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Volumn 1814, Issue 6, 2011, Pages 785-796

How different oxidation states of crystalline myoglobin are influenced by X-rays

Author keywords

Crystal structure; Metalloprotein; Peroxidase; Radiation damage; Spectroscopy; X ray

Indexed keywords

ASCORBIC ACID; FERRIC ION; FERRYLMYOGLOBIN; MYOGLOBIN;

EID: 79955830201     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.07.019     Document Type: Article
Times cited : (48)

References (56)
  • 1
    • 33644877757 scopus 로고    scopus 로고
    • Cryocooling and radiation damage in macromolecular crystallography
    • E.F. Garman, and R.L. Owen Cryocooling and radiation damage in macromolecular crystallography Acta Crystallogr., D Biol. Crystallogr. 62 2006 32 47
    • (2006) Acta Crystallogr., D Biol. Crystallogr. , vol.62 , pp. 32-47
    • Garman, E.F.1    Owen, R.L.2
  • 2
    • 61449151996 scopus 로고    scopus 로고
    • A beginner's guide to radiation damage
    • J.M. Holton A beginner's guide to radiation damage J. Synchrotron Radiat. 16 2009 133 142
    • (2009) J. Synchrotron Radiat. , vol.16 , pp. 133-142
    • Holton, J.M.1
  • 3
    • 33749179561 scopus 로고    scopus 로고
    • Radiation damage in macromolecular cryocrystallography
    • DOI 10.1016/j.sbi.2006.08.001, PII S0959440X06001369, Carbohydrates and Glycoconjugates / Biophysical Methods
    • R.B.G. Ravelli, and E.F. Garman Radiation damage in macromolecular cryocrystallography Curr. Opin. Chem. Biol. 16 2006 624 629 (Pubitemid 44472608)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 624-629
    • Ravelli, R.B.1    Garman, E.F.2
  • 4
    • 0037161809 scopus 로고    scopus 로고
    • The catalytic pathway of horseradish peroxidase at high resolution
    • DOI 10.1038/417463a
    • G.I. Berglund, G.H. Carlsson, A.T. Smith, H. Szöke, A. Henriksen, and J. Hajdu The catalytic pathway of horseradish peroxidase at high resolution Nature 417 2002 463 468 (Pubitemid 34563541)
    • (2002) Nature , vol.417 , Issue.6887 , pp. 463-468
    • Berglund, G.I.1    Carlsson, G.H.2    Smith, A.T.3    Szoke, H.4    Henriksen, A.5    Hajdu, J.6
  • 5
    • 0036086458 scopus 로고    scopus 로고
    • A microspectrophotometer for UV-visible absorption and fluorescence studies of protein crystals
    • DOI 10.1107/S0021889802003837
    • D. Bourgeois, X. Vernede, V. Adam, E. Fioravanti, and T. Ursby A microspectrophotometer for UV-visible absorption and fluoresence studies of protein crystals J. Appl. Crystallogr. 35 2002 319 326 (Pubitemid 34662861)
    • (2002) Journal of Applied Crystallography , vol.35 , Issue.3 , pp. 319-326
    • Bourgeois, D.1    Vernede, X.2    Adam, V.3    Fioravanti, E.4    Ursby, T.5
  • 6
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction
    • DOI 10.1021/bi010715u
    • V. Srajer, Z. Ren, T.-Y. Teng, M. Schmidt, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff, and K. Moffat Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction Biochemistry 40 2001 13802 13815 (Pubitemid 33078849)
    • (2001) Biochemistry , vol.40 , Issue.46 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.-Y.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 7
    • 0036282685 scopus 로고    scopus 로고
    • Defining redox state of X-ray crystal structures by single-crystal ultraviolet-visible microspectrophotometry
    • DOI 10.1016/S0076-6879(02)53057-3
    • C.M. Wilmot, T. Sjögren, G.H. Carlsson, G.I. Berglund, and J. Hajdu Defining redox state of X-ray crystal structures by single-crystal ultraviolet-visible microspectrophometry Meth. Enzymol. 353 2002 301 318 (Pubitemid 34625600)
    • (2002) Methods in Enzymology , vol.353 , pp. 301-318
    • Wilmot, C.M.1    Sjogren, T.2    Carlsson, G.H.3    Berglund, G.I.4    Hajdu, J.5
  • 9
    • 0025071357 scopus 로고
    • Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction
