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Volumn 20, Issue 5, 2010, Pages 649-656

From structure to cellular mechanism with infrared microspectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; COLLAGEN; ELASTIN; GREEN FLUORESCENT PROTEIN;

EID: 78049441237     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2010.07.007     Document Type: Review
Times cited : (120)

References (60)
  • 1
    • 33747336237 scopus 로고    scopus 로고
    • Chemical imaging of biological tissue with synchrotron infrared light
    • Miller L.M., Dumas P. Chemical imaging of biological tissue with synchrotron infrared light. Biochim Biophys Acta 2006, 1758:846-857.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 846-857
    • Miller, L.M.1    Dumas, P.2
  • 3
    • 84879165732 scopus 로고    scopus 로고
    • About the use of synchrotron radiation in infrared microscopy for biomedical applications
    • IOS Press, P. Haris (Ed.)
    • Miller L., Tobin M.J., Srichan S., Dumas P. About the use of synchrotron radiation in infrared microscopy for biomedical applications. Biomedical Applications of FTIR Spectroscopy 2008, IOS Press. P. Haris (Ed.).
    • (2008) Biomedical Applications of FTIR Spectroscopy
    • Miller, L.1    Tobin, M.J.2    Srichan, S.3    Dumas, P.4
  • 4
    • 0036670983 scopus 로고    scopus 로고
    • Generalized implementation of rapid-scan Fourier transform infrared spectroscopic imaging
    • Huffman S.W., Bhargava R., Levin I.W. Generalized implementation of rapid-scan Fourier transform infrared spectroscopic imaging. Appl Spectrosc 2002, 56:965-969.
    • (2002) Appl Spectrosc , vol.56 , pp. 965-969
    • Huffman, S.W.1    Bhargava, R.2    Levin, I.W.3
  • 7
    • 35348877899 scopus 로고    scopus 로고
    • Synchrotron infrared microspectroscopy imaging using a multi-element detector (IRMSI-MED) for diffraction-limited chemical imaging
    • Nasse M.J., Reininger R., Kubala T., Janowski S., Hirschmugl C.J. Synchrotron infrared microspectroscopy imaging using a multi-element detector (IRMSI-MED) for diffraction-limited chemical imaging. Nucl Instrum Methods Phys Res A 2007, 582:107-110.
    • (2007) Nucl Instrum Methods Phys Res A , vol.582 , pp. 107-110
    • Nasse, M.J.1    Reininger, R.2    Kubala, T.3    Janowski, S.4    Hirschmugl, C.J.5
  • 9
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 10
    • 33646196840 scopus 로고    scopus 로고
    • Evaluation of the information content in infrared spectra for protein secondary structure determination
    • Goormaghtigh E., Ruysschaert J.M., Raussens V. Evaluation of the information content in infrared spectra for protein secondary structure determination. Biophys J 2006, 90:2946-2957.
    • (2006) Biophys J , vol.90 , pp. 2946-2957
    • Goormaghtigh, E.1    Ruysschaert, J.M.2    Raussens, V.3
  • 11
    • 0025906210 scopus 로고
    • Protein secondary structure from Fourier transform infrared spectroscopy: a data base analysis
    • Sarver R.W., Krueger W.C. Protein secondary structure from Fourier transform infrared spectroscopy: a data base analysis. Anal Biochem 1991, 194:89-100.
    • (1991) Anal Biochem , vol.194 , pp. 89-100
    • Sarver, R.W.1    Krueger, W.C.2
  • 12
    • 0035478472 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics
    • Wallace B.A., Janes R.W. Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics. Curr Opin Chem Biol 2001, 5:567-571.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 567-571
    • Wallace, B.A.1    Janes, R.W.2
  • 14
    • 0027482684 scopus 로고
    • Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra
    • Pribic R., Van Stokkum I.H.M., Chapman D., Haris P.I., Bloemendal M. Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra. Anal Biochem 1993, 214:336-378.
