
    • RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer
    • Emberley E.D., Gietz R.D., Campbell J.D., HayGlass K.T., Murphy L.C., and Watson P.H. RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer. BMC Cancer 2 (2002) 28-35
    • (2002) BMC Cancer , vol.2 , pp. 28-35
    • Emberley, E.D.1    Gietz, R.D.2    Campbell, J.D.3    HayGlass, K.T.4    Murphy, L.C.5    Watson, P.H.6
  • 231
  • 232
    • 0023944868 scopus 로고
    • Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation
    • Lagasse E., and Clerc R.G. Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation. Mol. Cell. Biol. 8 (1988) 2402-2410
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2402-2410
    • Lagasse, E.1    Clerc, R.G.2
  • 233
    • 0025506195 scopus 로고
    • A protein complex expressed during terminal differentiation of monomyelocytic cells is an inhibitor of cell growth
    • Murao S., Collart F., and Huberman E. A protein complex expressed during terminal differentiation of monomyelocytic cells is an inhibitor of cell growth. Cell. Growth Differ. 1 (1990) 447-454
    • (1990) Cell. Growth Differ. , vol.1 , pp. 447-454
    • Murao, S.1    Collart, F.2    Huberman, E.3
  • 234
    • 0029094733 scopus 로고
    • Purification and characterization of the cytotoxic factor in rat peritoneal exudate cells: its identification as the calcium binding protein complex, calprotectin
    • Yui S., Mikami M., and Yamazaki M. Purification and characterization of the cytotoxic factor in rat peritoneal exudate cells: its identification as the calcium binding protein complex, calprotectin. J. Leukocyte Biol. 58 (1995) 307-316
    • (1995) J. Leukocyte Biol. , vol.58 , pp. 307-316
    • Yui, S.1    Mikami, M.2    Yamazaki, M.3
  • 235
  • 236
    • 0029155870 scopus 로고
    • Differential expression of leucocyte protein L1 (calprotectin) by monocytes and intestinal macrophages
    • Rugtveit J., Scott H., Halstensen T.S., Fausa O., and Brandtzaeg P. Differential expression of leucocyte protein L1 (calprotectin) by monocytes and intestinal macrophages. Adv. Exp. Med. Biol. 371A (1995) 207-210
    • (1995) Adv. Exp. Med. Biol. , vol.371 A , pp. 207-210
    • Rugtveit, J.1    Scott, H.2    Halstensen, T.S.3    Fausa, O.4    Brandtzaeg, P.5
  • 237
    • 0024442773 scopus 로고
    • Calgranulin expression in inflammatory dermatoses
    • Kelly S.E., Jones D.B., and Fleming S. Calgranulin expression in inflammatory dermatoses. J. Pathol. 159 (1989) 17-21
    • (1989) J. Pathol. , vol.159 , pp. 17-21
    • Kelly, S.E.1    Jones, D.B.2    Fleming, S.3
  • 238
    • 0033474494 scopus 로고    scopus 로고
    • Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry
    • Vogl T., Roth J., Sorg C., Hillenkamp F., and Strupat K. Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 10 (1999) 1124-1130
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 1124-1130
    • Vogl, T.1    Roth, J.2    Sorg, C.3    Hillenkamp, F.4    Strupat, K.5
  • 239
    • 33751179656 scopus 로고    scopus 로고
    • Biophysical characterization of S100A8 and S100A9 in the absence and presence of bivalent cations
    • Vogl T., Leukert N., Barczyk K., Strupat K., and Roth J. Biophysical characterization of S100A8 and S100A9 in the absence and presence of bivalent cations. Biochim. Biophys. Acta 1763 (2006) 1298-1306
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1298-1306
    • Vogl, T.1    Leukert, N.2    Barczyk, K.3    Strupat, K.4    Roth, J.5
  • 240
    • 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., and 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. 370 (2007) 887-898
    • (2007) J. Mol. Biol. , vol.370 , pp. 887-898
    • Korndorfer, I.P.1    Brueckner, F.2    Skerra, A.3
  • 241
    • 0034114180 scopus 로고    scopus 로고
    • The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution
    • Ishikawa K., Nakagawa A., Tanaka I., Suzuki M., and Nishihira J. The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution. Acta Crystallogr., D Biol. Crystallogr. 56 Pt. 5 (2000) 559-566
    • (2000) Acta Crystallogr., D Biol. Crystallogr. , vol.56 , Issue.PART 5 , pp. 559-566
    • Ishikawa, K.1    Nakagawa, A.2    Tanaka, I.3    Suzuki, M.4    Nishihira, J.5
  • 242
    • 0036290247 scopus 로고    scopus 로고
    • The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process
    • Itou H., Yao M., Fujita I., Watanabe N., Suzuki M., Nishihira J., and Tanaka I. The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process. J. Mol. Biol. 316 (2002) 265-276
