메뉴 건너뛰기




Volumn 102, Issue 1, 2012, Pages 136-143

NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 16); AMYLOID BETA-PROTEIN (1-16); PEPTIDE FRAGMENT; ZINC;

EID: 84855426967     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.11.4006     Document Type: Article
Times cited : (54)

References (54)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 0037188472 scopus 로고    scopus 로고
    • The galvanization of β-amyloid in Alzheimer's disease
    • A.I. Bush, and R.E. Tanzi The galvanization of β-amyloid in Alzheimer's disease Proc. Natl. Acad. Sci. USA 99 2002 7317 7319
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7317-7319
    • Bush, A.I.1    Tanzi, R.E.2
  • 6
    • 72949094439 scopus 로고    scopus 로고
    • Copper and zinc binding to amyloid-β: Coordination, dynamics, aggregation, reactivity and metal-ion transfer
    • P. Faller Copper and zinc binding to amyloid-β: coordination, dynamics, aggregation, reactivity and metal-ion transfer ChemBioChem 10 2009 2837 2845
    • (2009) ChemBioChem , vol.10 , pp. 2837-2845
    • Faller, P.1
  • 8
    • 79952614047 scopus 로고    scopus 로고
    • 2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy
    • 2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy J. Am. Chem. Soc. 133 2011 3390 3400
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3390-3400
    • Parthasarathy, S.1    Long, F.2    Ishii, Y.3
  • 9
    • 33845665797 scopus 로고    scopus 로고
    • High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide
    • DOI 10.1111/j.1742-4658.2006.05563.x
    • J. Danielsson, and R. Pierattelli A. Gräslund High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide FEBS J. 274 2007 46 59 (Pubitemid 44952897)
    • (2007) FEBS Journal , vol.274 , Issue.1 , pp. 46-59
    • Danielsson, J.1    Pierattelli, R.2    Banci, L.3    Graslund, A.4
  • 12
    • 33644530354 scopus 로고    scopus 로고
    • 2+ binding to amyloid-β peptide (Aβ) of Alzheimer's disease
    • 2+ binding to amyloid-β peptide (Aβ) of Alzheimer's disease Biochim. Biophys. Acta 1764 2006 246 256
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 246-256
    • Syme, C.D.1    Viles, J.H.2
  • 13
    • 36749044742 scopus 로고    scopus 로고
    • Zinc binding to amyloid-β: Isothermal titration calorimetry and Zn competition experiments with Zn sensors
    • DOI 10.1021/bi701355j
    • C. Talmard, A. Bouzan, and P. Faller Zinc binding to amyloid-β: isothermal titration calorimetry and Zn competition experiments with Zn sensors Biochemistry 46 2007 13658 13666 (Pubitemid 350209961)
    • (2007) Biochemistry , vol.46 , Issue.47 , pp. 13658-13666
    • Talmard, C.1    Bouzan, A.2    Faller, P.3
  • 14
    • 0033747946 scopus 로고    scopus 로고
    • Examining the zinc binding site of the amyloid-β peptide
    • D.S. Yang, and J. McLaurin P.E. Fraser Examining the zinc binding site of the amyloid-β peptide Eur. J. Biochem. 267 2000 6692 6698
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6692-6698
    • Yang, D.S.1    McLaurin, J.2    Fraser, P.E.3
  • 15
    • 80052489511 scopus 로고    scopus 로고
    • Effect of zinc binding on β-amyloid structure and dynamics: Implications for Aβ aggregation
    • N. Rezaei-Ghaleh, and K. Giller M. Zweckstetter Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation Biophys. J. 101 2011 1202 1211
    • (2011) Biophys. J. , vol.101 , pp. 1202-1211
    • Rezaei-Ghaleh, N.1    Giller, K.2    Zweckstetter, M.3
  • 16
    • 79952640802 scopus 로고    scopus 로고
    • Zinc-induced dimerization of the amyloid-β metal-binding domain 1-16 is mediated by residues 11-14
    • S.A. Kozin, and Y.V. Mezentsev A.A. Makarov Zinc-induced dimerization of the amyloid-β metal-binding domain 1-16 is mediated by residues 11-14 Mol. Biosyst. 7 2011 1053 1055
    • (2011) Mol. Biosyst. , vol.7 , pp. 1053-1055
    • Kozin, S.A.1    Mezentsev, Y.V.2    Makarov, A.A.3
  • 17
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-β(1-42) fibrils
