메뉴 건너뛰기




Volumn 391, Issue 1, 2009, Pages 39-44

Characterization of Ca2+ and phosphocholine interactions with C-reactive protein using a surface plasmon resonance biosensor

Author keywords

C reactive protein (CRP); Calcium binding; Conformational change; pH dependency; Phosphocholine; SPR biosensor

Indexed keywords

BIOSENSORS; CONFORMATIONS; PLASMONS; PROTEINS;

EID: 67349231433     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.04.037     Document Type: Article
Times cited : (60)

References (33)
  • 1
    • 0034869253 scopus 로고    scopus 로고
    • Human C-reactive protein: expression, structure, and function
    • Volanakis J.E. Human C-reactive protein: expression, structure, and function. Mol. Immunol. 38 (2001) 189-197
    • (2001) Mol. Immunol. , vol.38 , pp. 189-197
    • Volanakis, J.E.1
  • 3
    • 0033081409 scopus 로고    scopus 로고
    • The physiological structure of human C-reactive protein and its complex with phosphocholine
    • Thompson D., Pepys M.B., and Wood S.P. The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure 7 (1999) 169-177
    • (1999) Structure , vol.7 , pp. 169-177
    • Thompson, D.1    Pepys, M.B.2    Wood, S.P.3
  • 5
    • 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., and Feinstein A. Analogues in other mammals and in fish of human plasma proteins, C-reactive protein and amyloid P component. Nature 273 (1978) 168-170
    • (1978) Nature , vol.273 , pp. 168-170
    • Pepys, M.B.1    Dash, A.C.2    Fletcher, T.C.3    Richardson, N.4    Munn, E.A.5    Feinstein, A.6
  • 6
    • 10644271456 scopus 로고    scopus 로고
    • Interaction of calcium-bound C-reactive protein with fibronectin is controlled by pH: in vivo implications
    • Suresh M.V., Singh S.K., and Agrawal A. Interaction of calcium-bound C-reactive protein with fibronectin is controlled by pH: in vivo implications. J. Biol. Chem. 279 (2004) 52552-52557
    • (2004) J. Biol. Chem. , vol.279 , pp. 52552-52557
    • Suresh, M.V.1    Singh, S.K.2    Agrawal, A.3
  • 9
    • 0035584032 scopus 로고    scopus 로고
    • Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance
    • Gestwicki J.E., Hsieh H.V., and Pitner J.B. Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance. Anal. Chem. 73 (2001) 5732-5737
    • (2001) Anal. Chem. , vol.73 , pp. 5732-5737
    • Gestwicki, J.E.1    Hsieh, H.V.2    Pitner, J.B.3
  • 10
    • 0035879403 scopus 로고    scopus 로고
    • Use of surface plasmon resonance for real-time measurements of the global conformational transition in human phenylalanine hydroxylase in response to substrate binding and catalytic activation
    • Flatmark T., Stokka A.J., and Berge S.V. Use of surface plasmon resonance for real-time measurements of the global conformational transition in human phenylalanine hydroxylase in response to substrate binding and catalytic activation. Anal. Biochem. 294 (2001) 95-101
    • (2001) Anal. Biochem. , vol.294 , pp. 95-101
    • Flatmark, T.1    Stokka, A.J.2    Berge, S.V.3
  • 11
    • 8444241450 scopus 로고    scopus 로고
    • Studies of substrate-induced conformational changes in human cytomegalovirus protease using optical biosensor technology
    • Geitmann M., and Danielson U.H. Studies of substrate-induced conformational changes in human cytomegalovirus protease using optical biosensor technology. Anal. Biochem. 332 (2004) 203-214