    • (2002) J. Mol. Biol. , vol.316 , pp. 265-276
    • Itou, H.1    Yao, M.2    Fujita, I.3    Watanabe, N.4    Suzuki, M.5    Nishihira, J.6    Tanaka, I.7
  • 243
    • 0023917095 scopus 로고
    • Two calcium-binding proteins associated with specific stages of myeloid cell differentiation are expressed by subsets of macrophages in inflammatory tissues
    • Zwadlo G., Bruggen J., Gerhards G., Schlegel R., and Sorg C. Two calcium-binding proteins associated with specific stages of myeloid cell differentiation are expressed by subsets of macrophages in inflammatory tissues. Clin. Exp. Immunol. 72 (1988) 510-515
    • (1988) Clin. Exp. Immunol. , vol.72 , pp. 510-515
    • Zwadlo, G.1    Bruggen, J.2    Gerhards, G.3    Schlegel, R.4    Sorg, C.5
  • 244
    • 0033796465 scopus 로고    scopus 로고
    • Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14)
    • Sohnle P.G., Hunter M.J., Hahn B., and Chazin W.J. Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14). J. Infect. Dis. 182 (2000) 1272-1275
    • (2000) J. Infect. Dis. , vol.182 , pp. 1272-1275
    • Sohnle, P.G.1    Hunter, M.J.2    Hahn, B.3    Chazin, W.J.4
  • 248
    • 0031014663 scopus 로고    scopus 로고
    • Expression of the S-100 proteins MRP-8 and -14 in ischemic brain lesions
    • Postler E., Lehr A., Schluesener H., and Meyermann R. Expression of the S-100 proteins MRP-8 and -14 in ischemic brain lesions. Glia 19 (1997) 27-34
    • (1997) Glia , vol.19 , pp. 27-34
    • Postler, E.1    Lehr, A.2    Schluesener, H.3    Meyermann, R.4
  • 249
    • 0028261779 scopus 로고
    • Expression of MRP14, 27E10, interferon-alpha and leukocyte common antigen by reactive microglia in postmortem human brain tissue
    • Akiyama H., Ikeda K., Katoh M., McGeer E.G., and McGeer P.L. Expression of MRP14, 27E10, interferon-alpha and leukocyte common antigen by reactive microglia in postmortem human brain tissue. J. Neuroimmunol. 50 (1994) 195-201
    • (1994) J. Neuroimmunol. , vol.50 , pp. 195-201
    • Akiyama, H.1    Ikeda, K.2    Katoh, M.3    McGeer, E.G.4    McGeer, P.L.5
  • 250
    • 0032435515 scopus 로고    scopus 로고
    • Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9)
    • Kerkhoff C., Klempt M., and Sorg C. Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). Biochim. Biophys. Acta 1448 (1998) 200-211
    • (1998) Biochim. Biophys. Acta , vol.1448 , pp. 200-211
    • Kerkhoff, C.1    Klempt, M.2    Sorg, C.3
  • 251
    • 33846847550 scopus 로고    scopus 로고
    • Roles of calcium-binding proteins, S100A8 and S100A9, in invasive phenotype of human gastric cancer cells
    • Yong H.Y., and Moon A. Roles of calcium-binding proteins, S100A8 and S100A9, in invasive phenotype of human gastric cancer cells. Arch. Pharm. Res. 30 (2007) 75-81
    • (2007) Arch. Pharm. Res. , vol.30 , pp. 75-81
    • Yong, H.Y.1    Moon, A.2
  • 252
    • 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., De Servi B., Medunjanin S., Tessier P.A., and 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. 312 (2006) 184-197
    • (2006) Exp. Cell Res. , vol.312 , pp. 184-197
    • Hermani, A.1    De Servi, B.2    Medunjanin, S.3    Tessier, P.A.4    Mayer, D.5
  • 253
    • 0032902356 scopus 로고    scopus 로고
    • The analysis of S100A9 and S100A8 expression in matched sets of macroscopically normal colon mucosa and colorectal carcinoma: the S100A9 and S100A8 positive cells underlie and invade tumor mass
    • Stulik J., Osterreicher J., Koupilova K., Knizek, Macela A., Bures J., Jandik P., Langr F., Dedic K., and Jungblut P.R. The analysis of S100A9 and S100A8 expression in matched sets of macroscopically normal colon mucosa and colorectal carcinoma: the S100A9 and S100A8 positive cells underlie and invade tumor mass. Electrophoresis 20 (1999) 1047-1054
    • (1999) Electrophoresis , vol.20 , pp. 1047-1054
    • Stulik, J.1    Osterreicher, J.2    Koupilova, K.3    Knizek4    Macela, A.5    Bures, J.6    Jandik, P.7    Langr, F.8    Dedic, K.9    Jungblut, P.R.10
  • 255
    • 0033566735 scopus 로고    scopus 로고
    • A null mutation in the inflammation-associated S100 protein S100A8 causes early resorption of the mouse embryo
    • Passey R.J., Williams E., Lichanska A.M., Wells C., Hu S., Geczy C.L., Little M.H., and Hume D.A. A null mutation in the inflammation-associated S100 protein S100A8 causes early resorption of the mouse embryo. J. Immunol. 163 (1999) 2209-2216
    • (1999) J. Immunol. , vol.163 , pp. 2209-2216
