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Volumn 79, Issue 2, 2010, Pages 176-184

Biomedical applications of X-ray absorption and vibrational spectroscopic microscopies in obtaining structural information from complex systems

Author keywords

Cells; FTIR microprobe; Raman microprobes; Tissues; X ray absorption spectroscopy; X ray microprobe

Indexed keywords

BIOMEDICAL APPLICATIONS; COMPLEX SYSTEMS; FTIR MICROPROBE; IN-SITU; METALLO-PROTEINS; MICRO-PROBES; NMR SPECTROSCOPY; PROTEIN CRYSTALLOGRAPHY; RAMAN MICROPROBES; STRUCTURAL BIOLOGY; STRUCTURAL INFORMATION; WHOLE CELL; X-RAY MICROPROBE;

EID: 70350783684     PISSN: 0969806X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.radphyschem.2009.03.068     Document Type: Article
Times cited : (36)

References (93)
  • 3
    • 33847228088 scopus 로고    scopus 로고
    • Combined spectroscopic and topographic characterization of nanoscale domains and their distributions of a redox protein on bacterial cell surfaces
    • Biju V., Pan D., Gorby Y.A., Fredrickson J., McLean J., Saffarini D., and Lu H.P. Combined spectroscopic and topographic characterization of nanoscale domains and their distributions of a redox protein on bacterial cell surfaces. Langmuir 23 (2007) 1333-1338
    • (2007) Langmuir , vol.23 , pp. 1333-1338
    • Biju, V.1    Pan, D.2    Gorby, Y.A.3    Fredrickson, J.4    McLean, J.5    Saffarini, D.6    Lu, H.P.7
  • 4
    • 34250319354 scopus 로고    scopus 로고
    • Laser-based measurements in cell biology
    • Botvinick E.L., and Shah J.V. Laser-based measurements in cell biology. Methods Cell Biol. 82 (2007) 81-109
    • (2007) Methods Cell Biol. , vol.82 , pp. 81-109
    • Botvinick, E.L.1    Shah, J.V.2
  • 5
    • 33751225050 scopus 로고    scopus 로고
    • Finite difference method calculations of X-ray absorption fine structure for copper
    • Bourke J.D., Chantler C.T., and Witte C. Finite difference method calculations of X-ray absorption fine structure for copper. Phys. Lett. A 360 (2006) 702-706
    • (2006) Phys. Lett. A , vol.360 , pp. 702-706
    • Bourke, J.D.1    Chantler, C.T.2    Witte, C.3
  • 6
    • 33847671839 scopus 로고    scopus 로고
    • Bulk and interface investigations of scaffolds and tissue-engineered bones by X-ray microtomography and X-ray microdiffraction
    • Cancedda R., Cedola A., Giuliani A., Komlev V., Lagomarsino S., Mastrogiacomo M., Peyrin F., and Rustichelli F. Bulk and interface investigations of scaffolds and tissue-engineered bones by X-ray microtomography and X-ray microdiffraction. Biomaterials 28 (2007) 2505-2524
    • (2007) Biomaterials , vol.28 , pp. 2505-2524
    • Cancedda, R.1    Cedola, A.2    Giuliani, A.3    Komlev, V.4    Lagomarsino, S.5    Mastrogiacomo, M.6    Peyrin, F.7    Rustichelli, F.8
  • 7
    • 48249123480 scopus 로고    scopus 로고
    • Nano-imaging of trace metals by synchrotron X-ray fluorescence into dopaminergic single cells and neurite-like processes
    • Carmona A., Cloetens P., Devès G., Bohic S., and Ortega R. Nano-imaging of trace metals by synchrotron X-ray fluorescence into dopaminergic single cells and neurite-like processes. J. Anal. At. Spectrom. 23 (2008) 1083-1088
    • (2008) J. Anal. At. Spectrom. , vol.23 , pp. 1083-1088
    • Carmona, A.1    Cloetens, P.2    Devès, G.3    Bohic, S.4    Ortega, R.5
  • 10
    • 0034957177 scopus 로고    scopus 로고
    • Studies on the genotoxicity of chromium: from the test tube to the cell
