Familial conformational diseases and dementias
- 27 June 2002
- journal article
- review article
- Published by Hindawi Limited in Human Mutation
- Vol. 20 (1) , 1-14
- https://doi.org/10.1002/humu.10100
Abstract
Familial conformational diseases occur when a mutation alters the conformation of a protein resulting in abnormal intermolecular interactions, protein aggregation, and consequent tissue damage. The molecular mechanisms of conformational disease are best understood for the serine protease inhibitor (serpin) superfamily of proteins. The serpinopathies include α1‐antitrypsin (SERPINA1) deficiency and the newly characterized familial encephalopathy with neuroserpin inclusion bodies (FENIB) resulting from mutations in the neuroserpin (SERPINI1) gene. This review discusses how insights gained from the study of the serpins may be used to guide our research into other common diseases such as Alzheimer disease, Huntington disease, and Parkinson disease.Keywords
This publication has 142 references indexed in Scilit:
- The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formationNature Neuroscience, 2001
- A Novel Apolipoprotein A-1 Variant, Arg173Pro, Associated with Cardiac and Cutaneous AmyloidosisBiochemical and Biophysical Research Communications, 1999
- Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's diseaseFEBS Letters, 1998
- Synthetic filaments assembled from C‐terminally truncated α‐synucleinFEBS Letters, 1998
- Tau is a candidate gene for chromosome 17 frontotemporal dementiaAnnals of Neurology, 1998
- AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's diseaseNature Genetics, 1998
- Genetic evidence for the involvement of τ in progressive supranuclear palsyAnnals of Neurology, 1997
- Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the α1A-voltage-dependent calcium channelNature Genetics, 1997
- Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's diseaseNature, 1991
- Pro→Leu change at position 102 of prinon protein is the most common but not the sole mutation related to Gerstmann-Sträussler syndromeBiochemical and Biophysical Research Communications, 1989