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Volumn 67, Issue 2, 2013, Pages 645-656

Computational Analysis of C-Reactive Protein for Assessment of Molecular Dynamics and Interaction Properties

Author keywords

Autoimmune and cardiovascular disease; C reactive protein (CRP); In silico analysis; Interaction properties; Molecular dynamics

Indexed keywords

C REACTIVE PROTEIN; DISULFIDE; SOLVENT;

EID: 84886599612     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-013-9553-4     Document Type: Article
Times cited : (10)

References (85)
  • 3
    • 0017872572 scopus 로고
    • Analogues in other mammals and in fish of human plasma proteins C-reactive protein and amyloid P component
    • Pepys, M. B., Dash, A. C., Fletcher, T. C., Richardson, N., Munn, E. A., et al. (1978). Analogues in other mammals and in fish of human plasma proteins C-reactive protein and amyloid P component. Nature, 273, 168-177.
    • (1978) Nature , vol.273 , pp. 168-177
    • Pepys, M.B.1    Dash, A.C.2    Fletcher, T.C.3    Richardson, N.4    Munn, E.A.5
  • 4
    • 31444437678 scopus 로고    scopus 로고
    • What does minor elevation of C-reactive protein signify?
    • Kushner, I., Rzewnicki, D., & Samols, D. (2006). What does minor elevation of C-reactive protein signify? American Journal of Medicine, 119(166), e17-e28.
    • (2006) American Journal of Medicine , vol.119 , Issue.166
    • Kushner, I.1    Rzewnicki, D.2    Samols, D.3
  • 7
    • 0033081409 scopus 로고    scopus 로고
    • The physiological structure of human C-reactive protein and its complex with phosphocholine
    • Thompson, D., Pepys, M. B., & Wood, S. P. (1999). The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure, 7, 169-177.
    • (1999) Structure , vol.7 , pp. 169-177
    • Thompson, D.1    Pepys, M.B.2    Wood, S.P.3
  • 9
    • 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., & 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. Clinica Chimica Acta, 409, 143-144.
    • (2009) Clinica Chimica Acta , vol.409 , pp. 143-144
    • Singh, S.K.1    Hammond Jr., D.J.2    Beeler, B.W.3    Agrawal, A.4
  • 12
    • 0023273456 scopus 로고
    • Expression, detection and assay of a neoantigen (Neo-CRP) associated with a free, human C-reactive protein subunit
    • Potempa, L. A., Siegel, J. N., Fiedel, B. A., Potempa, R. T., & Gewurz, H. (1987). Expression, detection and assay of a neoantigen (Neo-CRP) associated with a free, human C-reactive protein subunit. Molecular Immunology, 24, 531-541.
    • (1987) Molecular Immunology , vol.24 , pp. 531-541
    • Potempa, L.A.1    Siegel, J.N.2    Fiedel, B.A.3    Potempa, R.T.4    Gewurz, H.5
  • 13
    • 2142698581 scopus 로고    scopus 로고
    • C-reactive protein, structure affects function
    • Verma, S., Szmitko, P. E., & Yeh, E. T. (2004). C-reactive protein, structure affects function. Circulation, 109, 1914-1917.
    • (2004) Circulation , vol.109 , pp. 1914-1917
    • Verma, S.1    Szmitko, P.E.2    Yeh, E.T.3
  • 14
    • 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
    • Ji, S. R., Wu, Y., Potempa, L. A., Qiu, Q., & Zhao, J. (2006). Interactions of C-reactive protein with low-density lipoproteins, implications for an active role of modified C-reactive protein in atherosclerosis. International Journal of Biochemistry & Cell Biology, 38, 648-661.
