Your search for: 'author:("Zaidi, Syed I.A.")' has returned 2 results. (0.019s) Save search

Authors: Capellari, Sabina | Zaidi, Syed I.A. | Long, Amy C. | Kwon, Eunice E. | Petersen, Robert B.

Article Type: Research Article

Abstract: The abnormal form of the prion protein has increased resistance to protease digestion and is insoluble in non-ionic detergents. The normal prion protein is modified by the non-obligatory addition of two N-linked glycans. One pathogenic mutation, Thr to Ala at residue 183 of the human prion protein, blocks addition of the first glycan to the Asp residue 181. This mutation has been reported to result in intracellular retention of the mutant protein and its acquisition of pathogenic properties, presumably due to the lack of the glycan. We report that the lack of the N-linked glycan at residue 181 is not …responsible for the block in transport or the acquisition of pathogen-like properties, rather, the Thr to Ala mutation is itself the probable cause of the pathogenic phenotype. Show more

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DOI: 10.3233/JAD-2000-2104

Citation: Journal of Alzheimer's Disease, vol. 2, no. 1, pp. 27-35, 2000

Authors: Zaidi, Syed I.A. | Richardson, Sandra L. | Capellari, Sabina | Song, Li | Smith, Mark A. | Ghetti, Bernardino | Sy, Man-Sun | Gambetti, Pierluigi | Petersen, Robert B.

Article Type: Research Article

Abstract: Prion diseases are associated with the accumulation of a misfolded, protease resistant form of the prion protein, PrPres . In humans there are a variety of different prion related diseases that are sporadic, inherited, or acquired by infection. Gerstmann-Straussler-Sheinker syndrome (GSS) is an inherited prion disease in which PrPres accumulates as amorphous aggregates as well as in amyloid plaques. GSS has been associated with a variety of point mutations in the prion protein: 102, 105, 117, 131, 145, 187, 198, 202, 212, 217, and 232. The F198S mutation was discovered in a large Indiana kindred. Previous studies in vitro have …shown that the 198 mutation results in structural instability of the prion protein. In the current study, we demonstrate in a cell model that the F198S mutant protein can be folded properly in a cellular context, but is unable to refold to a native state after denaturation. Further, the F198S mutation significantly affects glycosylation of the mutant protein. Show more

DOI: 10.3233/JAD-2005-7209

Citation: Journal of Alzheimer's Disease, vol. 7, no. 2, pp. 159-171, 2005