메뉴 건너뛰기




Volumn 287, Issue 5, 2012, Pages 3550-3558

Exposing a hidden functional site of C-reactive protein by site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; DISEASES; MUTAGENESIS; PHYSIOLOGY;

EID: 84863044357     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.310011     Document Type: Article
Times cited : (27)

References (63)
  • 2
    • 0028306646 scopus 로고
    • Calcium ion binding regions in C-reactive protein: Location and regulation of conformational changes
    • DOI 10.1016/0161-5890(94)90169-4
    • Mullenix, M. C., and Mortensen, R. F. (1994) Calcium ion binding regions in C-reactive protein. Location and regulation of conformational changes. Mol. Immunol. 31, 615-622 (Pubitemid 24175029)
    • (1994) Molecular Immunology , vol.31 , Issue.8 , pp. 615-622
    • Mullenix, M.C.1    Mortensen, R.F.2
  • 3
    • 0015010578 scopus 로고
    • Specificity of C-reactive protein for choline phosphate residues of pneumococcal C-polysaccharide
    • Volanakis, J. E., and Kaplan, M. H. (1971) Specificity of C-reactive protein for choline phosphate residues of pneumococcal C-polysaccharide. Proc. Soc. Exp. Biol. Med. 136, 612-614
    • (1971) Proc. Soc. Exp. Biol. Med. , vol.136 , pp. 612-614
    • Volanakis, J.E.1    Kaplan, M.H.2
  • 4
    • 0028217625 scopus 로고
    • Effects of calcium, magnesium, and phosphorylcholine on secondary structures of human C-reactive protein and serum amyloid P component observed by infrared spectroscopy
    • Dong, A., Caughey, W. S., and Du Clos, T. W. (1994) Effects of calcium, magnesium, and phosphorylcholine on secondary structures of human C-reactive protein and serum amyloid P component observed by infrared spectroscopy. J. Biol. Chem. 269, 6424-6430 (Pubitemid 24191015)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.9 , pp. 6424-6430
    • Dong, A.1    Caughey, W.S.2    Du, C.T.W.3
  • 5
    • 70349843234 scopus 로고    scopus 로고
    • The binding of C-reactive protein, in the presence of phosphoethanolamine, to low-density lipoproteins is due to phosphoethanolamine- generated acidic pH
    • Singh, S. K., Hammond, D. J., Jr., Beeler, B. W., and Agrawal, A. (2009) The binding of C-reactive protein, in the presence of phosphoethanolamine, to low-density lipoproteins is due to phosphoethanolamine-generated acidic pH. Clin. Chim. Acta 409, 143-144
    • (2009) Clin. Chim. Acta , vol.409 , pp. 143-144
    • Singh, S.K.1    Hammond Jr., D.J.2    Beeler, B.W.3    Agrawal, A.4
  • 7
    • 0000205893 scopus 로고
    • Studies of acute phase protein. I. An immunohistochemical method for the localization of Cx-reactive protein in rabbits. Association with necrosis in local inflammatory lesions
    • Kushner, I., and Kaplan, M. H. (1961) Studies of acute phase protein. I. An immunohistochemical method for the localization of Cx-reactive protein in rabbits. Association with necrosis in local inflammatory lesions. J. Exp. Med. 114, 961-974
    • (1961) J. Exp. Med. , vol.114 , pp. 961-974
    • Kushner, I.1    Kaplan, M.H.2
  • 8
    • 0032851173 scopus 로고    scopus 로고
    • Complement and atherogenesis: Binding of CRP to degraded, nonoxidized LDL enhances complement activation
    • Bhakdi, S., Torzewski, M., Klouche, M., and Hemmes, M. (1999) Complement and atherogenesis. Binding of CRP to degraded, nonoxidized LDL enhances complement activation. Arterioscler. Thromb. Vasc. Biol. 19, 2348-2354 (Pubitemid 29477835)
    • (1999) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.19 , Issue.10 , pp. 2348-2354
    • Bhakdi, S.1    Torzewski, M.2    Klouche, M.3    Hemmes, M.4
  • 10
    • 77950382938 scopus 로고    scopus 로고
    • A unifying biologic explanation for "high-sensitivity" C-reactive protein and "low-grade" inflammation
    • Kushner, I., Samols, D., and Magrey, M. (2010) A unifying biologic explanation for "high-sensitivity" C-reactive protein and "low-grade" inflammation. Arthritis Care Res. 62, 442-446
    • (2010) Arthritis Care Res. , vol.62 , pp. 442-446
    • Kushner, I.1    Samols, D.2    Magrey, M.3
  • 12
    • 79956319051 scopus 로고    scopus 로고
    • Progress and challenges in translating the biology of atherosclerosis
    • Libby, P., Ridker, P. M., and Hansson, G. K. (2011) Progress and challenges in translating the biology of atherosclerosis. Nature 473, 317-325
    • (2011) Nature , vol.473 , pp. 317-325
    • Libby, P.1    Ridker, P.M.2    Hansson, G.K.3
  • 13
    • 0023882543 scopus 로고
    • Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts
    • Silver, I. A., Murrills, R. J., and Etherington, D. J. (1988) Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts. Exp. Cell Res. 175, 266-276
    • (1988) Exp. Cell Res. , vol.175 , pp. 266-276
    • Silver, I.A.1    Murrills, R.J.2    Etherington, D.J.3
  • 14
    • 0030956262 scopus 로고    scopus 로고
    • Does an acidic pH explain why low density lipoprotein is oxidised in atherosclerotic lesions?
