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Results: 31
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
Franziska Kundel, Liu Hong, Benjamin Falcon, William A McEwan, Thomas CT Michaels, Georg Meisl, Noemi Esteras, Andrey Y Abramov, Tuomas JP Knowles, Michel Goedert, David Klenerman
Jul 13, 2018
The ordered assembly of amyloidogenic proteins causes a wide spectrum of common neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. These diseases share common features with prion diseases, in which...
A conformational switch controlling the toxicity of the prion protein.
Karl Frontzek, Marco Bardelli, Assunta Senatore, Anna Henzi, Regina R Reimann, Seden Bedir, Marika Marino, Rohanah Hussain, Simon Jurt, Georg Meisl, Mattia Pedotti, Federica Mazzola, Giuliano Siligardi, Oliver Zerbe, Marco Losa, Tuomas Knowles, Asvin Lakkaraju, Caihong Zhu, Petra Schwarz, Simone Hornemann, Matthew G Holt, Luca Simonelli, Luca Varani, Adriano Aguzzi
Sep 10, 2022
Prion infections cause conformational changes of the cellular prion protein (PrPC) and lead to progressive neurological impairment. Here we show that toxic, prion-mimetic ligands induce an intramolecular R208-H140 hydrogen bond...
Inhibition of cytosolic Phospholipase A2 prevents prion peptide-induced neuronal damage and co-localisation with Beta III Tubulin.
Analysis of Variance Animals Arachidonic Acid Cell Death Cells Cultured Cerebral Cortex Dose-Response Relationship Drug Drug Interactions Embryo Mammalian Enzyme Activation Enzyme Inhibitors Gene Expression Regulation Humans Ionomycin Ketones Mice Neurons Peptide Fragments Phospholipases A2 Cytosolic Prions Protein Transport Synaptophysin Tetradecanoylphorbol Acetate Time Factors Tritium Tubulin
A new model for sensitive detection of zoonotic prions by PrP transgenic Drosophila.
Prions are transmissible protein pathogens most reliably detected by a bioassay in a suitable host, typically mice. However, the mouse bioassay is slow and cumbersome, and relatively insensitive to low titers of prion...
Determining Functional Interactions Between Ribosomal Co-translational Chaperone Complexes RAC and NAC (Btt1) in Saccharomyces cerevisiae
Caitlin Wrinn
Jan 01, 0001
Proteins are essential, functionally diverse macromolecules found in all living cells. Their structure is integral to their function, and they can fold in a variety of different conformations, which results in a change or loss...
Prions co-translational chaperones ribosome associated complex (RAC) nascent chain associated complex (NAC) Yeast Stress Biochemistry, Biophysics, and Structural Biology Cell Biology Genetics Life Sciences Molecular Biology
Published by: Ursinus College
Can the Yeast Ribosome-Associated Complex Chaperones Zuo1 and Ssz1 be Functionally Replaced With Their Human Homologs Mpp11 and Hsp70L1?
Yusef G Ahmed
Jan 01, 0001
Proteins are important molecules that are needed for structure, function, and other important processes in the cell. Proteins are synthesized by molecular machines called ribosomes, and they exit from ribosomes as chains of...
Prions ribosome-associated complex RAC Mpp11 Hsp70L1 Yeast Biochemistry Biochemistry, Biophysics, and Structural Biology Life Sciences Molecular Biology
Published by: Ursinus College
Human Orthologs of the Ribosome-Associated Complex (RAC) can Functionally Replace the Yeast RAC in S. cerevisiae
Nikole Fandino Pachon
Jan 01, 0001
Proteins are very important for many different functions in our bodies. However, they are prone to misfold, which could make them acquire new toxic functions. In order to prevent these incidents, a special type of proteins...
Published by: Ursinus College
Scaling analysis reveals the mechanism and rates of prion replication in vivo.
Georg Meisl, Timothy Kurt, Itzel Condado-Morales, Cyrus Bett, Silvia Sorce, Mario Nuvolone, Thomas CT Michaels, Daniel Heinzer, Merve Avar, Samuel IA Cohen, Simone Hornemann, Adriano Aguzzi, Christopher M Dobson, Christina J Sigurdson, Tuomas PJ Knowles
Feb 15, 2021
Prions consist of pathological aggregates of cellular prion protein and have the ability to replicate, causing neurodegenerative diseases, a phenomenon mirrored in many other diseases connected to protein aggregation, including...
Innovation of a Novel Prion Reporter System in Saccharomyces cerevisiae
Daniel Selechnik
Jan 01, 0001
Prions are misfolded proteins that become infectious and propagate themselves by causing the misfolding of other copies of the same type of protein. The [PSI+] prion results from misfolded conformations of the translation...
Published by: Ursinus College
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.
Marija Iljina, Gonzalo A Garcia, Mathew H Horrocks, Laura Tosatto, Minee L Choi, Kristina A Ganzinger, Andrey Y Abramov, Sonia Gandhi, Nicholas W Wood, Nunilo Cremades, Christopher M Dobson, Tuomas PJ Knowles, David Klenerman
Feb 04, 2016
Developing a Yeast Model System to Study the Human Orthologs of the Ribosome-Associated Complex
Amanda Marley
Jan 01, 0001
Prions are a class of misfolded proteins that are infectious due to their ability to self-propagate and form protein aggregates, which are associated with diseases like Mad-Cow Disease and Creutzfeldt-Jakob. Fortunately, our...
