메뉴 건너뛰기




Volumn 1824, Issue 9, 2012, Pages 1016-1023

Metal binding properties and structure of a type III metallothionein from the metal hyperaccumulator plant Noccaea caerulescens

Author keywords

Heavy metal; IR spectroscopy; Mass spectrometry; Metal binding; Metallothionein; Plant

Indexed keywords

CADMIUM; COPPER; DEUTERIUM; LEAD; METALLOTHIONEIN III; ZINC;

EID: 84862599601     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.05.010     Document Type: Article
Times cited : (20)

References (69)
  • 1
    • 59849085357 scopus 로고    scopus 로고
    • Molecular mechanisms of metal hyperaccumulation in plants
    • N. Verbruggen, C. Hermans, and H. Schat Molecular mechanisms of metal hyperaccumulation in plants New Phytol. 181 2009 759 776
    • (2009) New Phytol. , vol.181 , pp. 759-776
    • Verbruggen, N.1    Hermans, C.2    Schat, H.3
  • 2
    • 77952497470 scopus 로고    scopus 로고
    • Hyperaccumulation in plants
    • Kramer U. Metal Hyperaccumulation in plants Annu. Rev. Plant Biol. 61 2010 517 534
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 517-534
    • Metal, K.U.1
  • 4
    • 7544242621 scopus 로고    scopus 로고
    • Evidence for copper homeostasis function of metallothionein (MT3) in the hyperaccumulator Thlaspi caerulescens
    • DOI 10.1016/j.febslet.2004.08.084, PII S0014579304011688
    • N.H. Roosens, C. Bernard, R. Leplae, and N. Verbruggen Evidence for copper homeostasis function metallothionein of metallothionein (MT3) in the hyperaccumulator Thlaspi caerulescens FEBS Lett. 577 2004 9 16 (Pubitemid 39452354)
    • (2004) FEBS Letters , vol.577 , Issue.1-2 , pp. 9-16
    • Roosens, N.H.1    Bernard, C.2    Leplae, R.3    Verbruggen, N.4
  • 6
    • 33751119021 scopus 로고    scopus 로고
    • Large expression differences in genes for iron and zinc homeostasis, stress response, and lignin biosynthesis distinguish roots of Arabidopsis thaliana and the related metal hyperaccumulator Thlaspi caerulescens
    • DOI 10.1104/pp.106.082073
    • J.E. van de Mortel, V.L. Almar, H. Schat, J. Kwekkeboom, S. Coughlan, P.D. Moerland, v.T. Ver Loren, M. Koornneef, and M.G. Aarts Large expression differences in genes for iron and zinc homeostasis, stress response, and lignin biosynthesis distinguish roots of Arabidopsis thaliana and the related metal hyperaccumulator Thlaspi caerulescens Plant Physiol. 142 2006 1127 1147 (Pubitemid 44764637)
    • (2006) Plant Physiology , vol.142 , Issue.3 , pp. 1127-1147
    • Van De Mortel, J.E.1    Villanueva, L.A.2    Schat, H.3    Kwekkeboom, J.4    Coughlan, S.5    Moerland, P.D.6    Van Themaat, E.V.L.7    Koornneef, M.8    Aarts, M.G.M.9
  • 7
    • 38849135951 scopus 로고    scopus 로고
    • Expression differences for genes involved in lignin, glutathione and sulphate metabolism in response to cadmium in Arabidopsis thaliana and the related Zn/Cd-hyperaccumulator Thlaspi caerulescens
    • DOI 10.1111/j.1365-3040.2007.01764.x
    • J.E. van de Mortel, H. Schat, P.D. Moerland, v.T. Ver Loren, E.S. van der, H. Blankestijn, A. Ghandilyan, S. Tsiatsiani, and M.G. Aarts Expression differences for genes involved in lignin, glutathione and sulphate metabolism in response to cadmium in Arabidopsis thaliana and the related Zn/Cd-hyperaccumulator Thlaspi caerulescens Plant Cell Environ. 31 2008 301 324 (Pubitemid 351207254)
    • (2008) Plant, Cell and Environment , vol.31 , Issue.3 , pp. 301-324
    • Van De Mortel, J.E.1    Schat, H.2    Moerland, P.D.3    Van Themaat, E.V.L.4    Van Der Ent, S.5    Blankestijn, H.6    Ghandilyan, A.7    Tsiatsiani, S.8    Aarts, M.G.M.9
  • 8
    • 33947463103 scopus 로고    scopus 로고
