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Gilead S, Gazit E (August 2004). "Inhibition of amyloid fibril formation by peptide analogues modified with α-aminoisobutyric acid". Angewandte Chemie. 43 (31): 4041–4. doi:10.1002/anie.200353565. PMID15300690.
Finder VH, Vodopivec I, Nitsch RM, Glockshuber R (February 2010). "The recombinant amyloid-β peptide Aβ1-42 aggregates faster and is more neurotoxic than synthetic Aβ-42". Journal of Molecular Biology. 396 (1): 9–18. doi:10.1016/j.jmb.2009.12.016. PMID20026079.
Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM (July 2005). "Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases". Journal of Molecular Biology. 350 (2): 379–92. doi:10.1016/j.jmb.2005.04.016. PMID15925383.
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Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, et al. (November 2000). "Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR". Biochemistry. 39 (45): 13748–59. doi:10.1021/bi0011330. PMID11076514. S2CID17232045.
Chiang PK, Lam MA, Luo Y (September 2008). "The many faces of amyloid β in Alzheimer's disease". Current Molecular Medicine. 8 (6): 580–4. doi:10.2174/156652408785747951. PMID18781964.
Weydt P, La Spada AR (August 2006). "Targeting protein aggregation in neurodegeneration--lessons from polyglutamine disorders". Expert Opinion on Therapeutic Targets. 10 (4): 505–13. doi:10.1517/14728222.10.4.505. PMID16848688. S2CID24483289.
Höppener JW, Ahrén B, Lips CJ (August 2000). "Islet amyloid and type 2 diabetes mellitus". The New England Journal of Medicine. 343 (6): 411–9. doi:10.1056/NEJM200008103430607. PMID10933741.
Serag AA, Altenbach C, Gingery M, Hubbell WL, Yeates TO (October 2002). "Arrangement of subunits and ordering of β-strands in an amyloid sheet". Nature Structural Biology. 9 (10): 734–9. doi:10.1038/nsb838. PMID12219081. S2CID23926428.
Jarrett JT, Berger EP, Lansbury PT (May 1993). "The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease". Biochemistry. 32 (18): 4693–7. doi:10.1021/bi00069a001. PMID8490014.
Gilead S, Gazit E (August 2004). "Inhibition of amyloid fibril formation by peptide analogues modified with α-aminoisobutyric acid". Angewandte Chemie. 43 (31): 4041–4. doi:10.1002/anie.200353565. PMID15300690.
Finder VH, Vodopivec I, Nitsch RM, Glockshuber R (February 2010). "The recombinant amyloid-β peptide Aβ1-42 aggregates faster and is more neurotoxic than synthetic Aβ-42". Journal of Molecular Biology. 396 (1): 9–18. doi:10.1016/j.jmb.2009.12.016. PMID20026079.
Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM (July 2005). "Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases". Journal of Molecular Biology. 350 (2): 379–92. doi:10.1016/j.jmb.2005.04.016. PMID15925383.
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Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, et al. (November 2000). "Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR". Biochemistry. 39 (45): 13748–59. doi:10.1021/bi0011330. PMID11076514. S2CID17232045.
Weydt P, La Spada AR (August 2006). "Targeting protein aggregation in neurodegeneration--lessons from polyglutamine disorders". Expert Opinion on Therapeutic Targets. 10 (4): 505–13. doi:10.1517/14728222.10.4.505. PMID16848688. S2CID24483289.
Serag AA, Altenbach C, Gingery M, Hubbell WL, Yeates TO (October 2002). "Arrangement of subunits and ordering of β-strands in an amyloid sheet". Nature Structural Biology. 9 (10): 734–9. doi:10.1038/nsb838. PMID12219081. S2CID23926428.