    • (2004) Anal. Biochem. , vol.332 , pp. 203-214
    • Geitmann, M.1    Danielson, U.H.2
  • 12
    • 0035875951 scopus 로고    scopus 로고
    • Observation of charge state and conformational change in immobilized protein using surface plasmon resonance sensor
    • Mannen T., Yamaguchi S., Honda J., Sugimoto S., Kitayama A., and Nagamune T. Observation of charge state and conformational change in immobilized protein using surface plasmon resonance sensor. Anal. Biochem. 293 (2001) 185-193
    • (2001) Anal. Biochem. , vol.293 , pp. 185-193
    • Mannen, T.1    Yamaguchi, S.2    Honda, J.3    Sugimoto, S.4    Kitayama, A.5    Nagamune, T.6
  • 13
    • 0035125496 scopus 로고    scopus 로고
    • Monitoring of the refolding process for immobilized firefly luciferase with a biosensor based on surface plasmon resonance
    • Zako T., Harada K., Mannen T., Yamaguchi S., Kitayama A., Ueda H., and Nagamune T. Monitoring of the refolding process for immobilized firefly luciferase with a biosensor based on surface plasmon resonance. J. Biochem. 129 (2001) 1-4
    • (2001) J. Biochem. , vol.129 , pp. 1-4
    • Zako, T.1    Harada, K.2    Mannen, T.3    Yamaguchi, S.4    Kitayama, A.5    Ueda, H.6    Nagamune, T.7
  • 15
    • 0031281546 scopus 로고    scopus 로고
    • Avoiding interferences from Good's buffers: a contiguous series of noncomplexing tertiary amine buffers covering the entire range of pH 3-11
    • Yu Q., Kandegedara A., Xu Y., and Rorabacher D.B. Avoiding interferences from Good's buffers: a contiguous series of noncomplexing tertiary amine buffers covering the entire range of pH 3-11. Anal. Biochem. 253 (1997) 50-56
    • (1997) Anal. Biochem. , vol.253 , pp. 50-56
    • Yu, Q.1    Kandegedara, A.2    Xu, Y.3    Rorabacher, D.B.4
  • 16
    • 33748749807 scopus 로고    scopus 로고
    • 2+ interactions with matrix metallopeptidase-12: implications for matrix metallopeptidase regulation
    • 2+ interactions with matrix metallopeptidase-12: implications for matrix metallopeptidase regulation. Biochem. J. 398 (2006) 393-398
    • (2006) Biochem. J. , vol.398 , pp. 393-398
    • Gossas, T.1    Danielson, U.H.2
  • 17
    • 0000102194 scopus 로고
    • Studies on the binding specificity of human C-reactive protein for phosphorylcholine
    • Anderson J.K., Stroud R.M., and Volanakis J.E. Studies on the binding specificity of human C-reactive protein for phosphorylcholine. Fed. Proc. 37 (1978) 1495
    • (1978) Fed. Proc. , vol.37 , pp. 1495
    • Anderson, J.K.1    Stroud, R.M.2    Volanakis, J.E.3
  • 18
    • 0042744797 scopus 로고    scopus 로고
    • C-reactive protein: a critical update
    • Pepys M.B., and Hirschfield G.M. C-reactive protein: a critical update. J. Clin. Invest. 111 (2003) 1805-1812
    • (2003) J. Clin. Invest. , vol.111 , pp. 1805-1812
    • Pepys, M.B.1    Hirschfield, G.M.2
  • 19
    • 0018581616 scopus 로고
    • Interaction of C-reactive protein with artificial phosphatidylcholine bilayers
    • Volanakis J.E., and Wirtz K.W. Interaction of C-reactive protein with artificial phosphatidylcholine bilayers. Nature 281 (1979) 155-157
    • (1979) Nature , vol.281 , pp. 155-157
    • Volanakis, J.E.1    Wirtz, K.W.2
  • 20
    • 0019514869 scopus 로고
    • Interaction of C-reactive protein with liposomes: III. Membrane requirements for binding