    • A cadmium protein from equine kidney cortex
    • M. Margoshes, and B.L. Vallee A cadmium protein from equine kidney cortex J. Am. Chem. Soc. 79 2002 4813 4814
    • (2002) J. Am. Chem. Soc. , vol.79 , pp. 4813-4814
    • Margoshes, M.1    Vallee, B.L.2
  • 9
    • 0002599375 scopus 로고    scopus 로고
    • Metallothionein: Molecular evolution and classification
    • C.D. Klaassen, Birkhauser Verlag Basel
    • P.A. Binz, and J.H. Kägi Metallothionein: molecular evolution and classification C.D. Klaassen, Metallothionein IV 1999 Birkhauser Verlag Basel 7 13
    • (1999) Metallothionein IV , pp. 7-13
    • Binz, P.A.1    Kägi, J.H.2
  • 10
    • 80755189923 scopus 로고    scopus 로고
    • Structural features specific to plant metallothioneins
    • E. Freisinger Structural features specific to plant metallothioneins J. Biol. Inorg. Chem. 16 2011 1035 1045
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 1035-1045
    • Freisinger, E.1
  • 12
    • 0020478715 scopus 로고
    • Structure of an invertebrate metallothionein from Scylla serrata
    • J.D. Otvos, R.W. Olafson, and I.M. Armitage Structure of an invertebrate metallothionein from Scylla serrata J. Biol. Chem. 257 1982 2427 2431
    • (1982) J. Biol. Chem. , vol.257 , pp. 2427-2431
    • Otvos, J.D.1    Olafson, R.W.2    Armitage, I.M.3
  • 14
    • 61349154809 scopus 로고    scopus 로고
    • The beta(E)-domain of wheat E(c)-1 metallothionein: A metal-binding domain with a distinctive structure
    • E.A. Peroza, R. Schmucki, P. Guntert, E. Freisinger, and O. Zerbe The beta(E)-domain of wheat E(c)-1 metallothionein: a metal-binding domain with a distinctive structure J. Mol. Biol. 387 2009 207 218
    • (2009) J. Mol. Biol. , vol.387 , pp. 207-218
    • Peroza, E.A.1    Schmucki, R.2    Guntert, P.3    Freisinger, E.4    Zerbe, O.5
  • 15
    • 80051551700 scopus 로고    scopus 로고
    • Protein and metal cluster structure of the wheat metallothionein domain gamma-E(c)-1: The second part of the puzzle
    • J. Loebus, E.A. Peroza, N. Bluthgen, T. Fox, W. Meyer-Klaucke, O. Zerbe, and E. Freisinger Protein and metal cluster structure of the wheat metallothionein domain gamma-E(c)-1: the second part of the puzzle J. Biol. Inorg. Chem. 16 2011 683 694
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 683-694
    • Loebus, J.1    Peroza, E.A.2    Bluthgen, N.3    Fox, T.4    Meyer-Klaucke, W.5    Zerbe, O.6    Freisinger, E.7
  • 17
    • 33645466820 scopus 로고    scopus 로고
    • Determination of the Cd/S cluster stoichiometry in Fucus vesiculosus metallothionein
    • M.E. Merrifield, J. Chaseley, P. Kille, and M.J. Stillman Determination of the Cd/S cluster stoichiometry in Fucus vesiculosus metallothionein Chem. Res. Toxicol. 19 2006 365 375
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 365-375
    • Merrifield, M.E.1    Chaseley, J.2    Kille, P.3    Stillman, M.J.4
  • 18
    • 34547430481 scopus 로고    scopus 로고
    • II-binding abilities of recombinant Quercus suber metallothionein: Bridging the gap between phytochelatins and metallothioneins
    • DOI 10.1007/s00775-007-0241-y
    • J. Domenech, R. Orihuela, G. Mir, M. Molinas, S. Atrian, and M. Capdevila The Cd(II)-binding abilities of recombinant Quercus suber metallothionein: bridging the gap between phytochelatins and metallothioneins J. Biol. Inorg. Chem. 12 2007 867 882 (Pubitemid 47174876)
    • (2007) Journal of Biological Inorganic Chemistry , vol.12 , Issue.6 , pp. 867-882
    • Domenech, J.1    Orihuela, R.2    Mir, G.3    Molinas, M.4    Atrian, S.5    Capdevila, M.6
  • 19
    • 34250317473 scopus 로고    scopus 로고
    • Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: Insights by vibrational spectroscopy
    • DOI 10.1002/bip.20729
    • J. Domenech, A. Tinti, M. Capdevila, S. Atrian, and A. Torreggiani Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy Biopolymers 86 2007 240 248 (Pubitemid 46910395)
    • (2007) Biopolymers , vol.86 , Issue.3 , pp. 240-248
    • Domenech, J.1    Tinti, A.2    Capdevila, M.3    Atrian, S.4    Torreggiani, A.5
  • 20
    • 34147110950 scopus 로고    scopus 로고
    • c-1 metallothionein: Evidence supporting two separate metal thiolate clusters
    • DOI 10.1007/s00775-006-0195-5
    • E.A. Peroza, and E. Freisinger Metal ion binding properties of Triticum aestivum Ec-1 metallothionein: evidence supporting two separate metal thiolate clusters J. Biol. Inorg. Chem. 12 2007 377 391 (Pubitemid 46569281)
    • (2007) Journal of Biological Inorganic Chemistry , vol.12 , Issue.3 , pp. 377-391
    • Peroza, E.A.1    Freisinger, E.2
  • 21
    • 3042589727 scopus 로고    scopus 로고
    • A novel CPx-ATPase from the cadmium hyperaccumulator Thlaspi caerulescens
    • DOI 10.1016/j.febslet.2004.05.036, PII S0014579304006775
    • C. Bernard, N. Roosens, P. Czernic, M. Lebrun, and N. Verbruggen A novel CPx-ATPase from the cadmium hyperaccumulator Thlaspi caerulescens FEBS Lett. 569 2004 140 148 (Pubitemid 38844607)
    • (2004) FEBS Letters , vol.569 , Issue.1-3 , pp. 140-148
    • Bernard, C.1    Roosens, N.2    Czernic, P.3    Lebrun, M.4    Verbruggen, N.5
  • 22
    • 27644589548 scopus 로고    scopus 로고
    • Variations in plant metallothioneins: The heavy metal hyperaccumulator Thlaspi caerulescens as a study case
    • DOI 10.1007/s00425-005-0006-1
    • N.H. Roosens, R. Leplae, C. Bernard, and N. Verbruggen Variations in plant metallothioneins: the heavy metal hyperaccumulator Thlaspi caerulescens as a study case Planta 222 2005 716 729 (Pubitemid 41567035)
    • (2005) Planta , vol.222 , Issue.4 , pp. 716-729
    • Roosens, N.H.1    Leplae, R.2    Bernard, C.3    Verbruggen, N.4
  • 23
    • 15744374025 scopus 로고    scopus 로고
    • Microwave-assisted acid hydrolysis of proteins combined with liquid chromatography MALDI MS/MS for protein identification
    • DOI 10.1016/j.jasms.2004.12.017, PII S1044030504008529
    • H. Zhong, S.L. Marcus, and L. Li Microwave-assisted acid hydrolysis of proteins combined with liquid chromatography MALDI MS/MS for protein identification J. Am. Soc. Mass Spectrom. 16 2005 471 481 (Pubitemid 40410033)
    • (2005) Journal of the American Society for Mass Spectrometry , vol.16 , Issue.4 , pp. 471-481
    • Zhong, H.1    Marcus, S.L.2    Li, L.3
  • 26
    • 4243514781 scopus 로고
    • Subtraction of atmospheric water contribution in Fourier transform infrared spectroscopy of biological membranes and proteins
    • E. Goormaghtigh, and J.M. Ruysschaert Subtraction of atmospheric water contribution in Fourier transform infrared spectroscopy of biological membranes and proteins Spectrochim. Acta 50A 1994 2137 2144
    • (1994) Spectrochim. Acta , vol.50 A , pp. 2137-2144
    • Goormaghtigh, E.1    Ruysschaert, J.M.2
  • 27
    • 0027999624 scopus 로고
    • +-ATPase monitored by hydrogen/deuterium exchange kinetics. A Fourier transformed infrared spectroscopy approach
    • +-ATPase monitored by hydrogen/deuterium exchange kinetics. A Fourier transformed infrared spectroscopy approach J. Biol. Chem. 269 1994 27409 27413
    • (1994) J. Biol. Chem. , vol.269 , pp. 27409-27413
    • Goormaghtigh, E.1    Vigneron, L.2    Scarborough, G.A.3    Ruysschaert, J.M.4
  • 28
