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Volumn 88, Issue 2, 2010, Pages 347-358

Nanopore analysis of the interaction of metal ions with prion proteins and peptides

Author keywords

Metal ion binding; Nanopores; Prion protein; Protein folding; hemolysin

Indexed keywords

BLOOD; COMPLEXATION; CONFORMATIONS; MANGANESE; MANGANESE COMPOUNDS; METAL ANALYSIS; METAL IONS; METALS; MOLECULES; PEPTIDES; PROTEIN FOLDING; ZINC; ZINC COMPOUNDS;

EID: 77950616187     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-176     Document Type: Conference Paper
Times cited : (35)

References (55)
  • 1
    • 33645118457 scopus 로고    scopus 로고
    • Generation of antibodies against bovine recombinant prion protein in various strains of mice
    • doi:10.1128/CVI.13.1.98-105.2006. PMID:16426006
    • Andrievskaia, O., McRae, H., Elmgren, C., Huang, H., Balachandran, A., and Nielsen, K. 2006. Generation of antibodies against bovine recombinant prion protein in various strains of mice. Clin. Vaccine Immunol. 13(1): 98-105. doi:10.1128/CVI.13.1. 98-105.2006. PMID:16426006.
    • (2006) Clin. Vaccine Immunol. , vol.13 , Issue.1 , pp. 98-105
    • Andrievskaia, O.1    McRae, H.2    Elmgren, C.3    Huang, H.4    Balachandran, A.5    Nielsen, K.6
  • 2
    • 0023720483 scopus 로고
    • Ion modulation of membrane permeability: Effect of cations on intact cells and on cells and phospholipid bilayers treated with pore-forming agents
    • doi:10.1007/BF01871934. PMID:2846846
    • Bashford, C.L., Alder, G.M., Graham, J.M., Menestrina, G., and Pasternak, C.A. 1988. Ion modulation of membrane permeability: effect of cations on intact cells and on cells and phospholipid bilayers treated with pore-forming agents. J. Membr. Biol. 103(1): 79-94. doi:10.1007/BF01871934. PMID:2846846.
    • (1988) J. Membr. Biol. , vol.103 , Issue.1 , pp. 79-94
    • Bashford, C.L.1    Alder, G.M.2    Graham, J.M.3    Menestrina, G.4    Pasternak, C.A.5
  • 3
    • 5444232817 scopus 로고    scopus 로고
    • Preventing misfolding of the prion protein by trimethylamine N-oxide
    • doi:10.1021/bi0486379. PMID: 15476389
    • Bennion, B.J., DeMarco, M.L., and Daggett, V. 2004. Preventing misfolding of the prion protein by trimethylamine N-oxide. Biochemistry, 43(41): 12955-12963. doi:10.1021/bi0486379. PMID: 15476389.
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 12955-12963
    • Bennion, B.J.1    DeMarco, M.L.2    Daggett, V.3
  • 4
    • 45149107529 scopus 로고    scopus 로고
    • Manganese binding to the prion protein
    • doi:10.1074/jbc.M709820200. PMID:18332141
    • Brazier, M.W., Davies, P., Player, E., Marken, F., Viles, J.H., and Brown, D.R. 2008. Manganese binding to the prion protein. J. Biol. Chem. 283(19): 12831-12839. doi:10.1074/jbc.M709820200. PMID:18332141.
    • (2008) J. Biol. Chem. , vol.283 , Issue.19 , pp. 12831-12839
    • Brazier, M.W.1    Davies, P.2    Player, E.3    Marken, F.4    Viles, J.H.5    Brown, D.R.6
  • 5
    • 0037646939 scopus 로고    scopus 로고
    • Copper coordination in the full-length, recombinant prion protein
    • doi:10.1021/bi027138+. PMID:12779334
    • Burns, C.S., Aronoff-Spencer, E., Legname, G., Prusiner, S.B., Antholine, W.E., Gerfen, G.J., et al. 2003. Copper coordination in the full-length, recombinant prion protein. Biochemistry, 42(22): 6794-6803. doi:10.1021/ bi027138+. PMID:12779334.
