Results 11 to 20 of about 16,662 (259)

Saccharomyces cerevisiae in neuroscience: how unicellular organism helps to better understand prion protein?

Neural Regeneration Research, 2021
The baker’s yeast Saccharomyces (S.) cerevisiae is a single-celled eukaryotic model organism widely used in research on life sciences. Being a unicellular organism, S. cerevisiae has some evident limitations in application to neuroscience. However, yeast
Takao Ishikawa
doaj   +1 more source

Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation. [PDF]

PLoS ONE, 2014
Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast.
Djamel Harbi, Paul M Harrison
doaj   +1 more source

ALK1 controls hepatic vessel formation, angiodiversity, and angiocrine functions in hereditary hemorrhagic telangiectasia of the liver

Hepatology, EarlyView., 2022
Hepatic endothelial Alk1 signaling protects from development of vascular malformations while maintaining organ‐specific endothelial differentiation and angiocrine portmanteau of the names Wingless and Int‐1 signaling. Abstract Background and Aims In hereditary hemorrhagic telangiectasia (HHT), severe liver vascular malformations are associated with ...
Christian David Schmid, Victor Olsavszky, Manuel Reinhart, Vanessa Weyer, Felix A. Trogisch, Carsten Sticht, Manuel Winkler, Sina W. Kürschner, Johannes Hoffmann, Roxana Ola, Theresa Staniczek, Joerg Heineke, Beate K. Straub, Jens Mittler, Kai Schledzewski, Peter ten Dijke, Karsten Richter, Steven Dooley, Cyrill Géraud, Sergij Goerdt, Philipp‐Sebastian Koch   +20 more
wiley   +1 more source

Chronic Wasting Disease Prion Strain Emergence and Host Range Expansion

Emerging Infectious Diseases, 2017
Human and mouse prion proteins share a structural motif that regulates resistance to common chronic wasting disease (CWD) prion strains. Successful transmission of an emergent strain of CWD prion, H95+, into mice resulted in infection. Thus, emergent CWD
Allen Herbst, Camilo Duque Velásquez, Elizabeth Triscott, Judd M. Aiken, Debbie McKenzie   +4 more
doaj   +1 more source

Amyloid prions in fungi [PDF]

, 2016
Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi, Aguzzi, Aigle, Alberti, Aron, Balguerie, Ball, Bardill, Baudin-Baillieu, Baxa, Baxa, Borchsenius, Brachmann, Bradley, Brown, Byers, Cai, Chakrabortee, Chen, Chernoff, Collinge, Coustou, Coustou-Linares, Cox, Daskalov, Daskalov, Daskalov, Daskalov, Derkatch, Derkatch, Derkatch, Diaz-Avalos, DiSalvo, Douglas, Eichner, Espinosa Angarica, Fan, Garcia, Glover, Glover, Gorkovskiy, Griswold, Habenstein, Halfmann, Halfmann, Harrison, Higurashi, Holmes, Huang, Jarosz, Jarosz, Jung, Kabir, Kajava, Kajava, Kelly, King, King, Koch, Kochneva-Pervukhova, Krishnan, Kryndushkin, Kumar, Kunz, Lancaster, Li, Lum, Malato, Masel, Masison, Masison, Mathur, McGlinchey, Mizuno, Nakayashiki, Nelson, Newnam, Ohhashi, Patel, Patino, Paushkin, Prusiner, Rajon, Ritter, Rizet, Roberts, Ross, Ross, Schlieker, Schlumpberger, Sen, Seuring, Shewmaker, Shorter, Sondheimer, Sondheimer, Speldewinde, Stein, Taneja, Tapia, Tessier, Tipton, Tompa, Toyama, True, True, Tsai, Tycko, Tyedmers, Uptain, Van Melckebeke, Verges, Wan, Wasmer, Watts, Westergard, Wickner, Wickner, Wickner, Wickner, Wickner, Wickner, Zhou   +122 more
core   +2 more sources

Assessing Prion Infectivity of Human Urine in Sporadic Creutzfeldt-Jakob Disease

Emerging Infectious Diseases, 2012
Prion diseases are neurodegenerative conditions associated with a misfolded and infectious protein, scrapie prion protein (PrPSc). PrPSc propagate prion diseases within and between species and thus pose risks to public health.
Silvio Notari, Liuting Qing, Maurizio Pocchiari, Ayuna Dagdanova, Kristin Hatcher, Arend Dogterom, Jose F. Groisman, Ib Bo Lumholtz, Maria Puopolo, Corinne Lasmezas, Shu G. Chen, Qingzhong Kong, Pierluigi Gambetti   +12 more
doaj   +1 more source

Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery

Molecules, 2019
Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature).
Tatiana A. Chernova, Yury O. Chernoff, Keith D. Wilkinson   +2 more
doaj   +1 more source

Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease [PDF]

, 2008
Prion diseases are fatal, transmissible, neurodegenerative diseases caused by the misfolding of the prion protein (PrP). At present, the molecular pathways underlying prion-mediated neurotoxicity are largely unknown.
Aguzzi, Adriano, Borkowski, Andrew W., Heppner, Frank L., Hutter, Gregor, Jackson, Walter S., King, Oliver D., Lindquist, Susan, Raymond, Gregory J., Steele, Andrew D.   +8 more
core   +3 more sources

The anti‐prion RNA aptamer R12 disrupts the Alzheimer's disease‐related complex between prion and amyloid β [PDF]

The FEBS Journal, 2019
The neurodegenerative disorder Alzheimer's disease (AD) is associated with the accumulation of misfolded proteins. Some recent studies suggested that amyloid beta (Aβ) forms soluble oligomers, protofibrils, and fibrils; the Aβ oligomers being more toxic than the fibrils.
Mamiko, Iida, Tsukasa, Mashima, Yudai, Yamaoki, Masatomo, So, Takashi, Nagata, Masato, Katahira   +5 more
openaire   +2 more sources

PrionHome: a database of prions and other sequences relevant to prion phenomena.

PLoS ONE, 2012
Prions are units of propagation of an altered state of a protein or proteins; prions can propagate from organism to organism, through cooption of other protein copies.
Djamel Harbi, Marimuthu Parthiban, Deena M A Gendoo, Sepehr Ehsani, Manish Kumar, Gerold Schmitt-Ulms, Ramanathan Sowdhamini, Paul M Harrison   +7 more
doaj   +1 more source