[1] ALVIN S D,ZOU W Q.Prions:Beyond a single protein[J].Clinical Microbiology Reviews,2016,29(3):633-658. [2] CASTLE A R,GILLA C.Physiological functions of the cellular prion protein[J].Frontiers in Molecular Biosciences,2017,4:19. [3] PEPYS M B,HAWKINS P N,BOOTH D R,et al.Human lysozyme gene mutations cause hereditary systemic amyloidosis[J].Nature,1993,362(6420):553-557. [4] BOOTH D R,SUNDE M,BELLOTTI V,et al.Instability,unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis[J].Nature,1997,385(6619):787-793. [5] NASR S H,DASARI S,MILLS J R,et al.Hereditary lysozyme amyloidosis variant p.Leu102Ser associates with unique phenotype[J].Journal of the American Society of Nephrology,2017,28(2):431-438. [6] COBB N J,APETRI A C,SUREWIEZW K.Prion protein amyloid formation under native-like conditions involves refolding of the C-terminal alpha-helical domain[J].Journal of Biological Chistry,2008,283(50):34704-34711. [7] WANG L Q,ZHAO K,YUAN H Y,et al.Cryo-EM structure of an amyloid fibril formed by full-length human prion protein[J].Nature Structural & Molecular Biology,2020,27(6):598-602. [8] FELICE D G,VIERIAM N,MEIRELLESM N,et al.Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure[J].FASEB Journal,2004,18(10):1099-1101. [9] MARINO L,PAUWELS K,CASASNOVAS R,et al.Ortho-methylated 3-hydroxypyridines hinder hen egg-white lysozyme fibrillogenesis[J].Scientific Reports,2015,5:12052. [10] FENG S,SONG X H,ZENG C M.Inhibition of amyloid fibrillation of lysozyme by phenolic compounds involves quinoprotein formation[J].FEBS Letters,2012,586(22):3951-3955. [11] KREBS M R,WILKINS D K,CHUNG E W,et al.Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain[J].Journal of Molecular Biology,2000,300(3):541-549. [12] SWAMINATHAN R,RAVI V K,KUMAR S,et al.Lysozyme:A model protein for amyloid research[J].Advances in Protein Chemistry and Structural Biology,2011,84:63-111. [13] MAHDAVIMEHR M,MERATAN A A,GHOBEH M,et al.Inhibition of HEWL fibril formation by taxifolin:Mechanism of action[J].PLoS One,2017,12(11):e0187841. [14] MICSONAI A,WIEN F,KERNYA L,et al.Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy[J].Proceedings of the National Academy of Sciences of the United States of America,2015,112(24):E3095-E3103. [15] SNEIDERIS T,DARGUZIS D,BOTYRIUTE A,et al.pH-driven polymorphism of insulin amyloid-like fibrils[J].PLoS One,2015,10(8):e0136602. [16] JAYAMANI J,SHANMUGAM G.Gallic acid,one of the components in many plant tissues,is a potential inhibitor for insulin amyloid fibril formation[J].European Journal of Medicinal Chemistry,2014,85:352-358. [17] VISHWANATH S,NALLA L P,NEETU S,et al.Wild-type hen egg white lysozyme aggregation in vitro can form self-seeding amyloid conformational variants[J].Biophysical Chemistry,2016,219:28-37. [18] RAJARAMAN K,SUSAN L L.Structural insights into a yeast prion illuminate nucleation and strain diversity[J].Nature,2005,435:765-772. [19] LU X L,ZENG J,GAO Y,et al.The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions:A replica exchange molecular dynamics study[J].Journal of Molecular Modeling,2013,19(11):4897-4908. [20] LIMA A N,OLIVEIRA R J,BRAZ A S K,et al.Effects of pH and aggregation in the human prion conversion into scrapie form:A study using molecular dynamics with excited normal modes[J].European Biophysics Journal,2018,47(5):583-590. [21] GU W,WANG T T,ZHU J,et al.Molecular dynamics simulation of the unfolding of the human prion protein domain under low pH and high temperature conditions[J].Biophysical Chemistry,2003,104(1):79-94. |