Linked Life Data

8761624

Source:http://linkedlifedata.com/resource/pubmed/id/8761624

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-10-10
pubmed:abstractText
The abnormal protein which accumulates in the extracellular space in the central nervous system in Alzheimer's disease and prion diseases could result from similar mechanisms. Many studies have demonstrated that the abnormal protein is resistant to proteolytic agents. This resistance is correlated with a modification in the conformation of the protein, inverting the ratio of alpha and beta helix structures. This change in conformation could be the cause of the central nervous system lesions. The mechanism of the modification in conformation could be related to a process of hydrophobisation of the protein resulting from mutation. A hydrophilic amino acid would be replaced by a hydrophobic amino acid or in sporadic forms, modifications in the environment of the peptide may lead to physical and chemical aggressions. Hydrophobisation of the two proteins could later lead to formation of polymers and then insoluble aggregates with the physical and chemical characteristics of the amyloid substance. Polymerisation could be triggered by the formation of protein dimers which would be, in one case, an endogenous protein, PrP, and in the other exogenous proteins coming from the environment.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0035-3787
pubmed:author
pubmed:issnType
Print
pubmed:volume
152
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
153-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
[Amyloidosis, protein conformation dynamics and neurologic diseases].
pubmed:affiliation
Service des Maladies du Système Nerveux et du Muscle, Hôpitaux Universitaires de Strasbourg.
pubmed:publicationType
Journal Article, English Abstract, Review