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Logo of procrsmedFormerly medchtJournal of the Royal Society of MedicineProceedings of the Royal Society of Medicine
 
Proc R Soc Med. 1973 July; 66(7): 705–710.
PMCID: PMC1645093

An ABC of amyloid.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Barth WF, Willerson JT, Waldmann TA, Decker JL. Primary amyloidosis. Clinical, immunochemical and immunoglobulin metabolism. Studies in fifteen patients. Am J Med. 1969 Aug;47(2):259–273. [PubMed]
  • Benditt EP, Eriksen N, Hermodson MA, Ericsson LH. The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett. 1971 Dec 1;19(2):169–173. [PubMed]
  • BLUM A, SOHAR E. The diagnosis of amyloidosis. Ancillary procedures. Lancet. 1962 Apr 7;1(7232):721–724. [PubMed]
  • Cohen AS. Amyloidosis. N Engl J Med. 1967 Sep 7;277(10):522–contd. [PubMed]
  • COHEN AS, CALKINS E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature. 1959 Apr 25;183(4669):1202–1203. [PubMed]
  • Eanes ED, Glenner GG. X-ray diffraction studies on amyloid filaments. J Histochem Cytochem. 1968 Nov;16(11):673–677. [PubMed]
  • Ein D, Kimura S, Terry WD, Magnotta J, Glenner GG. Amino acid sequence of an amyloid fibril protein of unknown origin. J Biol Chem. 1972 Sep 10;247(17):5653–5655. [PubMed]
  • Franklin EC, Pras M, Levin M, Frangione B. The partial amino acid sequence of the major low molecular weight component of two human amyloid fibrils. FEBS Lett. 1972 Apr 15;22(1):121–123. [PubMed]
  • Glenner GG, Terry W, Harada M, Isersky C, Page D. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971 Jun 11;172(3988):1150–1151. [PubMed]
  • Harada M, Isersky C, Cuatrecasas P, Page D, Bladen HA, Eanes ED, Keiser HR, Glenner GG. Human amyloid protein: chemical variability and homogeneity. J Histochem Cytochem. 1971 Jan;19(1):1–15. [PubMed]
  • HOBBS JR, MORGAN AD. FLUORESCENCE MICROSCOPY WITH THIOFLAVINE-T IN THE DIAGNOSIS OF AMYLOID. J Pathol Bacteriol. 1963 Oct;86:437–442. [PubMed]
  • Husby G, Natvig JB. Immunological characterization of amyloid fibrils in tissue sections. Clin Exp Immunol. 1972 Jul;11(3):357–366. [PubMed]
  • Jones NF, Hilton PJ, Tighe JR, Hobbs JR. Treatment of "primary" renal amyloidosis with melphalan. Lancet. 1972 Sep 23;2(7778):616–619. [PubMed]
  • LACHMANN PJ, MULLER-EBERHARD HJ, KUNKEL HG, PARONETTO F. The localization of in vivo bound complement in tissue section. J Exp Med. 1962 Jan 1;115:63–82. [PMC free article] [PubMed]
  • Conn NK. A study of some of the methods of urinary collecon in children. J Clin Pathol. 1970 Feb;23(1):81–84. [PMC free article] [PubMed]
  • MISSMAHL HP, GAFNI J. PERI-COLLAGEN AND PERI-RECTICULAR AMYLOIDOSIS. THEIR DIFFERENTIATION BY POLARIZATION MICROSCOPY. Pathol Microbiol (Basel) 1964;27:826–832. [PubMed]
  • OSSERMAN EF, TAKATSUKI K, TALAL N. MULTIPLE MYELOMA I. THE PATHOGENESIS OF "AMYLOIDOSIS. Semin Hematol. 1964 Jan;1:3–85. [PubMed]
  • Pras M, Reshef T. The acid-soluble fraction of amyloid--a fibril forming protein. Biochim Biophys Acta. 1972 Jun 22;271(1):193–203. [PubMed]
  • Solomon A, Killander J, Grey HM, Kunkel HG. Low-molecular-weight proteins related to Bence Jones proteins in multiple myeloma. Science. 1966 Mar 11;151(3715):1237–1239. [PubMed]
  • VASSAR PS, CULLING CF. Fluorescent stains, with special reference to amyloid and connective tissues. Arch Pathol. 1959 Nov;68:487–498. [PubMed]

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