    • 0029813440 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange kinetics of apolipophorin-III in lipid-free and phospholipid-bound states. An analysis by Fourier transform infrared spectroscopy
    • DOI 10.1074/jbc.271.38.23089
    • V. Raussens, V. Narayanaswami, E. Goormaghtigh, R.O. Ryan, and J.M. Ruysschaert Hydrogen/deuterium exchange kinetics of apolipophorin-III in lipid-free and phospholipid-bound states. An analysis by Fourier transform infrared spectroscopy J. Biol. Chem. 271 1996 23089 23095 (Pubitemid 26314742)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.38 , pp. 23089-23095
    • Raussens, V.1    Narayanaswami, V.2    Goormaghtigh, E.3    Ryan, R.O.4    Ruysschaert, J.-M.5
  • 30
    • 33846859548 scopus 로고    scopus 로고
    • Biochemical interaction analysis on ATR devices: A wet chemistry approach for surface functionalization
    • DOI 10.1021/la061627j
    • M. Voue, E. Goormaghtigh, F. Homble, J. Marchand-Brynaert, J. Conti, S. Devouge, and J. De Coninck Biochemical interaction analysis on ATR devices: a wet chemistry approach for surface functionalization Langmuir 23 2007 949 955 (Pubitemid 46226616)
    • (2007) Langmuir , vol.23 , Issue.2 , pp. 949-955
    • Voue, M.1    Goormaghtigh, E.2    Homble, F.3    Marchand-Brynaert, J.4    Conti, J.5    Devouge, S.6    De Coninck, J.7
  • 32
    • 0001511119 scopus 로고    scopus 로고
    • +-ATPase between the E1 and E2 conformations. An attenuated total reflection infrared spectroscopy, UV circular dichroism and raman spectroscopy study
    • DOI 10.1046/j.1432-1327.1999.00365.x
    • +-ATPase between the E1 and E2 conformations an attenuated total reflection infrared spectroscopy, UV circular dichroism and Raman spectroscopy study Eur. J. Biochem. 262 1999 176 183 (Pubitemid 29242624)
    • (1999) European Journal of Biochemistry , vol.262 , Issue.1 , pp. 176-183
    • Raussens, V.1    Pezolet, M.2    Ruysschaert, J.-M.3    Goormaghtigh, E.4
  • 33
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method
    • DOI 10.1016/S0003-2697(03)00285-9
    • V. Raussens, J.M. Ruysschaert, and E. Goormaghtigh Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method Anal. Biochem. 319 2003 114 121 (Pubitemid 36802149)
    • (2003) Analytical Biochemistry , vol.319 , Issue.1 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 34
    • 0028986621 scopus 로고
    • Reaction of 111Cd7-metallothionein with EDTA. A reappraisal
    • T. Gan, A. Munoz, C.F. Shaw III, and D.H. Petering Reaction of 111Cd7-metallothionein with EDTA. A reappraisal J. Biol. Chem. 270 1995 5339 5345
    • (1995) J. Biol. Chem. , vol.270 , pp. 5339-5345
    • Gan, T.1    Munoz, A.2    Shaw Iii, C.F.3    Petering, D.H.4
  • 35
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • S. Krimm, and J. Bandekar Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Adv. Protein Chem. 38 1986 181 364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 36
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures, subcell
    • E. Goormaghtigh, V. Cabiaux, and J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures, subcell Biochemistry 23 1994 405 450
    • (1994) Biochemistry , vol.23 , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 37
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds, subcell
    • E. Goormaghtigh, V. Cabiaux, and J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds, subcell Biochemistry 23 1994 329 362
    • (1994) Biochemistry , vol.23 , pp. 329-362
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 38
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • DOI 10.1017/S0033583502003815