    • Codd R., Dillon C.T., Levina A., and Lay P.A. Studies on the genotoxicity of chromium: from the test tube to the cell. Coord. Chem. Rev. 216-217 (2001) 537-582
    • (2001) Coord. Chem. Rev. , vol.216-217 , pp. 537-582
    • Codd, R.1    Dillon, C.T.2    Levina, A.3    Lay, P.A.4
  • 12
    • 57849090528 scopus 로고    scopus 로고
    • A combined microRaman and microdiffraction set-up at the European synchrotron radiation facility ID13 beamline
    • Davies R.J., Burghammer M., and Riekel C. A combined microRaman and microdiffraction set-up at the European synchrotron radiation facility ID13 beamline. J. Synchrotron Radiat. 16 (2009) 22-29
    • (2009) J. Synchrotron Radiat. , vol.16 , pp. 22-29
    • Davies, R.J.1    Burghammer, M.2    Riekel, C.3
  • 13
    • 18444373555 scopus 로고    scopus 로고
    • Measurement of the X-ray mass attenuation coefficient and determination of the imaginary component of the atomic form-factor of molybdenum over the energy range of 13.5-41.5 keV
    • de Jonge M.D., Tran C.Q., Chantler C.T., Barnea Z., Dhal B.B., Cookson D.J., Lee W.-K., and Mashayekhi A. Measurement of the X-ray mass attenuation coefficient and determination of the imaginary component of the atomic form-factor of molybdenum over the energy range of 13.5-41.5 keV. Phys. Rev. A 71 (2005) 032702
    • (2005) Phys. Rev. A , vol.71 , pp. 032702
    • de Jonge, M.D.1    Tran, C.Q.2    Chantler, C.T.3    Barnea, Z.4    Dhal, B.B.5    Cookson, D.J.6    Lee, W.-K.7    Mashayekhi, A.8
  • 14
    • 0030916622 scopus 로고    scopus 로고
    • Microprobe X-ray absorption spectroscopic determination of the oxidation state of intracellular chromium following exposure of V79 Chinese hamster lung cells to genotoxic chromium complexes
    • Dillon C.T., Lay P.A., Cholewa M., Legge G.J.F., Bonin A.M., Collins T.J., Kostka K.L., and Shea-McCarthy G. Microprobe X-ray absorption spectroscopic determination of the oxidation state of intracellular chromium following exposure of V79 Chinese hamster lung cells to genotoxic chromium complexes. Chem. Res. Toxicol. 10 (1997) 533-535
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 533-535
    • Dillon, C.T.1    Lay, P.A.2    Cholewa, M.3    Legge, G.J.F.4    Bonin, A.M.5    Collins, T.J.6    Kostka, K.L.7    Shea-McCarthy, G.8
  • 15
    • 0036937686 scopus 로고    scopus 로고
    • Hard X-ray microprobe studies of chromium(VI)-treated V79 Chinese hamster lung cells: intracellular mapping of the biotransformation products of a chromium carcinogen
    • Dillon C.T., Lay P.A., Kennedy B.J., Stampfl A.P.J., Cai Z., Ilinski P., Rodrigues W., Legnini D.G., Lai B., and Maser J. Hard X-ray microprobe studies of chromium(VI)-treated V79 Chinese hamster lung cells: intracellular mapping of the biotransformation products of a chromium carcinogen. J. Biol. Inorg. Chem. 7 (2002) 640-645
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 640-645
    • Dillon, C.T.1    Lay, P.A.2    Kennedy, B.J.3    Stampfl, A.P.J.4    Cai, Z.5    Ilinski, P.6    Rodrigues, W.7    Legnini, D.G.8    Lai, B.9    Maser, J.10
  • 19
    • 60549108737 scopus 로고    scopus 로고
    • Effect of alkaline treatment on cellulose supramolecular structure studied with combined confocal Raman spectroscopy and atomic force microscopy
    • Eronen P., Österberg M., and Jääskeläinen A.-S. Effect of alkaline treatment on cellulose supramolecular structure studied with combined confocal Raman spectroscopy and atomic force microscopy. Cellulose 16 (2009) 167-178
