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Volumn 46, Issue 47, 2007, Pages 13658-13666

Zinc binding to amyloid-β: Isothermal titration calorimetry and Zn competition experiments with Zn sensors

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; CHELATION; CHEMICAL SENSORS; NEURONS; STARCH; TITRATION; TOXIC MATERIALS;

EID: 36749044742     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701355j     Document Type: Article
Times cited : (99)

References (67)
  • 1
    • 0036736218 scopus 로고    scopus 로고
    • Amyloid precursor protein, presenilins, and alpha-synuclein: Molecular pathogenesis and pharmacological applications in Alzheimer's disease
    • Suh, Y. H., and Checler, F. (2002) Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease, Pharmacol. Rev. 54, 469-525.
    • (2002) Pharmacol. Rev , vol.54 , pp. 469-525
    • Suh, Y.H.1    Checler, F.2
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics, Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein, W. L., Stine, W. B., Jr., and Teplow, D. B. (2004) Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease, Neurobiol. Aging 25, 569-580.
    • (2004) Neurobiol. Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr., W.B.2    Teplow, D.B.3
  • 4
    • 0032605616 scopus 로고    scopus 로고
    • Metal binding and radical generation of proteins in human neurological diseases and aging
    • Multhaup, G., and Masters, C. L. (1999) Metal binding and radical generation of proteins in human neurological diseases and aging, Met. Ions Biol. Syst. 36, 365-387.
    • (1999) Met. Ions Biol. Syst , vol.36 , pp. 365-387
    • Multhaup, G.1    Masters, C.L.2
  • 5
    • 0027980901 scopus 로고    scopus 로고
    • Bush, A. I., Pettingell, W. H., Multhaup, G., d Paradis, M., Vonsattel, J. P., Gusella, J. F., Beyreuther, K., Masters, C. L., and Tanzi, R. E. (1994) Rapid induction of Alzheimer A beta amyloid formation by zinc, Science 265, 1464-1467.
    • Bush, A. I., Pettingell, W. H., Multhaup, G., d Paradis, M., Vonsattel, J. P., Gusella, J. F., Beyreuther, K., Masters, C. L., and Tanzi, R. E. (1994) Rapid induction of Alzheimer A beta amyloid formation by zinc, Science 265, 1464-1467.
  • 6
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. (2001) Alzheimer's disease: genes, proteins, and therapy, Physiol. Rev. 81, 741-766.
    • (2001) Physiol. Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 7
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush, A. I. (2003) The metallobiology of Alzheimer's disease, Trends Neurosci. 26, 207-214.
    • (2003) Trends Neurosci , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 10
    • 13244287771 scopus 로고    scopus 로고
    • Metal-binding properties of the peptide APP170-188: A model of the ZnII-binding site of amyloid precursor protein (APP)
    • Ciuculescu, E. D., Mekmouche, Y., and Faller, P. (2005) Metal-binding properties of the peptide APP170-188: a model of the ZnII-binding site of amyloid precursor protein (APP), Chemistry 11, 903-909.
    • (2005) Chemistry , vol.11 , pp. 903-909
    • Ciuculescu, E.D.1    Mekmouche, Y.2    Faller, P.3
  • 11
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee, J. Y., Cole, T. B., Palmiter, R. D., Suh, S. W., and Koh, J. Y. (2002) Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice, Proc. Natl. Acad. Sci. U.S.A. 99, 7705-7710.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 13
    • 4644238758 scopus 로고    scopus 로고
    • The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice
    • Lee, J. Y., Friedman, J. E., Angel, I., Kozak, A., and Koh, J. Y. (2004) The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice, Neurobiol. Aging 25, 1315-1321.
    • (2004) Neurobiol. Aging , vol.25 , pp. 1315-1321
    • Lee, J.Y.1    Friedman, J.E.2    Angel, I.3    Kozak, A.4    Koh, J.Y.5
  • 14
    • 33751074919 scopus 로고    scopus 로고
    • Metals and Alzheimer's disease
    • Adlard, P. A., and Bush, A. I. (2006) Metals and Alzheimer's disease, J. Alzheimer's Dis. 10, 145-163.