    • (2003) Biochemistry , vol.42 , Issue.22 , pp. 6794-6803
    • Burns, C.S.1    Aronoff-Spencer, E.2    Legname, G.3    Prusiner, S.B.4    Antholine, W.E.5    Gerfen, G.J.6
  • 7
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • doi:10.1038/nature05294. PMID:17051207
    • Caughey, B., and Baron, G.S. 2006. Prions and their partners in crime. Nature, 443(7113): 803-810. doi:10.1038/nature05294. PMID:17051207.
    • (2006) Nature , vol.443 , Issue.7113 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 8
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • doi:10.1146/annurev.biochem.72.121801.161837. PMID:15189155
    • Chien, P., Weissman, J.S., and DePace, A.H. 2004. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73(1): 617-656. doi:10.1146/annurev.biochem.72.121801.161837. PMID:15189155.
    • (2004) Annu. Rev. Biochem. , vol.73 , Issue.1 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 9
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • doi:10.1146/annurev.biochem.75.101304.123901. PMID: 16756495
    • Chiti, F., and Dobson, C.M. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75(1): 333-366. doi:10.1146/annurev. biochem.75.101304.123901. PMID: 16756495.
    • (2006) Annu. Rev. Biochem. , vol.75 , Issue.1 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 10
    • 65249161100 scopus 로고    scopus 로고
    • Prion diseases and their biochemical mechanisms
    • doi:10.1021/bi900108v. PMID:19239250
    • Cobb, N.J., and Surewicz, W.K. 2009. Prion diseases and their biochemical mechanisms. Biochemistry, 48(12): 2574-2585. doi:10.1021/bi900108v. PMID:19239250.
    • (2009) Biochemistry , vol.48 , Issue.12 , pp. 2574-2585
    • Cobb, N.J.1    Surewicz, W.K.2
  • 11
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • doi:10.1126/science.1138718. PMID:17991853
    • Collinge, J., and Clarke, A.R. 2007. A general model of prion strains and their pathogenicity. Science, 318(5852): 930-936. doi:10.1126/science.1138718. PMID:17991853.
    • (2007) Science , vol.318 , Issue.5852 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 12
  • 13
    • 34248351114 scopus 로고    scopus 로고
    • Solid-state nanopores
    • Dekker, C. 2007. Solid-state nanopores. Nature, 2: 209-215.
    • (2007) Nature , vol.2 , pp. 209-215
    • Dekker, C.1
  • 14
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • doi:10.1038/nature01979. PMID:14562104
    • Deleault, N.R., Lucassen, R.W., and Supattapone, S. 2003. RNA molecules stimulate prion protein conversion. Nature, 425(6959): 717-720. doi:10.1038/nature01979. PMID:14562104.
    • (2003) Nature , vol.425 , Issue.6959 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 15
    • 12444341883 scopus 로고    scopus 로고
    • Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies
    • doi:10.1021/ja045958z. PMID:15656638
    • Gaggelli, E., Bernardi, F., Molteni, E., Pogni, R., Valensin, D., Valensin, G., et al. 2005. Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies. J. Am. Chem. Soc. 127(3): 996-1006. doi:10.1021/ja045958z. PMID:15656638.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.3 , pp. 996-1006
    • Gaggelli, E.1    Bernardi, F.2    Molteni, E.3    Pogni, R.4    Valensin, D.5    Valensin, G.6
  • 16
    • 33745726690 scopus 로고    scopus 로고
    • Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis)
    • doi:10.1021/cr040410w. PMID:16771441
    • Gaggelli, E., Kozlowski, H., Valensin, D., and Valensin, G. 2006. Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis). Chem. Rev. 106(6): 1995-2044. doi:10.1021/cr040410w. PMID:16771441.