    • T. Lührs, and C. Ritter R. Riek 3D structure of Alzheimer's amyloid-β(1-42) fibrils Proc. Natl. Acad. Sci. USA 102 2005 17342 17347
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17342-17347
    • Lührs, T.1    Ritter, C.2    Riek, R.3
  • 18
    • 77953113490 scopus 로고    scopus 로고
    • Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states
    • Y. Miller, B. Ma, and R. Nussinov Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states Proc. Natl. Acad. Sci. USA 107 2010 9490 9495
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 9490-9495
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 19
    • 77954892793 scopus 로고    scopus 로고
    • Polymorphism in Alzheimer Aβ amyloid organization reflects conformational selection in a rugged energy landscape
    • Y. Miller, B. Ma, and R. Nussinov Polymorphism in Alzheimer Aβ amyloid organization reflects conformational selection in a rugged energy landscape Chem. Rev. 110 2010 4820 4838
    • (2010) Chem. Rev. , vol.110 , pp. 4820-4838
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 20
    • 0024005801 scopus 로고
    • Alzheimer's disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact
    • B.D. Shivers, and C. Hilbich P.H. Seeburg Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact EMBO J. 7 1988 1365 1370
    • (1988) EMBO J. , vol.7 , pp. 1365-1370
    • Shivers, B.D.1    Hilbich, C.2    Seeburg, P.H.3
  • 21
    • 0028892096 scopus 로고
    • Production of intracellular amyloid-containing fragments in hippocampal neurons expressing human amyloid precursor protein and protection against amyloidogenesis by subtle amino acid substitutions in the rodent sequence
    • B. De Strooper, and M. Simons C.G. Dotti Production of intracellular amyloid-containing fragments in hippocampal neurons expressing human amyloid precursor protein and protection against amyloidogenesis by subtle amino acid substitutions in the rodent sequence EMBO J. 14 1995 4932 4938
    • (1995) EMBO J. , vol.14 , pp. 4932-4938
    • De Strooper, B.1    Simons, M.2    Dotti, C.G.3
  • 22
    • 59449097016 scopus 로고    scopus 로고
    • Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
    • P. Faller, and C. Hureau Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide Dalton Trans. 7 2009 1080 1094
    • (2009) Dalton Trans. , Issue.7 , pp. 1080-1094
    • Faller, P.1    Hureau, C.2
  • 23
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the Aβ peptide of Alzheimer's disease
    • S.T. Liu, G. Howlett, and C.J. Barrow Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the Aβ peptide of Alzheimer's disease Biochemistry 38 1999 9373 9378
    • (1999) Biochemistry , vol.38 , pp. 9373-9378
    • Liu, S.T.1    Howlett, G.2    Barrow, C.J.3
  • 24
    • 3943055547 scopus 로고    scopus 로고
    • The solution structure of rat Aβ-(1-28) and its interaction with zinc ion: Insights into the scarcity of amyloid deposition in aged rat brain
    • J. Huang, and Y. Yao W.X. Tang Dagger The solution structure of rat Aβ-(1-28) and its interaction with zinc ion: insights into the scarcity of amyloid deposition in aged rat brain J. Biol. Inorg. Chem. 9 2004 627 635 (Pubitemid 39050158)
    • (2004) Journal of Biological Inorganic Chemistry , vol.9 , Issue.5 , pp. 627-635
    • Huang, J.1    Yao, Y.2    Lin, J.3    Ye, Y.-H.4    Sun, W.-Y.5    Tang, W.-X.6
  • 25
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • F. Delaglio, and S. Grzesiek A. Bax NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 28
    • 0029335636 scopus 로고
    • Determination of stereospecific assignments, torsion-angle constraints, and rotamer populations in proteins using the program AngleSearch
    • V.I. Polshakov, and T.A. Frenkiel J. Feeney Determination of stereospecific assignments, torsion-angle constraints, and rotamer populations in proteins using the program AngleSearch J. Magn. Reson. B 108 1995 31 43
    • (1995) J. Magn. Reson. B , vol.108 , pp. 31-43