    • (2006) J. Alzheimer's Dis , vol.10 , pp. 145-163
    • Adlard, P.A.1    Bush, A.I.2
  • 15
    • 27744456516 scopus 로고    scopus 로고
    • Preparation of cyclo-phen-type ligands: Chelators of metal ions as potential therapeutic agents in the treatment of neurodegenerative diseases
    • Boldron, C., Van der Auwera, I., Deraeve, C., Gornitzka, H., Wera, S., Pitie, M., Van Leuven, F., and Meunier, B. (2005) Preparation of cyclo-phen-type ligands: chelators of metal ions as potential therapeutic agents in the treatment of neurodegenerative diseases, ChemBioChem 6, 1976-1980.
    • (2005) ChemBioChem , vol.6 , pp. 1976-1980
    • Boldron, C.1    Van der Auwera, I.2    Deraeve, C.3    Gornitzka, H.4    Wera, S.5    Pitie, M.6    Van Leuven, F.7    Meunier, B.8
  • 16
    • 0027327488 scopus 로고
    • Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of beta-amyloid peptide
    • Mantyh, P. W., Ghilardi, J. R., Rogers, S., DeMaster, E., Allen, C. J., Stimson, E. R., and Maggio, J. E. (1993) Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of beta-amyloid peptide, J. Neurochem. 61, 1171-1174.
    • (1993) J. Neurochem , vol.61 , pp. 1171-1174
    • Mantyh, P.W.1    Ghilardi, J.R.2    Rogers, S.3    DeMaster, E.4    Allen, C.J.5    Stimson, E.R.6    Maggio, J.E.7
  • 17
    • 0028180196 scopus 로고
    • Modulation of A beta adhesiveness and secretase site cleavage by zinc
    • Bush, A. I., Pettingell, W. H., Jr., Paradis, M. D., and Tanzi, R. E. (1994) Modulation of A beta adhesiveness and secretase site cleavage by zinc, J. Biol. Chem. 269, 12152-12158.
    • (1994) J. Biol. Chem , vol.269 , pp. 12152-12158
    • Bush, A.I.1    Pettingell Jr., W.H.2    Paradis, M.D.3    Tanzi, R.E.4
  • 18
    • 33846912266 scopus 로고    scopus 로고
    • Amyloid-beta peptide forms monomeric complexes with Cu(II) and Zn(II) prior to aggregation
    • Talmard, C., Guilloreau, L., Coppel, Y., Mazarguil, H., and Faller, P. (2007) Amyloid-beta peptide forms monomeric complexes with Cu(II) and Zn(II) prior to aggregation, ChemBioChem 8, 163-165.
    • (2007) ChemBioChem , vol.8 , pp. 163-165
    • Talmard, C.1    Guilloreau, L.2    Coppel, Y.3    Mazarguil, H.4    Faller, P.5
  • 19
    • 0033747946 scopus 로고    scopus 로고
    • Examining the zinc binding site of the amyloid-beta peptide
    • Yang, D. S., McLaurin, J., Qin, K., Westaway, D., and Fraser, P. E. (2000) Examining the zinc binding site of the amyloid-beta peptide, Eur. J. Biochem. 267, 6692-6698.
    • (2000) Eur. J. Biochem , vol.267 , pp. 6692-6698
    • Yang, D.S.1    McLaurin, J.2    Qin, K.3    Westaway, D.4    Fraser, P.E.5
  • 20
    • 18144374793 scopus 로고    scopus 로고
    • Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid {beta} peptide
    • Raman, B., Ban, T., Yamaguchi, K., Sakai, M., Kawai, T., Naiki, H., and Goto, Y. (2005) Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid {beta} peptide, J. Biol. Chem. 280, 16157-16162.
    • (2005) J. Biol. Chem , vol.280 , pp. 16157-16162
    • Raman, B.1    Ban, T.2    Yamaguchi, K.3    Sakai, M.4    Kawai, T.5    Naiki, H.6    Goto, Y.7
  • 21
    • 0242362596 scopus 로고    scopus 로고
    • Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral Ph
    • Klug, G. M., Losic, D., Subasinghe, S. S., Aguilar, M. I., Martin, L. L., and Small, D. H. (2003) Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral Ph, Eur. J. Biochem. 270, 4282-4293.
    • (2003) Eur. J. Biochem , vol.270 , pp. 4282-4293
    • Klug, G.M.1    Losic, D.2    Subasinghe, S.S.3    Aguilar, M.I.4    Martin, L.L.5    Small, D.H.6
  • 23
    • 3042666730 scopus 로고    scopus 로고
    • Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Abeta42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease
    • House, E., Collingwood, J., Khan, A., Korchazkina, O., Berthon, G., and Exley, C. (2004) Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Abeta42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease, J. Alzheimer's Dis. 6, 291-301.