    • (2006) Chem. Rev. , vol.106 , Issue.6 , pp. 1995-2044
    • Gaggelli, E.1    Kozlowski, H.2    Valensin, D.3    Valensin, G.4
  • 17
    • 0025885702 scopus 로고
    • Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene
    • doi:10.1073/pnas.88.23.10926
    • Goldfarb, L.G., Brown, P., McCombie, W.R., Goldgaber, D., Swergold, G.D., Wills, P.R., et al. 1991. Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene. Prc. Natl. Acad. Sci. 88(23): 10926-10930. doi:10.1073/pnas.88.23. 10926.
    • (1991) Prc. Natl. Acad. Sci. , vol.88 , Issue.23 , pp. 10926-10930
    • Goldfarb, L.G.1    Brown, P.2    McCombie, W.R.3    Goldgaber, D.4    Swergold, G.D.5    Wills, P.R.6
  • 18
    • 34247528242 scopus 로고    scopus 로고
    • Single-molecule electrophoresis of beta-hairpin peptides by electrical recordings and Langevin dynamics simulations
    • doi:10.1021/jp071364h. PMID: 17388500
    • Goodrich, C.P., Kirmizialtin, S., Huyghues-Despointes, B.M., Zhu, A., Scholtz, J.M., Makarov, D.E., and Movileanu, L. 2007. Single-molecule electrophoresis of beta-hairpin peptides by electrical recordings and Langevin dynamics simulations. J. Phys. Chem. B, 111(13): 3332-3335. doi:10.1021/ jp071364h. PMID: 17388500.
    • (2007) J. Phys. Chem. B , vol.111 , Issue.13 , pp. 3332-3335
    • Goodrich, C.P.1    Kirmizialtin, S.2    Huyghues-Despointes, B.M.3    Zhu, A.4    Scholtz, J.M.5    Makarov, D.E.6    Movileanu, L.7
  • 19
    • 0035169385 scopus 로고    scopus 로고
    • Prolonged residence time of a noncovalent molecular adapter, β-cyclodextrin, within the lumen of mutant α-hemolysin pores
    • doi:10.1085/jgp.118.5.481. PMID:11696607
    • Gu, L.Q., Cheley, S., and Bayley, H. 2001. Prolonged residence time of a noncovalent molecular adapter, β-cyclodextrin, within the lumen of mutant α-hemolysin pores. J. Gen. Physiol. 118(5): 481-494. doi:10.1085/jgp.118. 5.481. PMID:11696607.
    • (2001) J. Gen. Physiol. , vol.118 , Issue.5 , pp. 481-494
    • Gu, L.Q.1    Cheley, S.2    Bayley, H.3
  • 20
    • 25844461753 scopus 로고    scopus 로고
    • Detecting single porphyrin molecules in a conically shaped synthetic nanopore
    • doi:10.1021/nl050925i. PMID:16159231
    • Heins, E.A., Siwy, Z.S., Baker, L.A., and Martin, C.R. 2005. Detecting single porphyrin molecules in a conically shaped synthetic nanopore. Nano Lett. 5(9): 1824-1829. doi:10.1021/nl050925i. PMID:16159231.
    • (2005) Nano Lett. , vol.5 , Issue.9 , pp. 1824-1829
    • Heins, E.A.1    Siwy, Z.S.2    Baker, L.A.3    Martin, C.R.4
  • 21
    • 67749111706 scopus 로고    scopus 로고
    • Specific nucleotide binding and rebinding to individual DNA polymerase complexes captured on a nanopore
    • doi:10.1021/ja809663f. PMID:19275265
    • Hurt, N., Wang, H., Akeson, M., and Lieberman, K.R. 2009. Specific nucleotide binding and rebinding to individual DNA polymerase complexes captured on a nanopore. J. Am. Chem. Soc. 131(10): 3772-3778. doi:10.1021/ja809663f. PMID:19275265.
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.10 , pp. 3772-3778
    • Hurt, N.1    Wang, H.2    Akeson, M.3    Lieberman, K.R.4
  • 22
    • 0035838471 scopus 로고    scopus 로고
    • Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126
    • doi:10.1021/bi0029088. PMID:11434776
    • Jobling, M.F., Huang, X., Stewart, L.R., Barnham, K.J., Curtain, C., Volitakis, I., et al. 2001. Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126. Biochemistry, 40(27): 8073-8084. doi:10.1021/bi0029088. PMID:11434776.