    • A. Barth, and C. Zscherp What vibrations tell us about proteins Q. Rev. Biophys. 35 2002 369 430 (Pubitemid 36207229)
    • (2002) Quarterly Reviews of Biophysics , vol.35 , Issue.4 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 40
    • 33646196840 scopus 로고    scopus 로고
    • Evaluation of the information content in infrared spectra for protein secondary structure determination
    • E. Goormaghtigh, J.M. Ruysschaert, and V. Raussens Evaluation of the information content in infrared spectra for protein secondary structure determination Biophys. J. 90 2006 2946 2957
    • (2006) Biophys. J. , vol.90 , pp. 2946-2957
    • Goormaghtigh, E.1    Ruysschaert, J.M.2    Raussens, V.3
  • 41
    • 0042510990 scopus 로고    scopus 로고
    • Rationally selected basis proteins: A new approach to selecting proteins for spectroscopic secondary structure analysis
    • DOI 10.1110/ps.0354703
    • K.A. Oberg, J.M. Ruysschaert, and E. Goormaghtigh Rationally selected basis proteins: a new approach to selecting proteins for spectroscopic secondary structure analysis Prot. Sci. 12 2003 2015 2031 (Pubitemid 37022823)
    • (2003) Protein Science , vol.12 , Issue.9 , pp. 2015-2031
    • Oberg, K.A.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 43
    • 66349121915 scopus 로고    scopus 로고
    • Zinc and cadmium complexes of a plant metallothionein under radical stress: Desulfurisation reactions associated with the formation of trans-lipids in model membranes
    • A. Torreggiani, J. Domènech, R. Orihuela, C. Ferreri, S. Atrian, M. Capdevila, and C. Chatgilialoglu Zinc and cadmium complexes of a plant metallothionein under radical stress: desulfurisation reactions associated with the formation of trans-lipids in model membranes Chemistry 15 2009 6015 6024
    • (2009) Chemistry , vol.15 , pp. 6015-6024
    • Torreggiani, A.1    Domènech, J.2    Orihuela, R.3    Ferreri, C.4    Atrian, S.5    Capdevila, M.6    Chatgilialoglu, C.7
  • 44
    • 58149340121 scopus 로고    scopus 로고
    • Raman study of in vivo synthesized Zn(II)-metallothionein complexes: Structural insight into metal clusters and protein folding
    • A. Torreggiani, J. Domenech, S. Atrian, M. Capdevila, and A. Tinti Raman study of in vivo synthesized Zn(II)-metallothionein complexes: structural insight into metal clusters and protein folding Biopolymers 89 2008 1114 1124
    • (2008) Biopolymers , vol.89 , pp. 1114-1124
    • Torreggiani, A.1    Domenech, J.2    Atrian, S.3    Capdevila, M.4    Tinti, A.5
  • 45
    • 14844328678 scopus 로고    scopus 로고
    • Sensor applications of attenuated total reflection infrared spectroscopy
    • DOI 10.1016/j.talanta.2004.07.052, PII S0039914004005995, Optical Waveguide Analysis
    • C. Vigano, J.M. Ruyssehaert, and E. Goormaghtigh Sensor applications of attenuated total reflection infrared spectroscopy Talanta 65 2005 1132 1142 (Pubitemid 40348668)
    • (2005) Talanta , vol.65 , Issue.5 , pp. 1132-1142
    • Vigano, C.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 46
    • 4143125835 scopus 로고    scopus 로고
    • +-ATPase monitored by difference Fourier-transform infrared spectroscopy and hydrogen/deuterium exchange
    • DOI 10.1042/BJ20040277
    • +-ATPase monitored by difference Fourier-transform infrared spectroscopy and hydrogen/deuterium exchange Biochem. J. 382 2004 121 129 (Pubitemid 39141573)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , pp. 121-129
    • Scheirlinckx, F.1    Raussens, V.2    Ruysschaert, J.-M.3    Goormaghtigh, E.4
  • 47
    • 0022020855 scopus 로고
    • Hydrogen-exchange evidence for distinct structural classes in globular proteins
