Results 81 to 90 of about 73,750 (253)

Construction of pathogenic Sec16a mutation mouse model using CRISPR/Cas9

Animal Models and Experimental Medicine, EarlyView.
Yaqiang Hu et al. engineered a pathogenic Sec16a mutant mouse model using CRISPR/Cas9 technology. They observed that the Sec16a mutant mice displayed diminished learning and memory capabilities, along with a limb‐clasping phenotype upon tail suspension.
Yaqiang Hu, Zhiyang Zeng, Xinyu Ming, Shuming Yin, Yuting Guan, Liangcai Gao, Dali Li   +6 more
wiley   +1 more source

Equine models in translational medicine: A comparative approach to human health

Animal Models and Experimental Medicine, EarlyView.
This diagram summarizes and contrasts rodent and equine models, outlining their strengths, limitations, and applications. Horses offer naturally occurring diseases, genetic and physiological similarities to humans, and suitability for longitudinal and clinical‐scale studies.
Shayan Boozarjomehri Amnieh, Katarzyna Ropka‐Molik   +1 more
wiley   +1 more source

PrPCWD lymphoid cell targets in early and advanced chronic wasting disease of mule deer [PDF]

, 2002
Up to 15% of free-ranging mule deer in northeastern Colorado and southeastern Wyoming, USA, are afflicted with a prion disease, or transmissible spongiform encephalopathy (TSE), known as chronic wasting disease (CWD).
Barillas-Mury, C., Hoover, E.A., Keulen, L.J.M., van, Langeveld, J.P.M., Miller, M.W., Oesch, B., Sigurdson, C.J.   +6 more
core   +2 more sources

Prion disease

Rinsho Shinkeigaku, 2010
Human prion diseases are classified into 3 categories according to etiologies: idiopathic of unknown cause, acquired of infectious origin, and genetic by PRNP mutation. The surveillance committee have analyzed 2,494 cases and identified 1,402 as prion diseases.
openaire   +4 more sources

Single-cell transcriptomics unveils molecular signatures of neuronal vulnerability in a mouse model of prion disease that overlap with Alzheimer’s disease

Nature Communications
Understanding why certain neurons are more sensitive to dysfunction and death caused by misfolded proteins could provide therapeutically relevant insights into neurodegenerative disorders.
Jessy A. Slota, Lise Lamoureux, Kathy L. Frost, Babu V. Sajesh, Stephanie A. Booth   +4 more
doaj   +1 more source

Canadian Creutzfeldt-Jakob disease incidence remained stable during the coronavirus disease (COVID-19) pandemic

Frontiers in Neurology
IntroductionHealthcare disruptions imposed by the coronavirus disease (COVID-19) pandemic and possible biological links between SARS-CoV-2 and prion misfolding might influence the prevalence or characteristics of Creutzfeldt-Jakob Disease (CJD).
Jessy A. Slota, Dobrila Todoric, Vanessa Bergeron, Kristen Avery, Clark Phillipson, Dominic M. S. Kielich, Jennifer Myskiw, Lise Lamoureux, Kathy Frost, Sharon L. R. Simon, Ben A. Bailey-Elkin, Stephanie A. Booth, Stephanie A. Booth   +12 more
doaj   +1 more source

Neural Stem Cell Differentiation and Prion Infection

Bio-Protocol, 2014
Prion diseases are transmissible, fatal, neurodegenerative diseases in human and animals. The molecular basis of neurodegeneration in prion diseases is largely unclear. Developing a cellular model capable of monitoring prion-induced cytotoxicity would be
Yoshi Iwamaru, Takato Takenouchi, Hiroshi Kitani   +2 more
doaj   +1 more source

A Review on the Salt Bridge Between ASP177 and ARG163 of Wild-Type Rabbit Prion Protein

, 2015
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and goats, cattle, deer, elks, humans and mice etc., but rabbits have a low susceptibility to be infected ...
Wang, Feng, Zhang, Jiapu
core   +2 more sources

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Andrew C. Gill, Ansari AA, Atvinder K. Rullay, Bertozzi CR, Blanch EW, Borchelt D, Caughey B, Caughey B, Caughey B, Caughey BW, Critchley P, David H. Crout, Eberl H, Ferris A, Georges C, Gill AC, Govaerts C, Haire LF, Harris DA, Hornemann S, Ian D. Sylvester, Imanpreet K. Bath, Kazlauskaite J, Kazlauskaite J, Kenyon GL, King SA, Kirby L, Klein TR, Kocienski PJ, Legname G, Matthew R. Hicks, Mui B, Nosjean O, Pan KM, Poss AJ, Safar J, Seddon AM, Shyng SL, Stahl N, Stahl N, Teresa J. T. Pinheiro, Whitesell JK, Wuthrich K, Zahn R, Zhang ZY   +44 more
core   +1 more source

Prion disease genetics [PDF]

European Journal of Human Genetics, 2006
Prion diseases have stimulated intense scientific scrutiny since it was proposed that the infectious agent was devoid of nucleic acid. Despite this finding, genetics has played a key role in understanding the pathobiology and clinical aspects of prion disease through the effects of a series of polymorphisms and mutations in the prion protein gene (PRNP)
openaire   +2 more sources