    • (2001) Biochemistry , vol.40 , Issue.27 , pp. 8073-8084
    • Jobling, M.F.1    Huang, X.2    Stewart, L.R.3    Barnham, K.J.4    Curtain, C.5    Volitakis, I.6
  • 23
    • 34447504712 scopus 로고    scopus 로고
    • Trace elements and prion diseases: A review of the interactions of copper, manganese and zinc with the prion protein
    • Leach, S.P., Salman, M.D., and Hamar, D. 2006. Trace elements and prion diseases: a review of the interactions of copper, manganese and zinc with the prion protein. Anim. Health Res. Rev. 7(1/2): 97-105.
    • (2006) Anim. Health Res. Rev. , vol.7 , Issue.1-2 , pp. 97-105
    • Leach, S.P.1    Salman, M.D.2    Hamar, D.3
  • 24
    • 33645639813 scopus 로고    scopus 로고
    • The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions
    • doi:10.1074/jbc.M510606200. PMID:16352600
    • Leliveld, S.R., Dame, R.T., Wuite, G.J.L., Stitz, L., and Korth, C. 2006. The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions. J. Biol. Chem. 281(6): 3268-3275. doi:10.1074/jbc.M510606200. PMID:16352600.
    • (2006) J. Biol. Chem. , vol.281 , Issue.6 , pp. 3268-3275
    • Leliveld, S.R.1    Dame, R.T.2    Wuite, G.J.L.3    Stitz, L.4    Korth, C.5
  • 25
    • 33746605957 scopus 로고    scopus 로고
    • Structural insights into the interaction between prion protein and nucleic acid
    • doi:10.1021/bi060532d. PMID:16866364
    • Lima, L.M.T.R., Cordeiro, Y., Tinoco, L.W., Marques, A.F., Oliveira, C.L.P., Sampath, S., et al. 2006. Structural insights into the interaction between prion protein and nucleic acid. Biochemistry, 45(30): 9180-9187. doi:10.1021/bi060532d. PMID: 16866364.
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9180-9187
    • Lima, L.M.T.R.1    Cordeiro, Y.2    Tinoco, L.W.3    Marques, A.F.4    Oliveira, C.L.P.5    Sampath, S.6
  • 26
    • 61749084334 scopus 로고    scopus 로고
    • Computer simulations and theory of protein translocation
    • doi:10.1021/ar800128x
    • Makarov, D.E. 2009. Computer simulations and theory of protein translocation. Acc. Chem. Res. 42(2): 281-289. doi:10.1021/ar800128x.
    • (2009) Acc. Chem. Res. , vol.42 , Issue.2 , pp. 281-289
    • Makarov, D.E.1
  • 27
    • 34247169511 scopus 로고    scopus 로고
    • Scavenger, transducer, RNA chaperone? What ligands of the prion protein teach us about its function
    • doi:10.1007/s00018-007-6370-1. PMID:17256089
    • Marc, D., Mercey, R., and Lantier, F. 2007. Scavenger, transducer, RNA chaperone? What ligands of the prion protein teach us about its function. Cell. Mol. Life Sci. 64(7-8): 815-829. doi:10.1007/s00018-007-6370-1. PMID:17256089.
    • (2007) Cell. Mol. Life Sci. , vol.64 , Issue.7-8 , pp. 815-829
    • Marc, D.1    Mercey, R.2    Lantier, F.3
  • 28
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • doi:10.1007/BF01869935. PMID:2425095
    • Menestrina, G. 1986. Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membr. Biol. 90(2): 177-190. doi:10.1007/BF01869935. PMID:2425095.
    • (1986) J. Membr. Biol. , vol.90 , Issue.2 , pp. 177-190
    • Menestrina, G.1
  • 29
    • 1242316297 scopus 로고    scopus 로고
    • Copper binding in the prion protein
    • doi:10.1021/ar0301678. PMID:14967054
    • Millhauser, G.L. 2004. Copper binding in the prion protein. Acc. Chem. Res. 37(2): 79-85. doi:10.1021/ar0301678. PMID:14967054.