    • (2009) Cellulose , vol.16 , pp. 167-178
    • Eronen, P.1    Österberg, M.2    Jääskeläinen, A.-S.3
  • 22
    • 44649180720 scopus 로고    scopus 로고
    • Focused field symmetries for background-free coherent anti-Stokes Raman spectroscopy
    • Gachet D., Billard F., and Rigneault H. Focused field symmetries for background-free coherent anti-Stokes Raman spectroscopy. Phys. Rev. A 77 (2008) 061802
    • (2008) Phys. Rev. A , vol.77 , pp. 061802
    • Gachet, D.1    Billard, F.2    Rigneault, H.3
  • 23
    • 34250161660 scopus 로고    scopus 로고
    • Imaging atomic structure and dynamics with ultrafast X-ray scattering
    • Gaffney K.J., and Chapman H.N. Imaging atomic structure and dynamics with ultrafast X-ray scattering. Science 316 (2007) 1444-1448
    • (2007) Science , vol.316 , pp. 1444-1448
    • Gaffney, K.J.1    Chapman, H.N.2
  • 24
    • 42649106834 scopus 로고    scopus 로고
    • Increasing FTIR spectromicroscopy speed and resolution through compressive imaging
    • Gallet J., Riley M., Hao Z., and Martin M.C. Increasing FTIR spectromicroscopy speed and resolution through compressive imaging. Infrared Phys. Technol. 51 (2008) 420-422
    • (2008) Infrared Phys. Technol. , vol.51 , pp. 420-422
    • Gallet, J.1    Riley, M.2    Hao, Z.3    Martin, M.C.4
  • 25
    • 36448985692 scopus 로고    scopus 로고
    • The analysis of X-ray absorption fine structure: beam-line independent interpretation
    • Glover J.L., and Chantler C.T. The analysis of X-ray absorption fine structure: beam-line independent interpretation. Meas. Sci. Technol. 18 (2007) 2916-2920
    • (2007) Meas. Sci. Technol. , vol.18 , pp. 2916-2920
    • Glover, J.L.1    Chantler, C.T.2
  • 26
    • 17644373413 scopus 로고    scopus 로고
    • Time-dependent uptake, distribution and biotransformation of chromium(VI) in individual and bulk human lung cells: application of synchrotron radiation techniques
    • Harris H.H., Levina A., Dillon C.T., Mulyani I., Lai B., Cai Z., and Lay P.A. Time-dependent uptake, distribution and biotransformation of chromium(VI) in individual and bulk human lung cells: application of synchrotron radiation techniques. J. Biol. Inorg. Chem. 10 (2005) 105-118
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 105-118
    • Harris, H.H.1    Levina, A.2    Dillon, C.T.3    Mulyani, I.4    Lai, B.5    Cai, Z.6    Lay, P.A.7
  • 27
    • 38649108190 scopus 로고    scopus 로고
    • A link between copper and dental caries in human teeth identified by XRF elemental mapping
    • Harris H.H., Vogt S., Eastgate H., and Lay P.A. A link between copper and dental caries in human teeth identified by XRF elemental mapping. J. Biol. Inorg. Chem. 13 (2008) 303-306
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 303-306
    • Harris, H.H.1    Vogt, S.2    Eastgate, H.3    Lay, P.A.4
  • 29
    • 65549087126 scopus 로고    scopus 로고
    • Harris, H.H., Vogt, S., Lay, P.A., 2009. Response to Guzzi & Pigatto's Comments on Migration of mercury from dental amalgam through human teeth by H.H. Harris et al. (2008) J. Synchrotron Radiat. 15, 123-128. J. Synchrotron Radiat. 16, 437-438.
    • Harris, H.H., Vogt, S., Lay, P.A., 2009. Response to Guzzi & Pigatto's Comments on Migration of mercury from dental amalgam through human teeth by H.H. Harris et al. (2008) J. Synchrotron Radiat. 15, 123-128. J. Synchrotron Radiat. 16, 437-438.
