Results 81 to 90 of about 5,269,629 (202)

A self-complementary recombinant adeno-associated virus vector coding for an anchorless prion protein carrying the G127V mutation extends survival in a rodent prion disease model.

PLoS Pathogens
The replacement of a single codon in the human prion gene, causing the substitution of glycine with valine at position 127 (G127V) of the prion protein (PrP), prevents development of prion disease.
Thomas Zerbes, Claire Verkuyl, Cunjie Zhang, Sophie Grunnesjoe, Shehab Eid, Hamza Arshad, Wenda Zhao, Zahra Nasser, Teaghan O'Shea, Ari Bel, Lise Lamoureux, Kathy L Frost, Jennifer Myskiw, Le Yao Li, Erica Stuart, Holger Wille, Stephanie Booth, Joel C Watts, Gerold Schmitt-Ulms   +18 more
doaj   +1 more source

The first report of prion protein gene sequences in Dybowski’s frog and the American bullfrog: high amyloid propensity of the frog prion protein

Frontiers in Animal Science
Prion diseases are fatal infectious neurodegenerative diseases caused by the proteinase K-sensitive form of prion protein (PrPSc). The exact origin of prion seeding and the transition factor of PrPSc has not been elucidated.
Sae-Young Won, Yong-Chan Kim
doaj   +1 more source

Endogenous Viral Etiology of Prion Diseases [PDF]

, 2009
Transmissible spongiform encephalopathies (TSEs), or prion diseases, are a group of incurable neurodegenerative disorders, including Kuru and Creutzfeldt-Jakob disease in humans, “mad cow” disease in cattle, and scrapie in sheep. This paper
Claudiu I. Bandea
core  

State-of-the-art review of goat TSE in the European Union, with special emphasis on PRNP genetics and epidemiology [PDF]

, 2009
Scrapie is a fatal, neurodegenerative disease of sheep and goats. It is also the earliest known member in the family of diseases classified as transmissible spongiform encephalopathies (TSE) or prion diseases, which includes Creutzfeldt-Jakob disease in ...
Olivier Andreéoletti, Groschup, Martin H., Simone Peletto, Foster, James, Barillet, F., Acin, Cristina, Pierluigi Acutis, Peletto, S., Langeveld, J., Theodoros Sklaviadis, Keulen, L.J.M., van, Bossers, Alex, Vaccari, G., Van Keulen, Lucien, Foster, J., Acin, C., Cristina Acin, Andreoletti, O., Jan Langeveld, Goldmann, Wilfred, Umberto Agrimi, Sklaviadis, T., Vaccari, Gabriele, Langeveld, Jan, van Keulen, L., Groschup, M.H., Peletto, Simone, Bossers, A., Gabriele Vaccari, James Foster, Panagiotidis, C.H., Cynthia H. Panagiotidis, Alex Bossers, Badiola, J. J., Badiola, J.J., van Keulen, L.J.M., Juan J. Badiola, Francis Barillet, Sklaviadis, Theodoros, Barillet, Francis, Langeveld, J.P.M., Wilfred Goldmann, Panagiotidis, Cynthia H., Acutis, Pierluigi, Andreeoletti, O., Badiola, Juan J., Goldmann, W., Panagiotidis, C. H., Groschup, M. H., Andreoletti, Olivier, Acutis, P., Agrimi, Umberto, Lucien Van Keulen, Martin H. Groschup, Agrimi, U.   +54 more
core   +1 more source

Human biomarker navigator

iMeta, EarlyView.
The Human Biomarker Navigator integrates the disease continuum, biomarker dynamics, cross‐organ biomarker networks, biomarker classification, and technology‐driven paradigms. It maps how biomarkers link multi‐system physiology and pathology across the nervous, respiratory, endocrine, circulatory, immune, digestive, urinary, reproductive, and ...
Meng‐Yao Li, Qian Zhang, Zijie Wang, Zeping Gui, Jing Liu, Jingda Li, Maojun Jiang, Zukang Chang, Qingqing Han, Bendong Yang, Tariq Saeed, Jun Li, Jinghan Jia, Chenghu Song, Tong Shao, Tianhuan Peng, Xueying Zhang, Pingping Guo, Jun Luo, Gangao Yang, Yuan Wan, Gokhan Zengin, Quan Yuan, Lingru Li, Xiaohui Fan, Yang Luo, Lvyun Zhu, Yanfei Zheng, Wenjun Mao, Wenlong Sun   +29 more
wiley   +1 more source

Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction [PDF]

, 2004
The aqueous solution structure of the full-length recombinant ovine prion protein PrP25-233, together with that of the N-terminal truncated version PrP94-233, have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular ...
Rhie, A G O, Nielsen, Kurt, Blanch, EW, Rhie, AGO, Gill, AC, Hope, James, Hecht, L, Gill, Andrew C., Gill, A C, Blanch, E W, Barron, Laurence D., Barron, L D, Nielsen, K, Hope, J, Hecht, Lutz, Barron, LD, Blanch, Ewan W., Rhie, Alexandre G. O., Rhie, Alexandre G O   +18 more
core   +1 more source

Scrapie susceptibility-associated indel polymorphism of shadow of prion protein gene (SPRN) in Korean native black goats

Scientific Reports, 2019
Prion diseases in sheep and goats are called scrapie and belong to a group of transmissible spongiform encephalopathies (TSEs) caused by the abnormal misfolding of the prion protein encoded by the prion protein gene (PRNP).
Yong-Chan Kim, Seon-Kwan Kim, Byung-Hoon Jeong   +2 more
doaj   +1 more source

Beginning with a single step: A social theory of change for managing chronic wasting disease

The Journal of Wildlife Management, EarlyView.
Following opinions of chronic wasting disease management experts, we identified and prioritized critical interventions to address the disease. We developed a theory of change for the most prioritized intervention that supports the implementation of engagement or social marketing strategies to increase support for management.
Nicholas W. Cole, Brad Milley, Jaclyn Lucas, Nick Salafsky, Natalie Sexton, Rudy Schuster   +5 more
wiley   +1 more source

Therapeutic Impact of GLP‐1 Receptor Agonists on Parkinson's Disease: A Scoping Review

Neurology and Clinical Neuroscience, EarlyView.
ABSTRACT No disease‐modifying treatment exists for Parkinson's disease (PD). Glucagon‐like peptide‐1 receptor agonists (GLP‐1 RAs) have gained attention as promising candidates for neuroprotection, given documented expression of GLP‐1 receptors within the central nervous system and the contribution of brain insulin resistance to dopaminergic ...
João Pedro Henriques, João Pedro Stringhetta Rahal, Rafael da Cunha Gomes Ribeiro, Enzo Bogucheski Ribeiro Machado, Carlos Antonio Negrato   +4 more
wiley   +1 more source

An overview of human prion diseases

Virology Journal, 2011
Prion diseases are transmissible, progressive and invariably fatal neurodegenerative conditions associated with misfolding and aggregation of a host-encoded cellular prion protein, PrPC.
Imran Muhammad, Mahmood Saqib
doaj   +1 more source