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Volumn 409, Issue 2, 2011, Pages 229-234

Photo-induced inhibition of insulin amyloid fibrillation on online laser measurement

Author keywords

Amyloid fibrillation; Amyloid related disease; Insulin; Laser irradiation; Structural change

Indexed keywords

AMYLOID; INSULIN; SODIUM CHLORIDE; THIOFLAVINE;

EID: 79957920202     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.04.132     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 25444485718 scopus 로고    scopus 로고
    • Protein folding and diseases
    • Lee C., Yu M.H. Protein folding and diseases. J. Biochem. Mol. Biol. 2005, 38:275-280.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 275-280
    • Lee, C.1    Yu, M.H.2
  • 2
    • 34250376918 scopus 로고    scopus 로고
    • Protein misfolding and aggregation
    • Murphy R.M., Kendrick B.S. Protein misfolding and aggregation. Biotechnol. Prog. 2007, 23:548-552.
    • (2007) Biotechnol. Prog. , vol.23 , pp. 548-552
    • Murphy, R.M.1    Kendrick, B.S.2
  • 3
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 2004, 430:631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 4
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson C.M. Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 2004, 15:3-16.
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 5
    • 67349112388 scopus 로고    scopus 로고
    • Common features between diabetes mellitus and Alzheimer's disease
    • Gotz J., Ittner L.M., Lim Y.A. Common features between diabetes mellitus and Alzheimer's disease. Cell. Mol. Life Sci. 2009, 66:1321-1325.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1321-1325
    • Gotz, J.1    Ittner, L.M.2    Lim, Y.A.3
  • 6
    • 0034974704 scopus 로고    scopus 로고
    • Unfolding and conformational distributions during protein precipitation
    • Chang S.T., Tobler S.A., Fernandez E.J. Unfolding and conformational distributions during protein precipitation. Biotechnol. Prog. 2001, 17:583-585.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 583-585
    • Chang, S.T.1    Tobler, S.A.2    Fernandez, E.J.3
  • 7
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • Arora A., Ha C., Park C.B. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett. 2004, 564:121-125.
    • (2004) FEBS Lett. , vol.564 , pp. 121-125
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 8
    • 69249141470 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the flavonoid-induced inhibition of α-synuclein fibrillation
    • Meng X.Y., Munishkina L.A., Fink A.L., Uversky V.N. Molecular mechanisms underlying the flavonoid-induced inhibition of α-synuclein fibrillation. Biochemistry 2009, 48:8206-8224.
    • (2009) Biochemistry , vol.48 , pp. 8206-8224
    • Meng, X.Y.1    Munishkina, L.A.2    Fink, A.L.3    Uversky, V.N.4
  • 11
    • 52449083570 scopus 로고    scopus 로고
    • Cold- and pressure-induced dissociation of protein aggregates and amyloid fibrils
    • Mishra R., Winter R. Cold- and pressure-induced dissociation of protein aggregates and amyloid fibrils. Angew. Chem. Int. Ed. 2008, 47:6518-6521.
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 6518-6521
    • Mishra, R.1    Winter, R.2
  • 12
    • 0033596963 scopus 로고    scopus 로고
    • Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin
    • Smeller L., Rubens P., Heremans K. Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin. Biochemistry 1999, 38:3816-3820.
    • (1999) Biochemistry , vol.38 , pp. 3816-3820
    • Smeller, L.1    Rubens, P.2    Heremans, K.3
  • 13
    • 0032879778 scopus 로고    scopus 로고
    • Analysis of protein structure by solution optical spectroscopy
    • Colon W. Analysis of protein structure by solution optical spectroscopy. Methods Enzymol. 1999, 309:605-632.
    • (1999) Methods Enzymol. , vol.309 , pp. 605-632
    • Colon, W.1
  • 15
    • 77954039898 scopus 로고    scopus 로고
    • Real-time imaging and quantification of amyloid-β peptide aggregates by novel quantum-dot nanoprobes
    • Tokuraku K., Marquardt M., Ikezu T. Real-time imaging and quantification of amyloid-β peptide aggregates by novel quantum-dot nanoprobes. PLoS One 2009, 4:e8492.
    • (2009) PLoS One , vol.4
    • Tokuraku, K.1    Marquardt, M.2    Ikezu, T.3
  • 16
    • 61449135187 scopus 로고    scopus 로고
    • Real-time analysis of amyloid fibril formation of α-synuclein using a fibrillation-state-specific fluorescent probe of JC-1
    • Lee J., Lee I., Choe Y., Kang S., Kim H.Y., Gai W., Hahn J., Paik S.R. Real-time analysis of amyloid fibril formation of α-synuclein using a fibrillation-state-specific fluorescent probe of JC-1. Biochem. J. 2009, 418:311-323.
    • (2009) Biochem. J. , vol.418 , pp. 311-323
    • Lee, J.1    Lee, I.2    Choe, Y.3    Kang, S.4    Kim, H.Y.5    Gai, W.6    Hahn, J.7    Paik, S.R.8
  • 17
    • 24944566705 scopus 로고    scopus 로고
    • Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry
    • Aye T.T., Low T.Y., Sze S.K. Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry. Anal. Chem. 2005, 77:5814-5822.
    • (2005) Anal. Chem. , vol.77 , pp. 5814-5822
    • Aye, T.T.1    Low, T.Y.2    Sze, S.K.3
  • 18
    • 72949108011 scopus 로고    scopus 로고
    • Insulin amyloid fibrillation studied by terahertz spectroscopy and other biophysical methods
    • Liu R., He M., Su R., Yu Y., Qi W., He Z. Insulin amyloid fibrillation studied by terahertz spectroscopy and other biophysical methods. Biochem. Biophys. Res. Commun. 2010, 391:862-867.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 862-867
    • Liu, R.1    He, M.2    Su, R.3    Yu, Y.4    Qi, W.5    He, Z.6
  • 20
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases
    • Whitmore L., Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008, 89:392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 22
    • 30044446633 scopus 로고    scopus 로고
    • Early events in the fibrillation of monomeric insulin
    • Ahmad A., Uversky V.N., Hong D., Fink A.L. Early events in the fibrillation of monomeric insulin. J. Biol. Chem. 2005, 280:42669-42675.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 23
    • 38649112930 scopus 로고    scopus 로고
    • Zinc-amyloid β interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species
    • Noy D., Solomonov I., Sinkevich O., Arad T., Kjaer K., Sagi I. Zinc-amyloid β interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species. J. Am. Chem. Soc. 2008, 130:1376-1383.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1376-1383
    • Noy, D.1    Solomonov, I.2    Sinkevich, O.3    Arad, T.4    Kjaer, K.5    Sagi, I.6
  • 24
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., Uversky V.N., Fink A.L. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001, 40:6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 25
    • 33748505439 scopus 로고    scopus 로고
    • New laser technology and future applications
    • Steiner R. New laser technology and future applications. Med. Laser Appl. 2006, 21:131-140.
    • (2006) Med. Laser Appl. , vol.21 , pp. 131-140
    • Steiner, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.