    • Passey, R.J.1    Williams, E.2    Lichanska, A.M.3    Wells, C.4    Hu, S.5    Geczy, C.L.6    Little, M.H.7    Hume, D.A.8
  • 256
    • 0037305848 scopus 로고    scopus 로고
    • Loss of S100A9 (MRP14) results in reduced interleukin-8-induced CD11b surface expression, a polarized microfilament system, and diminished responsiveness to chemoattractants in vitro
    • Manitz M.P., Horst B., Seeliger S., Strey A., Skryabin B.V., Gunzer M., Frings W., Schonlau F., Roth J., Sorg C., and Nacken W. Loss of S100A9 (MRP14) results in reduced interleukin-8-induced CD11b surface expression, a polarized microfilament system, and diminished responsiveness to chemoattractants in vitro. Mol. Cell. Biol. 23 (2003) 1034-1043
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1034-1043
    • Manitz, M.P.1    Horst, B.2    Seeliger, S.3    Strey, A.4    Skryabin, B.V.5    Gunzer, M.6    Frings, W.7    Schonlau, F.8    Roth, J.9    Sorg, C.10    Nacken, W.11
  • 258
    • 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., and Nacken W. Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells. Biochemistry 40 (2001) 241-248
    • (2001) Biochemistry , vol.40 , pp. 241-248
    • Kerkhoff, C.1    Sorg, C.2    Tandon, N.N.3    Nacken, W.4
  • 259
    • 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., and 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. 277 (2002) 3658-3665
    • (2002) J. Biol. Chem. , vol.277 , pp. 3658-3665
    • Robinson, M.J.1    Tessier, P.2    Poulsom, R.3    Hogg, N.4
  • 260
    • 14644404879 scopus 로고    scopus 로고
    • The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2
    • Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., and Doussiere J. The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2. FASEB J. 19 (2005) 467-469
    • (2005) FASEB J. , vol.19 , pp. 467-469
    • Kerkhoff, C.1    Nacken, W.2    Benedyk, M.3    Dagher, M.C.4    Sopalla, C.5    Doussiere, J.6
  • 262
    • 45149098188 scopus 로고    scopus 로고
    • S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via the receptor for advanced glycation end products
    • Boyd J.H., Kan B., Roberts H., Wang Y., and Walley K.R. S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via the receptor for advanced glycation end products. Circ. Res. 102 (2008) 1239-1246
    • (2008) Circ. Res. , vol.102 , pp. 1239-1246
    • Boyd, J.H.1    Kan, B.2    Roberts, H.3    Wang, Y.4    Walley, K.R.5
  • 264
    • 34548036986 scopus 로고    scopus 로고
    • The S100A8/A9 heterodimer amplifies proinflammatory cytokine production by macrophages via activation of nuclear factor kappa B and p38 mitogen-activated protein kinase in rheumatoid arthritis
    • Sunahori K., Yamamura M., Yamana J., Takasugi K., Kawashima M., Yamamoto H., Chazin W.J., Nakatani Y., Yui S., and Makino H. The S100A8/A9 heterodimer amplifies proinflammatory cytokine production by macrophages via activation of nuclear factor kappa B and p38 mitogen-activated protein kinase in rheumatoid arthritis. Arthritis. Res. Ther. 8 (2006) R69
    • (2006) Arthritis. Res. Ther. , vol.8
    • Sunahori, K.1    Yamamura, M.2    Yamana, J.3    Takasugi, K.4    Kawashima, M.5    Yamamoto, H.6    Chazin, W.J.7    Nakatani, Y.8    Yui, S.9    Makino, H.10
  • 268
    • 0030347485 scopus 로고    scopus 로고
    • 2+-binding properties of calgizzarin (S100C) isolated from chicken gizzard smooth muscle
    • 2+-binding properties of calgizzarin (S100C) isolated from chicken gizzard smooth muscle. Biochem. Cell. Biol. 74 (1996) 687-694
    • (1996) Biochem. Cell. Biol. , vol.74 , pp. 687-694
    • Allen, B.G.1    Durussel, I.2    Walsh, M.P.3    Cox, J.A.4
  • 269
    • 0031325145 scopus 로고    scopus 로고
    • Molecular cloning and expression of avian smooth muscle S100A11 (calgizzarin, S100C)
    • Schonekess B.O., and Walsh M.P. Molecular cloning and expression of avian smooth muscle S100A11 (calgizzarin, S100C). Biochem. Cell. Biol. 75 (1997) 771-775
    • (1997) Biochem. Cell. Biol. , vol.75 , pp. 771-775
    • Schonekess, B.O.1    Walsh, M.P.2
  • 270
    • 0038342516 scopus 로고    scopus 로고
    • Unmasking the annexin I interaction from the structure of Apo-S100A11
    • Dempsey A.C., Walsh M.P., and Shaw G.S. Unmasking the annexin I interaction from the structure of Apo-S100A11. Structure 11 (2003) 887-897
    • (2003) Structure , vol.11 , pp. 887-897
    • Dempsey, A.C.1    Walsh, M.P.2    Shaw, G.S.3
  • 271
    • 0038734222 scopus 로고    scopus 로고
    • Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I
    • Rety S., Osterloh D., Arie J.P., Tabaries S., Seeman J., Russo-Marie F., Gerke V., and Lewit-Bentley A. Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I. Struct. Fold Des. 8 (2000) 175-184
    • (2000) Struct. Fold Des. , vol.8 , pp. 175-184
    • Rety, S.1    Osterloh, D.2    Arie, J.P.3    Tabaries, S.4    Seeman, J.5    Russo-Marie, F.6    Gerke, V.7    Lewit-Bentley, A.8
  • 274
    • 14844292553 scopus 로고    scopus 로고
    • Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays: S100A6, S100A8, S100A9 and S100A11 are all overexpressed in common cancers
    • Cross S.S., Hamdy F.C., Deloulme J.C., and Rehman I. Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays: S100A6, S100A8, S100A9 and S100A11 are all overexpressed in common cancers. Histopathology 46 (2005) 256-259
    • (2005) Histopathology , vol.46 , pp. 256-259
    • Cross, S.S.1    Hamdy, F.C.2    Deloulme, J.C.3    Rehman, I.4
  • 276
  • 279
    • 1842457009 scopus 로고    scopus 로고
    • PKCalpha mediates TGFbeta-induced growth inhibition of human keratinocytes via phosphorylation of S100C/A11
    • Sakaguchi M., Miyazaki M., Sonegawa H., Kashiwagi M., Ohba M., Kuroki T., Namba M., and Huh N.H. PKCalpha mediates TGFbeta-induced growth inhibition of human keratinocytes via phosphorylation of S100C/A11. J. Cell Biol. 164 (2004) 979-984
    • (2004) J. Cell Biol. , vol.164 , pp. 979-984
    • Sakaguchi, M.1    Miyazaki, M.2    Sonegawa, H.3    Kashiwagi, M.4    Ohba, M.5    Kuroki, T.6    Namba, M.7    Huh, N.H.8
  • 280
    • 0242322055 scopus 로고    scopus 로고
    • Calgizarrin like gene (Cal) deficient mice undergo normal spermatogenesis
    • Mannan A.U., Nica G., Nayernia K., Mueller C., and Engel W. Calgizarrin like gene (Cal) deficient mice undergo normal spermatogenesis. Mol. Reprod. Dev. 66 (2003) 431-438
    • (2003) Mol. Reprod. Dev. , vol.66 , pp. 431-438
    • Mannan, A.U.1    Nica, G.2    Nayernia, K.3    Mueller, C.4    Engel, W.5
  • 281
    • 29144510038 scopus 로고    scopus 로고
    • Inflammation-induced chondrocyte hypertrophy is driven by receptor for advanced glycation end products
    • Cecil D.L., Johnson K., Rediske J., Lotz M., Schmidt A.M., and Terkeltaub R. Inflammation-induced chondrocyte hypertrophy is driven by receptor for advanced glycation end products. J. Immunol. 175 (2005) 8296-8302
    • (2005) J. Immunol. , vol.175 , pp. 8296-8302
    • Cecil, D.L.1    Johnson, K.2    Rediske, J.3    Lotz, M.4    Schmidt, A.M.5    Terkeltaub, R.6
  • 282
    • 50949122078 scopus 로고    scopus 로고
    • Transamidation by transglutaminase 2 transforms S100A11 calgranulin into a procatabolic cytokine for chondrocytes
    • Cecil D.L., and Terkeltaub R. Transamidation by transglutaminase 2 transforms S100A11 calgranulin into a procatabolic cytokine for chondrocytes. J. Immunol. 180 (2008) 8378-8385
    • (2008) J. Immunol. , vol.180 , pp. 8378-8385
    • Cecil, D.L.1    Terkeltaub, R.2
  • 284
    • 0029041454 scopus 로고
    • Identification and characterization of a novel human neutrophil protein related to the S100 family
    • Guignard F., Mauel J., and Markert M. Identification and characterization of a novel human neutrophil protein related to the S100 family. Biochem. J. 309 (1995) 395-401
    • (1995) Biochem. J. , vol.309 , pp. 395-401
    • Guignard, F.1    Mauel, J.2    Markert, M.3
  • 287
    • 41449118854 scopus 로고    scopus 로고
    • Structural stability and reversible unfolding of recombinant porcine S100A12
    • Garcia A.F., Garcia W., Nonato M.C., and Araujo A.P. Structural stability and reversible unfolding of recombinant porcine S100A12. Biophys. Chem. 134 (2008) 246-253
    • (2008) Biophys. Chem. , vol.134 , pp. 246-253
    • Garcia, A.F.1    Garcia, W.2    Nonato, M.C.3    Araujo, A.P.4
  • 288
    • 0028134998 scopus 로고
    • Primary structure and binding properties of calgranulin C, a novel S100-like calcium-binding protein from pig granulocytes
    • Dell'Angelica E.C., Schleicher C.H., and Santome J.A. Primary structure and binding properties of calgranulin C, a novel S100-like calcium-binding protein from pig granulocytes. J. Biol. Chem. 269 (1994) 28929-28936
    • (1994) J. Biol. Chem. , vol.269 , pp. 28929-28936
    • Dell'Angelica, E.C.1    Schleicher, C.H.2    Santome, J.A.3
  • 292
    • 0242441020 scopus 로고    scopus 로고
    • Expression of the pro-inflammatory protein S100A12 (EN-RAGE) in rheumatoid and psoriatic arthritis.