    • Leake, D. S. (1997) Does an acidic pH explain why low density lipoprotein is oxidised in atherosclerotic lesions? Atherosclerosis 129, 149-157
    • (1997) Atherosclerosis , vol.129 , pp. 149-157
    • Leake, D.S.1
  • 16
    • 27844583439 scopus 로고    scopus 로고
    • Decrease in pH strongly enhances binding of native, proteolyzed, lipolyzed, and oxidized low density lipoprotein particles to human aortic proteoglycans
    • DOI 10.1074/jbc.M508565200
    • Sneck, M., Kovanen, P. T., and Oörni, K. (2005) Decrease in pH strongly enhances binding of native, proteolyzed, lipolyzed, and oxidized low density lipoprotein particles to human aortic proteoglycans. J. Biol. Chem. 280, 37449-37454 (Pubitemid 41642352)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37449-37454
    • Sneck, M.1    Kovanen, P.T.2    Oorni, K.3
  • 17
    • 33645107179 scopus 로고    scopus 로고
    • Hypoxia-sensitive molecules may modulate the development of atherosclerosis in sleep apnoea syndrome
    • Hayashi, M., Fujimoto, K., Urushibata, K., Takamizawa, A., Kinoshita, O., and Kubo, K. (2006) Hypoxia-sensitive molecules may modulate the development of atherosclerosis in sleep apnoea syndrome. Respirology 11, 24-31
    • (2006) Respirology , vol.11 , pp. 24-31
    • Hayashi, M.1    Fujimoto, K.2    Urushibata, K.3    Takamizawa, A.4    Kinoshita, O.5    Kubo, K.6
  • 19
    • 73949150306 scopus 로고    scopus 로고
    • Macrophages create an acidic extracellular hydrolytic compartment to digest aggregated lipoproteins
    • Haka, A. S., Grosheva, I., Chiang, E., Buxbaum, A. R., Baird, B. A., Pierini, L. M., and Maxfield, F. R. (2009) Macrophages create an acidic extracellular hydrolytic compartment to digest aggregated lipoproteins. Mol. Biol. Cell 20, 4932-4940
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4932-4940
    • Haka, A.S.1    Grosheva, I.2    Chiang, E.3    Buxbaum, A.R.4    Baird, B.A.5    Pierini, L.M.6    Maxfield, F.R.7
  • 21
    • 33748575321 scopus 로고    scopus 로고
    • Enhanced extracellular lipid accumulation in acidic environments
    • DOI 10.1097/01.mol.0000245259.63505.c2, PII 0004143320061000000007
    • Oörni, K., and Kovanen, P. T. (2006) Enhanced extracellular lipid accumulation in acidic environments. Curr. Opin. Lipidol. 17, 534-540 (Pubitemid 44372684)
    • (2006) Current Opinion in Lipidology , vol.17 , Issue.5 , pp. 534-540
    • Oorni, K.1    Kovanen, P.T.2
  • 22
    • 0036791022 scopus 로고    scopus 로고
    • C-reactive protein binds to both oxidized LDL and apoptotic cells through recognition of a common ligand. Phosphorylcholine of oxidized phospholipids
    • Chang, M. K., Binder, C. J., Torzewski, M., and Witztum, J. L. (2002) C-reactive protein binds to both oxidized LDL and apoptotic cells through recognition of a common ligand. Phosphorylcholine of oxidized phospholipids. Proc. Natl. Acad. Sci. U.S.A. 99, 13043-13048
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13043-13048
    • Chang, M.K.1    Binder, C.J.2    Torzewski, M.3    Witztum, J.L.4
  • 23
    • 0037108874 scopus 로고    scopus 로고
    • Binding of C-reactive protein to modified low-density-lipoprotein particles: Identification of cholesterol as a novel ligand for C-reactive protein
    • DOI 10.1042/BJ20020492
    • Taskinen, S., Kovanen, P. T., Jarva, H., Meri, S., and Pentikäinen, M. O. (2002) Binding of C-reactive protein to modified low-density-lipoprotein particles. Identification of cholesterol as a novel ligand for C-reactive protein. Biochem. J. 367, 403-412 (Pubitemid 35216814)
    • (2002) Biochemical Journal , vol.367 , Issue.2 , pp. 403-412