  • 30
    • 34748873777 scopus 로고    scopus 로고
    • Characterization of nanoindentation-induced residual stresses in human enamel by Raman microspectroscopy
    • He L.H., Carter E.A., and Swain M.V. Characterization of nanoindentation-induced residual stresses in human enamel by Raman microspectroscopy. Anal. Bioanal. Chem. 389 (2007) 1185-1192
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 1185-1192
    • He, L.H.1    Carter, E.A.2    Swain, M.V.3
  • 34
    • 46849121779 scopus 로고    scopus 로고
    • Theory of diffraction from eukaryotic flagellar axonemes
    • Iwamoto H. Theory of diffraction from eukaryotic flagellar axonemes. Cell Motil. Cytoskeleton 65 (2008) 563-571
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 563-571
    • Iwamoto, H.1
  • 35
    • 0000260760 scopus 로고    scopus 로고
    • X-ray absorption near edge structure calculations beyond the muffin-tin approximation
    • Joly Y. X-ray absorption near edge structure calculations beyond the muffin-tin approximation. Phys. Rev. B 63 (2001) 125120-125129
    • (2001) Phys. Rev. B , vol.63 , pp. 125120-125129
    • Joly, Y.1
  • 37
    • 34248174356 scopus 로고    scopus 로고
    • Enhancing high-throughput technology and microfluidics with FTIR spectroscopic imaging
    • Kazarian S.G. Enhancing high-throughput technology and microfluidics with FTIR spectroscopic imaging. Anal. Bioanal. Chem. 388 (2007) 529-532
    • (2007) Anal. Bioanal. Chem. , vol.388 , pp. 529-532
    • Kazarian, S.G.1
  • 39
  • 41
    • 70350767499 scopus 로고    scopus 로고
    • The application of X-ray absorption spectroscopy and microprobe X-ray techniques to molecular biology
    • Lay P.A. The application of X-ray absorption spectroscopy and microprobe X-ray techniques to molecular biology. Aust. Biochem. 36 (2005) 63-67
    • (2005) Aust. Biochem. , vol.36 , pp. 63-67
    • Lay, P.A.1
  • 42
    • 42949161626 scopus 로고    scopus 로고
    • Electron tomography in nanoparticle imaging and analysis
    • Lengyel J.S., Milne J.L.S., and Subramaniam S. Electron tomography in nanoparticle imaging and analysis. Nanomedicine 3 (2008) 125-131
    • (2008) Nanomedicine , vol.3 , pp. 125-131
    • Lengyel, J.S.1    Milne, J.L.S.2    Subramaniam, S.3
  • 43
    • 11144331938 scopus 로고    scopus 로고
    • Three-dimensional structure determination using multiple-scattering analysis of XAFS: applications to metalloproteins and coordination chemistry
    • Levina A., Armstrong R.S., and Lay P.A. Three-dimensional structure determination using multiple-scattering analysis of XAFS: applications to metalloproteins and coordination chemistry. Coord. Chem. Rev. 249 (2005) 141-160
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 141-160
    • Levina, A.1    Armstrong, R.S.2    Lay, P.A.3
  • 44
    • 78751659963 scopus 로고    scopus 로고
    • Chromium in biology: nutritional aspects and toxicology
    • Levina A., Codd R., Dillon C.T., and Lay P.A. Chromium in biology: nutritional aspects and toxicology. Prog. Inorg. Chem. 51 (2003) 145-250
    • (2003) Prog. Inorg. Chem. , vol.51 , pp. 145-250
    • Levina, A.1    Codd, R.2    Dillon, C.T.3    Lay, P.A.4
  • 45
    • 32444437411 scopus 로고    scopus 로고
    • Binding of chromium(VI) to histones: Implications for chromium(VI)-induced genotoxicity
    • Levina A., Harris H.H., and Lay P.A. Binding of chromium(VI) to histones: Implications for chromium(VI)-induced genotoxicity. J. Biol. Inorg. Chem. 11 (2006) 225-234
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 225-234
    • Levina, A.1    Harris, H.H.2    Lay, P.A.3
  • 46
    • 33846798243 scopus 로고    scopus 로고
    • X-ray absorption and EPR spectroscopic studies of the biotransformations of chromium(VI) in mammalian cells. Is chromodulin an artifact of isolation methods?