    • (2004) Acc. Chem. Res. , vol.37 , Issue.2 , pp. 79-85
    • Millhauser, G.L.1
  • 30
    • 45849114386 scopus 로고    scopus 로고
    • Excursion of a single polypeptide into a protein pore: Simple physics, but complicated biology
    • doi:10.1007/s00249-008-0309-9. PMID:18368402
    • Mohammad, M.M., and Movileanu, L. 2008. Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology. Eur. Biophys. J. 37(6): 913-925. doi:10.1007/s00249-008-0309-9. PMID:18368402.
    • (2008) Eur. Biophys. J. , vol.37 , Issue.6 , pp. 913-925
    • Mohammad, M.M.1    Movileanu, L.2
  • 31
    • 41149181242 scopus 로고    scopus 로고
    • Controlling a single protein in a nanopore through electrostatic traps
    • doi:10.1021/ja710787a. PMID:18321107
    • Mohammad, M.M., Prakash, S., Matouschek, A., and Movileanu, L. 2008. Controlling a single protein in a nanopore through electrostatic traps. J. Am. Chem. Soc. 130(12): 4081-4088. doi:10. 1021/ja710787a. PMID:18321107.
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.12 , pp. 4081-4088
    • Mohammad, M.M.1    Prakash, S.2    Matouschek, A.3    Movileanu, L.4
  • 32
    • 1642523682 scopus 로고    scopus 로고
    • Inter-and intra-octarepeat Cu(II) site geometries in the prion protein: Implications in Cu(II) binding cooperativity and Cu(II)-mediated assemblies
    • doi:10.1074/jbc.M312860200. PMID:14703517
    • Morante, S., González-Iglesias, R., Potrich, C., Meneghini, C., Meyer-Klaucke, W., Menestrina, G., and Gasset, M. 2004. Inter-and intra-octarepeat Cu(II) site geometries in the prion protein: implications in Cu(II) binding cooperativity and Cu(II)-mediated assemblies. J. Biol. Chem. 279(12): 11753-11759. doi:10.1074/jbc.M312860200. PMID:14703517.
    • (2004) J. Biol. Chem. , vol.279 , Issue.12 , pp. 11753-11759
    • Morante, S.1    González-Iglesias, R.2    Potrich, C.3    Meneghini, C.4    Meyer-Klaucke, W.5    Menestrina, G.6    Gasset, M.7
  • 33
    • 0035849540 scopus 로고    scopus 로고
    • On the mechanism of α-helix to β-sheet transition in the recombinant prion protein
    • doi:10.1021/bi010232q. PMID:11389614
    • Morillas, M., Vanik, D.L., and Surewicz, W.K. 2001. On the mechanism of α-helix to β-sheet transition in the recombinant prion protein. Biochemistry, 40(23): 6982-6987. doi:10.1021/bi010232q. PMID:11389614.
    • (2001) Biochemistry , vol.40 , Issue.23 , pp. 6982-6987
    • Morillas, M.1    Vanik, D.L.2    Surewicz, W.K.3
  • 34
    • 23244467934 scopus 로고    scopus 로고
    • Interactions of peptides with a protein pore
    • doi:10.1529/biophysj.104.057406. PMID:15923222
    • Movileanu, L., Schmittschmitt, J.P., Scholtz, J.M., and Bayley, H. 2005. Interactions of peptides with a protein pore. Biophys. J. 89(2): 1030-1045. doi:10.1529/biophysj.104.057406. PMID:15923222.
    • (2005) Biophys. J. , vol.89 , Issue.2 , pp. 1030-1045
    • Movileanu, L.1    Schmittschmitt, J.P.2    Scholtz, J.M.3    Bayley, H.4
  • 35
    • 0031457157 scopus 로고    scopus 로고
    • Interaction of prion peptide HuPrP106-126 with nucleic acid
    • doi:10.1007/s007050050261. PMID:9672613
    • Nandi, P.K. 1997. Interaction of prion peptide HuPrP106-126 with nucleic acid. Arch. Virol. 142(12): 2537-2545. doi:10.1007/s007050050261. PMID:9672613.
