[1]. E. Agorogiannis, G. Agorogiannis, A. Papadimitriou, G. Hadjigeorgiou, Protein misfolding in neurodegenerative diseases. Neuropathol. Appl. Neurobiol., 30(2004), 215-224.
[2]. H. Aiking, Future protein supply. Trends Food Sci. Technol., 22(2011), 112-120.
[3]. S. Amin, G. V. Barnett, J. A. Pathak, C. J. Roberts, P. S. Sarangapani, Protein aggregation, particle formation, characterization & rheology. Curr. Opin. Colloid Interface Sci., 19(2014), 438-449.
[4]. V. L. Anderson, T. F. Ramlall, C. C. Rospigliosi, W. W. Webb, D. Eliezer, Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation. Proc. Natl. Acad. Sci., 107(2010), 18850-18855.
[5]. T. Arakawa, S. N. Timasheff, Preferential interactions of proteins with salts in concentrated solutions. Biochemistry, 21(1982), 6545-6552.
[6]. D. Baker, A surprising simplicity to protein folding. Nature, 405(2000), 39-42.
[7]. J. M. Barral, S. A. Broadley, G. Schaffar, F. U. Hartl, Roles of molecular chaperones in protein misfolding diseases. Paper presented at the Seminars in cell & developmental biology, (2004).
[8]. S. Benjwal, S. Verma, K. H. Röhm, O. Gursky, Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci., 15(2006), 635-639.
[9]. A. Berrill, J. Biddlecombe, D. Bracewell, Product quality during manufacture and supply. Peptide and Protein Delivery, (2011), 313-339: Elsevier.
[10]. C. W. Bertoncini, Y.-S. Jung, C. O. Fernandez, W. Hoyer, C. Griesinger, T. M. Jovin, M. Zweckstetter, Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein. Proc. Natl. Acad. Sci., 102(2005), 1430-1435.
[11]. R. W. Carrell, B. Gooptu, Conformational changes and disease—serpins, prions and Alzheimer's. Curr. Opin. Struct. Biol., 8(1998), 799-809.
[12]. R. W. Carrell, D. A. Lomas, Conformational disease. The Lancet, 350(1997), 134-138.
[13]. R. Carrotta, R. Bauer, R. Waninge, C. Rischel, Conformational characterization of oligomeric intermediates and aggregates in β‐lactoglobulin heat aggregation. Protein Sci., 10(2001), 1312-1318.
[14]. F. Chiti, C. M. Dobson, Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem., 75(2006), 333-366.
[15]. D. Constatinescu, C. Herrmann, H. Weingärtner, Patterns of protein unfolding and protein aggregation in ionic liquids. Phys. Chem. Chem. Phys., 12(2010), 1756-1763.
[16]. K. A. Conway, J. D. Harper, P. T. Lansbury, Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry, 39(2000), 2552-2563.
[17]. A. D’Souza, J. D. Theis, J. A. Vrana, A. Dogan, Pharmaceutical amyloidosis associated with subcutaneous insulin and enfuvirtide administration. Amyloid, 21(2014), 71-75.
[18]. R. J. Ellis, A. P. Minton, Protein aggregation in crowded environments. Biol. Chem., 387(2006), 485-497.
[19]. A. Es-haghi, A. Ebrahim-Habibi, M. Sabbaghian, M. Nemat-Gorgani, Amyloid-like aggregates formation by bovine apo-carbonic anhydrase in various alcohols: A comparative study. Int. J. Biol. Macromol., 92(2016), 573-580.
[20]. P. Fan, C. Bracken, J. Baum, Structural characterization of monellin in the alcohol-denatured state by NMR: Evidence for. beta.-sheet to. alpha.-helix conversion. Biochemistry, 32(1993), 1573-1582.
[21]. M. Fändrich, Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity. J. Mol. Biol., 421(2012), 427-440.
[22]. F. Ferrone, [17] Analysis of protein aggregation kinetics. Methods Enzymol., 309(1999), 256-274: Elsevier.
[23]. A. L. Fink, Protein aggregation: folding aggregates, inclusion bodies and amyloid. Folding Des., 3(1998), 9-23.
[24]. A. L. Fink, Chaperone-mediated protein folding. Physiol. Rev., 79(1999), 425-449.
[25]. G. Forloni, N. Angeretti, R. Chiesa, E. Monzani, M. Salmona, O. Bugiani, F. Tagliavini, Neurotoxicity of a prion protein fragment. Nature, 362(1993), 543-546.
[26]. G. Ganguly, S. Chakrabarti, U. Chatterjee, L. Saso, Proteinopathy, oxidative stress and mitochondrial dysfunction: cross talk in Alzheimer’s disease and Parkinson’s disease. Drug Des., Dev. Ther., 11(2017), 797.