    • 983
    • Levina A., Harris H.H., and Lay P.A. X-ray absorption and EPR spectroscopic studies of the biotransformations of chromium(VI) in mammalian cells. Is chromodulin an artifact of isolation methods?. J. Am. Chem. Soc. 129 (2007) 1065-1075 983
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1065-1075
    • Levina, A.1    Harris, H.H.2    Lay, P.A.3
  • 47
    • 11844264797 scopus 로고    scopus 로고
    • Mechanistic studies of relevance to the biological activities of chromium
    • Levina A., and Lay P.A. Mechanistic studies of relevance to the biological activities of chromium. Coord. Chem. Rev. 249 (2005) 281-298
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 281-298
    • Levina, A.1    Lay, P.A.2
  • 48
    • 41849147879 scopus 로고    scopus 로고
    • Chemical properties and toxicity of chromium(III) nutritional supplements
    • Levina A., and Lay P.A. Chemical properties and toxicity of chromium(III) nutritional supplements. Chem. Res. Toxicol. 21 (2008) 563-571
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 563-571
    • Levina, A.1    Lay, P.A.2
  • 49
    • 35348820603 scopus 로고    scopus 로고
    • Reactivity of potential anti-diabetic molybdenum(VI) complexes in biological media: a XANES spectroscopic study
    • Levina A., McLeod A.I., Seuring J., and Lay P.A. Reactivity of potential anti-diabetic molybdenum(VI) complexes in biological media: a XANES spectroscopic study. J. Inorg. Biochem. 101 (2007) 1586-1593
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 1586-1593
    • Levina, A.1    McLeod, A.I.2    Seuring, J.3    Lay, P.A.4
  • 50
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., and Biesiadka J. Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 438 (2005) 1040-1044
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 51
    • 43449092561 scopus 로고    scopus 로고
    • Transferrin and the transferrin receptor: of magic bullets and other concerns
    • Macedo M.F., and de Sousa M. Transferrin and the transferrin receptor: of magic bullets and other concerns. Inflamm. Allergy: Drug Targets 7 (2008) 41-52
    • (2008) Inflamm. Allergy: Drug Targets , vol.7 , pp. 41-52
    • Macedo, M.F.1    de Sousa, M.2
  • 52
    • 43249124207 scopus 로고    scopus 로고
    • Mercury(II) complex formation with glutathione in alkaline aqueous solution
    • Mah V., and Jalilehvand F. Mercury(II) complex formation with glutathione in alkaline aqueous solution. J. Biol. Inorg. Chem. 13 (2008) 541-553
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 541-553
    • Mah, V.1    Jalilehvand, F.2
  • 54
    • 33747336237 scopus 로고    scopus 로고
    • Chemical imaging of biological tissue with synchrotron infrared light
    • Miller L.M., and Dumas P. Chemical imaging of biological tissue with synchrotron infrared light. Biochim. Biophys. Acta-Biomembranes 1758 (2006) 846-857
    • (2006) Biochim. Biophys. Acta-Biomembranes , vol.1758 , pp. 846-857
    • Miller, L.M.1    Dumas, P.2
  • 55
    • 33847235379 scopus 로고    scopus 로고
    • A new sample substrate for imaging and correlating organic and trace metal composition in biological cells and tissues
    • Miller L.M., Wang Q., Smith R.J., Zhong H., Elliott D., and Warren J. A new sample substrate for imaging and correlating organic and trace metal composition in biological cells and tissues. Anal. Bioanal. Chem. 387 (2007) 1705-1715
    • (2007) Anal. Bioanal. Chem. , vol.387 , pp. 1705-1715
    • Miller, L.M.1    Wang, Q.2    Smith, R.J.3    Zhong, H.4    Elliott, D.5    Warren, J.6
  • 56
    • 4544259176 scopus 로고    scopus 로고
    • Biomimetic oxidation of chromium(III): does the antidiabetic activity of chromium(III) involve carcinogenic chromium(VI)?