    • Taskinen, S.1    Kovanen, P.T.2    Jarva, H.3    Meri, S.4    Pentikainen, M.O.5
  • 24
    • 16244407441 scopus 로고    scopus 로고
    • C-reactive protein and annexin A5 bind to distinct sites of negatively charged phospholipids present in oxidized low-density lipoprotein
    • DOI 10.1161/01.ATV.0000157979.51673.2c
    • van Tits, L., de Graaf, J., Toenhake, H., van Heerde, W., and Stalenhoef, A. (2005) C-reactive protein and annexin A5 bind to distinct sites of negatively charged phospholipids present in oxidized low-density lipoprotein. Arterioscler. Thromb. Vasc. Biol. 25, 717-722 (Pubitemid 40463859)
    • (2005) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.25 , Issue.4 , pp. 717-722
    • Van Tits, L.1    De Graaf, J.2    Toenhake, H.3    Van Heerde, W.4    Stalenhoef, A.5
  • 25
    • 30944445008 scopus 로고    scopus 로고
    • Interactions of C-reactive protein with low-density lipoproteins: Implications for an active role of modified C-reactive protein in atherosclerosis
    • DOI 10.1016/j.biocel.2005.11.004, PII S1357272505003845
    • Ji, S. R., Wu, Y., Potempa, L. A., Qiu, Q., and Zhao, J. (2006) Interactions of C-reactive protein with low-density lipoproteins. Implications for an active role of modified C-reactive protein in atherosclerosis. Int. J. Biochem. Cell Biol. 38, 648-661 (Pubitemid 43117588)
    • (2006) International Journal of Biochemistry and Cell Biology , vol.38 , Issue.4 , pp. 648-661
    • Ji, S.-R.1    Wu, Y.2    Potempa, L.A.3    Qiu, Q.4    Zhao, J.5
  • 26
    • 46949086807 scopus 로고    scopus 로고
    • Human C-reactive protein promotes oxidized low density lipoprotein uptake and matrix metalloproteinase-9 release in Wistar rats
    • Singh, U., Dasu, M. R., Yancey, P. G., Afify, A., Devaraj, S., and Jialal, I. (2008) Human C-reactive protein promotes oxidized low density lipoprotein uptake and matrix metalloproteinase-9 release in Wistar rats. J. Lipid Res. 49, 1015-1023
    • (2008) J. Lipid Res. , vol.49 , pp. 1015-1023
    • Singh, U.1    Dasu, M.R.2    Yancey, P.G.3    Afify, A.4    Devaraj, S.5    Jialal, I.6
  • 27
    • 44649152987 scopus 로고    scopus 로고
    • C-reactive protein-bound enzymatically modified low-density lipoprotein does not transform macrophages into foam cells
    • Singh, S. K., Suresh, M. V., Prayther, D. C., Moorman, J. P., Rusiñol, A. E., and Agrawal, A. (2008) C-reactive protein-bound enzymatically modified low-density lipoprotein does not transform macrophages into foam cells. J. Immunol. 180, 4316-4322
    • (2008) J. Immunol. , vol.180 , pp. 4316-4322
    • Singh, S.K.1    Suresh, M.V.2    Prayther, D.C.3    Moorman, J.P.4    Rusiñol, A.E.5    Agrawal, A.6
  • 32
    • 66449099335 scopus 로고    scopus 로고
    • Continously-infused human C-reactive protein is neither proatherosclerotic nor proinflammatory in apolipoprotein E-deficient mice
    • Ortiz, M. A., Campana, G. L., Woods, J. R., Boguslawski, G., Sosa, M. J., Walker, C. L., and Labarrere, C. A. (2009) Continously-infused human C-reactive protein is neither proatherosclerotic nor proinflammatory in apolipoprotein E-deficient mice. Exp. Biol. Med. 234, 624-631
    • (2009) Exp. Biol. Med. , vol.234 , pp. 624-631
    • Ortiz, M.A.1    Campana, G.L.2    Woods, J.R.3    Boguslawski, G.4    Sosa, M.J.5    Walker, C.L.6    Labarrere, C.A.7
  • 33
    • 79953190431 scopus 로고    scopus 로고
    • No reduction of atherosclerosis in C-reactive protein (CRP)-deficient mice
    • Teupser, D., Weber, O., Rao, T. N., Sass, K., Thiery, J., and Fehling, H. J. (2011) No reduction of atherosclerosis in C-reactive protein (CRP)-deficient mice. J. Biol. Chem. 286, 6272-6279