Proteins protein misfolding chaperones Prions prion suppression Neurodegenerative Diseases Biochemistry Biochemistry, Biophysics, and Structural Biology Biology Cell Biology
Published by: Ursinus College
Prions
Neurodegenerative diseases are characterized by the aggregation of misfolded proteins in the brain. Among these disorders are the prion diseases, which are transmissible, and in which the misfolded proteins ("prions") are also...
Alzheimer Disease Alzheimer's gene therapy neurodegeneration Neuroprotection Prion Unfolded Protein Response (UPR) adenine Alzheimer Disease Amyloid beta-Peptides Animals Humans Indoles Neurodegenerative Diseases Parkinson Disease Prion Diseases Prions Protein Conformation Protein Kinase Inhibitors Tauopathies Unfolded Protein Response ALPHA-SYNUCLEIN eIF-2 Kinase tau Proteins
The Role of Zuo1 Modification in Ribosome Association and Prion Formation in Saccharomyces cerevisiae
Sophia Lisowski
Jan 01, 0001
This study aims to elucidate the mechanism by which co-translational prion formation can be regulated by the association of a molecular chaperone known as the ribosome-associated complex (RAC) to the ribosome.
Prions RAC Zuo1 prion formation Yeast yeast prions Biochemistry, Biophysics, and Structural Biology Life Sciences Molecular Biology
Published by: Ursinus College
Can Saccharomyces cerevisiae Lacking Their Own Ribosome-associated Complex Chaperones Use the Human Orthologs to Suppress Prion Formation and the Toxicity of Disease-associated Proteins?
Amanda Marley
Jan 01, 0001
Proteins are complex macromolecules that carry out a variety of different functions like structural composition and regulation of cellular processes that are essential to all forms of life. In order to carry out their specific...
Proteins protein misfolding chaperones Prions polyQ toxicity prion suppression Biochemistry Biochemistry, Biophysics, and Structural Biology Life Sciences Molecular Biology
Published by: Ursinus College
Proteotoxic Stress-induced Ribosome Stalling Does Not Significantly Impact Spontaneous Prion Formation of Sup35 or Poly-glutamine in Saccharomyces cerevisiae
Steven Janik
Jan 01, 0001
Proteins are one of the four main biological macromolecules that are central to life. Proteins are involved in a multitude of functions, such as cell signaling, intracellular regulation, and biochemical catalysis. These varying...
Published by: Ursinus College
Polymorphisms at amino acid residues 141 and 154 influence conformational variation in ovine PrP.
Sujeong Yang, Alana M Thackray, Lee Hopkins, Tom P Monie, David F Burke, Raymond Bujdoso
Oct 03, 2017
TrkB signaling regulates the cold-shock protein RBM3-mediated neuroprotection.
Diego Peretti, Heather L Smith, Nicholas Verity, Ibrahim Humoud, Lis de Weerd, Dean P Swinden, Joseph Hayes, Giovanna R Mallucci
Feb 15, 2021
Increasing levels of the cold-shock protein, RNA-binding motif 3 (RBM3), either through cooling or by ectopic over-expression, prevents synapse and neuronal loss in mouse models of neurodegeneration. To exploit this process...
Investigating the Cellular Control and Biological Consequences of Prion Formation in Yeast
Richard Wike
Jan 01, 0001
Proteins are macromolecules that must fold correctly to perform their functions in cells. Cells use several quality control systems to ensure proteins fold correctly. For example, chaperones are proteins that help to prevent...
Saccharomyces cerevisiae Prions chaperone proteins competition assay [psi-] vs. [PSI+] carbon sources Biochemistry Biochemistry, Biophysics, and Structural Biology Life Sciences Molecular Biology
Published by: Ursinus College
Tau assemblies do not behave like independently acting prion-like particles in mouse neural tissue.
Lauren VC Miller, Aamir S Mukadam, Claire S Durrant, Marina J Vaysburd, Taxiarchis Katsinelos, Benjamin J Tuck, Sophie Sanford, Olivia Sheppard, Claire Knox, Shi Cheng, Leo C James, Michael P Coleman, William A McEwan
Feb 24, 2021
neurodegeneration Organotypic hippocampal slice cultures Prion-like activity Tau seeded aggregation Tauopathies Alzheimer Disease Animals Disease Models Animal HEK293 Cells Hippocampus Humans In Vitro Techniques Mice Mice Transgenic Phosphorylation Prions protein aggregation Pathological Tauopathies Tissue Culture Techniques tau Proteins
An arrayed genome-wide perturbation screen identifies the ribonucleoprotein Hnrnpk as rate-limiting for prion propagation.
Merve Avar, Daniel Heinzer, Alana M Thackray, Yingjun Liu, Marian Hruska-Plochan, Stefano Sellitto, Elke Schaper, Daniel P Pease, Jiang-An Yin, Asvin Kk Lakkaraju, Marc Emmenegger, Marco Losa, Andra Chincisan, Simone Hornemann, Magdalini Polymenidou, Raymond Bujdoso, Adriano Aguzzi
Oct 18, 2022
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