[27]. D. J. Gelb, E. Oliver, S. Gilman, Diagnostic criteria for Parkinson disease. Arch Neurol., 56(1999), 33-39.
[28]. S. A. Ghadami, R. Khodarahmi, S. Ghobadi, M. Ghasemi, S. Pirmoradi, Amyloid fibril formation by native and modified bovine β-lactoglobulins proceeds through unfolded form of proteins: A comparative study. Biophys. Chem., 159(2011), 311-320.
[29]. H. Gliguem, I. Birlouez-Aragon, Effects of sterilization, packaging, and storage on vitamin C degradation, protein denaturation, and glycation in fortified milks. J. Dairy Sci., 88(2005), 891-899.
[30]. A. L. Goldberg, Protein degradation and protection against misfolded or damaged proteins. Nature, 426(2003), 895-899.
[31]. J. Gsponer, M. Vendruscolo, Theoretical approaches to protein aggregation. Protein Pept. Lett., 13(2006), 287-293.
[32]. S. J. Hamodrakas, Protein aggregation and amyloid fibril formation prediction software from primary sequence: towards controlling the formation of bacterial inclusion bodies. FEBS J., 278(2011), 2428-2435.
[33]. D. Harris, P. Peters, A. Taraboulos, V. Lingappa, S. DeArmond, S. Prusiner, Prion Biology and Diseases. Cold Spring Harbor Laboratory Cold Spring Harbor, (2004).
[34]. F. U. Hartl, Molecular chaperones in cellular protein folding. Nature, 381(1996), 571-580.
[35]. R. D. Hills Jr, C. L. Brooks III, Hydrophobic cooperativity as a mechanism for amyloid nucleation. J. Mol. Biol., 368(2007), 894-901.
[36]. J. Hofrichter, M. Krohn, T. Schumacher, C. Lange, B. Feistel, B. Walbroel, J. Pahnke, Reduced Alzheimer's disease pathology by St. John's Wort treatment is independent of hyperforin and facilitated by ABCC1 and microglia activation in mice. Curr. Alzheimer Res., 10(2013), 1057-1069.
[37]. E. T. Jaikaran, A. Clark, Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochim. Biophys. Acta Mol. Basis Dis., 1537(2001), 179-203.
[38]. K. A. Jellinger, Multiple system atrophy: an oligodendroglioneural synucleinopathy. J. Alzheimer's Dis., 62(2018), 1141-1179.
[39]. K. A. Josephs, J. L. Holton, M. N. Rossor, H. Braendgaard, T. Ozawa, N. C. Fox, P. Rosa, Neurofilament inclusion body disease: a new proteinopathy? Brain, 126(2003), 2291-2303.
[40]. M. Jucker, Y. Christen, Proteopathic Seeds and Neurodegenerative Diseases, (2013): Springer.
[41]. M. Kastelic, Y. V. Kalyuzhnyi, B. Hribar-Lee, K. A. Dill, V. Vlachy, Protein aggregation in salt solutions. Proc. Natl. Acad. Sci., 112(2015), 6766-6770.
[42]. M. S. Khan, S. Tabrez, S. A. Bhat, N. Rabbani, A. M. Al‐Senaidy, B. Bano, Effect of trifluoroethanol on α‐crystallin: folding, aggregation, amyloid, and cytotoxicity analysis. J. Mol. Recognit., 29(2016), 33-40.
[43]. R. Khurana, V. N. Uversky, L. Nielsen, A. L. Fink, Is Congo red an amyloid-specific dye? J. Biol. Chem., 276(2001), 22715-22721.
[44]. M. C. Kiernan, S. Vucic, B. C. Cheah, M. R. Turner, A. Eisen, O. Hardiman, M. C. Zoing, Amyotrophic lateral sclerosis. The Lancet, 377(2011), 942-955.
[45]. D. Kishore, S. Kundu, A. M. Kayastha, Thermal, chemical and pH induced denaturation of a multimeric β-galactosidase reveals multiple unfolding pathways. PloS one, 7(2012), e50380.
[46]. V. Kumar, N. Dixit, L. L. Zhou, W. Fraunhofer, Impact of short range hydrophobic interactions and long range electrostatic forces on the aggregation kinetics of a monoclonal antibody and a dual-variable domain immunoglobulin at low and high concentrations. Int. J. Pharm., 421(2011), 82-93.
[47]. F. M. LaFerla, K. N. Green, S. Oddo, (2007). Intracellular amyloid-β in Alzheimer's disease. Nat. Rev. Neurosci., 8(2007), 499-509.