    • Foell D., Kane D., Bresnihan B., Vogl T., Nacken W., Sorg C., Fitzgerald O., and Roth J. Expression of the pro-inflammatory protein S100A12 (EN-RAGE) in rheumatoid and psoriatic arthritis. Rheumatology 42 (2003) 1383-1389
    • (2003) Rheumatology , vol.42 , pp. 1383-1389
    • Foell, D.1    Kane, D.2    Bresnihan, B.3    Vogl, T.4    Nacken, W.5    Sorg, C.6    Fitzgerald, O.7    Roth, J.8
  • 293
    • 0038576426 scopus 로고    scopus 로고
    • Neutrophil derived human S100A12 (EN-RAGE) is strongly expressed during chronic active inflammatory bowel disease
    • Foell D., Kucharzik T., Kraft M., Vogl T., Sorg C., Domschke W., and Roth J. Neutrophil derived human S100A12 (EN-RAGE) is strongly expressed during chronic active inflammatory bowel disease. Gut 52 (2003) 847-853
    • (2003) Gut , vol.52 , pp. 847-853
    • Foell, D.1    Kucharzik, T.2    Kraft, M.3    Vogl, T.4    Sorg, C.5    Domschke, W.6    Roth, J.7
  • 296
    • 41149109122 scopus 로고    scopus 로고
    • Fecal S100A12 and fecal calprotectin as noninvasive markers for inflammatory bowel disease in children
    • Sidler M.A., Leach S.T., and Day A.S. Fecal S100A12 and fecal calprotectin as noninvasive markers for inflammatory bowel disease in children. Inflamm. Bowel. Dis. 14 (2008) 359-366
    • (2008) Inflamm. Bowel. Dis. , vol.14 , pp. 359-366
    • Sidler, M.A.1    Leach, S.T.2    Day, A.S.3
  • 297
    • 67349125299 scopus 로고    scopus 로고
    • Human S100A12: a novel key player in inflammation?
    • [Electronic publication ahead of print]
    • Pietzsch J., and Hoppmann S. Human S100A12: a novel key player in inflammation?. Amino Acids (2008) [Electronic publication ahead of print]
    • (2008) Amino Acids
    • Pietzsch, J.1    Hoppmann, S.2
  • 299
    • 46749147976 scopus 로고    scopus 로고
    • S100 calgranulin proteins S100A8, S100A9 and S100A12 are expressed in the inflamed gastric mucosa of Helicobacter pylori-infected children
    • Leach S.T., Mitchell H.M., Geczy C.L., Sherman P.M., and Day A.S. S100 calgranulin proteins S100A8, S100A9 and S100A12 are expressed in the inflamed gastric mucosa of Helicobacter pylori-infected children. Can. J. Gastroenterol. 22 (2008) 461-464
    • (2008) Can. J. Gastroenterol. , vol.22 , pp. 461-464
    • Leach, S.T.1    Mitchell, H.M.2    Geczy, C.L.3    Sherman, P.M.4    Day, A.S.5
  • 301
    • 4544343310 scopus 로고    scopus 로고
    • Identification of intracellular target proteins of the calcium-signaling protein S100A12
    • Hatakeyama T., Okada M., Shimamoto S., Kubota Y., and Kobayashi R. Identification of intracellular target proteins of the calcium-signaling protein S100A12. Eur. J. Biochem. 271 (2004) 3765-3775
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3765-3775
    • Hatakeyama, T.1    Okada, M.2    Shimamoto, S.3    Kubota, Y.4    Kobayashi, R.5
  • 302
    • 0030583594 scopus 로고    scopus 로고
    • Characterization of the human and mouse cDNAs coding for S100A13, a new member of the S100 protein family
    • Wicki R., Schäfer B.W., Erne P., and Heizmann C.W. Characterization of the human and mouse cDNAs coding for S100A13, a new member of the S100 protein family. Biochem. Biophys. Res. Commun. 227 (1996) 594-599
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 594-599
    • Wicki, R.1    Schäfer, B.W.2    Erne, P.3    Heizmann, C.W.4
  • 303
    • 0039599133 scopus 로고    scopus 로고
    • S100A13. Biochemical characterization and subcellular localization in different cell lines
    • Ridinger K., Schäfer B.W., Durussel I., Cox J.A., and Heizmann C.W. S100A13. Biochemical characterization and subcellular localization in different cell lines. J. Biol. Chem. 275 (2000) 8686-8694
    • (2000) J. Biol. Chem. , vol.275 , pp. 8686-8694
    • Ridinger, K.1    Schäfer, B.W.2    Durussel, I.3    Cox, J.A.4    Heizmann, C.W.5
  • 304
    • 33748457143 scopus 로고    scopus 로고
    • Copper binding affinity of S100A13, a key component of the FGF-1 nonclassical copper-dependent release complex
    • Sivaraja V., Kumar T.K., Rajalingam D., Graziani I., Prudovsky I., and Yu C. Copper binding affinity of S100A13, a key component of the FGF-1 nonclassical copper-dependent release complex. Biophys. J. 91 (2006) 1832-1843
    • (2006) Biophys. J. , vol.91 , pp. 1832-1843
    • Sivaraja, V.1    Kumar, T.K.2    Rajalingam, D.3    Graziani, I.4    Prudovsky, I.5    Yu, C.6
  • 306
    • 37149002585 scopus 로고    scopus 로고
    • Indentification of a novel, functionnal role for S100A13 in invasive lung cancer cell lines.
