Structure/function in neuroprotection and apoptosis

Ann Neurol. 1998 Sep;44(3 Suppl 1):S65-71. doi: 10.1002/ana.410440711.

Abstract

The three-dimensional conformation of proteins influences their potential to function correctly within the cell. Protein conformational issues are particularly important in neurodegeneration, as has been shown by misfolded protein forming the basis of plaques in Alzheimer's disease and prion diseases. This article focuses on protein structure/function specifically for proteins important in the pathogenesis of neurodegenerative conditions and those involved in apoptosis. The proteins used as examples in this review include alpha-synuclein, the promyelocytic leukemia protein, and glyceraldehyde 3-phosphate dehydrogenase.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Apoptosis / physiology*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry
  • Humans
  • Molecular Sequence Data
  • Neoplasm Proteins / chemistry
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / physiology
  • Neuroprotective Agents / chemistry*
  • Neuroprotective Agents / metabolism
  • Peptide Fragments / chemistry
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Synucleins
  • alpha-Synuclein

Substances

  • Neoplasm Proteins
  • Nerve Tissue Proteins
  • Neuroprotective Agents
  • Peptide Fragments
  • SNCA protein, human
  • Synucleins
  • alpha-Synuclein
  • glyceraldehyde 3-phosphate dehydrogenase (304-313)
  • Glyceraldehyde-3-Phosphate Dehydrogenases