    • (1997) Arch. Virol. , vol.142 , Issue.12 , pp. 2537-2545
    • Nandi, P.K.1
  • 36
    • 34147108667 scopus 로고    scopus 로고
    • Unfolding of Proteins and Long Transient Conformations Detected by Single Nanopore Recording
    • doi:10.1103/PhysRevLett.98.158101
    • Oukhaled, G., Mathé, J., Biance, A.-L., Bacri, L., Betton, J.-M., Lairez, D., et al. 2007. Unfolding of Proteins and Long Transient Conformations Detected by Single Nanopore Recording. PRL, 98(15): 158101-158104. doi:10.1103/PhysRevLett.98.158101.
    • (2007) PRL , vol.98 , Issue.15 , pp. 158101-158104
    • Oukhaled, G.1    Mathé, J.2    Biance, A.-L.3    Bacri, L.4    Betton, J.-M.5    Lairez, D.6
  • 37
    • 0035902194 scopus 로고    scopus 로고
    • Neurodegenerative diseases and prions
    • doi:10.1056/NEJM200105173442006. PMID:11357156
    • Prusiner, S.B. 2001. Neurodegenerative diseases and prions. N. Engl. J. Med. 344(20): 1516-1526. doi:10.1056/NEJM200105173442006. PMID:11357156.
    • (2001) N. Engl. J. Med. , vol.344 , Issue.20 , pp. 1516-1526
    • Prusiner, S.B.1
  • 38
    • 0035815738 scopus 로고    scopus 로고
    • Copper Converts the Cellular Prion Protein into a Protease-resistant Species That Is Distinct from the Scrapie Isoform
    • doi:10.1074/jbc.M009666200
    • Quaglio, E., Chiesa, R., and Harris, D.A. 2001. Copper Converts the Cellular Prion Protein into a Protease-resistant Species That Is Distinct from the Scrapie Isoform. J. Biol. Chem. 276(14): 11432-11438. doi:10.1074/jbc. M009666200.
    • (2001) J. Biol. Chem. , vol.276 , Issue.14 , pp. 11432-11438
    • Quaglio, E.1    Chiesa, R.2    Harris, D.A.3
  • 39
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • doi:10.1038/35081095. PMID:11459061
    • Saborio, G.P., Permanne, B., and Soto, C. 2001. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature, 411(6839): 810-813. doi:10.1038/35081095. PMID:11459061.
    • (2001) Nature , vol.411 , Issue.6839 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 40
    • 17144391818 scopus 로고    scopus 로고
    • Protein biosensors based on biofunctionalized conical gold nanotubes
    • doi:10.1021/ja043910f. PMID:15810817
    • Siwy, Z., Trofin, L., Kohli, P., Baker, L.A., Trautmann, C., and Martin, C.R. 2005. Protein biosensors based on biofunctionalized conical gold nanotubes. J. Am. Chem. Soc. 127(14): 5000-5001. doi:10.1021/ja043910f. PMID:15810817.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.14 , pp. 5000-5001
    • Siwy, Z.1    Trofin, L.2    Kohli, P.3    Baker, L.A.4    Trautmann, C.5    Martin, C.R.6
  • 41
    • 55349108537 scopus 로고    scopus 로고
    • Nanopore analysis of the folding of zinc fingers
    • doi:10.1002/smll.200800585. PMID:18819138
    • Stefureac, R.I., and Lee, J.S. 2008. Nanopore analysis of the folding of zinc fingers. Small, 4(10): 1646-1650. doi:10.1002/smll.200800585. PMID:18819138.
    • (2008) Small , vol.4 , Issue.10 , pp. 1646-1650
    • Stefureac, R.I.1    Lee, J.S.2
  • 42
    • 33746590221 scopus 로고    scopus 로고
    • Transport of α-helical peptides through alpha-hemolysin and aerolysin pores
    • doi:10.1021/bi0604835. PMID:16866363
    • Stefureac, R., Long, Y.T., Kraatz, H.B., Howard, P., and Lee, J.S. 2006. Transport of α-helical peptides through alpha-hemolysin and aerolysin pores. Biochemistry, 45(30): 9172-9179. doi:10.1021/bi0604835. PMID:16866363.