    • Pierce A., Barron N., Linehan R., Ryan E., O'Driscoll L., Daly C., and Clynes M. Indentification of a novel, functionnal role for S100A13 in invasive lung cancer cell lines. Eur. J. Cancer 44 (2008) 151-159
    • (2008) Eur. J. Cancer , vol.44 , pp. 151-159
    • Pierce, A.1    Barron, N.2    Linehan, R.3    Ryan, E.4    O'Driscoll, L.5    Daly, C.6    Clynes, M.7
  • 308
    • 40949086888 scopus 로고    scopus 로고
    • 2+ requirements of the FGF1-S100A13 interaction measured by quartz crystal microbalance: an initial step in amlexanox-reversible non-classical release of FGF1
    • 2+ requirements of the FGF1-S100A13 interaction measured by quartz crystal microbalance: an initial step in amlexanox-reversible non-classical release of FGF1. Neurochem. Int. 52 (2008) 1076-1085
    • (2008) Neurochem. Int. , vol.52 , pp. 1076-1085
    • Matsunaga, H.1    Ueda, H.2
  • 309
    • 1642294816 scopus 로고    scopus 로고
    • S100 protein translocation in response to extracellular S100 is mediated by receptor for advanced glycation endproducts in human endothelial cells
    • Hsieh H.L., Schäfer B.W., Weigle B., and Heizmann C.W. S100 protein translocation in response to extracellular S100 is mediated by receptor for advanced glycation endproducts in human endothelial cells. Biochem. Biophys. Res. Commun. 316 (2004) 949-959
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 949-959
    • Hsieh, H.L.1    Schäfer, B.W.2    Weigle, B.3    Heizmann, C.W.4
  • 313
    • 23944470477 scopus 로고    scopus 로고
    • Immediate up-regulation of the calcium-binding protein S100P and its involvement in the cytokinin-induced differentiation of human myeloid leukemia cells
    • Ishii Y., Kasukabe T., and Honma Y. Immediate up-regulation of the calcium-binding protein S100P and its involvement in the cytokinin-induced differentiation of human myeloid leukemia cells. Biochim. Biophys. Acta 1745 (2005) 156-165
    • (2005) Biochim. Biophys. Acta , vol.1745 , pp. 156-165
    • Ishii, Y.1    Kasukabe, T.2    Honma, Y.3
  • 314
  • 315
    • 0034131796 scopus 로고    scopus 로고
    • S100P calcium-binding protein overexpression is associated with immortalization of human breast epithelial cells in vitro and early stages of breast cancer development in vivo
    • Guerreiro Da Silva I.D., Hu Y.F., Russo I.H., Ao X., Salicioni A.M., Yang X., and Russo J. S100P calcium-binding protein overexpression is associated with immortalization of human breast epithelial cells in vitro and early stages of breast cancer development in vivo. Int. J. Oncol. 16 (2000) 231-240
    • (2000) Int. J. Oncol. , vol.16 , pp. 231-240
    • Guerreiro Da Silva, I.D.1    Hu, Y.F.2    Russo, I.H.3    Ao, X.4    Salicioni, A.M.5    Yang, X.6    Russo, J.7
  • 317
    • 0038647458 scopus 로고    scopus 로고
    • Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P
    • Koltzscher M., Neumann C., Konig S., and Gerke V. Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P. Mol. Biol. Cell 14 (2003) 2372-2384
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2372-2384
    • Koltzscher, M.1    Neumann, C.2    Konig, S.3    Gerke, V.4
  • 318
    • 57649194806 scopus 로고    scopus 로고
    • Characterization of the Ca2+-regulated ezrin-S100P interaction and its role in tumor cell migration
    • Austermann J., Nazmi A.R., Muller-Tidow C., and Gerke V. Characterization of the Ca2+-regulated ezrin-S100P interaction and its role in tumor cell migration. J. Biol. Chem. 283 (2008) 29331-29340
    • (2008) J. Biol. Chem. , vol.283 , pp. 29331-29340
    • Austermann, J.1    Nazmi, A.R.2    Muller-Tidow, C.3    Gerke, V.4
  • 320
    • 1242272130 scopus 로고    scopus 로고
    • S100P stimulates cell proliferation and survival via receptor for activated glycation end products (RAGE)
    • Arumugam T., Simeone D.M., Schmidt A.M., and Logsdon C.D. S100P stimulates cell proliferation and survival via receptor for activated glycation end products (RAGE). J. Biol. Chem. 279 (2004) 5059-5065
    • (2004) J. Biol. Chem. , vol.279 , pp. 5059-5065
    • Arumugam, T.1    Simeone, D.M.2    Schmidt, A.M.3    Logsdon, C.D.4
  • 322
    • 0027965622 scopus 로고
    • Inhibition of protein kinase C- and casein kinase II-mediated phosphorylation of GAP-43 by S100 beta
    • Lin L.H., Van Eldik L.J., Osheroff N., and Norden J.J. Inhibition of protein kinase C- and casein kinase II-mediated phosphorylation of GAP-43 by S100 beta. Brain Res. Mol. Brain Res. 25 (1994) 297-304
    • (1994) Brain Res. Mol. Brain Res. , vol.25 , pp. 297-304
    • Lin, L.H.1    Van Eldik, L.J.2    Osheroff, N.3    Norden, J.J.4
  • 323
    • 0023875705 scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. J. Biol. Chem. 263 (1988) 5876-5883
    • (1988) J. Biol. Chem. , vol.263 , pp. 5876-5883
    • Baudier, J.1    Cole, R.D.2
  • 324
