title: N-terminal heterogenicity of amyloid protein examined in Alzheimer's disease.
abstract: Alzheimer's disease is the major cause of dementia in humans. The affected brain shows characteristic abnormal filamentous proteins that accumulate intracellularly as neurofibrillary tangles, and extracellularly as senile plaques, as well as in cerebral blood vessels. The extracellular deposits are an amyloid protein, which is highly insoluble. In our study, we intended to show that the N-terminus of amyloid A4 protein can change in length and sequence in Alzheimer's disease, and possibly in other dementias.
authors.affiliation: Department of Medical Biology and Genetic, Ataturk University, Erzurum, Turkey.
authors.forename: Ibrahim
authors.initials: I
authors.lastname: Pirim
authors.forename: Ali Riza
authors.initials: AR
authors.lastname: Erdogan
authors.forename: Uner
authors.initials: U
authors.lastname: Tan
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D001923:Brain Chemistry; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D058225:Plaque, Amyloid / Q000378:metabolism; D020539:Sequence Analysis, Protein
chemical_list: D016229:Amyloid beta-Peptides