    • (2011) J. Biol. Chem. , vol.286 , pp. 6272-6279
    • Teupser, D.1    Weber, O.2    Rao, T.N.3    Sass, K.4    Thiery, J.5    Fehling, H.J.6
  • 38
    • 0028774537 scopus 로고
    • Comparative analyses of pentraxins. Implications for protomer assembly and ligand binding
    • Srinivasan, N., White, H. E., Emsley, J., Wood, S. P., Pepys, M. B., and Blundell, T. L. (1994) Comparative analyses of pentraxins. Implications for protomer assembly and ligand binding. Structure 2, 1017-1027
    • (1994) Structure , vol.2 , pp. 1017-1027
    • Srinivasan, N.1    White, H.E.2    Emsley, J.3    Wood, S.P.4    Pepys, M.B.5    Blundell, T.L.6
  • 39
    • 0033081409 scopus 로고    scopus 로고
    • The physiological structure of human C-reactive protein and its complex with phosphocholine
    • DOI 10.1016/S0969-2126(99)80023-9
    • Thompson, D., Pepys, M. B., and Wood, S. P. (1999) The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure Fold. Des. 7, 169-177 (Pubitemid 29159702)
    • (1999) Structure , vol.7 , Issue.2 , pp. 169-177
    • Thompson, D.1    Pepys, M.B.2    Wood, S.P.3
  • 40
    • 0027121379 scopus 로고
    • Probing the phosphocholine-binding site of human C-reactive protein by site-directed mutagenesis
    • Agrawal, A., Xu, Y., Ansardi, D., Macon, K. J., and Volanakis, J. E. (1992) Probing the phosphocholine-binding site of human C-reactive protein by site-directed mutagenesis. J. Biol. Chem. 267, 25352-25358
    • (1992) J. Biol. Chem. , vol.267 , pp. 25352-25358
    • Agrawal, A.1    Xu, Y.2    Ansardi, D.3    Macon, K.J.4    Volanakis, J.E.5
  • 41
    • 33646058924 scopus 로고    scopus 로고
    • Role of the property of C-reactive protein to activate the classical pathway of complement in protecting mice from pneumococcal infection
    • Suresh, M. V., Singh, S. K., Ferguson, D. A., Jr., and Agrawal, A. (2006) Role of the property of C-reactive protein to activate the classical pathway of complement in protecting mice from pneumococcal infection. J. Immunol. 176, 4369-4374 (Pubitemid 44264417)
    • (2006) Journal of Immunology , vol.176 , Issue.7 , pp. 4369-4374
    • Suresh, M.V.1    Singh, S.K.2    Ferguson Jr., D.A.3    Agrawal, A.4
  • 42
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum
    • Havel, R. J., Eder, H. A., and Bragdon, J. H. (1955) The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J. Clin. Invest. 34, 1345-1353
    • (1955) J. Clin. Invest. , vol.34 , pp. 1345-1353
    • Havel, R.J.1    Eder, H.A.2    Bragdon, J.H.3
  • 43
    • 0030820068 scopus 로고    scopus 로고
    • 7-Hydroperoxycholesterol and its products in oxidized low density lipoprotein and human atherosclerotic plaque
    • Brown, A. J., Leong, S. L., Dean, R. T., and Jessup, W. (1997) 7-Hydroperoxycholesterol and its products in oxidized low density lipoprotein and human atherosclerotic plaque. J. Lipid Res. 38, 1730-1745 (Pubitemid 27411265)
    • (1997) Journal of Lipid Research , vol.38 , Issue.9 , pp. 1730-1745
    • Brown, A.J.1    Leong, S.-L.2    Dean, R.T.3    Jessup, W.4
  • 44
    • 0020684529 scopus 로고
    • Kinetic and thermodynamic analysis of the control of C3b by the complement regulatory proteins factors H and I
    • DOI 10.1021/bi00270a026
    • Pangburn, M. K., and Müller-Eberhard, H. J. (1983) Kinetic and thermodynamic analysis of the control of C3b by the complement regulatory proteins factors H and I. Biochemistry 22, 178-185 (Pubitemid 13154157)
    • (1983) Biochemistry , vol.22 , Issue.1 , pp. 178-185
    • Pangburn, M.K.1    Muller, E.H.J.2
  • 45
