메뉴 건너뛰기




Volumn 345, Issue 2, 2006, Pages 886-893

Femtosecond dynamics of proteoheparan sulfate (HS-PG) after UV excitation-A readout for arteriosclerotic nanoplaque formation?

Author keywords

Arteriosclerotic plaque; Atherogenesis; Heparan sulfate proteoglycan; LDL receptor; Protein conformation and solvation; Transient excited state absorption; Ultrashort laser pulses

Indexed keywords

CALCIUM SALT; PROTEOHEPARAN SULFATE; TRYPTOPHAN;

EID: 33646850225     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.04.164     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 0033016145 scopus 로고    scopus 로고
    • Physicochemical binding properties of the proteoglycan receptor for serum lipoproteins
    • Siegel G., Malmsten M., Klüßendorf D., and Leonhardt W. Physicochemical binding properties of the proteoglycan receptor for serum lipoproteins. Atherosclerosis 144 (1999) 59-67
    • (1999) Atherosclerosis , vol.144 , pp. 59-67
    • Siegel, G.1    Malmsten, M.2    Klüßendorf, D.3    Leonhardt, W.4
  • 2
    • 0038206738 scopus 로고    scopus 로고
    • Reduction of arteriosclerotic nanoplaque formation and size by fluvastatin in a receptor-based biosensor model
    • Siegel G., Abletshauser C., Malmsten M., Schmidt A., and Winkler K. Reduction of arteriosclerotic nanoplaque formation and size by fluvastatin in a receptor-based biosensor model. Cardiovasc. Res. 58 (2003) 696-705
    • (2003) Cardiovasc. Res. , vol.58 , pp. 696-705
    • Siegel, G.1    Abletshauser, C.2    Malmsten, M.3    Schmidt, A.4    Winkler, K.5
  • 3
    • 0035137154 scopus 로고    scopus 로고
    • Tryptophan fluorescence of yeast actin resolved via conserved mutations
    • Doyle T.C., Hansen J.E., and Reisler E. Tryptophan fluorescence of yeast actin resolved via conserved mutations. Biophys. J. 80 (2001) 427-434
    • (2001) Biophys. J. , vol.80 , pp. 427-434
    • Doyle, T.C.1    Hansen, J.E.2    Reisler, E.3
  • 4
    • 17144369178 scopus 로고    scopus 로고
    • Unfolding and refolding of the glutamine-binding protein from Escherichia coli and its complex with glutamine induced by guanidine hydrochloride
    • Staiano M., Scognamiglio V., Rossi M., D'Auria S., Stepanenko O.V., Kuznetsova I.M., and Turoverov K.K. Unfolding and refolding of the glutamine-binding protein from Escherichia coli and its complex with glutamine induced by guanidine hydrochloride. Biochemistry 44 (2005) 5625-5633
    • (2005) Biochemistry , vol.44 , pp. 5625-5633
    • Staiano, M.1    Scognamiglio, V.2    Rossi, M.3    D'Auria, S.4    Stepanenko, O.V.5    Kuznetsova, I.M.6    Turoverov, K.K.7
  • 5
    • 0343851580 scopus 로고    scopus 로고
    • A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data
    • Sillen A., Diaz J.F., and Engelborghs Y. A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data. Protein Sci. 9 (2000) 158-169
    • (2000) Protein Sci. , vol.9 , pp. 158-169
    • Sillen, A.1    Diaz, J.F.2    Engelborghs, Y.3
  • 6
    • 0000567017 scopus 로고    scopus 로고
    • Förster energy transfer from tryptophan to flavin in glucose oxidase enzyme
    • Haouz A., Twist C., Zentz C., de Kersabiec A., Pin S., and Alpert B. Förster energy transfer from tryptophan to flavin in glucose oxidase enzyme. Chem. Phys. Lett. 294 (1998) 197-203
    • (1998) Chem. Phys. Lett. , vol.294 , pp. 197-203
    • Haouz, A.1    Twist, C.2    Zentz, C.3    de Kersabiec, A.4    Pin, S.5    Alpert, B.6
  • 8
    • 0037039412 scopus 로고    scopus 로고
    • Femtosecond dynamics of rubredoxin: tryptophan solvation and resonance energy transfer in the protein
    • Zhong D., Pal S.K., Zhang D., Chan S.I., and Zewail A.H. Femtosecond dynamics of rubredoxin: tryptophan solvation and resonance energy transfer in the protein. Proc. Natl. Acad. Sci. USA 99 (2002) 13-18
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13-18
    • Zhong, D.1    Pal, S.K.2    Zhang, D.3    Chan, S.I.4    Zewail, A.H.5
  • 9
    • 0004154123 scopus 로고
    • Gregory R.B. (Ed), Dekker, New York
    • In: Gregory R.B. (Ed). Protein-Solvent Interactions (1995), Dekker, New York
    • (1995) Protein-Solvent Interactions
  • 10
    • 0026535070 scopus 로고
    • Protein solvation in allosteric regulation: a water effect on hemoglobin
    • Colombo M.F., Rau D.C., and Parsegian V.A. Protein solvation in allosteric regulation: a water effect on hemoglobin. Science 256 (1992) 655-659
