메뉴 건너뛰기




Volumn 586, Issue 22, 2012, Pages 3951-3955

Inhibition of amyloid fibrillation of lysozyme by phenolic compounds involves quinoprotein formation

Author keywords

Amyloid fibrillation; Benzoquinone; Catechol; Hydroquinone; Lysozyme; Phenol; Phenolic compound; Quinoprotein; Resorcinol

Indexed keywords

BENZOQUINONE; CATECHOL; HYDROQUINONE; LYSOZYME; POLYPHENOL DERIVATIVE; PROTEIN; QUINOPROTEIN; RESORCINOL; UNCLASSIFIED DRUG;

EID: 84868572235     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.09.037     Document Type: Article
Times cited : (67)

References (30)
  • 1
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • M. Stefani Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world Biochim. Biophys. Acta 1739 2004 5 25
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 3
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative disease Nat. Med. 10 2004 S10 S17
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 4
    • 0027506498 scopus 로고
    • Human lysozyme gene mutations cause hereditary systemic amyloidosis
    • M.B. Pepys, P.N. Hawkins, and D.R. Booth Human lysozyme gene mutations cause hereditary systemic amyloidosis Nature 363 1993 553 557
    • (1993) Nature , vol.363 , pp. 553-557
    • Pepys, M.B.1    Hawkins, P.N.2    Booth, D.R.3
  • 5
    • 3042673992 scopus 로고    scopus 로고
    • A highly amyloidogenic region of hen lysozyme
    • E. Frare, P.P. deLaureto, and J. Zurdo A highly amyloidogenic region of hen lysozyme J. Mol. Biol. 340 2004 1153 1165
    • (2004) J. Mol. Biol. , vol.340 , pp. 1153-1165
    • Frare, E.1    Delaureto, P.P.2    Zurdo, J.3
  • 6
    • 67649616343 scopus 로고    scopus 로고
    • Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking
    • B. Huang, J. He, and J. Ren Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking Biochemistry 48 2009 5794 5800
    • (2009) Biochemistry , vol.48 , pp. 5794-5800
    • Huang, B.1    He, J.2    Ren, J.3
  • 7
    • 33846023647 scopus 로고    scopus 로고
    • Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways
    • A.L. Gharibyan, V. Zamotin, and K. Yanamandra Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways J. Mol. Biol. 365 2007 1337 1349
    • (2007) J. Mol. Biol. , vol.365 , pp. 1337-1349
    • Gharibyan, A.L.1    Zamotin, V.2    Yanamandra, K.3
  • 8
    • 79960621436 scopus 로고    scopus 로고
    • Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein
    • M.F. Mossuto, B. Bolognesi, and B. Guixer Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein Angew. Chem.; Int. Ed. Engl. 50 2011 7048 7051
    • (2011) Angew. Chem.; Int. Ed. Engl. , vol.50 , pp. 7048-7051
    • Mossuto, M.F.1    Bolognesi, B.2    Guixer, B.3
  • 9
    • 77951912863 scopus 로고    scopus 로고
    • 42 protofibrils with morin: Mechanistic insights from molecular dynamics simulations
    • 42 protofibrils with morin: mechanistic insights from molecular dynamics simulations Biochemistry 49 2010 3935 3946
    • (2010) Biochemistry , vol.49 , pp. 3935-3946
    • Lemkul, J.A.1    Bevan, D.R.2
  • 10
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • Y. Porat, A. Abramowitz, and E. Gazit Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism Chem. Biol. Drug Des. 67 2006 27 37
    • (2006) Chem. Biol. Drug Des. , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 11
    • 79953304980 scopus 로고    scopus 로고
    • Targeting insulin amyloid assembly by small aromatic molecules: Toward rational design of aggregation inhibitors
    • M. Levy-sakin, M. Shreberk, and Y. Daniel Targeting insulin amyloid assembly by small aromatic molecules: toward rational design of aggregation inhibitors Islets 1 2009 210 215