    • Mold C., Rodgers C.P., Richards R.L., Alving C.R., and Gewurz H. Interaction of C-reactive protein with liposomes: III. Membrane requirements for binding. J. Immunol. 126 (1981) 856-860
    • (1981) J. Immunol. , vol.126 , pp. 856-860
    • Mold, C.1    Rodgers, C.P.2    Richards, R.L.3    Alving, C.R.4    Gewurz, H.5
  • 21
    • 0020000304 scopus 로고
    • C-reactive protein binding specificities: artificial and natural phospholipid bilayers
    • Narkates A.J., and Volanakis J.E. C-reactive protein binding specificities: artificial and natural phospholipid bilayers. Ann. NY Acad. Sci. 389 (1982) 172-182
    • (1982) Ann. NY Acad. Sci. , vol.389 , pp. 172-182
    • Narkates, A.J.1    Volanakis, J.E.2
  • 22
    • 0032523411 scopus 로고    scopus 로고
    • Detection of conformational changes in an immobilized protein using surface plasmon resonance
    • Sota H., Hasegawa Y., and Iwakura M. Detection of conformational changes in an immobilized protein using surface plasmon resonance. Anal. Chem. 70 (1998) 2019-2024
    • (1998) Anal. Chem. , vol.70 , pp. 2019-2024
    • Sota, H.1    Hasegawa, Y.2    Iwakura, M.3
  • 25
    • 40149084169 scopus 로고    scopus 로고
    • Hypercalcaemic and hypocalcaemic conditions due to calcium-sensing receptor mutations
    • Egbuna O.I., and Brown E.M. Hypercalcaemic and hypocalcaemic conditions due to calcium-sensing receptor mutations. Best Pract. Res. Clin. Rheumatol. 22 (2008) 129-148
    • (2008) Best Pract. Res. Clin. Rheumatol. , vol.22 , pp. 129-148
    • Egbuna, O.I.1    Brown, E.M.2
  • 26
    • 0142200478 scopus 로고    scopus 로고
    • Investigating interactions of the pentraxins serum amyloid P component and C-reactive protein by mass spectrometry
    • Aquilina J.A., and Robinson C.V. Investigating interactions of the pentraxins serum amyloid P component and C-reactive protein by mass spectrometry. Biochem. J. 375 (2003) 323-328
    • (2003) Biochem. J. , vol.375 , pp. 323-328
    • Aquilina, J.A.1    Robinson, C.V.2
  • 28
    • 33745966622 scopus 로고    scopus 로고
    • 2+, and heparin by human serum amyloid P component in affinity capillary electrophoresis
    • 2+, and heparin by human serum amyloid P component in affinity capillary electrophoresis. Electrophoresis 27 (2006) 2609-2615
    • (2006) Electrophoresis , vol.27 , pp. 2609-2615
    • Heegaard, N.H.1    He, X.2    Blomberg, L.G.3
  • 30
    • 0018579560 scopus 로고
    • Determination of manganese in whole blood and serum
    • Pleban P.A., and Pearson K.H. Determination of manganese in whole blood and serum. Clin. Chem. 25 (1979) 1915-1918
    • (1979) Clin. Chem. , vol.25 , pp. 1915-1918
    • Pleban, P.A.1    Pearson, K.H.2
  • 31
    • 0023711081 scopus 로고
    • Determination of copper and zinc in serum and whole blood by ion chromatography
    • Ong C.N., Ong H.Y., and Chua L.H. Determination of copper and zinc in serum and whole blood by ion chromatography. Anal. Biochem. 173 (1988) 64-69
    • (1988) Anal. Biochem. , vol.173 , pp. 64-69
    • Ong, C.N.1    Ong, H.Y.2    Chua, L.H.3
  • 32
    • 67349087734 scopus 로고    scopus 로고
    • Magnesium metabolism in health and disease
    • Musso C.G. Magnesium metabolism in health and disease. Int. Urol. Nephrol. 41 (2009) 357-362
    • (2009) Int. Urol. Nephrol. , vol.41 , pp. 357-362
    • Musso, C.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.