Publication Detail

The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in PubMed. This abstract is what is used to create the fingerprint of the publication. If any grants are referenced by the publication, they will be listed here as well.

Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern.

P D Gorevic; E M Castano; R Sarma; B Frangione (Profiled Author: Frangione, Blas)

Biochemical and biophysical research communications 1987;147(2):854-62.

The molecular basis of fibril formation in Alzheimers disease was explored by electron micrographic and x-ray diffraction analysis of a series of synthetic peptides corresponding to portions of the amino acid sequence of beta protein and that of its putative precursor. A minimum 14 residue peptide was identified that formed typical amyloid fibrils under physiological conditions. Of these 14 residues, 10 were sufficient to give an identical 4.76 A and 10.6 A diffraction pattern as that recently described for isolated neurofibrillary tangles, amyloid plaque cores and leptomeningeal amyloid fibrils.

3 Originating Grant

• 1.

  Frangione, Blas

  Amyloidosis and Alzheimer's Disease

  1 July 1985 - 30 June 2007

  NATIONAL INSTITUTE ON AGING

  Total Funding: $ 4,467,436

• 2.

  FRANGIONE, BLAS

  AMYLOIDOSIS AND ALZHEIMERS DISEASE

  1 July 1985 - 30 June 1997

  NATIONAL INSTITUTE ON AGING

  Total Funding: $ 3,049,140

• 3.

  FRANGIONE, BLAS

  RHEUMATIC DISEASES--CONNECTIVE TISSUE AND MEMBRANE PROTEINS

  1 January 1976 - 31 December 1984

  NAT INST OF ARTHRITIS, DIABETES, DIGESTIVE & KIDNEY DISEASES

  Total Funding: $ 1,851,290

Scientific Context

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