    • (1993) Anal Biochem , vol.214 , pp. 336-378
    • Pribic, R.1    Van Stokkum, I.H.M.2    Chapman, D.3    Haris, P.I.4    Bloemendal, M.5
  • 15
    • 0035443168 scopus 로고    scopus 로고
    • Two-dimensional infrared spectroscopy: a promising new method for the time resolution of structures
    • Zanni M.T., Hochstrasser R.M. Two-dimensional infrared spectroscopy: a promising new method for the time resolution of structures. Curr Opin Struct Biol 2001, 11:516-522.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 516-522
    • Zanni, M.T.1    Hochstrasser, R.M.2
  • 17
    • 70349303076 scopus 로고    scopus 로고
    • Resonant Mie scattering in infrared spectroscopy of biological materials-understanding the "dispersion artifact"
    • Bassan P., Byrne H.J., Bonnier F., Lee J., Dumas P., Gardner P. Resonant Mie scattering in infrared spectroscopy of biological materials-understanding the "dispersion artifact" Analyst 2009, 134:1586-1593.
    • (2009) Analyst , vol.134 , pp. 1586-1593
    • Bassan, P.1    Byrne, H.J.2    Bonnier, F.3    Lee, J.4    Dumas, P.5    Gardner, P.6
  • 19
    • 33749547707 scopus 로고    scopus 로고
    • Infrared micro-spectroscopy of human cells: causes for the spectral variance of oral mucosa (buccal) cells
    • Romeo M., Mohlenhoff B., Diem M. Infrared micro-spectroscopy of human cells: causes for the spectral variance of oral mucosa (buccal) cells. Vib Spectrosc 2006, 42:9-14.
    • (2006) Vib Spectrosc , vol.42 , pp. 9-14
    • Romeo, M.1    Mohlenhoff, B.2    Diem, M.3
  • 21
  • 22
    • 0029839357 scopus 로고    scopus 로고
    • In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy
    • Choo L.P., Wetzel D.L., Halliday W.C., Jackson M., LeVine S.M., Mantsch H.H. In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy. Biophys J 1996, 71:1672-1679.
    • (1996) Biophys J , vol.71 , pp. 1672-1679
    • Choo, L.P.1    Wetzel, D.L.2    Halliday, W.C.3    Jackson, M.4    LeVine, S.M.5    Mantsch, H.H.6
  • 23
    • 33745004381 scopus 로고    scopus 로고
    • Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with beta-amyloid deposits in Alzheimer's disease
    • Miller L.M., Wang Q., Telivala T.P., Smith R.J., Lanzirotti A., Miklossy J. Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with beta-amyloid deposits in Alzheimer's disease. J Struct Biol 2006, 155:30-37.
    • (2006) J Struct Biol , vol.155 , pp. 30-37
    • Miller, L.M.1    Wang, Q.2    Telivala, T.P.3    Smith, R.J.4    Lanzirotti, A.5    Miklossy, J.6
  • 24
    • 35948932167 scopus 로고    scopus 로고
    • Dense-core and diffuse Abeta plaques in TgCRND8 mice studied with synchrotron FTIR microspectroscopy
    • Rak M., Del Bigio M.R., Mai S., Westaway D., Gough K. Dense-core and diffuse Abeta plaques in TgCRND8 mice studied with synchrotron FTIR microspectroscopy. Biopolymers 2007, 87:207-217.
    • (2007) Biopolymers , vol.87 , pp. 207-217
    • Rak, M.1    Del Bigio, M.R.2    Mai, S.3    Westaway, D.4    Gough, K.5
  • 25
    • 77950418327 scopus 로고    scopus 로고
    • Fourier Transform Infrared imaging showing reduced unsaturated lipid content in the hippocampus of a mouse model of Alzheimer's disease
    • Leskovjan A.C., Kretlow A., Miller L.M. Fourier Transform Infrared imaging showing reduced unsaturated lipid content in the hippocampus of a mouse model of Alzheimer's disease. Anal Chem 2010, 82:2711-2716.