    • (2006) International Journal of Biochemistry & Cell Biology , vol.38 , pp. 648-661
    • Ji, S.R.1    Wu, Y.2    Potempa, L.A.3    Qiu, Q.4    Zhao, J.5
  • 15
    • 33846001313 scopus 로고    scopus 로고
    • Cell membranes and liposomes dissociate C-reactive protein (CRP) to form a new, biologically active structural intermediate, mCRP(m)
    • Ji, S. R., Wu, Y., Zhu, L., Potempa, L. A., Sheng, F. L., et al. (2007). Cell membranes and liposomes dissociate C-reactive protein (CRP) to form a new, biologically active structural intermediate, mCRP(m). Journal of Federation of American Societies for Experimental Biology, 21, 284-294.
    • (2007) Journal of Federation of American Societies for Experimental Biology , vol.21 , pp. 284-294
    • Ji, S.R.1    Wu, Y.2    Zhu, L.3    Potempa, L.A.4    Sheng, F.L.5
  • 16
    • 67249137343 scopus 로고    scopus 로고
    • Regulation of cell function by isoforms of C-reactive protein, a comparative analysis
    • Boncler, M., & Watała, C. (2009). Regulation of cell function by isoforms of C-reactive protein, a comparative analysis. Acta Biochimica Polonica, 56, 17-31.
    • (2009) Acta Biochimica Polonica , vol.56 , pp. 17-31
    • Boncler, M.1    Watała, C.2
  • 17
    • 68049112204 scopus 로고    scopus 로고
    • Dissociation of pentameric to monomeric C-reactive protein on activated platelets localizes inflammation to atherosclerotic plaques
    • Eisenhardt, S. U., Habersberger, J., Murphy, A., Chen, Y. C., Woollard, K. J., et al. (2009). Dissociation of pentameric to monomeric C-reactive protein on activated platelets localizes inflammation to atherosclerotic plaques. Circulation Research, 105, 128-137.
    • (2009) Circulation Research , vol.105 , pp. 128-137
    • Eisenhardt, S.U.1    Habersberger, J.2    Murphy, A.3    Chen, Y.C.4    Woollard, K.J.5
  • 18
    • 33646366683 scopus 로고    scopus 로고
    • Targeting C-reactive protein for the treatment of cardiovascular disease
    • Pepys, M. B., Hirschfield, G. M., Tennent, G. A., Gallimore, J. R., Kahan, M. C., et al. (2006). Targeting C-reactive protein for the treatment of cardiovascular disease. Nature, 440, 1217-1221.
    • (2006) Nature , vol.440 , pp. 1217-1221
    • Pepys, M.B.1    Hirschfield, G.M.2    Tennent, G.A.3    Gallimore, J.R.4    Kahan, M.C.5
  • 21
    • 81755166541 scopus 로고    scopus 로고
    • Protein amino acid composition, a genomic signature of encephalization in mammals
    • Gutierrez, H., Castillo, A., Monzon, J., & Urrutia, A. O. (2011). Protein amino acid composition, a genomic signature of encephalization in mammals. PLoS ONE, 6, e27261.
    • (2011) PLoS ONE , vol.6
    • Gutierrez, H.1    Castillo, A.2    Monzon, J.3    Urrutia, A.O.4
  • 23
    • 14644442348 scopus 로고    scopus 로고
    • Disulfide bonds, their stereospecific environment and conservation in protein structures
    • Bhattacharyya, R., Pal, D., & Chakrabarti, P. (2004). Disulfide bonds, their stereospecific environment and conservation in protein structures. Protein Engineering, Design & Selection, 17, 795-808.
    • (2004) Protein Engineering, Design & Selection , vol.17 , pp. 795-808
    • Bhattacharyya, R.1    Pal, D.2    Chakrabarti, P.3
  • 24
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg, P. J. (2003). Disulfide bonds as switches for protein function. Trends in Biochemical Sciences, 28, 210-214.
    • (2003) Trends in Biochemical Sciences , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 25
    • 0000497918 scopus 로고    scopus 로고
    • Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A
    • Klink, T. A., Woycechowsky, K. J., Taylor, K. M., & Raines, R. T. (2000). Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A. European Journal of Biochemistry, 267, 566-572.