    • 0031791750 scopus 로고    scopus 로고
    • The S100B protein inhibits phosphorylation of GFAP and vimentin in a cytoskeletal fraction from immature rat hippocampus
    • Ziegler D.R., Innocente C.E., Leal R.B., Rodnight R., and Goncalves C.A. The S100B protein inhibits phosphorylation of GFAP and vimentin in a cytoskeletal fraction from immature rat hippocampus. Neurochem. Res. 23 (1998) 1259-1263
    • (1998) Neurochem. Res. , vol.23 , pp. 1259-1263
    • Ziegler, D.R.1    Innocente, C.E.2    Leal, R.B.3    Rodnight, R.4    Goncalves, C.A.5
  • 326
    • 0032407132 scopus 로고    scopus 로고
    • Association of S100B with intermediate filaments and microtubules in glial cells
    • Sorci G., Agneletti A.L., Bianchi R., and Donato R. Association of S100B with intermediate filaments and microtubules in glial cells. Biochim. Biophys. Acta 1448 (1998) 277-289
    • (1998) Biochim. Biophys. Acta , vol.1448 , pp. 277-289
    • Sorci, G.1    Agneletti, A.L.2    Bianchi, R.3    Donato, R.4
  • 327
    • 0031773538 scopus 로고    scopus 로고
    • Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments
    • Garbuglia M., Verzini M., and Donato R. Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments. Cell Calcium 24 (1998) 177-191
    • (1998) Cell Calcium , vol.24 , pp. 177-191
    • Garbuglia, M.1    Verzini, M.2    Donato, R.3
  • 329
    • 0037185410 scopus 로고    scopus 로고
    • Annexin V, annexin VI, S100A1 and S100B in developing and adult avian skeletal muscles
    • Arcuri C., Giambanco I., Bianchi R., and Donato R. Annexin V, annexin VI, S100A1 and S100B in developing and adult avian skeletal muscles. Neuroscience 109 (2002) 371-388
    • (2002) Neuroscience , vol.109 , pp. 371-388
    • Arcuri, C.1    Giambanco, I.2    Bianchi, R.3    Donato, R.4
  • 333
    • 0035968275 scopus 로고    scopus 로고
    • The giant protein AHNAK is a specific target for the calcium- and zinc-binding S100B protein: potential implications for Ca2+ homeostasis regulation by S100B
    • Gentil B.J., Delphin C., Mbele G.O., Deloulme J.C., Ferro M., Garin J., and Baudier J. The giant protein AHNAK is a specific target for the calcium- and zinc-binding S100B protein: potential implications for Ca2+ homeostasis regulation by S100B. J. Biol. Chem. 276 (2001) 23253-23261
    • (2001) J. Biol. Chem. , vol.276 , pp. 23253-23261
    • Gentil, B.J.1    Delphin, C.2    Mbele, G.O.3    Deloulme, J.C.4    Ferro, M.5    Garin, J.6    Baudier, J.7
  • 334
    • 0029801765 scopus 로고    scopus 로고
    • Identification of an S100A1/S100B target protein: phosphoglucomutase
    • Landar A., Caddell G., Chessher J., and Zimmer D.B. Identification of an S100A1/S100B target protein: phosphoglucomutase. Cell Calcium 20 (1996) 279-285
    • (1996) Cell Calcium , vol.20 , pp. 279-285
    • Landar, A.1    Caddell, G.2    Chessher, J.3    Zimmer, D.B.4
  • 335
    • 0022976875 scopus 로고
    • Identification of a molecular target for the calcium-modulated protein S100. Fructose-1,6-bisphosphate aldolase
    • Zimmer D.B., and Van Eldik L.J. Identification of a molecular target for the calcium-modulated protein S100. Fructose-1,6-bisphosphate aldolase. J. Biol. Chem. 261 (1986) 11424-11428
    • (1986) J. Biol. Chem. , vol.261 , pp. 11424-11428
    • Zimmer, D.B.1    Van Eldik, L.J.2
  • 336
    • 0027991511 scopus 로고
    • Calcium-dependent regulation of smooth muscle calponin by S100
    • Fujii T., Oomatsuzawa A., Kuzumaki N., and Kondo Y. Calcium-dependent regulation of smooth muscle calponin by S100. J. Biochem. 116 (1994) 121-127
    • (1994) J. Biochem. , vol.116 , pp. 121-127
    • Fujii, T.1    Oomatsuzawa, A.2    Kuzumaki, N.3    Kondo, Y.4
  • 337
    • 0024820746 scopus 로고
    • Interaction of smooth muscle caldesmon with S-100 protein
    • Skripnikova E.V., and Gusev N.B. Interaction of smooth muscle caldesmon with S-100 protein. FEBS Lett. 257 (1989) 380-382
    • (1989) FEBS Lett. , vol.257 , pp. 380-382
    • Skripnikova, E.V.1    Gusev, N.B.2
  • 338
    • 0028986404 scopus 로고
    • S100 beta is a target protein of neurocalcin delta, an abundant isoform in glial cells
    • Okazaki K., Obata N.H., Inoue S., and Hidaka H. S100 beta is a target protein of neurocalcin delta, an abundant isoform in glial cells. Biochem. J. 306 (1995) 551-555
    • (1995) Biochem. J. , vol.306 , pp. 551-555
    • Okazaki, K.1    Obata, N.H.2    Inoue, S.3    Hidaka, H.4
  • 339
    • 0029043797 scopus 로고
    • Characterization of S-100b binding epitopes. Identification of a novel target, the actin capping protein, CapZ
    • Ivanenkov V.V., Jamieson Jr. G.A., Gruenstein E., and Dimlich R.V. Characterization of S-100b binding epitopes. Identification of a novel target, the actin capping protein, CapZ. J. Biol. Chem. 270 (1995) 14651-14658
    • (1995) J. Biol. Chem. , vol.270 , pp. 14651-14658
