References analysis of the Wikipedia article "Amiloide" in the Galician version

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Marina Rami´rez-Alvarado, Jane S. Merkel, and Lynne Regan (2000). "A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro". PNAS 97 (16): 8979–8984. PMID 10908649. doi:10.1073/pnas.150091797.

Kyle R.A. (2001). "Amyloidosis: a convoluted story". Brit. J. Haem. 114 (3): 529–538. PMID 11552976. doi:10.1046/j.1365-2141.2001.02999.x.

Sipe J. D., Cohen A.S. (2000). "Review: History of the Amyloid Fibril". J. Struct. Biol. 130 (2-3): 88–98. PMID 10940217. doi:10.1006/jsbi.2000.4221.

Lin CY, Gurlo T, Kayed R; et al. (2007). "Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced beta-cell apoptosis in h-IAPP transgenic mice". Diabetes 56 (5): 1324–32. PMID 17353506. doi:10.2337/db06-1579.

Nilsson MR (2004). "Techniques to study amyloid fibril formation in vitro". Methods (San Diego, Calif.) 34 (1): 151–60. PMID 15283924. doi:10.1016/j.ymeth.2004.03.012.

Fändrich M (2007). "On the structural definition of amyloid fibrils and other polypeptide aggregates". Cellular and molecular life sciences : CMLS 64 (16): 2066–78. PMID 17530168. doi:10.1007/s00018-007-7110-2.

Chiang PK, Lam MA, Luo Y (2008). "The many faces of amyloid beta in Alzheimer's disease". Current molecular medicine 8 (6): 580–4. PMID 18781964. doi:10.2174/156652408785747951. Arquivado dende o orixinal o 06 de outubro de 2011. Consultado o 22 de agosto de 2018.

Irvine GB, El-Agnaf OM, Shankar GM, Walsh DM (2008). "Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases". Molecular medicine (Cambridge, Mass.) 14 (7-8): 451–64. PMC 2274891. PMID 18368143. doi:10.2119/2007-00100.Irvine.

Ferreira ST, Vieira MN, De Felice FG (2007). "Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases". IUBMB life 59 (4-5): 332–45. PMID 17505973. doi:10.1080/15216540701283882.

Haataja L, Gurlo T, Huang CJ, Butler PC (2008). "Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis". Endocrine Reviews 29 (3): 303–16. PMC 2528855. PMID 18314421. doi:10.1210/er.2007-0037.

Höppener JW, Ahrén B, Lips CJ (2000). "Islet amyloid and type 2 diabetes mellitus". The New England Journal of Medicine 343 (6): 411–9. PMID 10933741. doi:10.1056/NEJM200008103430607.

"More than just mad cow disease", Nature Structural Biology 8, 281 (2001) doi 10.1038/86132

Truant R, Atwal RS, Desmond C, Munsie L, Tran T (2008). "Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases". The FEBS journal 275 (17): 4252–62. PMID 18637947. doi:10.1111/j.1742-4658.2008.06561.x.

Weydt P, La Spada AR (2006). "Targeting protein aggregation in neurodegeneration--lessons from polyglutamine disorders". Expert opinion on therapeutic targets 10 (4): 505–13. PMID 16848688. doi:10.1517/14728222.10.4.505.

Dotti CG, De Strooper B (2009). "Alzheimer's dementia by circulation disorders: when trees hide the forest". Nat. Cell Biol. 11 (2): 114–6. PMID 19188916. doi:10.1038/ncb0209-114.

Sipe JD, Benson MD, Buxbaum JN; et al. (2010). "Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis". Amyloid 17 (3-4): 101–104. PMID 21039326. doi:10.3109/13506129.2010.526812.

Sunde M., Serpell L. C.; et al. (1997). "Common core structure of amyloid fibrils by synchrotron X-ray diffraction". J Mol Biol 273 (3): 729–39. PMID 9356260. doi:10.1006/jmbi.1997.1348.

Rebecca, Nelson; M. Sawaya, M. Balbirnie, A. Madsen, C. Riekel, R. Grothe, and D. Eisenberg (9). "Structure of the cross-beta spine of amyloid-like fibrils". Nature 435 (7043): 773–778. PMC 1479801. PMID 15944695. doi:10.1038/nature03680.

Sawaya, Michael; Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, McFarlane HT, Madsen AØ, Riekel C, Eisenberg D. (24). "Atomic structures of amyloid cross-beta spines reveal varied steric zippers". Nature 447 (7143): 453–457. PMID 17468747. doi:10.1038/nature05695.