    • (2000) European Journal of Biochemistry , vol.267 , pp. 566-572
    • Klink, T.A.1    Woycechowsky, K.J.2    Taylor, K.M.3    Raines, R.T.4
  • 26
    • 34547692957 scopus 로고    scopus 로고
    • Cysteine-cysteine contact preference leads to target-focusing in protein folding
    • Sardiu, M. E., Cheung, M. S., & Yi-Kuo, Y. (2007). Cysteine-cysteine contact preference leads to target-focusing in protein folding. Journal of Biophysics, 93, 938-951.
    • (2007) Journal of Biophysics , vol.93 , pp. 938-951
    • Sardiu, M.E.1    Cheung, M.S.2    Yi-Kuo, Y.3
  • 28
    • 33847076452 scopus 로고    scopus 로고
    • Contact patterns between helices and strands of sheet define protein folding patterns
    • Kamat, A. P., & Lesk, A. M. (2007). Contact patterns between helices and strands of sheet define protein folding patterns. Proteins, 66, 869-876.
    • (2007) Proteins , vol.66 , pp. 869-876
    • Kamat, A.P.1    Lesk, A.M.2
  • 29
    • 79951538322 scopus 로고    scopus 로고
    • Learning probabilistic models of hydrogen bond stability from molecular dynamics simulation trajectories
    • Chikalov, I., Yao, P., Moshkov, M., & Latombe, J. C. (2011). Learning probabilistic models of hydrogen bond stability from molecular dynamics simulation trajectories. BMC Bioinformatics, 12(Suppl 1), S34.
    • (2011) BMC Bioinformatics , vol.12 , Issue.SUPPL. 1
    • Chikalov, I.1    Yao, P.2    Moshkov, M.3    Latombe, J.C.4
  • 30
    • 40749144489 scopus 로고    scopus 로고
    • The contrasting properties of conservation and correlated phylogeny in protein functional residue prediction
    • Manning, J. R., Jefferson, E. R., & Barton, G. J. (2008). The contrasting properties of conservation and correlated phylogeny in protein functional residue prediction. BMC Bioinformatics, 9, 51.
    • (2008) BMC Bioinformatics , vol.9 , pp. 51
    • Manning, J.R.1    Jefferson, E.R.2    Barton, G.J.3
  • 31
    • 79952142750 scopus 로고    scopus 로고
    • Exploring the evolutionary relationship of insulin receptor substrate family using computational biology
    • Chakraborty, C., Agoramoorthy, G., & Hsu, M. J. (2011). Exploring the evolutionary relationship of insulin receptor substrate family using computational biology. PLoS ONE, 6, e16580.
    • (2011) PLoS ONE , vol.6
    • Chakraborty, C.1    Agoramoorthy, G.2    Hsu, M.J.3
  • 32
    • 37549002450 scopus 로고    scopus 로고
    • Identification of transient hub proteins and the possible structural basis for their multiple interactions
    • Higurashi, M., Ishida, T., & Kinoshita, K. (2008). Identification of transient hub proteins and the possible structural basis for their multiple interactions. Protein Science, 17, 72-78.
    • (2008) Protein Science , vol.17 , pp. 72-78
    • Higurashi, M.1    Ishida, T.2    Kinoshita, K.3
  • 33
    • 79551649916 scopus 로고    scopus 로고
    • Landscape mapping of functional proteins in insulin signal transduction and insulin resistance, a network-based protein-protein interaction analysis
    • Chakraborty, C., Roy, S. S., Hsu, M. J., & Agoramoorthy, G. (2011). Landscape mapping of functional proteins in insulin signal transduction and insulin resistance, a network-based protein-protein interaction analysis. PLoS ONE, 6, e16388.
    • (2011) PLoS ONE , vol.6
    • Chakraborty, C.1    Roy, S.S.2    Hsu, M.J.3    Agoramoorthy, G.4
  • 34
    • 0018588511 scopus 로고
    • Stability of proteins, small globular proteins
    • Privalov, P. L. (1979). Stability of proteins, small globular proteins. Advances in Protein Chemistry, 33, 167-241.