    • (2010) Anal Chem , vol.82 , pp. 2711-2716
    • Leskovjan, A.C.1    Kretlow, A.2    Miller, L.M.3
  • 28
    • 52249117910 scopus 로고    scopus 로고
    • Changes in protein structure and distribution observed at pre-clinical stages of scrapie pathogenesis
    • Kretlow A., Wang Q., Beekes M., Naumann D., Miller L.M. Changes in protein structure and distribution observed at pre-clinical stages of scrapie pathogenesis. Biochim Biophys Acta Mol Basis Dis 2008, 1782:559-565.
    • (2008) Biochim Biophys Acta Mol Basis Dis , vol.1782 , pp. 559-565
    • Kretlow, A.1    Wang, Q.2    Beekes, M.3    Naumann, D.4    Miller, L.M.5
  • 29
    • 0037092437 scopus 로고    scopus 로고
    • Molecular changes of preclinical scrapie can be detected by infrared spectroscopy
    • Kneipp J., Beekes M., Lasch P., Naumann D. Molecular changes of preclinical scrapie can be detected by infrared spectroscopy. J Neurosci 2002, 22:2989-2997.
    • (2002) J Neurosci , vol.22 , pp. 2989-2997
    • Kneipp, J.1    Beekes, M.2    Lasch, P.3    Naumann, D.4
  • 30
    • 77954751961 scopus 로고    scopus 로고
    • The use of synchrotron infrared microspectroscopy in the assessment of cutaneous T-cell lymphoma vs. pityriasis lichenoides chronica
    • Bedewi A., El Anany G., El Mofty M., Kretlow A., Park S., Miller L.M. The use of synchrotron infrared microspectroscopy in the assessment of cutaneous T-cell lymphoma vs. pityriasis lichenoides chronica. Photodermatol Photoimmunol Photomed 2010, 26:93-97.
    • (2010) Photodermatol Photoimmunol Photomed , vol.26 , pp. 93-97
    • Bedewi, A.1    El Anany, G.2    El Mofty, M.3    Kretlow, A.4    Park, S.5    Miller, L.M.6
  • 31
    • 70749101856 scopus 로고    scopus 로고
    • Early detection of the chemical changes occurring during the induction and prevention of autoimmune-mediated demyelination detected by FT-IR imaging
    • Heraud P., Caine S., Campanale N., Karnezis T., McNaughton D., Wood B.R., Tobin M.J., Bernard C.C.A. Early detection of the chemical changes occurring during the induction and prevention of autoimmune-mediated demyelination detected by FT-IR imaging. Neuroimage 2010, 49:1180-1189.
    • (2010) Neuroimage , vol.49 , pp. 1180-1189
    • Heraud, P.1    Caine, S.2    Campanale, N.3    Karnezis, T.4    McNaughton, D.5    Wood, B.R.6    Tobin, M.J.7    Bernard, C.C.A.8
  • 33
    • 68249127919 scopus 로고    scopus 로고
    • Fourier transform infrared microspectroscopic analysis of the effects of cereal type and variety within a type of grain on structural makeup in relation to rumen degradation kinetics
    • Walker A.M., Yu P.Q., Christensen C.R., Christensen D.A., McKinnon J.J. Fourier transform infrared microspectroscopic analysis of the effects of cereal type and variety within a type of grain on structural makeup in relation to rumen degradation kinetics. J Agric Food Chem 2009, 57:6871-6878.
    • (2009) J Agric Food Chem , vol.57 , pp. 6871-6878
    • Walker, A.M.1    Yu, P.Q.2    Christensen, C.R.3    Christensen, D.A.4    McKinnon, J.J.5
  • 35
    • 0043236212 scopus 로고    scopus 로고
    • Chemical heterogeneity in cell death: combined synchrotron IR and fluorescence microscopy studies of single apoptotic and necrotic cells
    • Jamin N., Miller L., Moncuit J., Fridman W.H., Dumas P., Teillaud J.L. Chemical heterogeneity in cell death: combined synchrotron IR and fluorescence microscopy studies of single apoptotic and necrotic cells. Biopolymers 2003, 72:366-373.
