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Volumn 22, Issue 4, 2013, Pages 467-474

Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein

Author keywords

AL amyloidosis; Alzheimer's disease; Heteronuclear NMR analysis; Preferential hydration; Sugar

Indexed keywords

AMYLOID; GLUCOSE; HISTIDINE; POLYPEPTIDE; SUCROSE; TREHALOSE;

EID: 84878321355     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2228     Document Type: Article
Times cited : (39)

References (31)
  • 1
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey PH, Clark ME, Hand SC, Bowlus RD, Somero GN (1982) Living with water stress: evolution of osmolyte systems. Science 217:1214-1222. (Pubitemid 13283134)
    • (1982) Science , vol.217 , Issue.4566 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 2
    • 79952023953 scopus 로고    scopus 로고
    • Naturally occurring organic osmolytes: From cell physiology to disease prevention
    • Khan SH, Ahmad N, Ahmad F, Kumar R (2010) Naturally occurring organic osmolytes: from cell physiology to disease prevention. IUBMB Life 62:891-895.
    • (2010) IUBMB Life , vol.62 , pp. 891-895
    • Khan, S.H.1    Ahmad, N.2    Ahmad, F.3    Kumar, R.4
  • 3
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • DOI 10.1016/S0014-5793(04)00326-6, PII S0014579304003266
    • Arora A, Ha C, Park CB (2004) Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett 564:121-125. (Pubitemid 38490710)
    • (2004) FEBS Letters , vol.564 , Issue.1-2 , pp. 121-125
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 4
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42
    • DOI 10.1016/j.nbd.2005.02.003, PII S0969996105000628
    • Liu R, Barkhordarian H, Emadi S, Park CB Sierks MR (2005) Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42. Neurobiol Dis 20:74-81. (Pubitemid 41219204)
    • (2005) Neurobiology of Disease , vol.20 , Issue.1 , pp. 74-81
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Chan, B.P.4    Sierks, M.R.5
  • 7
    • 70349272854 scopus 로고    scopus 로고
    • Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomerinduced membrane permeability
    • Qi W, Zhang A, Good TA, Fernandez EJ (2009) Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomerinduced membrane permeability. Biochemistry 48: 8908-8919.
    • (2009) Biochemistry , vol.48 , pp. 8908-8919
    • Qi, W.1    Zhang, A.2    Good, T.A.3    Fernandez, E.J.4
  • 8
    • 57049105810 scopus 로고    scopus 로고
    • Structural thermodynamics of protein preferential solvation: Osmolyte solvation of proteins, aminoacids, and peptides
    • Auton M, Bolen DW, Rosgen J (2008) Structural thermodynamics of protein preferential solvation: osmolyte solvation of proteins, aminoacids, and peptides. Proteins 73:802-813.
    • (2008) Proteins , vol.73 , pp. 802-813
    • Auton, M.1    Bolen, D.W.2    Rosgen, J.3
  • 9
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee JC, Timasheff SN (1981) The stabilization of proteins by sucrose. J Biol Chem 256:7193-7201.
    • (1981) J Biol Chem , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 10
    • 0036152775 scopus 로고    scopus 로고
    • Effect of osmolytes as folding aids on creatine kinase refolding pathway
    • Ou WB, Park YD, Zhou HM (2002) Effect of osmolytes as folding aids on creatine kinase refolding pathway. Int J Biochem Cell Biol 34:136-147.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 136-147
    • Ou, W.B.1    Park, Y.D.2    Zhou, H.M.3
  • 11
    • 0034764550 scopus 로고    scopus 로고
    • Aggregation and chemical reaction in hen lysozyme caused by heating at pH 6 are depressed by osmolytes, sucrose and trehalose
    • Ueda T, Nagata M, Imoto T (2001) Aggregation and chemical reaction in hen lysozyme caused by heating at pH 6 are depressed by osmolytes, sucrose and trehalose. J Biochem 130:491-496. (Pubitemid 33021592)
    • (2001) Journal of Biochemistry , vol.130 , Issue.4 , pp. 491-496
    • Ueda, T.1    Nagata, M.2    Imoto, T.3
  • 12
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T, Timasheff SN (1982) Stabilization of protein structure by sugars. Biochemistry 21:6536-6544.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 13
    • 34250822854 scopus 로고    scopus 로고
    • Hydration state change of proteins upon unfolding in sugar solutions
    • DOI 10.1016/j.bbapap.2007.05.008, PII S1570963907001161
    • Miyawaki O (2007) Hydration state change of proteins upon unfolding in sugar solutions. Biochim Biophys Acta 1774:928-935. (Pubitemid 46977844)
    • (2007) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1774 , Issue.7 , pp. 928-935
    • Miyawaki, O.1
  • 15
    • 0033855656 scopus 로고    scopus 로고
    • Review: Immunoglobulin light chain amyloidosis-The archetype of structural and pathogenic variability
    • Bellotti V, Mangione P, Merlini G (2000) Review: immunoglobulin light chain amyloidosis-the archetype of structural and pathogenic variability. J Struct Biol 130: 280-289.
    • (2000) J Struct Biol , vol.130 , pp. 280-289
    • Bellotti, V.1    Mangione, P.2    Merlini, G.3
  • 16
    • 0026771089 scopus 로고
    • Amyloidosis
    • Sipe JD (1992) Amyloidosis. Annu Rev Biochem 61: 947-975.
    • (1992) Annu Rev Biochem , vol.61 , pp. 947-975
