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Volumn 328, Issue 4, 2005, Pages 1067-1072

Contribution of simple saccharides to the stabilization of amyloid structure

Author keywords

Amyloid peptide; Circular dichroism; Cosolvent; Electron microscopy; Molecular crowding; Monosaccharide; Osmolyte

Indexed keywords

AMYLOID BETA PROTEIN; FRUCTOSE; GALACTOSE; GLUCOSE; HYDROGEN; MANNOSE; SUCROSE; SUGAR;

EID: 13744262405     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.01.068     Document Type: Article
Times cited : (54)

References (24)
  • 1
    • 0030043001 scopus 로고    scopus 로고
    • Solute excluded-volume effects on the stability of globular proteins: A statistical-thermodynamic theory
    • Y. Zhou, and C.K. Hall Solute excluded-volume effects on the stability of globular proteins: A statistical-thermodynamic theory Biopolymers 38 1996 273 284
    • (1996) Biopolymers , vol.38 , pp. 273-284
    • Zhou, Y.1    Hall, C.K.2
  • 2
    • 0034039755 scopus 로고    scopus 로고
    • Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: A statistical-thermodynamic model
    • A.P. Minton Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: A statistical-thermodynamic model Biophys. J. 78 2000 101 109
    • (2000) Biophys. J. , vol.78 , pp. 101-109
    • Minton, A.P.1
  • 5
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • R.J. Ellis Macromolecular crowding: Obvious but underappreciated Trends Biochem. Sci. 26 2001 597 604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 6
    • 0032755251 scopus 로고    scopus 로고
    • Manipulation the amyloid-β aggregation pathway with chemical chaperones
    • D.-S. Yang, C.M. Yip, T.H.J. Huang, A. Charabartty, and P.E. Fraser Manipulation the amyloid-β aggregation pathway with chemical chaperones J. Biol. Chem. 274 1999 32970 32974
    • (1999) J. Biol. Chem. , vol.274 , pp. 32970-32974
    • Yang, D.-S.1    Yip, C.M.2    Huang, T.H.J.3    Charabartty, A.4    Fraser, P.E.5
  • 7
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
    • D.M. Hatters, A.P. Minton, and G.J. Howlett Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II J. Biol. Chem. 277 2002 7824 7830
    • (2002) J. Biol. Chem. , vol.277 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 9
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • M.A. Singer, and S. Lindquist Multiple effects of trehalose on protein folding in vitro and in vivo Mol. Cell 1 1998 639 648
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 10
    • 0030797432 scopus 로고    scopus 로고
    • Carbohydrate protection of enzyme structure and function against guanidinium chloride treatment depends on the nature of carbohydrate and enzyme
    • M. Sola-Penna, A. Ferreira-Pereira, A.P. Lemos, and J.R. Meyer-Fernandes Carbohydrate protection of enzyme structure and function against guanidinium chloride treatment depends on the nature of carbohydrate and enzyme Eur. J. Biochem. 248 1997 24 29
    • (1997) Eur. J. Biochem. , vol.248 , pp. 24-29
    • Sola-Penna, M.1    Ferreira-Pereira, A.2    Lemos, A.P.3    Meyer-Fernandes, J.R.4
  • 11
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • M. Arrasate, S. Mitra, E.S. Schweitzer, M.R. Segal, and S. Finkbeiner Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death Nature 431 2004 805 810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 12
    • 0034118221 scopus 로고    scopus 로고
    • Pharmacological chaperones rescue cell-surface expression and function of misfolded VA vasopressin receptor mutants
    • J.P. Morello Pharmacological chaperones rescue cell-surface expression and function of misfolded VA vasopressin receptor mutants J. Clin. Invest. 105 2000 887 895
    • (2000) J. Clin. Invest. , vol.105 , pp. 887-895
    • Morello, J.P.1
  • 13
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant α1-antitrypsin (α1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in α1-AT deficiency
    • J.A.J. Burrows, L.K. Willis, and D.H. Perlmutter Chemical chaperones mediate increased secretion of mutant α1-antitrypsin (α1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in α1-AT deficiency Proc. Natl. Acad. Sci. USA 97 2000 1796 1801
