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Volumn 10, Issue 3, 2014, Pages 412-420

Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN;

EID: 84893481355     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/c3mb70420c     Document Type: Article
Times cited : (23)

References (49)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C. M. Dobson Protein folding and misfolding Nature 2003 426 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • F. U. Hartl Molecular chaperones in cellular protein folding Nature 1996 381 571 580
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 3
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • T. Eichner S. E. Radford A diversity of assembly mechanisms of a generic amyloid fold Mol. Cell 2011 43 8 18
    • (2011) Mol. Cell , vol.43 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Annual Reviews, Palo Alto
    • F. Chiti and C. M. Dobson, Protein misfolding, functional amyloid, and human disease, Annual Review of Biochemistry, Annual Reviews, Palo Alto, 2006, pp. 333-366
    • (2006) Annual Review of Biochemistry , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 80053596817 scopus 로고    scopus 로고
    • Understanding the complex mechanisms of beta 2-microglobulin amyloid assembly
    • T. Eichner S. E. Radford Understanding the complex mechanisms of beta 2-microglobulin amyloid assembly FEBS J. 2011 278 3868 3883
    • (2011) FEBS J. , vol.278 , pp. 3868-3883
    • Eichner, T.1    Radford, S.E.2
  • 8
    • 60949106895 scopus 로고    scopus 로고
    • A generic mechanism of beta(2)-Microglobulin amyloid assembly at neutral pH involving a specific proline switch
    • T. Eichner S. E. Radford A generic mechanism of beta(2)-Microglobulin amyloid assembly at neutral pH involving a specific proline switch J. Mol. Biol. 2009 386 1312 1326
    • (2009) J. Mol. Biol. , vol.386 , pp. 1312-1326
    • Eichner, T.1    Radford, S.E.2
  • 10
    • 66749133376 scopus 로고    scopus 로고
    • Metal binding sheds light on mechanisms of amyloid assembly
    • M. F. Calabrese A. D. Miranker Metal binding sheds light on mechanisms of amyloid assembly Prion 2009 3 1 4
    • (2009) Prion , vol.3 , pp. 1-4
    • Calabrese, M.F.1    Miranker, A.D.2
  • 11
    • 0035955555 scopus 로고    scopus 로고
    • Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
    • N. M. Kad N. H. Thomson D. P. Smith D. A. Smith S. E. Radford Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro J. Mol. Biol. 2001 313 559 571
    • (2001) J. Mol. Biol. , vol.313 , pp. 559-571
    • Kad, N.M.1    Thomson, N.H.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5
  • 12
    • 41149162020 scopus 로고    scopus 로고
    • Fibril growth kinetics reveal a region of beta(2)-microglobulin important for nucleation and elongation of aggregation
    • G. W. Platt K. E. Routledge S. W. Homans S. E. Radford Fibril growth kinetics reveal a region of beta(2)-microglobulin important for nucleation and elongation of aggregation J. Mol. Biol. 2008 378 251 263
    • (2008) J. Mol. Biol. , vol.378 , pp. 251-263
    • Platt, G.W.1    Routledge, K.E.2    Homans, S.W.3    Radford, S.E.4
  • 13
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of beta(2)-microglobulin into amyloid
    • W. S. Gosal I. J. Morten E. W. Hewitt D. A. Smith N. H. Thomson S. E. Radford Competing pathways determine fibril morphology in the self-assembly of beta(2)-microglobulin into amyloid J. Mol. Biol. 2005 351 850 864
    • (2005) J. Mol. Biol. , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5    Radford, S.E.6
  • 14
    • 33144471714 scopus 로고    scopus 로고
    • A systematic study of the effect of physiological factors on beta 2-microglobulin amyloid formation at neutral pH
    • S. L. Myers S. Jones T. R. Jahn I. J. Morten G. A. Tennent E. W. Hewitt S. E. Radford A systematic study of the effect of physiological factors on beta 2-microglobulin amyloid formation at neutral pH Biochemistry 2006 45 2311 2321
    • (2006) Biochemistry , vol.45 , pp. 2311-2321
    • Myers, S.L.1    Jones, S.2    Jahn, T.R.3    Morten, I.J.4    Tennent, G.A.5    Hewitt, E.W.6    Radford, S.E.7
  • 15
    • 0038575395 scopus 로고    scopus 로고
    • A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation
    • D. P. Smith S. Jones L. C. Serpell M. Sunde S. E. Radford A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation J. Mol. Biol. 2003 330 943 954
    • (2003) J. Mol. Biol. , vol.330 , pp. 943-954
    • Smith, D.P.1    Jones, S.2    Serpell, L.C.3    Sunde, M.4    Radford, S.E.5
  • 16
    • 77952759080 scopus 로고    scopus 로고
    • Stacked sets of parallel, in-register beta-strands of beta(2)-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling
    • C. L. Ladner M. Chen D. P. Smith G. W. Platt S. E. Radford R. Langen Stacked sets of parallel, in-register beta-strands of beta(2)-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling J. Biol. Chem. 2010 285 17137 17147
    • (2010) J. Biol. Chem. , vol.285 , pp. 17137-17147
    • Ladner, C.L.1    Chen, M.2    Smith, D.P.3    Platt, G.W.4    Radford, S.E.5    Langen, R.6
  • 19
    • 77953912267 scopus 로고    scopus 로고
    • Mass spectrometry and the amyloid problem-how far can we go in the gas phase?