    • Mulyani I., Levina A., and Lay P.A. Biomimetic oxidation of chromium(III): does the antidiabetic activity of chromium(III) involve carcinogenic chromium(VI)?. Angew. Chem. Int. Ed. 43 (2004) 4504-4507
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 4504-4507
    • Mulyani, I.1    Levina, A.2    Lay, P.A.3
  • 58
    • 44749086496 scopus 로고    scopus 로고
    • Recent advancement in the field of two-dimensional correlation spectroscopy
    • Noda I. Recent advancement in the field of two-dimensional correlation spectroscopy. J. Mol. Struct. 883-884 (2008) 2-26
    • (2008) J. Mol. Struct. , vol.883-884 , pp. 2-26
    • Noda, I.1
  • 59
    • 44349098158 scopus 로고    scopus 로고
    • Reactivity of chromium(III) nutritional supplements in biological media: an X-ray absorption spectroscopic study
    • Nguyen A., Mulyani I., Levina A., and Lay P.A. Reactivity of chromium(III) nutritional supplements in biological media: an X-ray absorption spectroscopic study. Inorg. Chem. 47 (2008) 4299-4309
    • (2008) Inorg. Chem. , vol.47 , pp. 4299-4309
    • Nguyen, A.1    Mulyani, I.2    Levina, A.3    Lay, P.A.4
  • 60
    • 70350746640 scopus 로고    scopus 로고
    • OMNIC™, 2001. Version 6.0, Thermo Nicolet, Madison, WI, USA
    • OMNIC™, 2001. Version 6.0, Thermo Nicolet, Madison, WI, USA.
  • 61
    • 70350767498 scopus 로고    scopus 로고
    • OMNIC™ Atlμs™, 2005. Version 7.2, Thermo Electron Corporation, Madison, WI, USA
    • OMNIC™ Atlμs™, 2005. Version 7.2, Thermo Electron Corporation, Madison, WI, USA.
  • 63
    • 33751561930 scopus 로고    scopus 로고
    • X-ray fluorescence microprobe imaging in biology and medicine
    • Paunesku T., Vogt S., Maser J., Lai B., and Woloschak G. X-ray fluorescence microprobe imaging in biology and medicine. J. Cell Biochem. 99 (2006) 1489-1502
    • (2006) J. Cell Biochem. , vol.99 , pp. 1489-1502
    • Paunesku, T.1    Vogt, S.2    Maser, J.3    Lai, B.4    Woloschak, G.5
  • 65
    • 45849109536 scopus 로고    scopus 로고
    • Bioimaging of cells and tissues using accelerator-based sources
    • Petibois C., and Guidi M.C. Bioimaging of cells and tissues using accelerator-based sources. Anal. Bioanal. Chem. 391 (2008) 1599-1608
    • (2008) Anal. Bioanal. Chem. , vol.391 , pp. 1599-1608
    • Petibois, C.1    Guidi, M.C.2
  • 67
    • 33750147036 scopus 로고    scopus 로고
    • Theory and calculations of X-ray spectra: XAS, XES, XRS, and NRIXS
    • Rehr J.J. Theory and calculations of X-ray spectra: XAS, XES, XRS, and NRIXS. Radiat. Phys. Chem. 75 (2006) 1547-1558
    • (2006) Radiat. Phys. Chem. , vol.75 , pp. 1547-1558
    • Rehr, J.J.1
  • 68
    • 11144309505 scopus 로고    scopus 로고
    • Progress in the theory and interpretation of XANES
    • Rehr J.J., and Ankudinov A.L. Progress in the theory and interpretation of XANES. Coord. Chem. Rev. 249 (2005) 131-140
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 131-140
    • Rehr, J.J.1    Ankudinov, A.L.2
  • 69
    • 70350752692 scopus 로고    scopus 로고
    • Renishaw, plc, 2009. 〈http://www.renishaw.com/en/6150.aspx〉, Renishaw, Wotton-under-Edge, UK.
