Associated Papers
Prion Mutations in Republic of Republic of Korea, China, and Japan.
Kim DY et al.
International Journal of Molecular Sciences, 2022
The First Evaluation of Proteinase K-Resistant Prion Protein (PrPSc) in Korean Appendix Specimens.
Won SY et al.
Medicina (kaunas, Lithuania), 2022
Genetic Prion Disease: Insight from the Features and Experience of China National Surveillance for Creutzfeldt-Jakob Disease.
Shi Q et al.
Neuroscience Bulletin, 2021
Phenotypic diversity of genetic Creutzfeldt-Jakob disease: a histo-molecular-based classification.
Baiardi S et al.
Acta Neuropathologica, 2021
Mechanism of misfolding of the human prion protein revealed by a pathological mutation.
Sanz-Hernández M et al.
Proceedings of the National Academy of Sciences of the United States of America, 2021
Genetic Creutzfeldt-Jakob disease.
Ladogana A et al.
Handbook of Clinical Neurology, 2018
Characterization of mutations in PRNP (prion) gene and their possible roles in neurodegenerative diseases.
Bagyinszky E et al.
Neuropsychiatric Disease and Treatment, 2018
The Features of Genetic Prion Diseases Based on Chinese Surveillance Program.
Shi Q et al.
Plos One, 2015
Systematic investigation of predicted effect of nonsynonymous SNPs in human prion protein gene: a molecular modeling and molecular dynamics study.
Jahandideh S et al.
Journal of Biomolecular Structure & Dynamics, 2014
Discriminant analysis of prion sequences for prediction of susceptibility.
Lee JH et al.
Experimental & Molecular Medicine, 2013
Glycoform-selective prion formation in sporadic and familial forms of prion disease.
Xiao X et al.
Plos One, 2013
Characterization of spontaneously generated prion-like conformers in cultured cells.
Zou RS et al.
Aging, 2011
Common structural traits across pathogenic mutants of the human prion protein and their implications for familial prion diseases.
Rossetti G et al.
Journal of Molecular Biology, 2011
Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.
Meli M et al.
Plos One, 2011
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.
van der Kamp MW et al.
Journal of Molecular Biology, 2010
Accessibility of a critical prion protein region involved in strain recognition and its implications for the early detection of prions.
Yuan J et al.
Cellular and Molecular Life Sciences : Cmls, 2008
Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations.
Kuznetsov IB et al.
Protein Science : a Publication of the Protein Society, 2004
Loss of glycosylation associated with the T183A mutation in human prion disease.
Grasbon-Frodl E et al.
Acta Neuropathologica, 2004
High capacity and low cost detection of prion protein gene variant alleles by denaturing HPLC.
Castro RM et al.
Journal of Neuroscience Methods, 2004
High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes.
Finckh U et al.
American Journal of Human Genetics, 2000
High frequency of mutations in four different disease genes in early-onset dementia.
Finckh U et al.
Annals of the New York Academy of Sciences, 2000