    • (2003) Biopolymers , vol.72 , pp. 366-373
    • Jamin, N.1    Miller, L.2    Moncuit, J.3    Fridman, W.H.4    Dumas, P.5    Teillaud, J.L.6
  • 36
    • 0036290651 scopus 로고    scopus 로고
    • Spatially resolved IR microspectroscopy of single cells
    • Lasch P., Pacifico A., Diem M. Spatially resolved IR microspectroscopy of single cells. Biopolymers 2002, 67:4-5.
    • (2002) Biopolymers , vol.67 , pp. 4-5
    • Lasch, P.1    Pacifico, A.2    Diem, M.3
  • 39
    • 58849137490 scopus 로고    scopus 로고
    • Discrimination between drug-resistant and non-resistant human melanoma cell lines by FTIR spectroscopy
    • Zwielly A., Gopas J., Brkic G., Mordechai S. Discrimination between drug-resistant and non-resistant human melanoma cell lines by FTIR spectroscopy. Analyst 2009, 134:294-300.
    • (2009) Analyst , vol.134 , pp. 294-300
    • Zwielly, A.1    Gopas, J.2    Brkic, G.3    Mordechai, S.4
  • 41
    • 39749105397 scopus 로고    scopus 로고
    • Stem-cell therapy for cardiac disease
    • Segers V.F., Lee R.T. Stem-cell therapy for cardiac disease. Nature 2008, 451:937-942.
    • (2008) Nature , vol.451 , pp. 937-942
    • Segers, V.F.1    Lee, R.T.2
  • 42
    • 39449134791 scopus 로고    scopus 로고
    • Special cells, special considerations: the challenges of bringing embryonic stem cells from the laboratory to the clinic
    • Addis R.C., Bulte J.W., Gearhart J.D. Special cells, special considerations: the challenges of bringing embryonic stem cells from the laboratory to the clinic. Clin Pharmacol Ther 2008, 83:386-389.
    • (2008) Clin Pharmacol Ther , vol.83 , pp. 386-389
    • Addis, R.C.1    Bulte, J.W.2    Gearhart, J.D.3
  • 43
    • 77953140984 scopus 로고    scopus 로고
    • Optical spectroscopy for noninvasive monitoring of stem cell differentiation
    • Downes A., Mouras R., Elfick A. Optical spectroscopy for noninvasive monitoring of stem cell differentiation. J Biomed Biotechnol 2010, 2010:1-10.
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 1-10
    • Downes, A.1    Mouras, R.2    Elfick, A.3
  • 44
    • 34347264847 scopus 로고    scopus 로고
    • Differentiation of individual human mesenchymal stem cells probed by FTIR microscopic imaging
    • Krafft C., Salzer R., Seitz S., Ern C., Schieker M. Differentiation of individual human mesenchymal stem cells probed by FTIR microscopic imaging. Analyst 2007, 132:647-653.
    • (2007) Analyst , vol.132 , pp. 647-653
    • Krafft, C.1    Salzer, R.2    Seitz, S.3    Ern, C.4    Schieker, M.5
  • 47
    • 76949084925 scopus 로고    scopus 로고
    • Neural differentiation of mouse embryonic stem cells studied by FTIR spectroscopy
    • Tanthanucha W., Thumanu K., Lorthongpanich C., Parnpai R., Heraud P. Neural differentiation of mouse embryonic stem cells studied by FTIR spectroscopy. J Mol Struct 2010, 967:189-195.
    • (2010) J Mol Struct , vol.967 , pp. 189-195
    • Tanthanucha, W.1    Thumanu, K.2    Lorthongpanich, C.3    Parnpai, R.4    Heraud, P.5
  • 48
  • 49
    • 77951256785 scopus 로고    scopus 로고
    • Toxicity and phototoxicity of hypocrellin A on malignant human cell lines, evidence of a synergistic action of photodynamic therapy with imatinib mesylate
    • Chio-Srichan S., Oudrhiri N., Bennaceur-Griscelli A., Turhan A.G., Dumas P., Refregiers M. Toxicity and phototoxicity of hypocrellin A on malignant human cell lines, evidence of a synergistic action of photodynamic therapy with imatinib mesylate. J Photochem Photobiol B Biol 2010, 99:100-104.