    • (1992) Science , vol.256 , pp. 655-659
    • Colombo, M.F.1    Rau, D.C.2    Parsegian, V.A.3
  • 11
    • 0027957222 scopus 로고
    • Distribution function implied dynamics versus residence times and correlations: solvation shells of myoglobin
    • Lounnas V., and Pettitt B.M. Distribution function implied dynamics versus residence times and correlations: solvation shells of myoglobin. Proteins 18 (1994) 148-160
    • (1994) Proteins , vol.18 , pp. 148-160
    • Lounnas, V.1    Pettitt, B.M.2
  • 12
    • 0031338986 scopus 로고    scopus 로고
    • Dielectric relaxation of biological water
    • Nandi N., and Bagchi B. Dielectric relaxation of biological water. J. Phys. Chem. B 101 (1997) 10954-10961
    • (1997) J. Phys. Chem. B , vol.101 , pp. 10954-10961
    • Nandi, N.1    Bagchi, B.2
  • 13
    • 0035913505 scopus 로고    scopus 로고
    • Aqueous solvation dynamics at the anionic surfactant air/water interface
    • Benderskii A.V., and Eisenthal K.B. Aqueous solvation dynamics at the anionic surfactant air/water interface. J. Phys. Chem. B 105 (2001) 6698-6703
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6698-6703
    • Benderskii, A.V.1    Eisenthal, K.B.2
  • 14
    • 0033690126 scopus 로고    scopus 로고
    • Dielectric relaxation and solvation dynamics of water in complex chemical and biological systems
    • Nandi N., Bhattacharyya K., and Bagchi B. Dielectric relaxation and solvation dynamics of water in complex chemical and biological systems. Chem. Rev. 100 (2000) 2013-2046
    • (2000) Chem. Rev. , vol.100 , pp. 2013-2046
    • Nandi, N.1    Bhattacharyya, K.2    Bagchi, B.3
  • 15
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling F.T., Weis W.I., Flaherty K.M., and Brunger A.T. Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science 271 (1996) 72-77
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brunger, A.T.4
  • 16
    • 0031807764 scopus 로고    scopus 로고
    • Diffusion of solvent around biomolecular solutes: a molecular dynamics simulation study
    • Makarov V.A., Feig M., Andrews B.K., and Pettitt M. Diffusion of solvent around biomolecular solutes: a molecular dynamics simulation study. Biophys. J. 75 (1998) 150-158
    • (1998) Biophys. J. , vol.75 , pp. 150-158
    • Makarov, V.A.1    Feig, M.2    Andrews, B.K.3    Pettitt, M.4
  • 17
    • 0025882875 scopus 로고
    • Neutron diffraction study of carbonmonoxymyoglobin
    • Cheng X., and Schoenborn B.P. Neutron diffraction study of carbonmonoxymyoglobin. J. Mol. Biol. 220 (1991) 381-399
    • (1991) J. Mol. Biol. , vol.220 , pp. 381-399
    • Cheng, X.1    Schoenborn, B.P.2
  • 18
    • 0029046396 scopus 로고
    • Molecular dynamics simulation of hydration in myoglobin
    • Gu W., and Schoenborn B.P. Molecular dynamics simulation of hydration in myoglobin. Proteins 22 (1995) 20-26
    • (1995) Proteins , vol.22 , pp. 20-26
    • Gu, W.1    Schoenborn, B.P.2
  • 19
    • 0022438054 scopus 로고
    • Dielectric behavior of water in biological solutions: studies on myoglobin, human low-density lipoprotein, and polyvinylpyrrolidone
    • Grant E.H., McClean V.E.R., Nightingale N.R.V., Sheppard R.J., and Chapman M.J. Dielectric behavior of water in biological solutions: studies on myoglobin, human low-density lipoprotein, and polyvinylpyrrolidone. Bioelectromagnetics 7 (1986) 151-162
    • (1986) Bioelectromagnetics , vol.7 , pp. 151-162
    • Grant, E.H.1    McClean, V.E.R.2    Nightingale, N.R.V.3    Sheppard, R.J.4    Chapman, M.J.5
  • 20
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • Otting G., Lipinsh E., and Wüthrich K. Protein hydration in aqueous solution. Science 254 (1991) 974-980
    • (1991) Science , vol.254 , pp. 974-980
    • Otting, G.1    Lipinsh, E.2    Wüthrich, K.3
  • 21
    • 2342527858 scopus 로고    scopus 로고
    • Dynamics of water in biological recognition
    • Pal S.K., and Zewail A.H. Dynamics of water in biological recognition. Chem. Rev. 104 (2004) 2099-2123
    • (2004) Chem. Rev. , vol.104 , pp. 2099-2123
    • Pal, S.K.1    Zewail, A.H.2
  • 22
    • 0037028161 scopus 로고    scopus 로고
    • Biological water: femtosecond dynamics of macromolecular hydration