    • R.B. Gregory, and R. Lumry Hydrogen-exchange evidence for distinct structural classes in globular proteins Biopolymers 24 1985 301 326
    • (1985) Biopolymers , vol.24 , pp. 301-326
    • Gregory, R.B.1    Lumry, R.2
  • 48
    • 0019011405 scopus 로고
    • Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants
    • D.G. Knox, and A. Rosenberg Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants Biopolymers 19 1980 1049 1068
    • (1980) Biopolymers , vol.19 , pp. 1049-1068
    • Knox, D.G.1    Rosenberg, A.2
  • 50
    • 0030728709 scopus 로고    scopus 로고
    • Amide-proton exchange of water-soluble proteins of different structural classes studied at the submolecular level by infrared spectroscopy
    • DOI 10.1021/bi971337p
    • H.H. de-Jongh, E. Goormaghtigh, and J.M. Ruysschaert Amide-proton exchange of water-soluble proteins of different structural classes studied at the submolecular level by infrared spectroscopy Biochemistry 36 1997 13603 13610 (Pubitemid 27481607)
    • (1997) Biochemistry , vol.36 , Issue.44 , pp. 13603-13610
    • De Jongh, H.H.J.1    Goormaghtigh, E.2    Ruysschaert, J.-M.3
  • 51
    • 36049049557 scopus 로고    scopus 로고
    • Infrared spectroscopy study on the conformational changes leading to pore formation of the toxin sticholysin II
    • DOI 10.1529/biophysj.106.102566
    • Alegre-Cebollada J., A.M. del Pozo, J.G. Gavilanes, and E. Goormaghtigh Infrared spectroscopy study on the conformational changes leading to pore formation of the toxin sticholysin II Biophys. J. 93 2007 3191 3201 (Pubitemid 350097109)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 3191-3201
    • Alegre-Cebollada, J.1    Del Pozo, A.M.2    Gavilanes, J.G.3    Goormaghtigh, E.4
  • 52
    • 1242294450 scopus 로고    scopus 로고
    • Phosphorylation-induced Conformational Changes of Cystic Fibrosis Transmembrane Conductance Regulator Monitored by Attenuated Total Reflection-Fourier Transform IR Spectroscopy and Fluorescence Spectroscopy
    • DOI 10.1074/jbc.M311014200
    • V. Grimard, C.H. Li, M. Ramjeesingh, C.E. Bear, E. Goormaghtigh, and J.M. Ruysschaert Phosphorylation-induced conformational changes of cystic fibrosis transmembrane conductance regulator monitored by attenuated total reflection-Fourier transform IR spectroscopy and fluorescence spectroscopy J. Biol. Chem. 279 2004 5528 5536 (Pubitemid 38220578)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5528-5536
    • Grimard, V.1    Li, C.2    Ramjeesingh, M.3    Bear, C.E.4    Goormaghtigh, E.5    Ruysschaert, J.-M.6
  • 53
    • 0029784872 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted P- glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis
    • DOI 10.1074/jbc.271.40.24617
    • N. Sonveaux, A.B. Shapiro, E. Goormaghtigh, V. Ling, and J.M. Ruysschaert Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis J. Biol. Chem. 271 1996 24617 24624 (Pubitemid 26333203)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.40 , pp. 24617-24624
    • Sonveaux, N.1    Shapiro, A.B.2    Goormaghtigh, E.3    Ling, V.4    Ruysschaert, J.-M.5
  • 54
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • DOI 10.1016/S0079-6107(00)00021-3, PII S0079610700000213
    • A. Barth The infrared absorption of amino acid side chains Prog. Biophys. Mol. Biol. 74 2000 141 173 (Pubitemid 32168153)
    • (2000) Progress in Biophysics and Molecular Biology , vol.74 , Issue.3-5 , pp. 141-173
    • Barth, A.1
  • 55
    • 0028723860 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange
    • E. Goormaghtigh, V. Cabiaux, and J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange Subcell. Biochem. 23 1994 363 403
