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Alternative conformations of amyloidogenic proteins govern their behavior

Academic Article
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Overview

authors

  • Kelly, Jeffery

publication date

  • February 1996

journal

  • Current Opinion in Structural Biology  Journal

abstract

  • Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis. In addition, newly available moderate to high resolution structural studies are bringing us closer to understanding the structure of amyloid.

subject areas

  • Adult
  • Aged
  • Aged, 80 and over
  • Alzheimer Disease
  • Amyloid
  • Amyloid Neuropathies
  • Amyloid beta-Peptides
  • Amyloidosis
  • Animals
  • Humans
  • Immunoglobulin Light Chains
  • Models, Molecular
  • Muramidase
  • Prealbumin
  • Protein Conformation
  • Protein Folding
  • Structure-Activity Relationship
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Identity

International Standard Serial Number (ISSN)

  • 0959-440X

Digital Object Identifier (DOI)

  • 10.1016/s0959-440x(96)80089-3

PubMed ID

  • 8696966
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Additional Document Info

start page

  • 11

end page

  • 17

volume

  • 6

issue

  • 1

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