    • R. Henderson Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction Proc. R. Soc. Lond. B 241 1990 6 8 (Pubitemid 20256941)
    • (1990) Proceedings of the Royal Society B: Biological Sciences , vol.241 , Issue.1300 , pp. 6-8
    • Henderson, R.1
  • 10
    • 33645498518 scopus 로고    scopus 로고
    • Experimental determination of the radiation dose limit for cryocooled protein crystals
    • R.L. Owen, E. Rudino-Pinera, and E.F. Garman Experimental determination of the radiation dose limit for cryocooled protein crystals Proc. Natl Acad. Sci. USA 103 2006 4912 4917
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4912-4917
    • Owen, R.L.1    Rudino-Pinera, E.2    Garman, E.F.3
  • 11
    • 33644870851 scopus 로고    scopus 로고
    • Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
    • H.K. Leiros, J. Timmins, R.B. Ravelli, and S.M. McSweeney Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection? Acta Crystallogr. D Biol. Crystallogr. 62 2006 125 132
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 125-132
    • Leiros, H.K.1    Timmins, J.2    Ravelli, R.B.3    McSweeney, S.M.4
  • 12
    • 75749092651 scopus 로고    scopus 로고
    • Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures
    • A. Meents, S. Gutmann, A. Wagner, and C. Schulze-Briese Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures Proc. Natl Acad. Sci. USA 107 2010 1094 1099
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1094-1099
    • Meents, A.1    Gutmann, S.2    Wagner, A.3    Schulze-Briese, C.4
  • 14
    • 44449131445 scopus 로고    scopus 로고
    • The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection
    • DOI 10.1042/BJ20070921
    • H.-P. Hersleth, Y.-W. Hsiao, U. Ryde, C.H. Görbitz, and K.K. Andersson The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection Biochem. J. 412 2008 257 264 (Pubitemid 351758231)
    • (2008) Biochemical Journal , vol.412 , Issue.2 , pp. 257-264
    • Hersleth, H.-P.1    Hsiao, Y.-W.2    Ryde, U.3    Gorbitz, C.H.4    Andersson, K.K.5
  • 15
    • 33846112664 scopus 로고    scopus 로고
    • XANES measurements of the rate of radiation damage to selenomethionine side chains
    • DOI 10.1107/S0909049506048898
    • J.M. Holton XANES measurements of the rate of radiation damage to selenomethionine side chains J. Synchrotron Rad. 14 2007 51 72 (Pubitemid 46058906)
    • (2007) Journal of Synchrotron Radiation , vol.14 , Issue.1 , pp. 51-72
    • Holton, J.M.1
  • 17
    • 16244392086 scopus 로고    scopus 로고
    • When X-rays modify the protein structure: Radiation damage at work
    • DOI 10.1016/j.tibs.2005.02.009
    • O. Carugo, and K.D. Carugo When X-rays modify the protein structure: radiation damage at work Trends Biochem. Sci. 30 2005 213 219 (Pubitemid 40463311)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.4 , pp. 213-219
    • Carugo, O.1    Carugo, K.D.2
  • 19
    • 33846050557 scopus 로고    scopus 로고
    • Cryoradiolytic reduction of crystalline heme proteins: Analysis by UV-Vis spectroscopy and X-ray crystallography
    • DOI 10.1107/S0909049506049806
    • T. Beitlich, K. Kühnel, C. Schulze-Briese, R.L. Shoeman, and I. Schlichting Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-vis spectroscopy and X-ray crystallography J. Synchrotron Radiat. 14 2007 11 23 (Pubitemid 46058902)
    • (2007) Journal of Synchrotron Radiation , vol.14 , Issue.1 , pp. 11-23
    • Seitlich, T.1    Kuhnel, K.2    Schulze-Briese, C.3    Shoeman, R.L.4    Schlichting, I.5
  • 21
    • 34247525538 scopus 로고    scopus 로고
    • Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme
    • DOI 10.1126/science.1138885
    • G. Katona, P. Carpentier, V. Niviere, P. Amara, V. Adam, J. Ohana, N. Tsanov, and D. Bourgeois Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme Science 316 2007 449 453 (Pubitemid 46656070)