    • (1994) Subcell. Biochem. , vol.23 , pp. 363-403
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 56
    • 0036479246 scopus 로고    scopus 로고
    • Study of amide-proton exchange of Escherichia coli melibiose permease by attenuated total reflection-fourier transform infrared spectroscopy. Evidence of structure modulation by substrate binding
    • DOI 10.1074/jbc.M105466200
    • N. Dave, V.A. Lorenz-Fonfria, J. Villaverde, R. Lemonnier, G. Leblanc, and E. Padros Study of amide-proton exchange of Escherichia coli melibiose permease by attenuated total reflection-Fourier transform infrared spectroscopy: evidence of structure modulation by substrate binding J. Biol. Chem. 277 2002 3380 3387 (Pubitemid 34953206)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3380-3387
    • Dave, N.1    Lorenz-Fonfria, V.A.2    Villaverde, J.3    Lemonnier, R.4    Leblanc, G.5    Padros, E.6
  • 57
    • 0025608693 scopus 로고
    • Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange
    • T.N. Earnest, J. Herzfeld, and K.J. Rothschild Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange Biophys. J. 58 1990 1539 1546
    • (1990) Biophys. J. , vol.58 , pp. 1539-1546
    • Earnest, T.N.1    Herzfeld, J.2    Rothschild, K.J.3
  • 58
    • 0028825381 scopus 로고
    • Structure of both the ligand- and lipid-dependent channel-inactive states of the nicotinic acetylcholine receptor probed by FTIR spectroscopy and hydrogen exchange
    • N. Methot, C.N. Demers, and J.E. Baenziger Structure of both the ligand- and lipid-dependent channel-inactive states of the nicotinic acetylcholine receptor probed by FTIR spectroscopy and hydrogen exchange Biochemistry 34 1995 15142 15149
    • (1995) Biochemistry , vol.34 , pp. 15142-15149
    • Methot, N.1    Demers, C.N.2    Baenziger, J.E.3
  • 59
    • 0031972563 scopus 로고    scopus 로고
    • Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups
    • P. Rath, W.J. DeGrip, and K.J. Rothschild Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups Biophys. J. 74 1998 192 198 (Pubitemid 28041749)
    • (1998) Biophysical Journal , vol.74 , Issue.1 , pp. 192-198
    • Rath, P.1    DeGrip, W.J.2    Rothschild, K.J.3
  • 60
    • 0026482964 scopus 로고
    • FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane alpha-helices of membrane proteins
    • Y.P. Zhang, R.N. Lewis, R.S. Hodges, and R.N. McElhaney FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane alpha-helices of membrane proteins Biochemistry 31 1992 11572 11578
    • (1992) Biochemistry , vol.31 , pp. 11572-11578
    • Zhang, Y.P.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 61
    • 33751547229 scopus 로고    scopus 로고
    • Spectroscopic characterization of a fruit-specific metallothionein: M. acuminata MT3
    • E. Freisinger Spectroscopic characterization of a fruit-specific metallothionein: M. acuminata MT3 Inorg. Chim. Acta 360 2007 369 380
    • (2007) Inorg. Chim. Acta , vol.360 , pp. 369-380
    • Freisinger, E.1
  • 62
    • 0036489620 scopus 로고    scopus 로고
    • Isolation and characterisation of two divergent type 3 metallothioneins from oil palm, Elaeis guineensis
    • DOI 10.1016/S0981-9428(02)01366-9, PII S0981942802013669
    • S.N.A. Abdullah, S.C. Cheah, and D.J. Murphy Isolation and characterisation of two divergent type 3 metallothioneins from oil palm, Elaeis guineensis Plant Physiol. Biochem. 40 2002 255 263 (Pubitemid 35235335)
    • (2002) Plant Physiology and Biochemistry , vol.40 , Issue.3 , pp. 255-263
    • Akmar Abdullah, S.N.1    Cheah, S.C.2    Murphy, D.J.3
  • 63
    • 0000140123 scopus 로고