    • A. E. Ashcroft Mass spectrometry and the amyloid problem-how far can we go in the gas phase? J. Am. Soc. Mass Spectrom. 2010 21 1087 1096
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1087-1096
    • Ashcroft, A.E.1
  • 20
    • 84876298403 scopus 로고    scopus 로고
    • Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry
    • D. M. Williams T. L. Pukala Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry Mass Spectrom. Rev. 2013 32 169 187
    • (2013) Mass Spectrom. Rev. , vol.32 , pp. 169-187
    • Williams, D.M.1    Pukala, T.L.2
  • 22
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain A-beta distinguish Alzheimer's disease from normal and pathologic aging
    • J. Wang D. W. Dickson J. Q. Trojanowski V. M. Y. Lee The levels of soluble versus insoluble brain A-beta distinguish Alzheimer's disease from normal and pathologic aging Exp. Neurol. 1999 158 328 337
    • (1999) Exp. Neurol. , vol.158 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 23
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
    • J. L. Tomic A. Pensalfini E. Head C. G. Glabe Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction Neurobiol. Dis. 2009 35 352 358
    • (2009) Neurobiol. Dis. , vol.35 , pp. 352-358
    • Tomic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, C.G.4
  • 25
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and non-native oligomers are the major cytotoxic species in tissue culture
    • N. Reixach S. Deechongkit X. Jiang J. W. Kelly J. N. Buxbaum Tissue damage in the amyloidoses: Transthyretin monomers and non-native oligomers are the major cytotoxic species in tissue culture Proc. Natl. Acad. Sci. U. S. A. 2004 101 2817 2822
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 27
    • 77951081386 scopus 로고    scopus 로고
    • Elongated oligomers in beta(2)-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
    • D. P. Smith S. E. Radford A. E. Ashcroft Elongated oligomers in beta(2)-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry Proc. Natl. Acad. Sci. U. S. A. 2010 107 6794 6798
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 6794-6798
    • Smith, D.P.1    Radford, S.E.2    Ashcroft, A.E.3
  • 28
    • 80052508937 scopus 로고    scopus 로고
    • Structure and dynamics of oligomeric intermediates in beta(2)-microglobulin self-assembly
    • D. P. Smith L. A. Woods S. E. Radford A. E. Ashcroft Structure and dynamics of oligomeric intermediates in beta(2)-microglobulin self-assembly Biophys. J. 2011 101 1238 1247
    • (2011) Biophys. J. , vol.101 , pp. 1238-1247
    • Smith, D.P.1    Woods, L.A.2    Radford, S.E.3    Ashcroft, A.E.4
  • 30
    • 58249094358 scopus 로고    scopus 로고
    • HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1
    • J. P. Hodkinson T. R. Jahn S. E. Radford A. E. Ashcroft HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1 J. Am. Soc. Mass Spectrom. 2009 20 278 286
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 278-286
    • Hodkinson, J.P.1    Jahn, T.R.2    Radford, S.E.3    Ashcroft, A.E.4
  • 33
    • 65849165676 scopus 로고    scopus 로고
    • Competition between intramolecular and intermolecular interactions in an amyloid-forming protein
    • K. E. Routledge G. G. Tartaglia G. W. Platt M. Vendrusco S. E. Radford Competition between intramolecular and intermolecular interactions in an amyloid-forming protein J. Mol. Biol. 2009 389 776 786
    • (2009) J. Mol. Biol. , vol.389 , pp. 776-786
    • Routledge, K.E.1    Tartaglia, G.G.2    Platt, G.W.3    Vendrusco, M.4    Radford, S.E.5
  • 34
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation
    • P. Hortschansky V. Schroeckh T. Christopeit G. Zandomeneghi M. Fandrich The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation Protein Sci. 2005 14 1753 1759
    • (2005) Protein Sci. , vol.14 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fandrich, M.5
  • 35
    • 0032030642 scopus 로고    scopus 로고
    • Characterization of the interactions between MHC class i subunits: A systematic approach for the engineering of higher affinity variants of beta(2)-microglobulin