    • (2007) Science , vol.316 , Issue.5823 , pp. 449-453
    • Katona, G.1    Carpentier, P.2    Niviere, V.3    Amara, P.4    Adam, V.5    Ohana, J.6    Tsanov, N.7    Bourgeois, D.8
  • 23
    • 35948986658 scopus 로고    scopus 로고
    • Structural characterization of the fleeting ferric peroxo species in myoglobin: Experiment and theory
    • DOI 10.1021/ja076108x
    • M. Unno, H. Chen, S. Kusama, S. Shaik, and M. Ikeda-Saito Structural characterization of the fleeting ferric peroxo species in myoglobin: experiment and theory J. Am. Chem. Soc. 129 2007 13394 13395 (Pubitemid 350071760)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.44 , pp. 13394-13395
    • Unno, M.1    Chen, H.2    Kusama, S.3    Shaik, S.4    Ikeda-Saito, M.5
  • 26
    • 3342939208 scopus 로고    scopus 로고
    • Myoglobin
    • G.N. Phillips Jr. Myoglobin A. Messerschmidt, R. Huber, T. Poulos, K. Wieghardt, Hanbook of Metalloproteins vol. 1 2001 John Wiley & Son, Ltd Chichester 5 15
    • (2001) Hanbook of Metalloproteins , vol.1 , pp. 5-15
    • Phillips Jr., G.N.1
  • 28
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin centre stage
    • DOI 10.1016/S0968-0004(01)01824-2, PII S0968000401018242
    • M. Brunori Nitrc oxide moves myoglobin centre stages Trends Biochem. Sci. 26 2001 209 210 (Pubitemid 32289229)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.4 , pp. 209-210
    • Brunori, M.1
  • 29
    • 8844260650 scopus 로고    scopus 로고
    • Role of myoglobin in the antioxidant defense of the heart
    • DOI 10.1096/fj.03-1382.fje
    • U. Flögel, A. Gödecke, L.-O. Klotz, and J. Schrader Role of myoglobin in the antioxidant defense of the heart FASEB J. 18 2004 1156 1158 (Pubitemid 39561555)
    • (2004) FASEB Journal , vol.18 , Issue.10 , pp. 1156-1158
    • Flogel, U.1    Godecke, A.2    Klotz, L.-O.3    Schrader, J.4
  • 31
    • 0037386033 scopus 로고    scopus 로고
    • Emerging roles for myoglobin in the heart
    • DOI 10.1016/S1050-1738(02)00256-6, PII S1050173802002566
    • D.J. Garry, S.B. Kanatous, and P.P.A. Mammen Emerging roles for myoglobin in the heart Trends Cardiovasc. Med. 13 2003 111 116 (Pubitemid 36411806)
    • (2003) Trends in Cardiovascular Medicine , vol.13 , Issue.3 , pp. 111-116
    • Garry, D.J.1    Kanatous, S.B.2    Mammen, P.P.A.3
  • 32
    • 27744458259 scopus 로고    scopus 로고
    • Hemoglobin and myoglobin associated oxidative stress: From molecular mechanisms to disease states
    • DOI 10.2174/092986705774463021
    • B.J. Reeder, and M.T. Wilson Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease states Curr. Med. Chem. 12 2005 2741 2751 (Pubitemid 41601571)
    • (2005) Current Medicinal Chemistry , vol.12 , Issue.23 , pp. 2741-2751
    • Reeder, B.J.1    Wilson, M.T.2
  • 33
    • 0040970877 scopus 로고
    • Reaction of metmyoglobin with hydrogen peroxide
    • P. George, and D.H. Irvine Reaction of metmyoglobin with hydrogen peroxide Nature 168 1951 164 165
    • (1951) Nature , vol.168 , pp. 164-165
    • George, P.1    Irvine, D.H.2
  • 34
    • 0019321508 scopus 로고
    • The sterochemistry of peroxidases
    • T.L. Poulos, and J. Kraut The sterochemistry of peroxidases J. Biol. Chem. 255 1980 8199 8205
    • (1980) J. Biol. Chem. , vol.255 , pp. 8199-8205
    • Poulos, T.L.1    Kraut, J.2
  • 35
    • 0034634543 scopus 로고    scopus 로고
    • Formation of compound i in the reaction of native myoglobins with hydrogen peroxide
    • T. Egawa, H. Shimada, and Y. Ishimura Formation of compound I in the reaction of native myoglobins with hydrogen peroxide J. Biol. Chem. 275 2000 34858 34866
    • (2000) J. Biol. Chem. , vol.275 , pp. 34858-34866
    • Egawa, T.1    Shimada, H.2    Ishimura, Y.3
  • 36
    • 0031468071 scopus 로고    scopus 로고
    • On the formation and reactivity of compound I of the His-64 myoglobin mutants