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9172-9179
    • Stefureac, R.1    Long, Y.T.2    Kraatz, H.B.3    Howard, P.4    Lee, J.S.5
  • 43
    • 38849087309 scopus 로고    scopus 로고
    • Nano-pore analysis of a small 86-residue protein
    • doi:10.1002/smll.200700402. PMID:18058890
    • Stefureac, R., Waldner, L., Howard, P., and Lee, J.S. 2008. Nano-pore analysis of a small 86-residue protein. Small, 4(1): 59-63. doi:10.1002/smll. 200700402. PMID:18058890.
    • (2008) Small , vol.4 , Issue.1 , pp. 59-63
    • Stefureac, R.1    Waldner, L.2    Howard, P.3    Lee, J.S.4
  • 44
    • 0037965529 scopus 로고    scopus 로고
    • Prion protein selectively binds copper(II) ions
    • doi:10.1021/bi972827k. PMID:9585530
    • Stöckel, J., Safar, J., Wallace, A.C., Cohen, F.E., and Prusiner, S.B. 1998. Prion protein selectively binds copper(II) ions. Biochemistry, 37(20): 7185-7193. doi:10.1021/bi972827k. PMID:9585530.
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7185-7193
    • Stöckel, J.1    Safar, J.2    Wallace, A.C.3    Cohen, F.E.4    Prusiner, S.B.5
  • 46
    • 34250802050 scopus 로고    scopus 로고
    • Dual polarisation interferometry analysis of copper binding to the prion protein: Evidence for two folding states
    • PMID:17573247
    • Thompsett, A.R., and Brown, D.R. 2007. Dual polarisation interferometry analysis of copper binding to the prion protein: evidence for two folding states. Biochim. Biophys. Acta, 1774(7): 920-927. PMID:17573247.
    • (2007) Biochim. Biophys. Acta , vol.1774 , Issue.7 , pp. 920-927
    • Thompsett, A.R.1    Brown, D.R.2
  • 47
    • 13844299007 scopus 로고    scopus 로고
    • Copper binding to prion octarepeat peptides, a combined metal chelate affinity and immunochemical approaches
    • doi:10.1016/j.jchromb.2004.10.011. PMID:15722047
    • Todorova-Balvay, D., Simon, S., Créminon, C., Grassi, J., Srikrishnan, T., and Vijayalakshmi, M.A. 2005. Copper binding to prion octarepeat peptides, a combined metal chelate affinity and immunochemical approaches. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 818(1): 75-82. doi:10.1016/j.jchromb.2004.10.011. PMID:15722047.
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.818 , Issue.1 , pp. 75-82
    • Todorova-Balvay, D.1    Simon, S.2    Créminon, C.3    Grassi, J.4    Srikrishnan, T.5    Vijayalakshmi, M.A.6
  • 48
    • 48249097986 scopus 로고    scopus 로고
    • 2 concept
    • doi:10.1146/annurev.biophys.37.032807.125924. PMID:18573080
    • 2 concept. Annu Rev Biophys, 37(1): 215-246. doi:10.1146/annurev. biophys.37.032807.125924. PMID:18573080.
    • (2008) Annu Rev Biophys , vol.37 , Issue.1 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 49
    • 33745761652 scopus 로고    scopus 로고
    • Role of copper in prion diseases: Deleterious or beneficial?
    • doi:10.2174/138161206777698873. PMID:16842180
    • Varela-Nallar, L., González, A., and Inestrosa, N.C. 2006. Role of copper in prion diseases: deleterious or beneficial? Curr. Pharm. Des. 12(20): 2587-2595. doi:10.2174/138161206777698873. PMID:16842180.