    • Polshakov, V.I.1    Frenkiel, T.A.2    Feeney, J.3
  • 29
    • 33748791718 scopus 로고    scopus 로고
    • Hydration thermodynamic properties of amino acid analogues: A systematic comparison of biomolecular force fields and water models
    • DOI 10.1021/jp0641029
    • B. Hess, and N.F. van der Vegt Hydration thermodynamic properties of amino acid analogues: a systematic comparison of biomolecular force fields and water models J. Phys. Chem. B 110 2006 17616 17626 (Pubitemid 44412512)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.35 , pp. 17616-17626
    • Hess, B.1    Van Der Vegt, N.F.A.2
  • 33
    • 78649999322 scopus 로고    scopus 로고
    • Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
    • A.N. Istrate, and A.B. Mantsyzov V.I. Polshakov Optimization of the methods for small peptide solution structure determination by NMR spectroscopy Mol. Biol. 44 2010 958 967
    • (2010) Mol. Biol. , vol.44 , pp. 958-967
    • Istrate, A.N.1    Mantsyzov, A.B.2    Polshakov, V.I.3
  • 35
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • M. Karplus, and G.A. Petsko Molecular dynamics simulations in biology Nature 347 1990 631 639
    • (1990) Nature , vol.347 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 36
    • 33846327607 scopus 로고    scopus 로고
    • A regularized and renormalized electrostatic coupling Hamiltonian for hybrid quantum-mechanical-molecular-mechanical calculations
    • P.K. Biswas, and V. Gogonea A regularized and renormalized electrostatic coupling Hamiltonian for hybrid quantum-mechanical-molecular-mechanical calculations J. Chem. Phys. 123 2005 164114
    • (2005) J. Chem. Phys. , vol.123 , pp. 164114
    • Biswas, P.K.1    Gogonea, V.2
  • 37
    • 0037156101 scopus 로고    scopus 로고
    • A Hamiltonian electrostatic coupling scheme for hybrid Car-Parrinello molecular dynamics simulations
    • A. Laio A Hamiltonian electrostatic coupling scheme for hybrid Car-Parrinello molecular dynamics simulations J. Chem. Phys. 116 2002 6941
    • (2002) J. Chem. Phys. , vol.116 , pp. 6941
    • Laio, A.1
  • 39
    • 4544344290 scopus 로고    scopus 로고
    • Green oxidation catalysts: Computational design of high-efficiency models of galactose oxidase
    • DOI 10.1002/anie.200454081
    • L. Guidoni, and K. Spiegel U. Röthlisberger Green oxidation catalysts: computational design of high-efficiency models of galactose oxidase Angew. Chem. Int. Ed. Engl. 43 2004 3286 3289 (Pubitemid 39257584)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.25 , pp. 3286-3289
    • Guidoni, L.1    Spiegel, K.2    Zumstein, M.3    Rothlisberger, U.4
  • 40
    • 1542305706 scopus 로고    scopus 로고
    • Cisplatin binding to DNA oligomers from hybrid Car-Parrinello/molecular dynamics simulations
    • K. Spiegel, U. Rothlisberger, and P. Carloni Cisplatin binding to DNA oligomers from hybrid Car-Parrinello/molecular dynamics simulations J. Phys. Chem. B 108 2004 2699 2707
    • (2004) J. Phys. Chem. B , vol.108 , pp. 2699-2707
    • Spiegel, K.1    Rothlisberger, U.2    Carloni, P.3
  • 41
    • 68849100968 scopus 로고    scopus 로고
    • 2+ binding in the 1-16 region of the amyloid β peptide involved in Alzheimer's disease
    • 2+ binding in the 1-16 region of the amyloid β peptide involved in Alzheimer's disease Phys. Chem. Chem. Phys. 11 2009 6468 6481
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6468-6481
    • Furlan, S.1    La Penna, G.2
  • 42
    • 47549108470 scopus 로고    scopus 로고
    • The role of metals in amyloid aggregation - Experiments and ab initio simulations
    • V. Minicozzi, and S. Morante K. Jansen The role of metals in amyloid aggregation - experiments and ab initio simulations Int. J. Quantum Chem. 108 2008 1992 2015
    • (2008) Int. J. Quantum Chem. , vol.108 , pp. 1992-2015
    • Minicozzi, V.1    Morante, S.2    Jansen, K.3
  • 43