    • (1979) Advances in Protein Chemistry , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 36
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990). Dominant forces in protein folding. Biochemistry, 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 37
    • 0025191376 scopus 로고
    • Charge effects on folded and unfolded proteins
    • Stigter, D., & Dill, K. A. (1990). Charge effects on folded and unfolded proteins. Biochemistry, 29, 1262-1271.
    • (1990) Biochemistry , vol.29 , pp. 1262-1271
    • Stigter, D.1    Dill, K.A.2
  • 38
    • 84855822854 scopus 로고    scopus 로고
    • The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density
    • Andjelković, U., Theisgen, S., Scheidt, H. A., Petković, M., Huster, D., et al. (2012). The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. Biochimie, 94, 510-515.
    • (2012) Biochimie , vol.94 , pp. 510-515
    • Andjelković, U.1    Theisgen, S.2    Scheidt, H.A.3    Petković, M.4    Huster, D.5
  • 40
    • 0031551577 scopus 로고    scopus 로고
    • Stabilization centers in proteins, identification, characterization and predictions
    • Dosztányi, Z., Fiser, A., & Simon, I. (1997). Stabilization centers in proteins, identification, characterization and predictions. Journal of Molecular Cell Biology, 272, 597-612.
    • (1997) Journal of Molecular Cell Biology , vol.272 , pp. 597-612
    • Dosztányi, Z.1    Fiser, A.2    Simon, I.3
  • 41
    • 0030777760 scopus 로고    scopus 로고
    • Predicting protein stability changes upon mutation using database-derived potentials, solvent accessibility determines the importance of local versus non-local interactions along the sequence
    • Gilis, D., & Rooman, M. (1997). Predicting protein stability changes upon mutation using database-derived potentials, solvent accessibility determines the importance of local versus non-local interactions along the sequence. Journal of Molecular Cell Biology, 272, 276-290.
    • (1997) Journal of Molecular Cell Biology , vol.272 , pp. 276-290
    • Gilis, D.1    Rooman, M.2
  • 45
  • 46
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum, summaries and analyses of PDB structures
    • Laskowski, R. A. (2001). PDBsum, summaries and analyses of PDB structures. Nucleic Acids Research, 29, 221-222.
    • (2001) Nucleic Acids Research , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 47
    • 13444254300 scopus 로고    scopus 로고
    • PDBsum more, new summaries and analyses of the known 3D structures of proteins and nucleic acids
    • Laskowski, R. A., Chistyakov, V. V., & Thornton, J. M. (2005). PDBsum more, new summaries and analyses of the known 3D structures of proteins and nucleic acids. Nucleic Acids Research, 33, D266-D268.
    • (2005) Nucleic Acids Research , vol.33
    • Laskowski, R.A.1    Chistyakov, V.V.2    Thornton, J.M.3
  • 49
    • 0025119856 scopus 로고
    • HERA, a program to draw schematic diagrams of protein secondary structures
    • Hutchinson, E. G., & Thornton, J. M. (1990). HERA, a program to draw schematic diagrams of protein secondary structures. Proteins, 8, 203-212.
    • (1990) Proteins , vol.8 , pp. 203-212
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 50
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010, calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., & Ben-Tal, N. (2010). ConSurf 2010, calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Research, 38, W529-W533.
    • (2010) Nucleic Acids Research , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 51
    • 0024278357 scopus 로고
    • Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds
    • Roseman, M. A. (1988). Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds. Journal of Molecular Biology, 200, 513-522.
    • (1988) Journal of Molecular Biology , vol.200 , pp. 513-522
    • Roseman, M.A.1
  • 52
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis (HCA), current status and perspectives
    • Callebaut, I., Labesse, G., Durand, P., Poupon, A., Canard, L., et al. (1997). Deciphering protein sequence information through hydrophobic cluster analysis (HCA), current status and perspectives. Cellular and Molecular Life Sciences, 53, 621-645.
