메뉴 건너뛰기




Volumn 44, Issue 6, 2010, Pages 958-967

Optimization of the methods for small peptide solution structure determination by NMR spectroscopy

Author keywords

amyloid; Alzheimer disease; molecular dynamics; NMR spectroscopy; peptide structure

Indexed keywords

RATTUS;

EID: 78649999322     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893310060130     Document Type: Article
Times cited : (4)

References (40)
  • 1
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • Aguzzi A., O'Connor T. 2010. Protein aggregation diseases: Pathogenicity and therapeutic perspectives. Nature Rev. Drug Discov. 9, 237-248.
    • (2010) Nature Rev. Drug Discov. , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 2
    • 34247512523 scopus 로고    scopus 로고
    • Molecular basis of Alzheimer's disease
    • Grigorenko A. P., Rogaev E. I. 2007. Molecular basis of Alzheimer's disease. Mol. Biol. (Moscow) 41, 294-307.
    • (2007) Mol. Biol. (Moscow) , vol.41 , pp. 294-307
    • Grigorenko, A.P.1    Rogaev, E.I.2
  • 3
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G. G., Wong C. W. 1984. Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122, 1131-1135.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 6
    • 38549117383 scopus 로고    scopus 로고
    • The N-domain of angiotensin-converting enzyme specifically hydrolyzes the Arg-5-His-6 bond of Alzheimer's Abeta-(1-16) peptide and its isoAsp-7 analogue with different efficiency as evidenced by quantitative matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Toropygin I. Y., Kugaevskaya E. V., Mirgorodskaya O. A., Elisseeva Y. E., Kozmin Y. P., Popov I. A., Nikolaev E. N., Makarov A. A., Kozin S. A. 2008. The N-domain of angiotensin-converting enzyme specifically hydrolyzes the Arg-5-His-6 bond of Alzheimer's Abeta-(1-16) peptide and its isoAsp-7 analogue with different efficiency as evidenced by quantitative matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 22, 231-239.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 231-239
    • Toropygin, I.Y.1    Kugaevskaya, E.V.2    Mirgorodskaya, O.A.3    Elisseeva, Y.E.4    Kozmin, Y.P.5    Popov, I.A.6    Nikolaev, E.N.7    Makarov, A.A.8    Kozin, S.A.9
  • 8
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids
    • Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., Davis D., Sinha S., et al. 1992. Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids. Nature. 359, 325-327.
    • (1992) Nature. , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3    Lee, M.4    Dovey, H.5    Davis, D.6    Sinha, S.7
  • 9
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J., 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
  • 11
    • 1842637853 scopus 로고    scopus 로고
    • Absolute structural constraints on amyloid fibrils from solid-state NMR spectroscopy of partially oriented samples
    • Oyler N. A., Tycko R. 2004. Absolute structural constraints on amyloid fibrils from solid-state NMR spectroscopy of partially oriented samples. J. Am. Chem. Soc. 126, 4478-4479.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4478-4479
    • Oyler, N.A.1    Tycko, R.2
  • 12
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova A. T., Yau W. M., Tycko R. 2006. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry. 45, 498-512.
    • (2006) Biochemistry. , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 13
    • 33751245122 scopus 로고    scopus 로고
    • Structural and thermodynamical properties of CuII amyloid-beta16/28 complexes associated with Alzheimer's disease
    • Guilloreau L., Damian L., Coppel Y., Mazarguil H., Winterhalter M., Faller P. 2006. Structural and thermodynamical properties of CuII amyloid-beta16/28 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
  • 14
  • 17
    • 70349858264 scopus 로고    scopus 로고
    • Effect of isomerization of aspartate-7 on the binding of copper (II) ion by the beta-amyloid peptide
    • Tsvetkov F. O., Makarov A. A., Archakov A. I., Kozin S. A. 2009. Effect of isomerization of aspartate-7 on the binding of copper (II) ion by the beta-amyloid peptide. Biofizika. 54, 197-201.
    • (2009) Biofizika. , vol.54 , pp. 197-201
    • Tsvetkov, F.O.1    Makarov, A.A.2    Archakov, A.I.3    Kozin, S.A.4
  • 18
    • 48649105912 scopus 로고    scopus 로고
    • Isomerization of the Asp7 residue results in zincinduced oligomerization of Alzheimer's disease amyloid beta(1-16) peptide
    • Tsvetkov P. O., Popov I. A., Nikolaev E. N., Archakov A. I., Makarov A. A., Kozin S. A. 2008. Isomerization of the Asp7 residue results in zincinduced oligomerization of Alzheimer's disease amyloid beta(1-16) peptide. Chembiochem. 9, 1564-1567.
    • (2008) Chembiochem. , vol.9 , pp. 1564-1567
    • Tsvetkov, P.O.1    Popov, I.A.2    Nikolaev, E.N.3    Archakov, A.I.4    Makarov, A.A.5    Kozin, S.A.6
  • 20
    • 77953113490 scopus 로고    scopus 로고
    • Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states
    • Miller Y., Ma B., Nussinov R. 2010. Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states. Proc. Natl. Acad. Sci. USA. 107, 9490-9495.
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 9490-9495
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 21