    • (2010) J Photochem Photobiol B Biol , vol.99 , pp. 100-104
    • Chio-Srichan, S.1    Oudrhiri, N.2    Bennaceur-Griscelli, A.3    Turhan, A.G.4    Dumas, P.5    Refregiers, M.6
  • 50
    • 0030823063 scopus 로고    scopus 로고
    • Time-resolved mid-infrared spectroscopy: methods and biological applications
    • Slayton R.M., Anfirud P.A. Time-resolved mid-infrared spectroscopy: methods and biological applications. Curr Opin Struct Biol 1997, 7:717-721.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 717-721
    • Slayton, R.M.1    Anfirud, P.A.2
  • 52
    • 59649126223 scopus 로고    scopus 로고
    • For structural biology. Try infrared instead
    • Hamm P. For structural biology. Try infrared instead. Structure 2009, 17:149-150.
    • (2009) Structure , vol.17 , pp. 149-150
    • Hamm, P.1
  • 53
    • 17744370742 scopus 로고    scopus 로고
    • Picosecond dynamics of ligand interconversion in the primary docking site of heme proteins
    • Kim S., Lim M. Picosecond dynamics of ligand interconversion in the primary docking site of heme proteins. J Am Chem Soc 2005, 127:5786-5787.
    • (2005) J Am Chem Soc , vol.127 , pp. 5786-5787
    • Kim, S.1    Lim, M.2
  • 54
    • 14044274349 scopus 로고    scopus 로고
    • A-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy
    • Bredenbeck J., Helbing J., Kumita J.R., Woolley G.A., Hamm P. a-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy. Proc Natl Acad Sci USA 2005, 102:2379-2384.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2379-2384
    • Bredenbeck, J.1    Helbing, J.2    Kumita, J.R.3    Woolley, G.A.4    Hamm, P.5
  • 55
    • 22144488143 scopus 로고    scopus 로고
    • IR micro spectroscopy of live cells
    • Moss D.A., Keese M., Pepperkok R. IR micro spectroscopy of live cells. Vib Spectrosc 2005, 38:185-191.
    • (2005) Vib Spectrosc , vol.38 , pp. 185-191
    • Moss, D.A.1    Keese, M.2    Pepperkok, R.3
  • 57
    • 76949087837 scopus 로고    scopus 로고
    • Fabrication of a microfluidic platform for investigating dynamic biochemical processes in living samples by FTIR microspectroscopy
    • Birarda G., Grenci G., Businaro L., Marmiroli B., Pacor S., Vaccari L. Fabrication of a microfluidic platform for investigating dynamic biochemical processes in living samples by FTIR microspectroscopy. Microelectron Eng 2010, 87:806-809.
    • (2010) Microelectron Eng , vol.87 , pp. 806-809
    • Birarda, G.1    Grenci, G.2    Businaro, L.3    Marmiroli, B.4    Pacor, S.5    Vaccari, L.6
  • 59
    • 70449857579 scopus 로고    scopus 로고
    • Real-time chemical imaging of bacterial activity in biofilms using open-channel microfluidics and synchrotron FTIR spectromicroscopy
    • Holman H.Y.N., Miles R., Hao Z., Wozei E., Anderson L.M., Yang H. Real-time chemical imaging of bacterial activity in biofilms using open-channel microfluidics and synchrotron FTIR spectromicroscopy. Anal Chem 2009, 81:8564-8570.
    • (2009) Anal Chem , vol.81 , pp. 8564-8570
    • Holman, H.Y.N.1    Miles, R.2    Hao, Z.3    Wozei, E.4    Anderson, L.M.5    Yang, H.6
  • 60
    • 61349198356 scopus 로고    scopus 로고
    • Chemical imaging of live cancer cells in the natural aqueous environment
    • Kuimova M.K., Andrew Chan K.L., Kazarian S.G. Chemical imaging of live cancer cells in the natural aqueous environment. Appl Spectrosc 2009, 63:164-171.
    • (2009) Appl Spectrosc , vol.63 , pp. 164-171
    • Kuimova, M.K.1    Andrew Chan, K.L.2    Kazarian, S.G.3


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