    • Sipe, J.D.1
  • 17
    • 69749122031 scopus 로고    scopus 로고
    • Residual structures in the acid-unfolded states of Vlambda6 proteins affect amyloid fibrillation
    • Mishima T, Ohkuri T, Monji A, Kanemaru T, Abe Y, Ueda T (2009) Residual structures in the acid-unfolded states of Vlambda6 proteins affect amyloid fibrillation. J Mol Biol 392:1033-1043.
    • (2009) J Mol Biol , vol.392 , pp. 1033-1043
    • Mishima, T.1    Ohkuri, T.2    Monji, A.3    Kanemaru, T.4    Abe, Y.5    Ueda, T.6
  • 18
    • 72949084168 scopus 로고    scopus 로고
    • Effects of His mutations on the fibrillation of amyloidogenic Vlambda6 protein Wil under acidic and physiological conditions
    • Mishima T, Ohkuri T, Monji A, Kanemaru T, Abe Y, Ueda T (2010) Effects of His mutations on the fibrillation of amyloidogenic Vlambda6 protein Wil under acidic and physiological conditions. Biochem Biophys Res Commun 391:615-620.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 615-620
    • Mishima, T.1    Ohkuri, T.2    Monji, A.3    Kanemaru, T.4    Abe, Y.5    Ueda, T.6
  • 19
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
    • DOI 10.1016/0003-2697(89)90046-8
    • Naiki H, Higuchi K, Hosokawa M, Takeda T (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 177:244-249. (Pubitemid 19088253)
    • (1989) Analytical Biochemistry , vol.177 , Issue.2 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 20
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • Dobson CM (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24:329-332. (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 21
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • DOI 10.1016/S0959-440X(98)80016-X
    • Kelly JW (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 8:101-106. (Pubitemid 28107921)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.1 , pp. 101-106
    • Kelly, J.W.1
  • 22
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • DOI 10.1016/j.bbapap.2003.12.008, PII S1570963904000020
    • Uversky VN, Fink AL (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698:131-153. (Pubitemid 38591469)
    • (2004) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1698 , Issue.2 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 24
    • 0030040794 scopus 로고    scopus 로고
    • On the role of surface tension in the stabilization of globular proteins
    • Lin TY, Timasheff SN (1996) On the role of surface tension in the stabilization of globular proteins. Protein Sci 5:372-381. (Pubitemid 26054294)
    • (1996) Protein Science , vol.5 , Issue.2 , pp. 372-381
    • Lin, T.-Y.1    Timasheff, S.N.2
  • 25
    • 0030759665 scopus 로고    scopus 로고
    • Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
    • DOI 10.1021/bi970049q
    • Schwalbe H, Fiebig KM, Buck M, Jones JA, Grimshaw SB, Spencer A, Glaser SJ, Smith LJ, Dobson CM (1997) Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. Biochemistry 36:8977-8991. (Pubitemid 27342545)
    • (1997) Biochemistry , vol.36 , Issue.29 , pp. 8977-8991
    • Schwalbe, H.1    Fiebig, K.M.2    Buck, M.3    Jones, J.A.4    Grimshaw, S.B.5    Spencer, A.6    Glaser, S.J.7    Smith, L.J.8    Dobson, C.M.9
  • 26
    • 0035215289 scopus 로고    scopus 로고
    • Amide proton temperature coefficients as hydrogen bond indicators in proteins
    • DOI 10.1023/A:1012911329730
    • Cierpicki T, Otlewski J (2001) Amide proton temperature coefficients as hydrogen bond indicators in proteins. J Biomol NMR 21:249-261. (Pubitemid 33133425)
    • (2001) Journal of Biomolecular NMR , vol.21 , Issue.3 , pp. 249-261
    • Cierpicki, T.1    Otlewski, J.2
  • 28
    • 33749321215 scopus 로고    scopus 로고
    • Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated
    • DOI 10.1110/ps.062258206
    • Mishima T, Ohkuri T, Monji A, Imoto T, Ueda T (2006) Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated. Protein Sci 15:2448-2452. (Pubitemid 44496399)
    • (2006) Protein Science , vol.15 , Issue.10 , pp. 2448-2452
    • Mishima, T.1    Ohkuri, T.2    Monji, A.3    Imoto, T.4    Ueda, T.5
  • 29
    • 33947658419 scopus 로고    scopus 로고
    • A particular hydrophobic cluster in the residual structure of reduced lysozyme drastically affects the amyloid fibrils formation
    • DOI 10.1016/j.bbrc.2007.03.043, PII S0006291X07005219
    • Mishima T, Ohkuri T, Monji A, Imoto T, Ueda T (2007) A particular hydrophobic cluster in the residual structure of reduced lysozyme drastically affects the amyloid fibrils formation. Biochem Biophys Res Commun 356: 769-772. (Pubitemid 46499032)
    • (2007) Biochemical and Biophysical Research Communications , vol.356 , Issue.3 , pp. 769-772
    • Mishima, T.1    Ohkuri, T.2    Monji, A.3    Imoto, T.4    Ueda, T.5
  • 30
    • 14144254725 scopus 로고    scopus 로고
    • Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form
    • DOI 10.1016/j.jmb.2005.01.022
    • Ohkuri T, Shioi S, Imoto T, Ueda T (2005) Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form. J Mol Biol 347:159- 168. (Pubitemid 40283636)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.1 , pp. 159-168
    • Ohkuri, T.1    Shioi, S.2    Imoto, T.3    Ueda, T.4


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