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-Pdb-Viewer. An environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 46
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar, S., and Nussinov, R. (2002) Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys. J. 83, 1595-1612 (Pubitemid 34977731)
    • (2002) Biophysical Journal , vol.83 , Issue.3 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 47
    • 70450224038 scopus 로고    scopus 로고
    • ESBRI. A web server for evaluating salt bridges in proteins
    • Costantini, S., Colonna, G., and Facchiano, A. M. (2008) ESBRI. A web server for evaluating salt bridges in proteins. Bioinformation 3, 137-138
    • (2008) Bioinformation , vol.3 , pp. 137-138
    • Costantini, S.1    Colonna, G.2    Facchiano, A.M.3
  • 48
    • 77956944504 scopus 로고    scopus 로고
    • Significance of the pH-induced conformational changes in the structure of C-reactive protein measured by dual polarization interferometry
    • Sheu, B. C., Lin, Y. H., Lin, C. C., Lee, A. S., Chang, W. C., Wu, J. H., Tsai, J. C., and Lin, S. (2010) Significance of the pH-induced conformational changes in the structure of C-reactive protein measured by dual polarization interferometry. Biosensors Bioelectron. 26, 822-827
    • (2010) Biosensors Bioelectron. , vol.26 , pp. 822-827
    • Sheu, B.C.1    Lin, Y.H.2    Lin, C.C.3    Lee, A.S.4    Chang, W.C.5    Wu, J.H.6    Tsai, J.C.7    Lin, S.8
  • 49
    • 0023750573 scopus 로고
    • Modulation of stimulus-dependent human platelet activation by C-reactive protein modified with active oxygen species
    • Miyazawa, K., Kiyono, S., and Inoue, K. (1988) Modulation of stimulus-dependent human platelet activation by C-reactive protein modified with active oxygen species. J. Immunol. 141, 570-574
    • (1988) J. Immunol. , vol.141 , pp. 570-574
    • Miyazawa, K.1    Kiyono, S.2    Inoue, K.3
  • 52
    • 49649112131 scopus 로고    scopus 로고
    • Plant immunity requires conformational changes of NPR1 via S-nitrosylation and thioredoxins
    • Tada, Y., Spoel, S. H., Pajerowska-Mukhtar, K., Mou, Z., Song, J., Wang, C., Zuo, J., and Dong, X. (2008) Plant immunity requires conformational changes of NPR1 via S-nitrosylation and thioredoxins. Science 321, 952-956
    • (2008) Science , vol.321 , pp. 952-956
    • Tada, Y.1    Spoel, S.H.2    Pajerowska-Mukhtar, K.3    Mou, Z.4    Song, J.5    Wang, C.6    Zuo, J.7    Dong, X.8
  • 53
    • 0021274453 scopus 로고
    • C-reactive protein inhibits pneumococcal activation of the alternative pathway by increasing the interaction between factor H and C3b
    • Mold, C., Kingzette, M., and Gewurz, H. (1984) C-reactive protein inhibits pneumococcal activation of the alternative pathway by increasing the interaction between factor H and C3b. J. Immunol. 133, 882-885 (Pubitemid 14093484)
    • (1984) Journal of Immunology , vol.133 , Issue.2 , pp. 882-885
    • Mold, C.1    Kingzette, M.2    Gewurz, H.3
  • 54
    • 0033214998 scopus 로고    scopus 로고
    • Regulation of complement activation by C-reactive protein: Targeting the complement inhibitory activity of factor H by an interaction with short consensus repeat domains 7 and 8-11
    • Jarva, H., Jokiranta, T. S., Hellwage, J., Zipfel, P. F., and Meri, S. (1999) Regulation of complement activation by C-reactive protein. Targeting the complement inhibitory activity of factor H by an interaction with short consensus repeat domains 7 and 8-11. J. Immunol. 163, 3957-3962 (Pubitemid 29450924)
    • (1999) Journal of Immunology , vol.163 , Issue.7 , pp. 3957-3962
    • Jarva, H.1    Jokiranta, T.S.2    Hellwage, J.3    Zipfel, P.F.4    Meri, S.5