    • DOI 10.1074/jbc.272.52.32735
    • T. Matsui, S.-i. Ozaki, and Y. Watanabe On the formation and reactivity of compound I of the His-64 myoglobin mutants J. Biol. Chem. 272 1997 32735 32738 (Pubitemid 28023603)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.52 , pp. 32735-32738
    • Matsui, T.1    Ozaki, S.-I.2    Watanabe, Y.3
  • 37
    • 58149337266 scopus 로고    scopus 로고
    • The influence of X-rays on the structural studies of peroxide-derived myoglobin intermediates
    • H.-P. Hersleth, Y.W. Hsiao, U. Ryde, C.H. Görbitz, and K.K. Andersson The influence of X-rays on the structural studies of peroxide-derived myoglobin intermediates Chem. Biodivers. 5 2008 2067 2089
    • (2008) Chem. Biodivers. , vol.5 , pp. 2067-2089
    • Hersleth, H.-P.1    Hsiao, Y.W.2    Ryde, U.3    Görbitz, C.H.4    Andersson, K.K.5
  • 39
    • 0036941303 scopus 로고    scopus 로고
    • An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2
    • DOI 10.1007/s007750100296
    • H.-P. Hersleth, B. Dalhus, C.H. Görbitz, and K.K. Andersson An iron hydroxide moiety in the 1.35 Å resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2 J. Biol. Inorg. Chem. 7 2002 299 304 (Pubitemid 36056381)
    • (2002) Journal of Biological Inorganic Chemistry , vol.7 , Issue.3 , pp. 299-304
    • Hersleth, H.-P.1    Dalhus, B.2    Gorbitz, C.H.3    Andersson, K.K.4
  • 41
    • 61449123145 scopus 로고    scopus 로고
    • A new on-axis multimode spectrometer for the macromolecular crystallography beamlines of the Swiss Light Source
    • R.L. Owen, A.R. Pearson, A. Meents, P. Boehler, V. Thominet, and C. Schulze-Briese A new on-axis multimode spectrometer for the macromolecular crystallography beamlines of the Swiss Light Source J. Synchrotron Radiat. 16 2009 173 182
    • (2009) J. Synchrotron Radiat. , vol.16 , pp. 173-182
    • Owen, R.L.1    Pearson, A.R.2    Meents, A.3    Boehler, P.4    Thominet, V.5    Schulze-Briese, C.6
  • 42
    • 4043099008 scopus 로고    scopus 로고
    • X-ray absorption by macromolecular crystals: The effects of wavelength and crystal composition on absorbed dose
    • J.W. Murray, R.B.G. Ravelli, and E.F. Garman X-ray absorption by macromolecular crystals: the effects of wavelength and crystal composition on absorbed dose J. Appl. Crystallogr. 37 2004 513 522
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 513-522
    • Murray, J.W.1    Ravelli, R.B.G.2    Garman, E.F.3
  • 43
    • 61449149590 scopus 로고    scopus 로고
    • Absorbed dose calculations for macromolecular crystals: Improvements to RADDOSE
    • K.S. Paithankar, R.L. Owen, and E.F. Garman Absorbed dose calculations for macromolecular crystals: improvements to RADDOSE J. Synchrotron Radiat. 16 2009 152 162
    • (2009) J. Synchrotron Radiat. , vol.16 , pp. 152-162
    • Paithankar, K.S.1    Owen, R.L.2    Garman, E.F.3
  • 45
    • 77950630771 scopus 로고    scopus 로고
    • Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate
    • Y.T. Meharenna, T. Doukov, H.Y. Li, S.M. Soltis, and T.L. Poulos Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate Biochemistry 49 2010 2984 2986
    • (2010) Biochemistry , vol.49 , pp. 2984-2986
    • Meharenna, Y.T.1    Doukov, T.2    Li, H.Y.3    Soltis, S.M.4    Poulos, T.L.5
  • 46
    • 0032558402 scopus 로고    scopus 로고
    • Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced forms
    • DOI 10.1021/bi981380s
    • M. Eriksson, A. Jordan, and H. Eklund Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced forms Biochemistry 37 1998 13359 13369 (Pubitemid 28449581)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13359-13369
    • Eriksson, M.1    Jordan, A.2    Eklund, H.3
  • 47
    • 0018802419 scopus 로고
    • Transient intermediates in the reduction of Fe(III) myoglobin-ligand complexes by electrons at low temperature