    • (1997) Cellular and Molecular Life Sciences , vol.53 , pp. 621-645
    • Callebaut, I.1    Labesse, G.2    Durand, P.3    Poupon, A.4    Canard, L.5
  • 53
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms, Lysozyme and insulin
    • Shrake, A., & Rupley, J. A. (1973). Environment and exposure to solvent of protein atoms, Lysozyme and insulin. Journal of Molecular Biology, 79, 351-371.
    • (1973) Journal of Molecular Biology , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 54
    • 2942522721 scopus 로고    scopus 로고
    • ASAView, database and tool for solvent accessibility representation in proteins
    • Ahmad, S., Gromiha, M., Fawareh, H., & Sarai, A. (2004). ASAView, database and tool for solvent accessibility representation in proteins. BMC Bioinformatics, 5, 51.
    • (2004) BMC Bioinformatics , vol.5 , pp. 51
    • Ahmad, S.1    Gromiha, M.2    Fawareh, H.3    Sarai, A.4
  • 55
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf, identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser, F., Pupko, T., Paz, I., Bell, R. E., Bechor-Shental, D., et al. (2003). ConSurf, identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics, 19, 163-164.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5
  • 56
    • 0037620640 scopus 로고    scopus 로고
    • SCide, identification of stabilization centers in proteins
    • Dosztányi, Z. S., Magyar, C. S., Tusnády, G. E., & Simon, I. (2003). SCide, identification of stabilization centers in proteins. Bioinformatics, 19, 899-900.
    • (2003) Bioinformatics , vol.19 , pp. 899-900
    • Dosztányi, Z.S.1    Magyar, C.S.2    Tusnády, G.E.3    Simon, I.4
  • 58
    • 1842532028 scopus 로고    scopus 로고
    • Locating the stabilizing residues in (alpha/beta)8 barrel proteins based on hydrophobicity, long-range interactions, and sequence conservation
    • Gromiha, M. M., Pujadas, G., Magyar, C., Selvaraj, S., & Simon, I. (2004). Locating the stabilizing residues in (alpha/beta)8 barrel proteins based on hydrophobicity, long-range interactions, and sequence conservation. Proteins, 55, 316-329.
    • (2004) Proteins , vol.55 , pp. 316-329
    • Gromiha, M.M.1    Pujadas, G.2    Magyar, C.3    Selvaraj, S.4    Simon, I.5
  • 61
    • 84859991791 scopus 로고    scopus 로고
    • Ligand-specific roles for transmembrane 5 serine residues in the binding and efficacy of dopamine D(1) receptor catechol agonists
    • Chemel, B. R., Bonner, L. A., Watts, V. J., & Nichols, D. E. (2012). Ligand-specific roles for transmembrane 5 serine residues in the binding and efficacy of dopamine D(1) receptor catechol agonists. Molecular Pharmacology, 81, 729-738.
    • (2012) Molecular Pharmacology , vol.81 , pp. 729-738
    • Chemel, B.R.1    Bonner, L.A.2    Watts, V.J.3    Nichols, D.E.4
  • 63
    • 81455154646 scopus 로고    scopus 로고
    • Conserved domains, conserved residues, and surface cavities of C-reactive protein (CRP)
    • Kumar, S. V., Ravunny, R. K., & Chakraborty, C. (2011). Conserved domains, conserved residues, and surface cavities of C-reactive protein (CRP). Applied Biochemistry and Biotechnology, 165, 497-505.