    • (2004) J. Alzheimer's Dis , vol.6 , pp. 291-301
    • House, E.1    Collingwood, J.2    Khan, A.3    Korchazkina, O.4    Berthon, G.5    Exley, C.6
  • 24
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease
    • Liu, S. T., Howlett, G., and Barrow, C. J. (1999) Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease, Biochemistry 38, 9373-9378.
    • (1999) Biochemistry , vol.38 , pp. 9373-9378
    • Liu, S.T.1    Howlett, G.2    Barrow, C.J.3
  • 25
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes
    • Miura, T., Suzuki, K., Kohata, N., and Takeuchi, H. (2000) Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes, Biochemistry 39, 7024-7031.
    • (2000) Biochemistry , vol.39 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 26
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain, C. C., Ali, F., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K., Barrow, C. J., Masters, C. L., Bush, A. I., and Barnham, K. J. (2001) Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits, J. Biol. Chem. 276, 20466-20473.
    • (2001) J. Biol. Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 27
    • 0034806472 scopus 로고    scopus 로고
    • Zinc binding to Alzheimer's Abeta(1-16) peptide results in stable soluble complex
    • Kozin, S. A., Zirah, S., Rebuffat, S., Hoa, G. H., and Debey, P. (2001) Zinc binding to Alzheimer's Abeta(1-16) peptide results in stable soluble complex, Biochem. Biophys. Res. Commun. 285, 959-964.
    • (2001) Biochem. Biophys. Res. Commun , vol.285 , pp. 959-964
    • Kozin, S.A.1    Zirah, S.2    Rebuffat, S.3    Hoa, G.H.4    Debey, P.5
  • 28
    • 24744432986 scopus 로고    scopus 로고
    • Characterization of the ZnII binding to the peptide amyloid-beta1-16 linked to Alzheimer's disease
    • Mekmouche, Y., Coppel, Y., Hochgrafe, K., Guilloreau, L., Talmard, C., Mazarguil, H., and Faller, P. (2005) Characterization of the ZnII binding to the peptide amyloid-beta1-16 linked to Alzheimer's disease, ChemBioChem 6, 1663-1671.
    • (2005) ChemBioChem , vol.6 , pp. 1663-1671
    • Mekmouche, Y.1    Coppel, Y.2    Hochgrafe, K.3    Guilloreau, L.4    Talmard, C.5    Mazarguil, H.6    Faller, P.7
  • 29
    • 33644530354 scopus 로고    scopus 로고
    • Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Abeta) of Alzheimer's disease
    • Syme, C. D., and Viles, J. H. (2006) Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Abeta) of Alzheimer's disease, Biochim. Biophys. Acta 1764, 246-256.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 246-256
    • Syme, C.D.1    Viles, J.H.2
  • 30
    • 0042744900 scopus 로고    scopus 로고
    • Zinc binding properties of the amyloid fragment Ab(1-16) studied by electrospray-ionization mass spectrometry
    • Zirah, S., Rebuffat, S., Kozin, S. A., Debey, P., Fournier, F., Lesage, D., and Tabet, J.-C. (2003) Zinc binding properties of the amyloid fragment Ab(1-16) studied by electrospray-ionization mass spectrometry, Int. J. Mass Spectrom. 228, 999-1016.
    • (2003) Int. J. Mass Spectrom , vol.228 , pp. 999-1016
    • Zirah, S.1    Rebuffat, S.2    Kozin, S.A.3    Debey, P.4    Fournier, F.5    Lesage, D.6    Tabet, J.-C.7
  • 31
    • 33644867988 scopus 로고    scopus 로고
    • Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging
    • Zirah, S., Kozin, S. A., Mazur, A. K., Blond, A., Cheminant, M., Segalas-Milazzo, I., Debey, P., and Rebuffat, S. (2006) Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging, J. Biol. Chem. 281, 2151-2161.
    • (2006) J. Biol. Chem , vol.281 , pp. 2151-2161
    • Zirah, S.1    Kozin, S.A.2    Mazur, A.K.3    Blond, A.4    Cheminant, M.5    Segalas-Milazzo, I.6    Debey, P.7    Rebuffat, S.8
  • 33
    • 33746335362 scopus 로고    scopus 로고
    • NMR reveals anomalous copper(II) binding to the amyloid Abeta peptide of Alzheimer's disease
    • Hou, L., and Zagorski, M. G. (2006) NMR reveals anomalous copper(II) binding to the amyloid Abeta peptide of Alzheimer's disease, J. Am. Chem. Soc. 128, 9260-9261.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 9260-9261
    • Hou, L.1    Zagorski, M.G.2
  • 34
    • 33845665797 scopus 로고    scopus 로고
    • High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide
    • Danielsson, J., Pierattelli, R., Banci, L., and Graslund, A. (2007) High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide, FEBS J. 274, 46-59.