    • Z. Gasyna Transient intermediates in the reduction of Fe(III) myoglobin-ligand complexes by electrons at low temperature Biochim. Biophys. Acta 577 1979 207 216
    • (1979) Biochim. Biophys. Acta , vol.577 , pp. 207-216
    • Gasyna, Z.1
  • 48
    • 0001098626 scopus 로고
    • Resonance Raman-spectra of octaethylporphyrinato-Ni(Ii) and meso-deuterated and N-15 substituted derivatives. 2. Normal coordinate analysis
    • M. Abe, T. Kitagawa, and Y. Kyogoku Resonance Raman-spectra of octaethylporphyrinato-Ni(Ii) and meso-deuterated and N-15 substituted derivatives. 2. Normal coordinate analysis J. Chem. Phys. 69 1978 4526 4534
    • (1978) J. Chem. Phys. , vol.69 , pp. 4526-4534
    • Abe, M.1    Kitagawa, T.2    Kyogoku, Y.3
  • 49
    • 0001098625 scopus 로고
    • Resonance Raman-spectra of octaethylporphyrinato-Ni(Ii) and meso-deuterated and N-15 substituted derivatives. 1. Observation and assignments of non-fundamental Raman lines
    • T. Kitagawa, M. Abe, and H. Ogoshi Resonance Raman-spectra of octaethylporphyrinato-Ni(Ii) and meso-deuterated and N-15 substituted derivatives. 1. Observation and assignments of non-fundamental Raman lines J. Chem. Phys. 69 1978 4516 4525
    • (1978) J. Chem. Phys. , vol.69 , pp. 4516-4525
    • Kitagawa, T.1    Abe, M.2    Ogoshi, H.3
  • 51
    • 38949111373 scopus 로고    scopus 로고
    • The impact of altered protein-heme interactions on the resonance raman spectra of heme proteins. Studies of heme rotational disorder
    • DOI 10.1002/bip.20887
    • F. Rwere, P.J. Mak, and J.R. Kincaid The impact of altered protein-heme interactions on the resonance Raman spectra of heme proteins. Studies of heme rotational disorder Biopolymers 89 2008 179 186 (Pubitemid 351220111)
    • (2008) Biopolymers , vol.89 , Issue.3 , pp. 179-186
    • Rwere, F.1    Mak, P.J.2    Kincaid, J.R.3
  • 52
    • 0000990855 scopus 로고
    • Raman intensities of the A1 lines of oxyanions
    • G.W. Chantry, and R.A. Plane Raman intensities of the A1 lines of oxyanions J. Chem. Phys. 32 1960 319 321
    • (1960) J. Chem. Phys. , vol.32 , pp. 319-321
    • Chantry, G.W.1    Plane, R.A.2
  • 53
    • 0021777960 scopus 로고
    • Resonance Raman spectroscopy as a probe of heme protein structure and dynamics
    • T.G. Spiro Resonance Raman spectroscopy as a probe of heme protein structure and dynamics Adv. Protein Chem. 37 1985 111 159
    • (1985) Adv. Protein Chem. , vol.37 , pp. 111-159
    • Spiro, T.G.1
  • 54
    • 0043097984 scopus 로고
    • Metalloporphyrin structure and dynamics from resonance Raman-spectroscopy
    • T.G. Spiro, R.S. Czernuszewicz, and X.Y. Li Metalloporphyrin structure and dynamics from resonance Raman-spectroscopy Coord. Chem. Rev. 100 1990 541 571
    • (1990) Coord. Chem. Rev. , vol.100 , pp. 541-571
    • Spiro, T.G.1    Czernuszewicz, R.S.2    Li, X.Y.3
  • 55
    • 77953522703 scopus 로고    scopus 로고
    • Tracking flavin conformations in protein crystal structures with Raman spectroscopy and QM/MM calculations
    • Å.K. Røhr, H.-P. Hersleth, and K.K. Andersson Tracking flavin conformations in protein crystal structures with Raman spectroscopy and QM/MM calculations Angew. Chem. Int. Ed. 49 2010 2324 2327
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 2324-2327
    • Røhr, Å.K.1    Hersleth, H.-P.2    Andersson, K.K.3
  • 56
    • 13844270250 scopus 로고    scopus 로고
    • The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: Quantum refinement
    • DOI 10.1529/biophysj.104.041590
    • K. Nilsson, H.-P. Hersleth, T.H. Rod, K.K. Andersson, and U. Ryde The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement Biophys. J. 87 2004 3437 3447 (Pubitemid 40468597)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 3437-3447
    • Nilsson, K.1    Hersleth, H.-P.2    Rod, T.H.3    Andersson, K.K.4    Ryde, U.5


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