A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis

References

• Merlini G, Bellotti V. Molecular mechanisms of Amyloidosis. N Engl J Med 2003; 349:583-596; PMID:12904524
   PubMed Web of Science ®Google Scholar
• Orwig S, Perry C, Kim L, Turnage K, Zhang R, Vollrath D, Schmidt-Krey I, Lieberman R. Amyloid fibril formation by the glaucoma-associated olfactomedin domain of myocilin. J Mol Biol 2012; 421(2-3):242-255; PMID:22197377; http://dx.doi.org/10.1016/j.jmb.2011.12.016
   PubMedGoogle Scholar
• Egorov V, Grudinina N, Lebedev D, Shaldzhyan A, Slita A, Sirotkin A, Vasin A, Shavlovsky M. Amyloidogenic peptide homologous to fragment 129–148 of human myocilin. Prion 2013; 7(3):248-252; PMID:23764838; http://dx.doi.org/10.4161/pri.24239
   PubMed Web of Science ®Google Scholar
• Chevalier C, A Al Bazzal J, Vidic V, Février C, Bourdieu E, Bouguyon R, Le Goffic J, Vautherot J, Bernard M, Moudjou S, et al. B1-F2 influenza A virus protein adopts a β-sheet conformation and forms amyloid fibers in membrane environments. J Biol Chem 2010; 285(17):13233-13243; PMID:20172856; http://dx.doi.org/10.1074/jbc.M109.067710
   PubMedGoogle Scholar
• Merlini G, Seldin D, Gertz M, Amyloidosis: pathogenesis and new therapeutic options. J Clin Oncol 2011; 29(14):1924-1933; PMID:21483018; http://dx.doi.org/10.1200/JCO.2010.32.2271
   PubMed Web of Science ®Google Scholar
• Egorov V, Solovyov K, Grudinina N, Lebedev D, Isaev-Ivanov V, Kiselev O, Shawlovsky M, Atomic force microscopy study of peptides homologous to β-domain of α-lactalbumins. Prot Pept Lett 2007; 14(5):411-414; http://dx.doi.org/10.2174/092986607780782858
   PubMed Web of Science ®Google Scholar
• Egorov V, Garmaj Y, Solovyov K, Grudinina N, Aleinikova T, Sirotkin A, Kiselev O, Shawlovsky M. Amyloidogenic peptide homologous to β-domain region of α-lactalbumin. Doklady Biochemistry Biophysics 2007; 414:152-154; PMID:17695325; http://dx.doi.org/10.1134/S1607672907030167
   PubMedGoogle Scholar
• Chipens GI, Ievina NG, Tsilinskis EE, Hidden symmetry of peptide and protein primary structures. Bioorg Khim 1992; 18(12):1445-1453; PMID:1300996
   PubMed Web of Science ®Google Scholar
• Shpakov AO. Internal symmetry of the mirror type in the primary structure of proteins: identification and the functional role. J Evol Biochem Physiol 2000; 36 (6):685- 700; http://dx.doi.org/10.1023/A:1017570620437
   Web of Science ®Google Scholar
• Sheari A, Kargar M, Katanforoush A, Arab S, Sadeghi M, Pezeshk H, Eslahchi C, Marashi SA. A tale of two symmetrical tails: structural and functional characteristics of palindromes in proteins. BMC Bioinformaticsn 2008; 9:274 ; http://dx.doi.org/10.1186/1471-2105-9-274
   PubMed Web of Science ®Google Scholar
• Sulkowski E, Aromatic palindrome motif in prion proteins, FASEB J 1992; 6(6):2363; PMID:1544547
   PubMed Web of Science ®Google Scholar
• Norstrom EM, Mastrianni JA. The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation, J Biol Chem 2005; 280(29):27236-43; PMID:15917252; http://dx.doi.org/10.1074/jbc.M413441200
   PubMed Web of Science ®Google Scholar
• Stephenson R, Clarke S, Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J Biol Chem 1989; 264(11):6164-6170; PMID:2703484
   PubMed Web of Science ®Google Scholar
• Chelius D, Rehder DS, Bondarenko PV, Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies. Anal Chem 2005; 77(18):6004-6011; PMID:16159134; http://dx.doi.org/10.1021/ac050672d
   PubMed Web of Science ®Google Scholar
• Girardet J-M, N’negue M-A, Egito AS, Campagna S, Lagrange A, Gaillard J-L. Multiple forms of equine α-lactalbumin: evidence for N-glycosylated and deamidated forms, Int Dairy J 2004; 14(3):207-217; http://dx.doi.org/10.1016/j.idairyj.2003.08.001
   Web of Science ®Google Scholar
• Selkoe D. Alzheimer disease: genes, proteins, and therapy, Physiological Rev 2001; 81(2):741-766; PMID:11274343
   PubMed Web of Science ®Google Scholar
• Solovyov K, Gasteva A, Egorov V, Aleinikova T, Sirotkin A, Shvartsman A, Shavlovsky M. Role of the C-terminal fragment of human transthyretin in abnormal fibrillogenesis. Biochemistry(Moscow) 2006; 71:672-680
   Google Scholar
• Mishra R, Sörgjerd K, Nyström S, Nordigården A, Yu Y-C, Hammarström P. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. J Mol Biol 2007; 336:1029-1044; PMID:17196616
   PubMed Web of Science ®Google Scholar
• Nguyen J, Baldwin M, Cohen F, Prusiner S, Prion protein peptides induce α-helix to β-sheet conformational transitions. Biochemistry 1995; 34(13):4186-4192; PMID:7703230; http://dx.doi.org/10.1021/bi00013a006
   PubMed Web of Science ®Google Scholar
• LeVine H, III. Thioflavin T interaction with amyloid β-sheet structures. Amyloid: Int J Exp Clin Invest 1995; 2:1-6
   Web of Science ®Google Scholar