    • (2007) FEBS J , vol.274 , pp. 46-59
    • Danielsson, J.1    Pierattelli, R.2    Banci, L.3    Graslund, A.4
  • 35
    • 0030024168 scopus 로고    scopus 로고
    • Aggregation and metal-binding properties of mutant forms of the amyloid A beta peptide of Alzheimer's disease
    • Clements, A., Allsop, D., Walsh, D. M., and Williams, C. H. (1996) Aggregation and metal-binding properties of mutant forms of the amyloid A beta peptide of Alzheimer's disease, J. Neurochem. 66, 740-747.
    • (1996) J. Neurochem , vol.66 , pp. 740-747
    • Clements, A.1    Allsop, D.2    Walsh, D.M.3    Williams, C.H.4
  • 36
    • 23844434035 scopus 로고    scopus 로고
    • Aluminum-triggered structural modifications and aggregation of beta-amyloids
    • Ricchelli, F., Drago, D., Filippi, B., Tognon, G., and Zatta, P. (2005) Aluminum-triggered structural modifications and aggregation of beta-amyloids, Cell. Mol. Life Sci. 62, 1724-1733.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 1724-1733
    • Ricchelli, F.1    Drago, D.2    Filippi, B.3    Tognon, G.4    Zatta, P.5
  • 37
    • 0033517053 scopus 로고    scopus 로고
    • Binding of Zn(II), Cu(II), and Fe(II) ions to Alzheimer's A beta peptide studied by fluorescence
    • Garzon-Rodriguez, W., Yatsimirsky, A. K., and Glabe, C. G. (1999) Binding of Zn(II), Cu(II), and Fe(II) ions to Alzheimer's A beta peptide studied by fluorescence, Bioorg. Med. Chem. Lett 9, 2243-2248.
    • (1999) Bioorg. Med. Chem. Lett , vol.9 , pp. 2243-2248
    • Garzon-Rodriguez, W.1    Yatsimirsky, A.K.2    Glabe, C.G.3
  • 40
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • Pierce, M. M., Raman, C. S., and Nall, B. T. (1999) Isothermal titration calorimetry of protein-protein interactions, Methods 19, 213-221.
    • (1999) Methods , vol.19 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 43
    • 1142303789 scopus 로고    scopus 로고
    • Florescent detection of zinc in biological systems: Recent develpoment on the design of chemosensors and biosensors
    • Jiang, P., and Gui, Z. (2004) Florescent detection of zinc in biological systems: recent develpoment on the design of chemosensors and biosensors, Coord. Chem. Rev. 248, 205-229.
    • (2004) Coord. Chem. Rev , vol.248 , pp. 205-229
    • Jiang, P.1    Gui, Z.2
  • 44
    • 0033572730 scopus 로고    scopus 로고
    • Aqueous coordination chemistry of quinoline-based fluorescence probes for the biological chemistry of zinc
    • Fahrni, C. J., and O'Halloran. (1999) Aqueous coordination chemistry of quinoline-based fluorescence probes for the biological chemistry of zinc, J. Am. Chem. Soc. 121, 11448-11458.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 11448-11458
    • Fahrni, C.J.1    O'Halloran2
  • 45
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson, M. R. (2004) Techniques to study amyloid fibril formation in vitro, Methods 34, 151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 46
    • 33846527387 scopus 로고    scopus 로고
    • Survey of the year 2005: Literature on applications of isothermal titration calorimetry
    • Ababou, A., and Ladbury, J. E. (2007) Survey of the year 2005: literature on applications of isothermal titration calorimetry, J. Mol. Recognit. 20, 4-14.
    • (2007) J. Mol. Recognit , vol.20 , pp. 4-14
    • Ababou, A.1    Ladbury, J.E.2
  • 47
    • 33846637900 scopus 로고    scopus 로고
    • Microcalorimetry of biological macromolecules
    • Privalov, P. L., and Dragan, A. I. (2007) Microcalorimetry of biological macromolecules, Biophys. Chem. 126, 16-24.