    • (2006) Curr. Pharm. Des. , vol.12 , Issue.20 , pp. 2587-2595
    • Varela-Nallar, L.1    González, A.2    Inestrosa, N.C.3
  • 50
    • 61449258353 scopus 로고    scopus 로고
    • Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein
    • doi:10.1016/j.str.2008.12.018. PMID:19278656
    • Walsh, P., Simonetti, K., and Sharpe, S. 2009. Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein. Structure, 17(3): 417-426. doi:10.1016/j.str.2008.12.018. PMID:19278656.
    • (2009) Structure , vol.17 , Issue.3 , pp. 417-426
    • Walsh, P.1    Simonetti, K.2    Sharpe, S.3
  • 51
    • 33751108289 scopus 로고    scopus 로고
    • The affinity of copper binding to the prion protein octarepeat domain: Evidence for negative cooperativity
    • doi:10.1021/bi060948r. PMID:17059225
    • Walter, E.D., Chattopadhyay, M., and Millhauser, G.L. 2006. The affinity of copper binding to the prion protein octarepeat domain: evidence for negative cooperativity. Biochemistry, 45(43): 13083-13092. doi:10.1021/bi060948r. PMID:17059225.
    • (2006) Biochemistry , vol.45 , Issue.43 , pp. 13083-13092
    • Walter, E.D.1    Chattopadhyay, M.2    Millhauser, G.L.3
  • 52
    • 33750571382 scopus 로고    scopus 로고
    • A reassessment of copper(II) binding in the full-length prion protein
    • doi:10.1042/BJ20060458. PMID:16824036
    • Wells, M.A., Jackson, G.S., Jones, S., Hosszu, L.L.P., Craven, C.J., Clarke, A.R., et al. 2006. A reassessment of copper(II) binding in the full-length prion protein. Biochem. J. 399(3): 435-444. doi:10.1042/BJ20060458. PMID:16824036.
    • (2006) Biochem. J. , vol.399 , Issue.3 , pp. 435-444
    • Wells, M.A.1    Jackson, G.S.2    Jones, S.3    Hosszu, L.L.P.4    Craven, C.J.5    Clarke, A.R.6
  • 53
    • 0347480547 scopus 로고    scopus 로고
    • Infrared Study of the Stability and Folding Kinetics of a 15-Residue β-Hairpin
    • doi:10.1021/ja037053b
    • Xu, Y., Oyola, R., and Gai, F. 2003. Infrared Study of the Stability and Folding Kinetics of a 15-Residue β-Hairpin. J. Am. Chem. Soc. 125(50): 15388-15394. doi:10.1021/ja037053b.
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.50 , pp. 15388-15394
    • Xu, Y.1    Oyola, R.2    Gai, F.3
  • 54
    • 65249122020 scopus 로고    scopus 로고
    • Study of peptide transport through engineered protein channels
    • doi:10.1021/jp809842g. PMID:19231820
    • Zhao, Q., Jayawardhana, D.A., Wang, D., and Guan, X. 2009. Study of peptide transport through engineered protein channels. J. Phys. Chem. B, 113(11): 3572-3578. doi:10.1021/jp809842g. PMID:19231820.
    • (2009) J. Phys. Chem. B , vol.113 , Issue.11 , pp. 3572-3578
    • Zhao, Q.1    Jayawardhana, D.A.2    Wang, D.3    Guan, X.4
  • 55
    • 39749155839 scopus 로고    scopus 로고
    • Raman optical activity and circular dichroism reveal dramatic differences in the influence of divalent copper and manganese ions on prion protein folding
    • doi:10.1021/bi7022893. PMID:18205409
    • Zhu, F., Davies, P., Thompsett, A.R., Kelly, S.M., Tranter, G.E., Hecht, L., et al. 2008. Raman optical activity and circular dichroism reveal dramatic differences in the influence of divalent copper and manganese ions on prion protein folding. Biochemistry, 47(8): 2510-2517. doi:10.1021/bi7022893. PMID:18205409.
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2510-2517
    • Zhu, F.1    Davies, P.2    Thompsett, A.R.3    Kelly, S.M.4    Tranter, G.E.5    Hecht, L.6


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