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Journal Abstract Search
274 related items for PubMed ID: 20662519
1. Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies. Debelouchina GT, Platt GW, Bayro MJ, Radford SE, Griffin RG. J Am Chem Soc; 2010 Aug 04; 132(30):10414-23. PubMed ID: 20662519 [Abstract] [Full Text] [Related]
2. Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6. Su Y, Sarell CJ, Eddy MT, Debelouchina GT, Andreas LB, Pashley CL, Radford SE, Griffin RG. J Am Chem Soc; 2014 Apr 30; 136(17):6313-25. PubMed ID: 24679070 [Abstract] [Full Text] [Related]
3. Intermolecular alignment in β2-microglobulin amyloid fibrils. Debelouchina GT, Platt GW, Bayro MJ, Radford SE, Griffin RG. J Am Chem Soc; 2010 Dec 08; 132(48):17077-9. PubMed ID: 21077676 [Abstract] [Full Text] [Related]
4. Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. McParland VJ, Kad NM, Kalverda AP, Brown A, Kirwin-Jones P, Hunter MG, Sunde M, Radford SE. Biochemistry; 2000 Aug 01; 39(30):8735-46. PubMed ID: 10913285 [Abstract] [Full Text] [Related]
5. Fibrillar vs crystalline full-length beta-2-microglobulin studied by high-resolution solid-state NMR spectroscopy. Barbet-Massin E, Ricagno S, Lewandowski JR, Giorgetti S, Bellotti V, Bolognesi M, Emsley L, Pintacuda G. J Am Chem Soc; 2010 Apr 28; 132(16):5556-7. PubMed ID: 20356307 [Abstract] [Full Text] [Related]
6. Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability. Pradhan T, Annamalai K, Sarkar R, Huhn S, Hegenbart U, Schönland S, Fändrich M, Reif B. J Biol Chem; 2020 Dec 25; 295(52):18474-18484. PubMed ID: 33093170 [Abstract] [Full Text] [Related]
7. Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange. Yamaguchi K, Katou H, Hoshino M, Hasegawa K, Naiki H, Goto Y. J Mol Biol; 2004 Apr 30; 338(3):559-71. PubMed ID: 15081813 [Abstract] [Full Text] [Related]
8. Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR. Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R. Biochemistry; 2000 Nov 14; 39(45):13748-59. PubMed ID: 11076514 [Abstract] [Full Text] [Related]
11. The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Iadanza MG, Silvers R, Boardman J, Smith HI, Karamanos TK, Debelouchina GT, Su Y, Griffin RG, Ranson NA, Radford SE. Nat Commun; 2018 Oct 30; 9(1):4517. PubMed ID: 30375379 [Abstract] [Full Text] [Related]
15. Beta2-microglobulin amyloid fragment organization and morphology and its comparison to Abeta suggests that amyloid aggregation pathways are sequence specific. Zheng J, Jang H, Nussinov R. Biochemistry; 2008 Feb 26; 47(8):2497-509. PubMed ID: 18215070 [Abstract] [Full Text] [Related]
19. Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils. Giorgetti S, Raimondi S, Pagano K, Relini A, Bucciantini M, Corazza A, Fogolari F, Codutti L, Salmona M, Mangione P, Colombo L, De Luigi A, Porcari R, Gliozzi A, Stefani M, Esposito G, Bellotti V, Stoppini M. J Biol Chem; 2011 Jan 21; 286(3):2121-31. PubMed ID: 21068391 [Abstract] [Full Text] [Related]