    • (2011) Applied Biochemistry and Biotechnology , vol.165 , pp. 497-505
    • Kumar, S.V.1    Ravunny, R.K.2    Chakraborty, C.3
  • 64
    • 0037174929 scopus 로고    scopus 로고
    • Loss of pentameric symmetry of C-reactive protein is associated with delayed apoptosis of human neutrophils
    • Khreiss, T., Jozsef, L., Hossain, S., Chan, J. S., Potempa, L. A., et al. (2002). Loss of pentameric symmetry of C-reactive protein is associated with delayed apoptosis of human neutrophils. The Journal of Biological Chemistry, 277, 40775-40781.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 40775-40781
    • Khreiss, T.1    Jozsef, L.2    Hossain, S.3    Chan, J.S.4    Potempa, L.A.5
  • 65
    • 0028144369 scopus 로고
    • Structure of pentameric human serum amyloid P component
    • Emsley, J., White, H. E., O'Hara, B. P., Oliva, G., Srinivasan, N., et al. (1994). Structure of pentameric human serum amyloid P component. Nature, 367, 338-345.
    • (1994) Nature , vol.367 , pp. 338-345
    • Emsley, J.1    White, H.E.2    O'Hara, B.P.3    Oliva, G.4    Srinivasan, N.5
  • 66
    • 77956022419 scopus 로고    scopus 로고
    • Enthalpically driven peptide stabilization by protective osmolytes
    • Politi, R., & Harries, D. (2010). Enthalpically driven peptide stabilization by protective osmolytes. Chemical Communications (Cambridge, England), 46, 6449-6451.
    • (2010) Chemical Communications (Cambridge, England) , vol.46 , pp. 6449-6451
    • Politi, R.1    Harries, D.2
  • 67
    • 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., et al. (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
  • 68
    • 80755150222 scopus 로고    scopus 로고
    • Unraveling the molecular mechanism of enthalpy driven peptide folding by polyol osmolytes
    • Politi, R., & Harries, D. (2011). Unraveling the molecular mechanism of enthalpy driven peptide folding by polyol osmolytes. Journal of Chemical Theory and Computation, 7, 3816-3828.
    • (2011) Journal of Chemical Theory and Computation , vol.7 , pp. 3816-3828
    • Politi, R.1    Harries, D.2
  • 69
    • 77949743743 scopus 로고    scopus 로고
    • Atomic analysis of protein-protein interfaces with known inhibitors, the 2P2I database
    • Bourgeas, R., Basse, M.-J., Morelli, X., & Roche, P. (2010). Atomic analysis of protein-protein interfaces with known inhibitors, the 2P2I database. PLoS ONE, 5, e9598.
    • (2010) PLoS ONE , vol.5
    • Bourgeas, R.1    Basse, M.-J.2    Morelli, X.3    Roche, P.4
  • 70
    • 0030057864 scopus 로고    scopus 로고
    • What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
    • Munson, M., Balasubramanian, S., Fleming, K. G., Nagi, A. D., O'Brien, R., et al. (1996). What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Science, 5, 1584-1593.
    • (1996) Protein Science , vol.5 , pp. 1584-1593
    • Munson, M.1    Balasubramanian, S.2    Fleming, K.G.3    Nagi, A.D.4    O'Brien, R.5
  • 71
    • 0028929556 scopus 로고
    • Principles of protein folding, a perspective from simple exact models
    • Dill, K. A., Bromberg, S., Yue, K., Fiebig, K. M., Yee, D. P., et al. (1995). Principles of protein folding, a perspective from simple exact models. Protein Science, 4, 561-602.
    • (1995) Protein Science , vol.4 , pp. 561-602
    • Dill, K.A.1    Bromberg, S.2    Yue, K.3    Fiebig, K.M.4    Yee, D.P.5
  • 74
    • 0037105627 scopus 로고    scopus 로고
    • A C-reactive protein mutant that does not bind to phosphocholine and pneumococcal C-polysaccharide
    • Agrawal, A., Simpson, M. J., Black, S., Carey, M. P., & Samols, D. (2002). A C-reactive protein mutant that does not bind to phosphocholine and pneumococcal C-polysaccharide. Journal of Immunology, 169, 3217-3222.