Gilead S, Gazit E (2004). "Inhibition of amyloid fibril formation by peptide analogues modified with alpha-aminoisobutyric acid". Angew. Chem. Int. Ed. Engl. 43 (31): 4041–4. PMID 15300690. doi:10.1002/anie.200353565.

Gazit E (2002). "A possible role for pi-stacking in the self-assembly of amyloid fibrils". FASEB J. 16 (1): 77–83. PMID 11772939. doi:10.1096/fj.01-0442hyp.

Pawar A. P., Dubay K. F.; et al. (2005). "Prediction of "Aggregation-prone" and "Aggregation-susceptible" Regions in Proteins Associated with Neurodegenerative Diseases". J Mol Biol 350 (2): 379–92. PMID 15925383. doi:10.1016/j.jmb.2005.04.016.

Demuro A, Mina E, Kayed R, Milton SC, Parker I, Glabe CG (2005). "Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers". The Journal of Biological Chemistry 280 (17): 17294–300. PMID 15722360. doi:10.1074/jbc.M500997200.>

Kadowaki H.; et al. (2005). "Amyloid beta induces neuronal cell death through ROS-mediated ASK1 activation". Cell Death Differ 12 (1): 19–24. PMID 15592360. doi:10.1038/sj.cdd.4401528.

Kochneva-Pervukhova, NV; Alexandrov, AI, Ter-Avanesyan, MD (2012). "Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast.". PLoS ONE 7 (1): e29832. PMC 3256205. PMID 22253794. doi:10.1371/journal.pone.0029832.

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ncbi.nlm.nih.gov

Kyle R.A. (2001). "Amyloidosis: a convoluted story". Brit. J. Haem. 114 (3): 529–538. PMID 11552976. doi:10.1046/j.1365-2141.2001.02999.x.

Sipe J. D., Cohen A.S. (2000). "Review: History of the Amyloid Fibril". J. Struct. Biol. 130 (2-3): 88–98. PMID 10940217. doi:10.1006/jsbi.2000.4221.

Nilsson MR (2004). "Techniques to study amyloid fibril formation in vitro". Methods (San Diego, Calif.) 34 (1): 151–60. PMID 15283924. doi:10.1016/j.ymeth.2004.03.012.

Höppener JW, Ahrén B, Lips CJ (2000). "Islet amyloid and type 2 diabetes mellitus". The New England Journal of Medicine 343 (6): 411–9. PMID 10933741. doi:10.1056/NEJM200008103430607.

Dotti CG, De Strooper B (2009). "Alzheimer's dementia by circulation disorders: when trees hide the forest". Nat. Cell Biol. 11 (2): 114–6. PMID 19188916. doi:10.1038/ncb0209-114.

Hammer ND, Wang X, McGuffie BA, Chapman MR (2008). "Amyloids: friend or foe?". Journal of Alzheimer's disease : JAD 13 (4): 407–19. PMC 2674399. PMID 18487849. Arquivado dende o orixinal o 03 de xaneiro de 2013. Consultado o 25 de decembro de 2012.

Bongiovanni, M.N.; et al. (2011). "Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading". Biomaterials 26: 6099–110.

Sunde M., Serpell L. C.; et al. (1997). "Common core structure of amyloid fibrils by synchrotron X-ray diffraction". J Mol Biol 273 (3): 729–39. PMID 9356260. doi:10.1006/jmbi.1997.1348.

Green J, Goldsbury C, Mini T, Sunderji S, Frey P, Kistler J, Cooper G, Aebi U. Full-length rat amylin forms fibrils following substitution of single residues from human amylin. J Mol Biol. 2003 Feb 28;326(4):1147-56. PMID 12589759. [1]

Morley JF, Brignull HR, Weyers JJ, Morimoto RI. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10417-22. Epub 2002 Jul 16. PMID 12122205. [2]

Ronald D. Hills, Jr. and Charles L. Brooks. Hydrophobic cooperativity as a mechanism for amyloid nucleation. J Mol Biol. 2007 May 4; 368(3): 894–901. Published online 2007 February 24. doi: 10.1016/j.jmb.2007.02.043. PMCID: PMC1997311. NIHMSID: NIHMS21930. [3]

Gazit E (2002). "A possible role for pi-stacking in the self-assembly of amyloid fibrils". FASEB J. 16 (1): 77–83. PMID 11772939. doi:10.1096/fj.01-0442hyp.

Kadowaki H.; et al. (2005). "Amyloid beta induces neuronal cell death through ROS-mediated ASK1 activation". Cell Death Differ 12 (1): 19–24. PMID 15592360. doi:10.1038/sj.cdd.4401528.

Amiloide (Galician Wikipedia)

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