    • Renishaw, plc, 2009. 〈http://www.renishaw.com/en/6150.aspx〉, Renishaw, Wotton-under-Edge, UK.
  • 70
    • 0032548142 scopus 로고    scopus 로고
    • Three-dimensional structure of the plant photosystem II reaction centre at 8 Å resolution
    • Rhee K.-H., Morris E.P., Barber J., and Kühlbrandt W. Three-dimensional structure of the plant photosystem II reaction centre at 8 Å resolution. Nature 396 (1998) 283-286
    • (1998) Nature , vol.396 , pp. 283-286
    • Rhee, K.-H.1    Morris, E.P.2    Barber, J.3    Kühlbrandt, W.4
  • 71
    • 36549000264 scopus 로고    scopus 로고
    • ATR-FTIR imaging of albumen photographic prints
    • Ricci C., Bloxham S., and Kazarian S.G. ATR-FTIR imaging of albumen photographic prints. J. Cult. Herit. 8 (2007) 387-395
    • (2007) J. Cult. Herit. , vol.8 , pp. 387-395
    • Ricci, C.1    Bloxham, S.2    Kazarian, S.G.3
  • 72
    • 0032576122 scopus 로고    scopus 로고
    • Determination of the Fe-ligand bond lengths and Fe-N-O bond angles in horse heart ferric and ferrous nitrosylmyoglobin using multiple-scattering XAFS analyses
    • Rich A.M., Armstrong R.S., Ellis P.J., and Lay P.A. Determination of the Fe-ligand bond lengths and Fe-N-O bond angles in horse heart ferric and ferrous nitrosylmyoglobin using multiple-scattering XAFS analyses. J. Am. Chem. Soc. 120 (1998) 10827-10836
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10827-10836
    • Rich, A.M.1    Armstrong, R.S.2    Ellis, P.J.3    Lay, P.A.4
  • 73
    • 0001163433 scopus 로고    scopus 로고
    • Determination of iron-ligand bond lengths in horse heart met- and deoxymyoglobin using multiple-scattering XAFS analyses
    • Rich A.M., Armstrong R.S., Ellis P.J., Freeman H.C., and Lay P.A. Determination of iron-ligand bond lengths in horse heart met- and deoxymyoglobin using multiple-scattering XAFS analyses. Inorg. Chem. 37 (1998) 5743-5753
    • (1998) Inorg. Chem. , vol.37 , pp. 5743-5753
    • Rich, A.M.1    Armstrong, R.S.2    Ellis, P.J.3    Freeman, H.C.4    Lay, P.A.5
  • 75
    • 49549090015 scopus 로고    scopus 로고
    • The effect of the microscopic and nanoscale structure on bone fragility
    • Ruppel M.E., Miller L.M., and Burr D.B. The effect of the microscopic and nanoscale structure on bone fragility. Osteopor. Int. 19 (2008) 1251-1265
    • (2008) Osteopor. Int. , vol.19 , pp. 1251-1265
    • Ruppel, M.E.1    Miller, L.M.2    Burr, D.B.3
  • 76
    • 33747349746 scopus 로고    scopus 로고
    • Iron regulation and the cell cycle: Identification of an iron-responsive element in the 3′-untranslated region of human cell division cycle 14 A mRNA by a refined microarray-based screening strategy
    • Sanchez M., Galy B., Dandekar T., Bengert P., Vainshtein Y., Stolte J., Muckenthaler M.U., and Hentze M.W. Iron regulation and the cell cycle: Identification of an iron-responsive element in the 3′-untranslated region of human cell division cycle 14 A mRNA by a refined microarray-based screening strategy. J. Biol. Chem. 281 (2006) 22865-22874
    • (2006) J. Biol. Chem. , vol.281 , pp. 22865-22874
    • Sanchez, M.1    Galy, B.2    Dandekar, T.3    Bengert, P.4    Vainshtein, Y.5    Stolte, J.6    Muckenthaler, M.U.7    Hentze, M.W.8
  • 77
    • 70350762094 scopus 로고    scopus 로고
    • Improved single molecule detection and tracing algorithms for the generation of a dynamic map of membrane diffusion in living cells