    • Ivanenkov, V.V.1    Jamieson Jr., G.A.2    Gruenstein, E.3    Dimlich, R.V.4
  • 340
    • 0027325342 scopus 로고
    • Identification of an S100 target protein: glycogen phosphorylase
    • Zimmer D.B., and Dubuisson J.G. Identification of an S100 target protein: glycogen phosphorylase. Cell Calcium 14 (1993) 323-332
    • (1993) Cell Calcium , vol.14 , pp. 323-332
    • Zimmer, D.B.1    Dubuisson, J.G.2
  • 342
    • 0023878297 scopus 로고
    • Calcium-independent, pH-regulated effects of S-100 proteins on assembly-disassembly of brain microtubule protein in vitro
    • Donato R. Calcium-independent, pH-regulated effects of S-100 proteins on assembly-disassembly of brain microtubule protein in vitro. J. Biol. Chem. 263 (1988) 106-110
    • (1988) J. Biol. Chem. , vol.263 , pp. 106-110
    • Donato, R.1
  • 343
    • 0029064808 scopus 로고
    • Interactions of myogenic bHLH transcription factors with calcium-binding calmodulin and S100a (alpha alpha) proteins
    • Baudier J., Bergeret E., Bertacchi N., Weintraub H., Gagnon J., and Garin J. Interactions of myogenic bHLH transcription factors with calcium-binding calmodulin and S100a (alpha alpha) proteins. Biochemistry 34 (1995) 7834-7846
    • (1995) Biochemistry , vol.34 , pp. 7834-7846
    • Baudier, J.1    Bergeret, E.2    Bertacchi, N.3    Weintraub, H.4    Gagnon, J.5    Garin, J.6
  • 344
    • 0033534740 scopus 로고    scopus 로고
    • Role of the C-terminal extension in the interaction of S100A1 with GFAP, tubulin, the S100A1- and S100B-inhibitory peptide, TRTK-12, and a peptide derived from p53, and the S100A1 inhibitory effect on GFAP polymerization
    • Garbuglia M., Verzini M., Rustandi R.R., Osterloh D., Weber D.J., Gerke V., and Donato R. Role of the C-terminal extension in the interaction of S100A1 with GFAP, tubulin, the S100A1- and S100B-inhibitory peptide, TRTK-12, and a peptide derived from p53, and the S100A1 inhibitory effect on GFAP polymerization. Biochem. Biophys. Res. Commun. 254 (1999) 36-41
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 36-41
    • Garbuglia, M.1    Verzini, M.2    Rustandi, R.R.3    Osterloh, D.4    Weber, D.J.5    Gerke, V.6    Donato, R.7
  • 346
    • 2642588900 scopus 로고    scopus 로고
    • S100A1 codistributes with synapsin I in discrete brain areas and inhibits the F-actin-bundling activity of synapsin I
    • Benfenati F., Ferrari R., Onofri F., Arcuri C., Giambanco I., and Donato R. S100A1 codistributes with synapsin I in discrete brain areas and inhibits the F-actin-bundling activity of synapsin I. J. Neurochem. 89 (2004) 1260-1270
    • (2004) J. Neurochem. , vol.89 , pp. 1260-1270
    • Benfenati, F.1    Ferrari, R.2    Onofri, F.3    Arcuri, C.4    Giambanco, I.5    Donato, R.6
  • 351
    • 1042301417 scopus 로고    scopus 로고
    • S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex
    • Okada M., Hatakeyama T., Itoh H., Tokuta N., Tokumitsu H., and Kobayashi R. S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex. J. Biol. Chem. 279 (2004) 4221-4233
    • (2004) J. Biol. Chem. , vol.279 , pp. 4221-4233
    • Okada, M.1    Hatakeyama, T.2    Itoh, H.3    Tokuta, N.4    Tokumitsu, H.5    Kobayashi, R.6
  • 353
    • 0028086183 scopus 로고
    • Metastasis-associated mts1 gene expression correlates with increased p53 detection in the B16 murine melanoma
    • Parker C., Lakshmi M.S., Piura B., and Sherbet G.V. Metastasis-associated mts1 gene expression correlates with increased p53 detection in the B16 murine melanoma. DNA Cell. Biol. 13 (1994) 343-351
    • (1994) DNA Cell. Biol. , vol.13 , pp. 343-351
    • Parker, C.1    Lakshmi, M.S.2    Piura, B.3    Sherbet, G.V.4
  • 354
    • 0029065162 scopus 로고
    • Interaction of metastasis associated Mts1 protein with nonmuscle myosin
    • Ford H.L., and Zain S.B. Interaction of metastasis associated Mts1 protein with nonmuscle myosin. Oncogene 10 (1995) 1597-1605
    • (1995) Oncogene , vol.10 , pp. 1597-1605
    • Ford, H.L.1    Zain, S.B.2
  • 356
    • 0029853874 scopus 로고    scopus 로고
    • p30, a novel protein target of mouse calcyclin (S100A6)
    • Filipek A., and Wojda U. p30, a novel protein target of mouse calcyclin (S100A6). Biochem. J. 320 (1996) 585-587
    • (1996) Biochem. J. , vol.320 , pp. 585-587
    • Filipek, A.1    Wojda, U.2
  • 357
    • 33845406931 scopus 로고    scopus 로고
    • Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2
    • Rintala-Dempsey A.C., Santamaria-Kisiel L., Liao Y., Lajoie G., and Shaw G.S. Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2. Biochemistry 45 (2006) 14695-14705
    • (2006) Biochemistry , vol.45 , pp. 14695-14705
    • Rintala-Dempsey, A.C.1    Santamaria-Kisiel, L.2    Liao, Y.3    Lajoie, G.4    Shaw, G.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.