Results 181 to 190 of about 5,604,422 (355)

Stochastic Modelling Approach to the Incubation Time of Prionic Diseases

, 2003
Transmissible spongiform encephalopathies like the bovine spongiform encephalopathy (BSE) and the Creutzfeldt-Jakob disease (CJD) in humans are neurodegenerative diseases for which prions are the attributed pathogenic agents.
A. S. Ferreira, A. L. Horwich, B. J. West, D. J. Stekel, G. C. Telling, J. C. Cressoni, J. Collinge, J. D. Murray, J. S. Griffith, M. A. A. da Silva, M. Eigen, R. G. Will, R. M. Anderson, S. B. Prusiner, S. B. Prusiner, S. B. Prusiner   +15 more
core   +1 more source

Phase separation of a yeast prion protein promotes cellular fitness

Science, 2018
Titus M. Franzmann, Marcus Jahnel, Andrei Pozniakovsky, J. Mahamid, A. Holehouse, Elisabeth Nüske, Doris Richter, W. Baumeister, S. Grill, R. Pappu, A. Hyman, S. Alberti   +11 more
semanticscholar   +1 more source

Stress‐inducible phosphoprotein 1 (Sti1/Stip1/Hop) sequesters misfolded proteins during stress

The FEBS Journal, EarlyView.
Stress‐inducible phosphoprotein 1 (Sti1/Stip1/Hop) is a major co‐chaperone to both Hsp90 and Hsp70. We find that misbalanced expression of Sti1 in yeast and mammalian cells causes severe growth defects. Deletion of STI1 causes an accumulation of soluble misfolded ubiquitinated proteins and a strong activation of the heat shock response.
Benjamin S. Rutledge, Young J. Kim, Donovan W. McDonald, Juan C. Jurado‐Coronel, Marco A. M. Prado, Jill L. Johnson, Wing‐Yiu Choy, Martin L. Duennwald   +7 more
wiley   +1 more source

A cellular model of TDP‐43 induces phosphorylated TDP‐43 aggregation with distinct changes in solubility and autophagy dysregulation

The FEBS Journal, EarlyView.
TDP‐43 protein plays a pathological role in sporadic and familial amyotrophic lateral sclerosis (ALS). Here, we developed a cellular model overexpressing TDP‐43 with three mutations linked to familial ALS, termed ‘3X‐TDP‐43’. Mutant 3X‐TDP‐43 expression showed deficits in autophagy flux and colocalization with stress granules.
Matthew B. Dopler, Muhammad I. Abeer, Sanaz Arezoumandan, Keyshawn Cox, Tyler L. Petersen, Esther H. Daniel, Carlton L. Cannon III, Angelica Bautista, Kennedy D. Blancher, Alysia M. Bland, Kylie J. Bond, Dominque A. Davis, Jessica M. Francois, Eliana J. McCray, Justin M. Morgan, Jessica L. Pulliam, Zymir A. Robinson, Mykia J. Taylor, James A. Dowell, Nigel J. Cairns, Michael A. Gitcho   +20 more
wiley   +1 more source

An Engineered Nonsense \u3cem\u3eURA3\u3c/em\u3e Allele Provides a Versatile System to Detect the Presence, Absence and Appearance of the [em\u3ePSI\u3c/em\u3e\u3csup\u3e+\u3c/sup\u3e] Prion in \u3cem\u3eSaccharomyces cerevisiae\u3c/em\u3e [PDF]

, 2006
Common methods to identify yeast cells containing the prion form of the Sup35 translation termination factor, [PSI+], involve a nonsense suppressor phenotype. Decreased function of Sup35p in [PSI+] cells leads to readthrough of certain nonsense mutations
Kirkland, Kathryn T., Liebman, Susan W., Manogaran, Anita L.   +2 more
core   +1 more source

Type I interferon signalling and interferon‐responsive microglia in health and disease

The FEBS Journal, EarlyView.
Recent insights reveal that type I interferon (IFN‐I) signalling plays critical roles in the nervous system beyond antiviral defence. Dysregulated IFN‐I activity is increasingly linked to neurological dysfunction and neurodegeneration, with microglia as central mediators. This review explores the broader impact of IFN‐I signalling on the nervous system
Jose P. Lopez‐Atalaya, Aysha M. Bhojwani‐Cabrera   +1 more
wiley   +1 more source

Strain-Specific Targeting and Destruction of Cells by Prions

Biology
Prion diseases are caused by the disease-specific self-templating infectious conformation of the host-encoded prion protein, PrPSc. Prion strains are operationally defined as a heritable phenotype of disease under controlled conditions.
Sara M. Simmons, Jason C. Bartz
doaj   +1 more source

The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog [PDF]

, 1997
Virginie Coustou, Carol Deleu, Sven J. Saupe, Joël Bégueret   +3 more
openalex   +1 more source

Spatial Sequestration and Oligomer Remodeling During \u3cem\u3ede novo\u3c/em\u3e [\u3cem\u3ePSI\u3c/em\u3e\u3csup\u3e+\u3c/sup\u3e] Formation [PDF]

, 2017
Prions are misfolded, aggregated, infectious proteins found in a range of organisms from mammals to bacteria. In mammals, prion formation is difficult to study because misfolding and aggregation take place prior to symptom presentation.
Lyke, Douglas, Manogaran, Anita L.
core   +1 more source

Stress alters hypothalamic gene expression in adolescent male Golden hamsters

Journal of Neuroendocrinology, EarlyView.
Abstract In Golden hamsters (Mesocricetus auratus), a two‐week exposure to chronic social stress in adolescence causes acceleration of agonistic behavior, enhanced adult aggression, impaired waiting impulsivity, and higher food intake, body fat, and long‐term increased body weight.
Kevin M. Moran, Tyler M. Milewski, James P. Curley, Yvon Delville   +3 more
wiley   +1 more source