    • (2007) Biophys. Chem , vol.126 , pp. 16-24
    • Privalov, P.L.1    Dragan, A.I.2
  • 48
    • 10044226082 scopus 로고    scopus 로고
    • Application of isothermal titration calorimetry in the biological sciences: Things are heating up!
    • Ladbury, J. E. (2004) Application of isothermal titration calorimetry in the biological sciences: things are heating up!, Biotechniques 37, 885-887.
    • (2004) Biotechniques , vol.37 , pp. 885-887
    • Ladbury, J.E.1
  • 49
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42
    • Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., and Bush, A. I. (2000) Characterization of copper interactions with alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta1-42, J. Neurochem. 75, 1219-1233.
    • (2000) J. Neurochem , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 50
    • 0036933125 scopus 로고    scopus 로고
    • Thermodynamic and spectroscopic study of Cu(II) and Ni(II) binding to bovine serum albumin
    • Zhang, Y., and Wilcox, D. E. (2002) Thermodynamic and spectroscopic study of Cu(II) and Ni(II) binding to bovine serum albumin, J. Biol. Inorg. Chem. 7, 327-337.
    • (2002) J. Biol. Inorg. Chem , vol.7 , pp. 327-337
    • Zhang, Y.1    Wilcox, D.E.2
  • 51
    • 0037126693 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of a coupled metal binding-protein folding reaction involving a zinc finger peptide
    • Blasie, C. A., and Berg, J. M. (2002) Structure-based thermodynamic analysis of a coupled metal binding-protein folding reaction involving a zinc finger peptide, Biochemistry 41, 15068-15073.
    • (2002) Biochemistry , vol.41 , pp. 15068-15073
    • Blasie, C.A.1    Berg, J.M.2
  • 52
    • 0037601769 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of copper(II) binding to apoazurin
    • Blasie, C. A., and Berg, J. M. (2003) Kinetics and thermodynamics of copper(II) binding to apoazurin, J. Am. Chem. Soc. 125, 6866-6867.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 6866-6867
    • Blasie, C.A.1    Berg, J.M.2
  • 53
    • 33751245122 scopus 로고    scopus 로고
    • Structural and thermodynamical properties of CuII amyloid-beta 16/28 complexes associated with Alzheimer's disease
    • Guilloreau, L., Damian, L., Coppel, Y., Mazarguil, H., Winterhalter, M., and Faller, P. (2006) Structural and thermodynamical properties of CuII amyloid-beta 16/28 complexes associated with Alzheimer's disease, J. Biol. Inorg. Chem. 11, 1024-1038.
    • (2006) J. Biol. Inorg. Chem , vol.11 , pp. 1024-1038
    • Guilloreau, L.1    Damian, L.2    Coppel, Y.3    Mazarguil, H.4    Winterhalter, M.5    Faller, P.6
  • 54
    • 0034631701 scopus 로고    scopus 로고
    • Isothermal titration calorimetry measurements of Ni(II) and Cu(II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: A critical evaluation
    • Zhang, Y., Akilesh, S., and Wilcox, D. E. (2000) Isothermal titration calorimetry measurements of Ni(II) and Cu(II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: a critical evaluation, Inorg. Chem. 39, 3057-3064.
    • (2000) Inorg. Chem , vol.39 , pp. 3057-3064
    • Zhang, Y.1    Akilesh, S.2    Wilcox, D.E.3
  • 55
    • 0032480810 scopus 로고    scopus 로고
    • Calorimetric investigation of proton linkage by monitoring both the enthalpy and association constant of binding: Application to the interaction of the Src SH2 domain with a high-affinity tyrosyl phosphopeptide
    • Bradshaw, J. M., and Waksman, G. (1998) Calorimetric investigation of proton linkage by monitoring both the enthalpy and association constant of binding: application to the interaction of the Src SH2 domain with a high-affinity tyrosyl phosphopeptide, Biochemistry 37, 15400-15407.
    • (1998) Biochemistry , vol.37 , pp. 15400-15407
    • Bradshaw, J.M.1    Waksman, G.2
  • 56
    • 2342659638 scopus 로고    scopus 로고
    • Zn-, Cd-, and Pb-transcription factor IIIA: Properties, DNA binding, and comparison with TFIIIA-finger 3 metal complexes
    • Huang, M., Krepkiy, D., Hu, W., and Petering, D. H. (2004) Zn-, Cd-, and Pb-transcription factor IIIA: properties, DNA binding, and comparison with TFIIIA-finger 3 metal complexes, J. Inorg. Biochem. 98, 775-785.