    • (2002) Journal of Immunology , vol.169 , pp. 3217-3222
    • Agrawal, A.1    Simpson, M.J.2    Black, S.3    Carey, M.P.4    Samols, D.5
  • 75
    • 0038394552 scopus 로고    scopus 로고
    • The phosphocholine and the polycation-binding sites on rabbit C-reactive protein are structurally and functionally distinct
    • Black, S., Agrawal, A., & Samols, D. (2003). The phosphocholine and the polycation-binding sites on rabbit C-reactive protein are structurally and functionally distinct. Molecular Immunology, 39, 1045-1054.
    • (2003) Molecular Immunology , vol.39 , pp. 1045-1054
    • Black, S.1    Agrawal, A.2    Samols, D.3
  • 76
    • 21644479304 scopus 로고    scopus 로고
    • Analysis of binding sites in human C-reactive protein for Fc{gamma}RI, Fc{gamma}RIIA, and C1q by site-directed mutagenesis
    • Bang, R., Marnell, L., Mold, C., Stein, M. P., Clos, K. T., et al. (2005). Analysis of binding sites in human C-reactive protein for Fc{gamma}RI, Fc{gamma}RIIA, and C1q by site-directed mutagenesis. The Journal of Biological Chemistry, 280, 25095-25102.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 25095-25102
    • Bang, R.1    Marnell, L.2    Mold, C.3    Stein, M.P.4    Clos, K.T.5
  • 77
    • 0029829219 scopus 로고    scopus 로고
    • Identification of a C-reactive protein binding site in two hepatic carboxylesterases capable of retaining C-reactive protein within the endoplasmic reticulum
    • Yue, C. C., Muller-Greven, J., Dailey, P., Lozanski, G., Anderson, V., & Macintyre, S. (1996). Identification of a C-reactive protein binding site in two hepatic carboxylesterases capable of retaining C-reactive protein within the endoplasmic reticulum. The Journal of Biological Chemistry, 271, 22245-22250.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 22245-22250
    • Yue, C.C.1    Muller-Greven, J.2    Dailey, P.3    Lozanski, G.4    Anderson, V.5    Macintyre, S.6
  • 79
    • 0344012497 scopus 로고    scopus 로고
    • The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties
    • Gaboriaud, C., Juanhuix, J., Gruez, A., Lacroix, M., & Darnault, C. (2003). The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. The Journal of Biological Chemistry, 278, 46974-46982.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 46974-46982
    • Gaboriaud, C.1    Juanhuix, J.2    Gruez, A.3    Lacroix, M.4    Darnault, C.5
  • 81
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V. I., Gutin, A. M., & Shakhnovich, E. I. (1995). Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. The Journal of Biological Chemistry, 252, 460-471.
    • (1995) The Journal of Biological Chemistry , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 82
    • 0030596063 scopus 로고    scopus 로고
    • How to drive a protein folding potential? A new approach to an old problem
    • Mirny, L. A., & Shakhnovich, E. (1996). How to drive a protein folding potential? A new approach to an old problem. The Journal of Biological Chemistry, 264, 1164-1179.
    • (1996) The Journal of Biological Chemistry , vol.264 , pp. 1164-1179
    • Mirny, L.A.1    Shakhnovich, E.2
  • 83
    • 0031566950 scopus 로고    scopus 로고
    • Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation
    • Bahar, I., & Jernigan, R. L. (1997). Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation. The Journal of Biological Chemistry, 266, 195-214.
    • (1997) The Journal of Biological Chemistry , vol.266 , pp. 195-214
    • Bahar, I.1    Jernigan, R.L.2
  • 84
    • 0031551577 scopus 로고    scopus 로고
    • Stabilization centers in proteins, identification, characterization and predictions
    • Dosztányi, Z., Fiser, A., & Simon, I. (1997). Stabilization centers in proteins, identification, characterization and predictions. The Journal of Biological Chemistry, 272, 597-612.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 597-612
    • Dosztányi, Z.1    Fiser, A.2    Simon, I.3


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