    • Spectroscopic studies and characterization of metallothioneins containing mercury, lead and bismuth
    • W. Bernhard, M. Good, M. Vasak, and J.H.R. Kagi Spectroscopic studies and characterization of metallothioneins containing mercury, lead and bismuth Inorg. Chim. Acta 79 1983 154 155
    • (1983) Inorg. Chim. Acta , vol.79 , pp. 154-155
    • Bernhard, W.1    Good, M.2    Vasak, M.3    Kagi, J.H.R.4
  • 64
    • 0002721858 scopus 로고
    • Biochemical interactions of mercury, cadmium and lead
    • J.O. Nriagu, Springer-Verlag Berlin
    • J.H.R. Kagi, and H.-J. Hapke Biochemical interactions of mercury, cadmium and lead J.O. Nriagu, Changing metal cycles and human health 1984 Springer-Verlag Berlin 237 250
    • (1984) Changing Metal Cycles and Human Health , pp. 237-250
    • Kagi, J.H.R.1    Hapke, H.-J.2
  • 65
    • 34548753956 scopus 로고    scopus 로고
    • Toward a property/function relationship for metallothioneins: Histidine coordination and unusual cluster composition in a zinc-metallothionein from plants
    • DOI 10.1002/prot.21463
    • O.I. Leszczyszyn, R. Schmid, and C.A. Blindauer Toward a property/function relationship for metallothioneins: histidine coordination and unusual cluster composition in a zinc-metallothionein from plants Proteins - Struct. Funct. Bioinf. 68 2007 922 935 (Pubitemid 47434714)
    • (2007) Proteins: Structure, Function and Genetics , vol.68 , Issue.4 , pp. 922-935
    • Leszczyszyn, O.I.1    Schmid, R.2    Blindauer, C.A.3
  • 66
    • 60149107848 scopus 로고    scopus 로고
    • Metallothioneins 2 and 3 contribute to the metal-adapted phenotype but are not directly linked to Zn accumulation in the metal hyperaccumulator, Thlaspi caerulescens
    • V.H. Hassinen, M. Tuomainen, S. Peraniemi, H. Schat, S.O. Karenlampi, and A.I. Tervahauta Metallothioneins 2 and 3 contribute to the metal-adapted phenotype but are not directly linked to Zn accumulation in the metal hyperaccumulator, Thlaspi caerulescens J. Exp. Bot. 60 2009 187 196
    • (2009) J. Exp. Bot. , vol.60 , pp. 187-196
    • Hassinen, V.H.1    Tuomainen, M.2    Peraniemi, S.3    Schat, H.4    Karenlampi, S.O.5    Tervahauta, A.I.6
  • 67
    • 58849114240 scopus 로고    scopus 로고
    • Spectroscopic characterization of Cicer arietinum metallothionein 1
    • O. Schicht, and E. Freisinger Spectroscopic characterization of Cicer arietinum metallothionein 1 Inorg. Chim. Acta 362 2009 714 724
    • (2009) Inorg. Chim. Acta , vol.362 , pp. 714-724
    • Schicht, O.1    Freisinger, E.2
  • 68
    • 33646028502 scopus 로고    scopus 로고
    • Chemometric tools for classification and elucidation of protein secondary structure from infrared and circular dichroism spectroscopic measurements
    • S. Navea, R. Tauler, E. Goormaghtigh, and A. de Juan Chemometric tools for classification and elucidation of protein secondary structure from infrared and circular dichroism spectroscopic measurements Proteins - Struct. Funct. Bioinf. 63 2006 527 541
    • (2006) Proteins - Struct. Funct. Bioinf. , vol.63 , pp. 527-541
    • Navea, S.1    Tauler, R.2    Goormaghtigh, E.3    De Juan, A.4
  • 69
    • 3242742115 scopus 로고    scopus 로고
    • The optimization of protein secondary structure determination with infrared and circular dichroism spectra
    • DOI 10.1111/j.1432-1033.2004.04220.x
    • K.A. Oberg, J.M. Ruysschaert, and E. Goormaghtigh The optimization of protein secondary structure determination with infrared and CD spectra Eur. J. Biochem. 271 2004 2937 2948 (Pubitemid 38980278)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.14 , pp. 2937-2948
    • Oberg, K.A.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.