[48]. M. Lanthier, R. Behrman, C. Nardinelli, Economic issues with follow-on protein products. Nat. Rev. Drug Discovery, 7(2008), 733-737.
[49]. P. Leandro, C. M. Gomes, Protein misfolding in conformational disorders: rescue of folding defects and chemical chaperoning. Mini Rev. Med. Chem., 8(2008), 901-911.
[50]. R. Li, Z. Wu, Y. Wangb, L. Ding, Y. Wang, Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin. Biotechnol. Rep., 9(2016), 46-52.
[51]. S. A. Lipton, Z. Gu, T. Nakamura, Inflammatory mediators leading to protein misfolding and uncompetitive/fast off‐rate drug therapy for neurodegenerative disorders. Int. Rev. Neurobiol., 82(2007), 1-27.
[52]. A. Lorenzo, M. Yuan, Z. Zhang, P. A. Paganetti, C. Sturchler-Pierrat, M. Staufenbiel, B. A. Yankner, Amyloid β interacts with the amyloid precursor protein: a potential toxic mechanism in Alzheimer's disease. Nat. Neurosci., 3(2000), 460-464.
[53]. C. Madhavaiah, S. Verma, Self-aggregation of reverse bis peptide conjugate derived from the unstructured region of the prion protein. Chem. Commun., (2004), 638-639.
[54]. G. I. Makhatadze, V. V. Loladze, D. N. Ermolenko, X. Chen, S. T. Thomas, Contribution of surface salt bridges to protein stability: guidelines for protein engineering. J. Mol. Biol., 327(2003), 1135-1148.
[55]. E. Masliah, E. Rockenstein, I. Veinbergs, Y. Sagara, M. Mallory, M. Hashimoto, L. Mucke, β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proc. Natl. Acad. Sci., 98(2001), 12245-12250.
[56]. L. Mazzei, N. G. Docherty, W. Manucha, Mediators and mechanisms of heat shock protein 70 based cytoprotection in obstructive nephropathy. Cell Stress Chaperones, 20(2015), 893-906.
[57]. D. McGowan, W. van Roon-Mom, H. Holloway, G. Bates, L. Mangiarini, G. Cooper, R. Snell, Amyloid-like inclusions in Huntington’s disease. J. Neurosci., 100(2000), 677-680.
[58]. G. C. Melkani, A. S. Trujillo, R. Ramos, R. Bodmer, S. I. Bernstein, K. Ocorr, Huntington's disease induced cardiac amyloidosis is reversed by modulating protein folding and oxidative stress pathways in the Drosophila heart. PLoS Genet, 9(2013), e1004024.
[59]. L. A. Munishkina, E. M. Cooper, V. N. Uversky, A. L. Fink, The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit., 17(2004), 456-464.
[60]. H. Naiki, F. Gejyo, [20] Kinetic analysis of amyloid fibril formation. Methods Enzymol., 309(1999), 305-318.
[61]. C. Onwulata, S. Isobe, P. Tomasula, P. Cooke, Properties of whey protein isolates extruded under acidic and alkaline conditions. J. Dairy Sci., 89(2006), 71-81.
[62]. D. Papy-Garcia, M. Christophe, H. Minh Bao, S. Fernando, S. Ludmilla, S. Diaz Julia Elisa, R.-V. Rita, Glycosaminoglycans, protein aggregation and neurodegeneration. Curr. Protein Pept. Sci., 12(2011), 258-268.
[63]. D. L. Parton, J. W. Klingelhoefer, M. S. Sansom, Aggregation of model membrane proteins, modulated by hydrophobic mismatch, membrane curvature, and protein class. Biophys. J., 101(2011), 691-699.
[64]. T. J. Peters, All about albumin: biochemistry, genetics, and medical applications, (1995): Elsevier.
[65]. J. S. Philo, T. Arakawa, Mechanisms of protein aggregation. Curr. Pharm. Biotechnol., 10(2009), 348-351.
[66]. M. Pievani, N. Filippini, M. P. Van Den Heuvel, S. F. Cappa, G. B. Frisoni, Brain connectivity in neurodegenerative diseases—from phenotype to proteinopathy. Nat. Rev. Neurol., 10(2014), 620.
[67]. R. N. Rambaran, L. C. Serpell, Amyloid fibrils: abnormal protein assembly. Prion, 2(2008), 112-117.
[68]. T. W. Randolph, M. Seefeldt, J. F. Carpenter, High hydrostatic pressure as a tool to study protein aggregation and amyloidosis. Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol., 1595(2002), 224-234.
[69]. L. Redecke, M. von Bergen, J. Clos, P. V. Konarev, D. I. Svergun, U. E. Fittschen, E. Mandelkow, Structural characterization of β-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro. J. Struct. Biol., 157(2007), 308-320.