    • Pal S.K., Peon J., Bagchi B., and Zewail A.H. Biological water: femtosecond dynamics of macromolecular hydration. J. Phys. Chem. B 106 (2002) 12376-12395
    • (2002) J. Phys. Chem. B , vol.106 , pp. 12376-12395
    • Pal, S.K.1    Peon, J.2    Bagchi, B.3    Zewail, A.H.4
  • 23
    • 0035812107 scopus 로고    scopus 로고
    • Subpicosecond fluorescence spectra of tryptophan in water
    • Shen X., and Knutson J.R. Subpicosecond fluorescence spectra of tryptophan in water. J. Phys. Chem. B 105 (2001) 6260-6265
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6260-6265
    • Shen, X.1    Knutson, J.R.2
  • 24
    • 0033089462 scopus 로고    scopus 로고
    • Femtosecond spectroscopy of condensed phases with chirped supercontinuum probing
    • Kovalenko S.A., Dobryakov A.L., Ruthmann J., and Ernsting N.P. Femtosecond spectroscopy of condensed phases with chirped supercontinuum probing. Phys. Rev. A 59 (1999) 2369-2384
    • (1999) Phys. Rev. A , vol.59 , pp. 2369-2384
    • Kovalenko, S.A.1    Dobryakov, A.L.2    Ruthmann, J.3    Ernsting, N.P.4
  • 25
    • 0000829808 scopus 로고    scopus 로고
    • Femtosecond hole-burning spectroscopy with stimulated emission pumping and supercontinuum probing
    • Kovalenko S.A., Ruthmann J., and Ernsting N.P. Femtosecond hole-burning spectroscopy with stimulated emission pumping and supercontinuum probing. J. Chem. Phys. 109 (1998) 1894-1900
    • (1998) J. Chem. Phys. , vol.109 , pp. 1894-1900
    • Kovalenko, S.A.1    Ruthmann, J.2    Ernsting, N.P.3
  • 26
    • 36449009157 scopus 로고
    • Femtosecond solvation dynamics determining the band shape of stimulated emission from a polar styryl dye
    • Bingemann D., and Ernsting N.P. Femtosecond solvation dynamics determining the band shape of stimulated emission from a polar styryl dye. J. Chem. Phys. 102 (1995) 2691-2700
    • (1995) J. Chem. Phys. , vol.102 , pp. 2691-2700
    • Bingemann, D.1    Ernsting, N.P.2
  • 29
    • 0035849245 scopus 로고    scopus 로고
    • Wave-packet-assisted decomposition of femtosecond transient ultraviolet-visible absorption spectra: application to excited-state intramolecular proton transfer in solution
    • Ernsting N.P., Kovalenko S.A., Senyushkina T., Saam J., and Farztdinov V. Wave-packet-assisted decomposition of femtosecond transient ultraviolet-visible absorption spectra: application to excited-state intramolecular proton transfer in solution. J. Phys. Chem. A 105 (2001) 3443-3453
    • (2001) J. Phys. Chem. A , vol.105 , pp. 3443-3453
    • Ernsting, N.P.1    Kovalenko, S.A.2    Senyushkina, T.3    Saam, J.4    Farztdinov, V.5
  • 30
    • 0030610813 scopus 로고    scopus 로고
    • b transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins
    • b transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 278 (1997) 113-150
    • (1997) Methods Enzymol. , vol.278 , pp. 113-150
    • Callis, P.R.1
  • 31
    • 0036201889 scopus 로고    scopus 로고
    • Femtosecond spectroscopy of p-dimethylaminocyanostilbene in solution-no evidence for dual fluorescence
    • Kovalenko S.A., Schanz R., Senyushkina T.A., and Ernsting N.P. Femtosecond spectroscopy of p-dimethylaminocyanostilbene in solution-no evidence for dual fluorescence. Phys. Chem. Chem. Phys. 4 (2002) 703-707
    • (2002) Phys. Chem. Chem. Phys. , vol.4 , pp. 703-707
    • Kovalenko, S.A.1    Schanz, R.2    Senyushkina, T.A.3    Ernsting, N.P.4
  • 32
    • 0027370063 scopus 로고
    • Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization
    • Koide S., Dyson H.J., and Wright P.E. Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization. Biochemistry 32 (1993) 12299-12310
    • (1993) Biochemistry , vol.32 , pp. 12299-12310
    • Koide, S.1    Dyson, H.J.2    Wright, P.E.3
  • 34
    • 0034669402 scopus 로고    scopus 로고
    • Structure of low density lipoprotein (LDL) particles: basis for understanding molecular changes in modified LDL
    • Hevonoja T., Pentikainen M.O., Hyvonen M.T., Kovanen P.T., and Ala-Korpela M. Structure of low density lipoprotein (LDL) particles: basis for understanding molecular changes in modified LDL. Biochim. Biophys. Acta 1488 (2000) 189-210
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 189-210
    • Hevonoja, T.1    Pentikainen, M.O.2    Hyvonen, M.T.3    Kovanen, P.T.4    Ala-Korpela, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.