    • (2004) J. Inorg. Biochem , vol.98 , pp. 775-785
    • Huang, M.1    Krepkiy, D.2    Hu, W.3    Petering, D.H.4
  • 59
    • 33749824175 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of amyloid fibril assembly
    • Wetzel, R. (2006) Kinetics and thermodynamics of amyloid fibril assembly, Acc. Chem. Res. 39, 671-679.
    • (2006) Acc. Chem. Res , vol.39 , pp. 671-679
    • Wetzel, R.1
  • 60
    • 0041817542 scopus 로고    scopus 로고
    • The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations
    • Sengupta, P., Garai, K., Sahoo, B., Shi, Y., Callaway, D. J., and Maiti, S. (2003) The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations, Biochemistry 42, 10506-10513.
    • (2003) Biochemistry , vol.42 , pp. 10506-10513
    • Sengupta, P.1    Garai, K.2    Sahoo, B.3    Shi, Y.4    Callaway, D.J.5    Maiti, S.6
  • 62
    • 34249786569 scopus 로고    scopus 로고
    • Stoichiometry and conditional stability constants of Cu(II) or Zn(II) clioquinol complexes; implications for Alzheimer's and Huntington's disease therapy
    • Ferrada, E., Arancibia, V., Loeb, B., Norambuena, E., Olea-Azar, C., and Huidobro-Toro, J. P. (2007) Stoichiometry and conditional stability constants of Cu(II) or Zn(II) clioquinol complexes; implications for Alzheimer's and Huntington's disease therapy, Neurotoxicology 28, 445-449.
    • (2007) Neurotoxicology , vol.28 , pp. 445-449
    • Ferrada, E.1    Arancibia, V.2    Loeb, B.3    Norambuena, E.4    Olea-Azar, C.5    Huidobro-Toro, J.P.6
  • 63
    • 2942750367 scopus 로고    scopus 로고
    • Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: Structural characterization of its zinc(II) and copper(II) complexes
    • Di Vaira, M., Bazzicalupi, C., Orioli, P., Messori, L., Bruni, B., and Zatta, P. (2004) Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: structural characterization of its zinc(II) and copper(II) complexes, Inorg. Chem. 43, 3795-3797.
    • (2004) Inorg. Chem , vol.43 , pp. 3795-3797
    • Di Vaira, M.1    Bazzicalupi, C.2    Orioli, P.3    Messori, L.4    Bruni, B.5    Zatta, P.6
  • 64
    • 4043098949 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation in ionic interactions probed in a zinc finger peptide
    • Blasie, C. A., and Berg, J. M. (2004) Entropy-enthalpy compensation in ionic interactions probed in a zinc finger peptide, Biochemistry 43, 10600-10604.
    • (2004) Biochemistry , vol.43 , pp. 10600-10604
    • Blasie, C.A.1    Berg, J.M.2
  • 65
    • 33751223540 scopus 로고    scopus 로고
    • Zinc-buffering capacity of a eukaryotic cell at physiological pZn
    • Krezel, A., and Maret, W. (2006) Zinc-buffering capacity of a eukaryotic cell at physiological pZn, J. Biol. Inorg. Chem. 11, 1049-1062.
    • (2006) J. Biol. Inorg. Chem , vol.11 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 66
    • 0030919897 scopus 로고    scopus 로고
    • Fluorescent chemosensors for divalent zinc based on zinc finger domains. Enhanced oxidative stability, metal binding affinity, and structural and functional characterization
    • Walkup, G. K., and Imperiali, B. (1997) Fluorescent chemosensors for divalent zinc based on zinc finger domains. Enhanced oxidative stability, metal binding affinity, and structural and functional characterization, J. Am. Chem. Soc. 119, 3443-3450.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 3443-3450
    • Walkup, G.K.1    Imperiali, B.2
  • 67
    • 0038802776 scopus 로고    scopus 로고
    • Coordination abilities of the 1-16 and 1-28 fragments of beta-amyloid peptide towards copper(II) ions: A combined potentiometric and spectroscopic study
    • Kowalik-Jankowska, T., Ruta, M., Wisniewska, K., and Lankiewicz, L. (2003) Coordination abilities of the 1-16 and 1-28 fragments of beta-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study, J. Inorg. Biochem. 95, 270-282.
    • (2003) J. Inorg. Biochem , vol.95 , pp. 270-282
    • Kowalik-Jankowska, T.1    Ruta, M.2    Wisniewska, K.3    Lankiewicz, L.4


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