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Y. Duan, and C. Wu P. Kollman A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations J. Comput. Chem. 24 2003 1999 2012
    • (2003) J. Comput. Chem. , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Kollman, P.3
  • 44
    • 4043164887 scopus 로고    scopus 로고
    • Accurate description of van der Waals complexes by density functional theory including empirical corrections
    • S. Grimme Accurate description of van der Waals complexes by density functional theory including empirical corrections J. Comput. Chem. 25 2004 1463 1473
    • (2004) J. Comput. Chem. , vol.25 , pp. 1463-1473
    • Grimme, S.1
  • 45
  • 46
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 47
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • S. Nose A unified formulation of the constant temperature molecular dynamics methods J. Chem. Phys. 81 1984 511 519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nose, S.1
  • 48
    • 0001172461 scopus 로고
    • Implementation of ultrasoft pseudopotentials in ab initio molecular dynamics
    • K. Laasonen, and R. Car D. Vanderbilt Implementation of ultrasoft pseudopotentials in ab initio molecular dynamics Phys. Rev. B Condens. Matter 43 1991 6796 6799
    • (1991) Phys. Rev. B Condens. Matter , vol.43 , pp. 6796-6799
    • Laasonen, K.1    Car, R.2    Vanderbilt, D.3
  • 49
    • 34247648401 scopus 로고
    • Car-Parrinello molecular dynamics with Vanderbilt ultrasoft pseudopotentials
    • K. Laasonen, and A. Pasquarello D. Vanderbilt Car-Parrinello molecular dynamics with Vanderbilt ultrasoft pseudopotentials Phys. Rev. B Condens. Matter 47 1993 10142 10153
    • (1993) Phys. Rev. B Condens. Matter , vol.47 , pp. 10142-10153
    • Laasonen, K.1    Pasquarello, A.2    Vanderbilt, D.3
  • 50
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • C.C. Curtain, and F. Ali K.J. Barnham Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits J. Biol. Chem. 276 2001 20466 20473
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Barnham, K.J.3
  • 51
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR Study
    • DOI 10.1016/j.jmb.2007.02.093, PII S0022283607003105
    • N.G. Sgourakis, and Y. Yan A.E. Garcia The Alzheimer's peptides Aβ40 and 42 adopt distinct conformations in water: a combined MD/NMR study J. Mol. Biol. 368 2007 1448 1457 (Pubitemid 46617600)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1448-1457
    • Sgourakis, N.G.1    Yan, Y.2    McCallum, S.A.3    Wang, C.4    Garcia, A.E.5
  • 52
    • 78650863624 scopus 로고    scopus 로고
    • Atomic-level characterization of the ensemble of the Aβ(1-42) monomer in water using unbiased molecular dynamics simulations and spectral algorithms
    • N.G. Sgourakis, and M. Merced-Serrano A.E. Garcia Atomic-level characterization of the ensemble of the Aβ(1-42) monomer in water using unbiased molecular dynamics simulations and spectral algorithms J. Mol. Biol. 405 2011 570 583
    • (2011) J. Mol. Biol. , vol.405 , pp. 570-583
    • Sgourakis, N.G.1    Merced-Serrano, M.2    Garcia, A.E.3
  • 53
    • 48649105912 scopus 로고    scopus 로고
    • Isomerization of the Asp7 residue results in zinc-induced oligomerization of Alzheimer's disease amyloid β(1-16) peptide
    • P.O. Tsvetkov, and I.A. Popov S.A. Kozin Isomerization of the Asp7 residue results in zinc-induced oligomerization of Alzheimer's disease amyloid β(1-16) peptide ChemBioChem 9 2008 1564 1567
    • (2008) ChemBioChem , vol.9 , pp. 1564-1567
    • Tsvetkov, P.O.1    Popov, I.A.2    Kozin, S.A.3
  • 54
    • 44849096899 scopus 로고    scopus 로고
    • Identifying the minimal copper- and zinc-binding site sequence in amyloid-β peptides
    • V. Minicozzi, and F. Stellato S. Morante Identifying the minimal copper- and zinc-binding site sequence in amyloid-β peptides J. Biol. Chem. 283 2008 10784 10792
    • (2008) J. Biol. Chem. , vol.283 , pp. 10784-10792
    • Minicozzi, V.1    Stellato, F.2    Morante, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.