    • M. J. Shields N. Assefi W. Hodgson E. J. Kim R. K. Ribaudo Characterization of the interactions between MHC class I subunits: A systematic approach for the engineering of higher affinity variants of beta(2)- microglobulin J. Immunol. 1998 160 2297 2307
    • (1998) J. Immunol. , vol.160 , pp. 2297-2307
    • Shields, M.J.1    Assefi, N.2    Hodgson, W.3    Kim, E.J.4    Ribaudo, R.K.5
  • 37
    • 0026611617 scopus 로고
    • H-1-NMR assignments and secondary structure of human beta-2-microglobulin in solution
    • M. Okon P. Bray D. Vucelic H-1-NMR assignments and secondary structure of human beta-2-microglobulin in solution Biochemistry 1992 31 8906 8915
    • (1992) Biochemistry , vol.31 , pp. 8906-8915
    • Okon, M.1    Bray, P.2    Vucelic, D.3
  • 39
    • 29344458564 scopus 로고    scopus 로고
    • Simulation of pH-dependent edge strand rearrangement in human beta 2-microglobulin
    • S. Park J. G. Saven Simulation of pH-dependent edge strand rearrangement in human beta 2-microglobulin Protein Sci. 2006 15 200 207
    • (2006) Protein Sci. , vol.15 , pp. 200-207
    • Park, S.1    Saven, J.G.2
  • 40
    • 77449095000 scopus 로고    scopus 로고
    • Structure of the pre-amyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry
    • V. L. Mendoza K. Antwi M. A. Baron-Rodriguez C. Blanco R. W. Vachet Structure of the pre-amyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry Biochemistry 2010 49 1522 1532
    • (2010) Biochemistry , vol.49 , pp. 1522-1532
    • Mendoza, V.L.1    Antwi, K.2    Baron-Rodriguez, M.A.3    Blanco, C.4    Vachet, R.W.5
  • 41
    • 79961041262 scopus 로고    scopus 로고
    • Structural insights into the pre-amyloid tetramer of beta-2-microglobulin from covalent labeling and mass spectrometry
    • V. L. Mendoza M. A. Baron-Rodriguez C. Blanco R. W. Vachet Structural insights into the pre-amyloid tetramer of beta-2-microglobulin from covalent labeling and mass spectrometry Biochemistry 2011 50 6711 6722
    • (2011) Biochemistry , vol.50 , pp. 6711-6722
    • Mendoza, V.L.1    Baron-Rodriguez, M.A.2    Blanco, C.3    Vachet, R.W.4
  • 42
    • 0344875516 scopus 로고    scopus 로고
    • Amyloid fibril formation in the context of full-length protein - Effects of proline mutations on the amyloid fibril formation of beta(2)-microglobulin
    • T. Chiba Y. Hagihara T. Higurashi K. Hasegawa H. Naiki Y. Goto Amyloid fibril formation in the context of full-length protein-effects of proline mutations on the amyloid fibril formation of beta(2)-microglobulin J. Biol. Chem. 2003 278 47016 47024
    • (2003) J. Biol. Chem. , vol.278 , pp. 47016-47024
    • Chiba, T.1    Hagihara, Y.2    Higurashi, T.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 43
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modelling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modelling Biophys. J. 2000 78 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 44
    • 33750294048 scopus 로고    scopus 로고
    • Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation-mass spectrometry
    • A. M. Smith T. R. Jahn A. E. Ashcroft S. E. Radford Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation-mass spectrometry J. Mol. Biol. 2006 364 9 19
    • (2006) J. Mol. Biol. , vol.364 , pp. 9-19
    • Smith, A.M.1    Jahn, T.R.2    Ashcroft, A.E.3    Radford, S.E.4
  • 45
    • 84858446912 scopus 로고    scopus 로고
    • A recurrent D-strand association interface is observed in beta 2-microglobulin oligomers
    • M. Colombo M. de Rosa V. Bellotti S. Ricagno M. Bolognesi A recurrent D-strand association interface is observed in beta 2-microglobulin oligomers FEBS J. 2012 279 1131 1143
    • (2012) FEBS J. , vol.279 , pp. 1131-1143
    • Colombo, M.1    De Rosa, M.2    Bellotti, V.3    Ricagno, S.4    Bolognesi, M.5
  • 49
    • 84869858716 scopus 로고    scopus 로고
    • Familial Alzheimer's disease mutations differentially alter amyloid beta-protein oligomerization
    • M. M. Gessel S. Bernstein M. Kemper D. B. Teplow M. T. Bowers Familial Alzheimer's disease mutations differentially alter amyloid beta-protein oligomerization ACS Chem. Neurosci. 2012 3 909 918
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 909-918
    • Gessel, M.M.1    Bernstein, S.2    Kemper, M.3    Teplow, D.B.4    Bowers, M.T.5


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