  • 55
    • 34249740145 scopus 로고    scopus 로고
    • The factor H variant associated with age-related macular degeneration (His-384) and the non-disease-associated form bind differentially to C-reactive protein, fibromodulin, DNA, and necrotic cells
    • DOI 10.1074/jbc.M610256200
    • Sjöberg, A. P., Trouw, L. A., Clark, S. J., Sjölander, J., Heinegård, D., Sim, R. B., Day, A. J., and Blom, A. M. (2007) The factor H variant associated with age-related macular degeneration (His-384) and the non-disease-associated form bind differentially to C-reactive protein, fibromodulin, DNA, and necrotic cells. J. Biol. Chem. 282, 10894-10900 (Pubitemid 47100772)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 10894-10900
    • Sjoberg, A.P.1    Trouw, L.A.2    Clark, S.J.3    Sjolander, J.4    Heinegard, D.5    Sim, R.B.6    Day, A.J.7    Blom, A.M.8
  • 57
    • 33846216867 scopus 로고    scopus 로고
    • Human C-reactive protein protects mice from Streptococcus pneumoniae infection without binding to pneumococcal C-polysaccharide
    • Suresh, M. V., Singh, S. K., Ferguson, D. A., Jr., and Agrawal, A. (2007) Human C-reactive protein protects mice from Streptococcus pneumoniae infection without binding to pneumococcal C-polysaccharide. J. Immunol. 178, 1158-1163 (Pubitemid 46095189)
    • (2007) Journal of Immunology , vol.178 , Issue.2 , pp. 1158-1163
    • Suresh, M.V.1    Singh, S.K.2    Ferguson Jr., D.A.3    Agrawal, A.4
  • 58
    • 58249084716 scopus 로고    scopus 로고
    • The protective function of human C-reactive protein in mouse models of Streptococcus pneumoniae infection
    • Agrawal, A., Suresh, M. V., Singh, S. K., and Ferguson, D. A., Jr. (2008) The protective function of human C-reactive protein in mouse models of Streptococcus pneumoniae infection. Endocr. Metab. Immune Disord. Drug Targets 8, 231-237
    • (2008) Endocr. Metab. Immune Disord. Drug Targets , vol.8 , pp. 231-237
    • Agrawal, A.1    Suresh, M.V.2    Singh, S.K.3    Ferguson Jr., D.A.4
  • 59
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 60
    • 31044446853 scopus 로고    scopus 로고
    • Prevention and reversal of nephritis in MRL/lpr mice with a single injection of C-reactive protein
    • DOI 10.1002/art.21556
    • Rodriguez, W., Mold, C., Marnell, L. L., Hutt, J., Silverman, G. J., Tran, D., and Du Clos, T. W. (2006) Prevention and reversal of nephritis in MRL/lpr mice with a single injection of C-reactive protein. Arthritis Rheum. 54, 325-335 (Pubitemid 43122216)
    • (2006) Arthritis and Rheumatism , vol.54 , Issue.1 , pp. 325-335
    • Rodriguez, W.1    Mold, C.2    Marnell, L.L.3    Hutt, J.4    Silverman, G.J.5    Tran, D.6    Du, C.T.W.7
  • 61
    • 74849100946 scopus 로고    scopus 로고
    • Lack of effect of a single injection of human C-reactive protein on murine lupus or nephrotoxic nephritis
    • Carlucci, F., Cook, H. T., Garg, A., Pepys, M. B., and Botto, M. (2010) Lack of effect of a single injection of human C-reactive protein on murine lupus or nephrotoxic nephritis. Arthritis Rheum. 62, 245-249
    • (2010) Arthritis Rheum. , vol.62 , pp. 245-249
    • Carlucci, F.1    Cook, H.T.2    Garg, A.3    Pepys, M.B.4    Botto, M.5
  • 63
    • 57149110049 scopus 로고    scopus 로고
    • C-reactive protein and systemic lupus erythematosus
    • Gaitonde, S., Samols, D., and Kushner, I. (2008) C-reactive protein and systemic lupus erythematosus. Arthritis Rheum. 59, 1814-1820
    • (2008) Arthritis Rheum. , vol.59 , pp. 1814-1820
    • Gaitonde, S.1    Samols, D.2    Kushner, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.