[70]. C. Reitz, C. Brayne, R. Mayeux, Epidemiology of Alzheimer disease. Nat. Rev. Neurol., 7(2011), 137-152.
[71]. N. Rezaei-Ghaleh, A. Ebrahim-Habibi, A. A. Moosavi-Movahedi, M. Nemat-Gorgani, Effect of polyamines on the structure, thermal stability and 2, 2, 2-trifluoroethanol-induced aggregation of α-chymotrypsin. Int. J. Biol. Macromol., 41(2007), 597-604.
[72]. C. J. Roberts, Protein aggregation and its impact on product quality. Curr. Opin. Biotechnol., 30(2014), 211-217.
[73]. M. Rosa, C. J. Roberts, M. A. Rodrigues, Connecting high-temperature and low-temperature protein stability and aggregation. PloS one, 12(2017), e0176748.
[74]. C. A. Ross, M. A. Poirier, Protein aggregation and neurodegenerative disease. Nat. Med., 10(2004), 10-17.
[75]. E. Sahin, A. O. Grillo, M. D. Perkins, C. J. Roberts, Comparative effects of pH and ionic strength on protein–protein interactions, unfolding, and aggregation for IgG1 antibodies. J. Pharm. Sci., 99(2010), 4830-4848.
[76]. J. Santos, V. Iglesias, J. Santos-Suárez, M. Mangiagalli, S. Brocca, I. Pallarès, S. Ventura, PH-dependent aggregation in intrinsically disordered proteins is determined by charge and lipophilicity. Cells, 9(2020), 145.
[77]. C. Scheckel, A. Aguzzi, Prions, prionoids and protein misfolding disorders. Nat. Rev. Genet., 19(2018), 405-418.
[78]. L. C. Serpell, Alzheimer’s amyloid fibrils: structure and assembly. Biochim. Biophys. Acta Mol. Basis Dis., 1502(2000), 16-30.
[79]. B. A. Shirley, Protein stability and folding: Theory and practice, 21(1995): Springer.
[80]. S. M. Singh, J. Cabello‐Villegas, R. L. Hutchings, K. M. Mallela, Role of partial protein unfolding in alcohol‐induced protein aggregation. Proteins: Struct., Funct., Bioinf., 78(2010), 2625-2637.
[81]. J. D. Sipe, M. D. Benson, J. N. Buxbaum, S.-i. Ikeda, G. Merlini, M. J. Saraiva, P. Westermark, Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines. Amyloid, 23(2016), 209-213.
[82]. J. D. Sipe, A. S. Cohen, History of the amyloid fibril. J. Struct. Biol., 130(2000), 88-98.
[83]. M. Stefani, C. M. Dobson, Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med., 81(2003), 678-699.
[84]. P. Strop, S. L. Mayo, Contribution of surface salt bridges to protein stability. Biochemistry, 39(2000), 1251-1255.
[85]. R. E. Tanzi, L. Bertram, Twenty years of the Alzheimer’s disease amyloid hypothesis: a genetic perspective. Cell, 120(2005), 545-555.
[86]. A. Tolkach, U. Kulozik, Reaction kinetic pathway of reversible and irreversible thermal denaturation of beta-lactoglobulin. Le Lait, 87(2007), 301-315.
[87]. J. Turk, Rudolf Virchow--father of cellular pathology. J. R. Soc. Med., 86(1993), 688.
[88]. V. N. Uversky, Mysterious oligomerization of the amyloidogenic proteins. FEBS J., 277(2010), 2940-2953.
[89]. R. Veerhuis, R. Boshuizen, A. Familian, Amyloid associated proteins in Alzheimer's and prion disease. Curr. Drug Targets. CNS Neurol. Disord., 4(2005), 235-248.
[90]. B. A. Vernaglia, J. Huang, E. D. Clark, Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme. Biomacromolecules, 5(2004), 1362-1370.
[91]. L. C. Walker, C. C. Ibegbu, C. W. Todd, H. L. Robinson, M. Jucker, H. LeVine III, S. Gandy, Emerging prospects for the disease-modifying treatment of Alzheimer's disease. Biochem. Pharmacol., 69(2005), 1001-1008.
[92]. L. C. Walker, H. LeVine 3rd, Proteopathy: the next therapeutic frontier? Curr. Opin. Invest. Drugs, 3(2002), 782.
[93]. L. C. Walker, H. LeVine III, M. P. Mattson, M. Jucker, Inducible proteopathies. Trends Neurosci., 29(2006), 438-443.
[94]. G. Walsh, Biopharmaceutical benchmarks 2010. Nat. Biotechnol., 28(2010), 917-924.