    • 0024005801 scopus 로고
    • Alzheimer's disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact
    • Shivers B. D., Hilbich C., Multhaup G., Salbaum M., Beyreuther K., Seeburg P. H. 1988. Alzheimer's disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact. EMBO J. 7, 1365-1370.
    • (1988) EMBO J. , vol.7 , pp. 1365-1370
    • Shivers, B.D.1    Hilbich, C.2    Multhaup, G.3    Salbaum, M.4    Beyreuther, K.5    Seeburg, P.H.6
  • 22
    • 55649119346 scopus 로고    scopus 로고
    • Solution NMR structure determination of proteins revisited
    • Billeter M., Wagner G., Wuthrich K. 2008. Solution NMR structure determination of proteins revisited. J. Biomol. NMR. 42, 155-158.
    • (2008) J. Biomol. NMR. , vol.42 , pp. 155-158
    • Billeter, M.1    Wagner, G.2    Wuthrich, K.3
  • 23
    • 0023008905 scopus 로고
    • Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin
    • Clore G. M., Brunger A. T., Karplus M., Gronenborn A. M. 1986. Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin. J. Mol. Biol. 191, 523-551.
    • (1986) J. Mol. Biol. , vol.191 , pp. 523-551
    • Clore, G.M.1    Brunger, A.T.2    Karplus, M.3    Gronenborn, A.M.4
  • 26
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • Linge J. P., Habeck M., Rieping W., Nilges M. 2003. ARIA: Automated NOE assignment and NMR structure calculation. Bioinformatics. 19, 315-316.
    • (2003) Bioinformatics. , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 27
    • 0033064496 scopus 로고    scopus 로고
    • Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
    • Linge J. P., Nilges M. 1999. Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation. J. Biomol. NMR. 13, 51-59.
    • (1999) J. Biomol. NMR. , vol.13 , pp. 51-59
    • Linge, J.P.1    Nilges, M.2
  • 29
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert P. 2004. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278, 353-378.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 30
    • 33645795710 scopus 로고    scopus 로고
    • Comparison of different torsion angle approaches for NMR structure determination
    • Bardiaux B., Malliavin T. E., Nilges M., Mazur A. K. 2006. Comparison of different torsion angle approaches for NMR structure determination. J. Biomol. NMR. 34, 153-166.
    • (2006) J. Biomol. NMR. , vol.34 , pp. 153-166
    • Bardiaux, B.1    Malliavin, T.E.2    Nilges, M.3    Mazur, A.K.4
  • 31
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak V., Abel R., Okur A., Strockbine B., Roitberg A., Simmerling C. 2006. Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins. 65, 712-725.
    • (2006) Proteins. , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 35
    • 0033061716 scopus 로고    scopus 로고
    • NMR structural characterization of cecropin A(1-8)-magainin 2(1-12) and cecropin A (1-8)-melittin (1-12) hybrid peptides
    • Oh D., Shin S. Y., Kang J. H., Hahm K. S., Kim K. L., Kim Y. 1999. NMR structural characterization of cecropin A(1-8)-magainin 2(1-12) and cecropin A (1-8)-melittin (1-12) hybrid peptides. J. Pept. Res. 53, 578-589.
    • (1999) J. Pept. Res. , vol.53 , pp. 578-589
    • Oh, D.1    Shin, S.Y.2    Kang, J.H.3    Hahm, K.S.4    Kim, K.L.5    Kim, Y.6
  • 36
    • 33748791718 scopus 로고    scopus 로고
    • Hydration thermodynamic properties of amino acid analogues: A systematic comparison of biomolecular force fields and water models
    • Hess B., van der Vegt N. F. 2006. Hydration thermodynamic properties of amino acid analogues: A systematic comparison of biomolecular force fields and water models. J. Phys. Chem. B. 110, 17616-17626.
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 17616-17626
    • Hess, B.1    van der Vegt, N.F.2
  • 37
    • 0035913754 scopus 로고    scopus 로고
    • Atomistic Brownian dynamics simulation of peptide phosphorylation
    • Shen T., Wong C. F., McCammon J. A. 2001. Atomistic Brownian dynamics simulation of peptide phosphorylation. J. Am. Chem. Soc. 123, 9107-9111.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9107-9111
    • Shen, T.1    Wong, C.F.2    McCammon, J.A.3
  • 38
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski R. A., Rullmannn J. A., MacArthur M. W., Kaptein R., Thornton J. M. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8, 477-486.
    • (1996) J. Biomol. NMR. , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 39
    • 0031083293 scopus 로고    scopus 로고
    • Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids
    • Kuszewski J., Gronenborn A. M., Clore G. M. 1997. Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J. Magn. Reson. 125, 171-177.
    • (1997) J. Magn. Reson. , vol.125 , pp. 171-177
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 40
    • 76149136021 scopus 로고    scopus 로고
    • Molecular simulation of ab initio protein folding for a millisecond folder NTL9(1-39)
    • Voelz V. A., Bowman G. R., Beauchamp K., Pande V. S. 2010. Molecular simulation of ab initio protein folding for a millisecond folder NTL9(1-39). J. Am. Chem. Soc. 132, 1526-1528.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1526-1528
    • Voelz, V.A.1    Bowman, G.R.2    Beauchamp, K.3    Pande, V.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.