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- BRENNER S., HORNE R. W. A negative staining method for high resolution electron microscopy of viruses. Biochim Biophys Acta. 1959 Jul;34:103–110. doi: 10.1016/0006-3002(59)90237-9. [DOI] [PubMed] [Google Scholar]
- Benditt E. P., Eriksen N. Amyloid. 3. A protein related to the subunit structure of human amyloid fibrils. Proc Natl Acad Sci U S A. 1966 Feb;55(2):308–316. doi: 10.1073/pnas.55.2.308. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bladen H. A., Nylen M. U., Glenner G. G. The ultrastructure of human amyloid as revealed by the negative staining technique. J Ultrastruct Res. 1966 Mar;14(5):449–459. doi: 10.1016/s0022-5320(66)80075-8. [DOI] [PubMed] [Google Scholar]
- COHEN A. S., CALKINS E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature. 1959 Apr 25;183(4669):1202–1203. doi: 10.1038/1831202a0. [DOI] [PubMed] [Google Scholar]
- COHEN A. S., CALKINS E. THE ISOLATION OF AMYLOID FIBRILS AND A STUDY OF THE EFFECT OF COLLAGENASE AND HYALURONIDASE. J Cell Biol. 1964 Jun;21:481–486. doi: 10.1083/jcb.21.3.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cathcart E. S., Wollheim F. A., Cohen A. S. Plasma protein constituents of amyloid fibrils. J Immunol. 1967 Aug;99(2):376–385. [PubMed] [Google Scholar]
- Filshie B. K., Fraser R. D., Macrae T. P., Rogers G. E. Appendix-X-ray-diffraction and electron-microscope observations on soluble derivatives of feather keratin. Biochem J. 1964 Jul;92(1):18.2–1819. doi: 10.1042/bj0920018. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GILLESPIE J. M., LENNOX F. G. Preparation of an electrophoretically homogenous keratin derivative from wool. Biochim Biophys Acta. 1953 Nov;12(3):481–482. doi: 10.1016/0006-3002(53)90169-3. [DOI] [PubMed] [Google Scholar]
- GROSS J. Influence of time on the reversible association between large molecules: the collagen system. Nature. 1958 Feb 22;181(4608):556–556. doi: 10.1038/181556a0. [DOI] [PubMed] [Google Scholar]
- Glenner G. G., Bladen H. A. Purification and reconstitution of the periodic fibril and unit structure of human amyloid. Science. 1966 Oct 14;154(3746):271–272. doi: 10.1126/science.154.3746.271. [DOI] [PubMed] [Google Scholar]
- HALL C. E., SLAYTER H. S. The fibrinogen molecule: its size, shape, and mode of polymerization. J Biophys Biochem Cytol. 1959 Jan 25;5(1):11–16. doi: 10.1083/jcb.5.1.11. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Leberman R. Use of uranyl formate as a negative stain. J Mol Biol. 1965 Sep;13(2):606–606. doi: 10.1016/s0022-2836(65)80124-3. [DOI] [PubMed] [Google Scholar]
- Newcombe D. S., Cohen A. S. Solubility characteristics of isolated amyloid fibrils. Biochim Biophys Acta. 1965 Jul 8;104(2):480–486. doi: 10.1016/0304-4165(65)90353-3. [DOI] [PubMed] [Google Scholar]
- RICE R. V. Conformation of individual macromolecular particles from myosin solution. Biochim Biophys Acta. 1961 Sep 30;52:602–604. doi: 10.1016/0006-3002(61)90427-9. [DOI] [PubMed] [Google Scholar]
- Shirahama T., Cohen A. S. High-resolution electron microscopic analysis of the amyloid fibril. J Cell Biol. 1967 Jun;33(3):679–708. doi: 10.1083/jcb.33.3.679. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shirahama T., Cohen A. S. Structure of amyloid fibrils after negative staining and high-resolution electron microscopy. Nature. 1965 May 15;206(985):737–738. doi: 10.1038/206737a0. [DOI] [PubMed] [Google Scholar]