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1796-1801
    • Burrows, J.A.J.1    Willis, L.K.2    Perlmutter, D.H.3
  • 14
    • 0033755865 scopus 로고    scopus 로고
    • Effect of amino acid substitutions on Alzheimer's amyloid-β peptide-glycosaminoglycan interactions
    • J. McLaurin, and P.E. Fraser Effect of amino acid substitutions on Alzheimer's amyloid-β peptide-glycosaminoglycan interactions Eur. J. Biochem. 267 2000 6353 6361
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6353-6361
    • McLaurin, J.1    Fraser, P.E.2
  • 15
    • 0035794123 scopus 로고    scopus 로고
    • Amyloid-β interactions with chondroitin sulfate-derived monosaccharides and disaccharides. Implications for drug development
    • P.E. Fraser, A.A. Darabie, and J. McLaurin Amyloid-β interactions with chondroitin sulfate-derived monosaccharides and disaccharides. Implications for drug development J. Biol. Chem. 276 2001 6412 6419
    • (2001) J. Biol. Chem. , vol.276 , pp. 6412-6419
    • Fraser, P.E.1    Darabie, A.A.2    McLaurin, J.3
  • 17
    • 0034773940 scopus 로고    scopus 로고
    • Solvent-induced collapse of α-synuclein and acid-denatured cytochrome c
    • A.S. Morar, A. Olteanu, G.B. Young, and G.J. Pielak Solvent-induced collapse of α-synuclein and acid-denatured cytochrome c Protein Sci. 10 2001 2195 2199
    • (2001) Protein Sci. , vol.10 , pp. 2195-2199
    • Morar, A.S.1    Olteanu, A.2    Young, G.B.3    Pielak, G.J.4
  • 18
    • 0035830398 scopus 로고    scopus 로고
    • Effects of crowding by mono-, di- and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: Comparing experiment to Theory
    • A.S. Morar, X. Wang, and G.J. Pielak Effects of crowding by mono-, di- and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: Comparing experiment to Theory Biochemistry 40 2001 281 285
    • (2001) Biochemistry , vol.40 , pp. 281-285
    • Morar, A.S.1    Wang, X.2    Pielak, G.J.3
  • 19
    • 0033562141 scopus 로고    scopus 로고
    • Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding
    • S.D. Allison, B. Chang, T.W. Randolph, and J.F. Carpenter Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding Arch. Biochem. Biophys. 365 1999 289 298
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 289-298
    • Allison, S.D.1    Chang, B.2    Randolph, T.W.3    Carpenter, J.F.4
  • 20
  • 21
    • 0032566348 scopus 로고    scopus 로고
    • Sugars and polyols inhibit fibrillogenesis of type I collagen by disrupting hydrogen-bonded water bridges between helices
    • N. Kuznetsova, S.L. Chi, and S. Leikin Sugars and polyols inhibit fibrillogenesis of type I collagen by disrupting hydrogen-bonded water bridges between helices Biochemistry 37 1998 11888 11895
    • (1998) Biochemistry , vol.37 , pp. 11888-11895
    • Kuznetsova, N.1    Chi, S.L.2    Leikin, S.3
  • 22
    • 0031555940 scopus 로고    scopus 로고
    • Fibrillogenesis of Alzheimer Abeta peptides studied by fluorescence energy transfer
    • T.H. Huang, P.E. Fraser, and A. Chakrabartty Fibrillogenesis of Alzheimer Abeta peptides studied by fluorescence energy transfer J. Mol. Biol. 269 1997 214 224
    • (1997) J. Mol. Biol. , vol.269 , pp. 214-224
    • Huang, T.H.1    Fraser, P.E.2    Chakrabartty, A.3
  • 23
    • 0034610180 scopus 로고    scopus 로고
    • Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange
    • I. Kheterpal, S. Zhou, K.D. Cook, and R. Wetzel Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange Proc. Natl. Acad. Sci. USA 97 2000 13597 13601
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13597-13601
    • Kheterpal, I.1    Zhou, S.2    Cook, K.D.3    Wetzel, R.4
  • 24
    • 3242772033 scopus 로고    scopus 로고
    • The interaction of trypsin with trehalose: An investigation of protein preservation mechanisms
    • E.C. Lopez-Diex, and S. Bone The interaction of trypsin with trehalose: An investigation of protein preservation mechanisms Biochim. Biophys. Acta 1673 2004 139 148
    • (2004) Biochim. Biophys. Acta , vol.1673 , pp. 139-148
    • Lopez-Diex, E.C.1    Bone, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.