    • (2009) Islets , vol.1 , pp. 210-215
    • Levy-Sakin, M.1    Shreberk, M.2    Daniel, Y.3
  • 12
    • 54049103538 scopus 로고    scopus 로고
    • Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS
    • H. Shoval, L. Weiner, and E. Gazit Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS Biochim. Biophys. Acta 1784 2008 1570 1577
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1570-1577
    • Shoval, H.1    Weiner, L.2    Gazit, E.3
  • 13
    • 33847025338 scopus 로고    scopus 로고
    • The anti-amyloidogenic effect is exerted against Alzheimer's β-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure
    • M. Hirohata, K. Hasegawa, and S. Tsutsumi-Yasuhara The anti-amyloidogenic effect is exerted against Alzheimer's β-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure Biochemistry 46 2007 1888 1899
    • (2007) Biochemistry , vol.46 , pp. 1888-1899
    • Hirohata, M.1    Hasegawa, K.2    Tsutsumi-Yasuhara, S.3
  • 14
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localization and implications
    • M.H. Krebs, E.C. Bromley, and A.M. Donald The binding of thioflavin-T to amyloid fibrils: localization and implications J. Struct. Biol. 149 2005 30 37
    • (2005) J. Struct. Biol. , vol.149 , pp. 30-37
    • Krebs, M.H.1    Bromley, E.C.2    Donald, A.M.3
  • 15
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
    • G. Bitan, M.D. Kirkitadze, and A. Lomakin Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways Proc. Natl. Acad. Sci. USA 100 2003 330 335
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3
  • 16
    • 33845555446 scopus 로고
    • One-electron redox potentials of phenols. Hydroxyl- and aminophenols and related compounds of biological interest
    • S. Steeken, and P. Neta One-electron redox potentials of phenols. Hydroxyl- and aminophenols and related compounds of biological interest J. Phys. Chem. 86 1982 3661 3667
    • (1982) J. Phys. Chem. , vol.86 , pp. 3661-3667
    • Steeken, S.1    Neta, P.2
  • 17
    • 79951954922 scopus 로고    scopus 로고
    • Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins
    • R. Chen, J.B. Wang, and X.Q. Zhang Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins Arch. Biochem. Biophys. 507 2011 343 349
    • (2011) Arch. Biochem. Biophys. , vol.507 , pp. 343-349
    • Chen, R.1    Wang, J.B.2    Zhang, X.Q.3
  • 18
    • 77956131582 scopus 로고    scopus 로고
    • The redox-sensing regulator YodB senses diamide and quinones via a thiol-disulfide switch in Bacillus subtilis
    • B.K. Chi, D. Albrecht, and K. Gronau The redox-sensing regulator YodB senses diamide and quinones via a thiol-disulfide switch in Bacillus subtilis Proteomics 10 2010 3155 3164
    • (2010) Proteomics , vol.10 , pp. 3155-3164
    • Chi, B.K.1    Albrecht, D.2    Gronau, K.3
  • 19
    • 50049125078 scopus 로고    scopus 로고
    • Depletion of thiol-containing proteins in response to quinones in Bacillus subtilis
    • M. Liebeke, D.C. Pöther, and N. van Duy Depletion of thiol-containing proteins in response to quinones in Bacillus subtilis Mol. Microbiol. 69 2008 1513 1529
    • (2008) Mol. Microbiol. , vol.69 , pp. 1513-1529
    • Liebeke, M.1    Pöther, D.C.2    Van Duy, N.3
  • 20
    • 0025967971 scopus 로고
    • Specific detection of quinoproteins by redox-cycling staining
    • M.A. Paz, R. Fluckiger, and A. Boak Specific detection of quinoproteins by redox-cycling staining J. Biol. Chem. 266 1991 689 692
    • (1991) J. Biol. Chem. , vol.266 , pp. 689-692
    • Paz, M.A.1    Fluckiger, R.2    Boak, A.3
  • 21
    • 33846562360 scopus 로고    scopus 로고
    • Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion
    • R. Mishra, K. Sörgjerd, and S. Nyström Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion J. Mol. Biol. 366 2007 1029 1044
    • (2007) J. Mol. Biol. , vol.366 , pp. 1029-1044
    • Mishra, R.1    Sörgjerd, K.2    Nyström, S.3
  • 22
    • 72449188669 scopus 로고    scopus 로고
    • Tea catechins induced the conversion of preformed lysozyme amyloid fibrils to amorphous aggregates
    • J. He, Y.F. Xing, and B. Huang Tea catechins induced the conversion of preformed lysozyme amyloid fibrils to amorphous aggregates J. Agric. Food Chem. 57 2009 11391 11396
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 11391-11396
    • He, J.1    Xing, Y.F.2    Huang, B.3
  • 23
    • 77349084360 scopus 로고    scopus 로고
    • Naturally occurring phytochemicals for the prevention of Alzheimer's disease
    • J. Kim, H.J. Lee, and K.W. Lee Naturally occurring phytochemicals for the prevention of Alzheimer's disease J. Neurochem. 112 2010 1415 1430
    • (2010) J. Neurochem. , vol.112 , pp. 1415-1430
    • Kim, J.1    Lee, H.J.2    Lee, K.W.3
  • 24
    • 77952346781 scopus 로고    scopus 로고
    • EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity
    • J. Bieschke, J. Russ, and R.P. Friedrich EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity Proc. Natl. Acad. Sci. USA 107 2010 7710 7715
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7710-7715
    • Bieschke, J.1    Russ, J.2    Friedrich, R.P.3
  • 25
    • 33947708348 scopus 로고    scopus 로고
    • The molecular mechanisms of the anti-amyloid effects of phenols
    • H. Shoval, D. Lichtenberg, and E. Gazit The molecular mechanisms of the anti-amyloid effects of phenols Amyloid 14 2007 73 87
    • (2007) Amyloid , vol.14 , pp. 73-87
    • Shoval, H.1    Lichtenberg, D.2    Gazit, E.3
  • 26
    • 77955550149 scopus 로고    scopus 로고
    • Comparable attenuation of Abeta(25-35)-induced neurotoxicity by quercitrin and 17beta-estradiol in cultured rat hippocampal neurons
    • S. Rattanajarasroj, and S. Unchern Comparable attenuation of Abeta(25-35)-induced neurotoxicity by quercitrin and 17beta-estradiol in cultured rat hippocampal neurons Neurochem. Res. 35 2010 1196 1205
    • (2010) Neurochem. Res. , vol.35 , pp. 1196-1205
    • Rattanajarasroj, S.1    Unchern, S.2
  • 27
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils
    • M. Zhu, S. Rajamani, and J. Kaylor The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils J. Biol. Chem. 279 2004 26846 26857
    • (2004) J. Biol. Chem. , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3
  • 28
    • 71749085436 scopus 로고    scopus 로고
    • Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity
    • N. Ferreira, I. Cardoso, and M.R. Domingues Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity FEBS Lett. 583 2009 3569 3576
    • (2009) FEBS Lett. , vol.583 , pp. 3569-3576
    • Ferreira, N.1    Cardoso, I.2    Domingues, M.R.3
  • 29
    • 44849087785 scopus 로고    scopus 로고
    • EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
    • D.E. Ehrnhoefer, J. Bieschke, and A. Boeddrich EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers Nat. Struct. Mol. Biol. 15 2008 558 566
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 558-566
    • Ehrnhoefer, D.E.1    Bieschke, J.2    Boeddrich, A.3
  • 30
    • 80051784700 scopus 로고    scopus 로고
    • EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2
    • I.R. Chandrashekaran, C.G. Adda, and C.A. MacRaild EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2 Arch. Biochem. Biophys. 513 2011 153 157
    • (2011) Arch. Biochem. Biophys. , vol.513 , pp. 153-157
    • Chandrashekaran, I.R.1    Adda, C.G.2    MacRaild, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.