    • Serge A., Bertaux N., Rigneault H., and Marguet D. Improved single molecule detection and tracing algorithms for the generation of a dynamic map of membrane diffusion in living cells. Biophys. J. Suppl. S (2007) 91A
    • (2007) Biophys. J. , Issue.SUPPL. S
    • Serge, A.1    Bertaux, N.2    Rigneault, H.3    Marguet, D.4
  • 81
    • 33750160442 scopus 로고    scopus 로고
    • Analysis of X-ray absorption fine structure using absolute X-ray mass attenuation coefficients: application to molybdenum
    • Smale L.F., Chantler C.T., de Jonge M.D., Barnea Z., and Tran C.Q. Analysis of X-ray absorption fine structure using absolute X-ray mass attenuation coefficients: application to molybdenum. Radiat. Phys. Chem. 75 (2006) 1559-1563
    • (2006) Radiat. Phys. Chem. , vol.75 , pp. 1559-1563
    • Smale, L.F.1    Chantler, C.T.2    de Jonge, M.D.3    Barnea, Z.4    Tran, C.Q.5
  • 82
    • 34247151663 scopus 로고    scopus 로고
    • FitIt: new software to extract structural information on the basis of XANES fitting
    • Smolentsev G., and Soldatov A.V. FitIt: new software to extract structural information on the basis of XANES fitting. Comp. Mater. Sci. 39 (2007) 569-574
    • (2007) Comp. Mater. Sci. , vol.39 , pp. 569-574
    • Smolentsev, G.1    Soldatov, A.V.2
  • 83
    • 11144273799 scopus 로고    scopus 로고
    • Ligand K-edge X-ray absorption spectroscopy: covalency of ligand-metal bonds
    • Solomon E.I., Hedman B., Hodgson K.O., Dey A., and Szilagyi R.K. Ligand K-edge X-ray absorption spectroscopy: covalency of ligand-metal bonds. Coord. Chem. Rev. 249 (2005) 97-129
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 97-129
    • Solomon, E.I.1    Hedman, B.2    Hodgson, K.O.3    Dey, A.4    Szilagyi, R.K.5
  • 85
    • 37549022317 scopus 로고    scopus 로고
    • Small-angle scattering and its interplay with crystallography, contrast variation in SAXS and SANS
    • Stuhrmann H.B. Small-angle scattering and its interplay with crystallography, contrast variation in SAXS and SANS. Acta Crystallogr. Sect. A 64 (2008) 181-191
    • (2008) Acta Crystallogr. Sect. A , vol.64 , pp. 181-191
    • Stuhrmann, H.B.1
  • 86
    • 0037687691 scopus 로고    scopus 로고
    • MAPS: a set of software tools for analysis and visualization of 3D X-ray fluorescence data sets
    • Vogt S. MAPS: a set of software tools for analysis and visualization of 3D X-ray fluorescence data sets. J. Phys. IV. 104 (2003) 635-638
    • (2003) J. Phys. IV. , vol.104 , pp. 635-638
    • Vogt, S.1
  • 92
    • 57449097881 scopus 로고    scopus 로고
    • Application of Synchrotron FTIR Techniques in Biomedical Fields
    • Yan J.P., Shao Z., Chen X., and Huang Y.F. Application of Synchrotron FTIR Techniques in Biomedical Fields. Prog. Chem. 20 (2008) 1768-1778
    • (2008) Prog. Chem. , vol.20 , pp. 1768-1778
    • Yan, J.P.1    Shao, Z.2    Chen, X.3    Huang, Y.F.4
  • 93
    • 41949099222 scopus 로고    scopus 로고
    • Towards atomic resolution structural determination by single-particle cryo-electron microscopy
    • Zhou Z.H. Towards atomic resolution structural determination by single-particle cryo-electron microscopy. Curr. Opin. Struct. Biol. 18 (2008) 218-228
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 218-228
    • Zhou, Z.H.1


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