A5085549758- Prion Diseases and Protein Misfolding
- RNA Research and Splicing
- Neurological diseases and metabolism
- Trace Elements in Health
- RNA regulation and disease
- Fungal and yeast genetics research
- Amino Acid Enzymes and Metabolism
- RNA and protein synthesis mechanisms
- Endoplasmic Reticulum Stress and Disease
- Microbial Natural Products and Biosynthesis
- Toxin Mechanisms and Immunotoxins
- CRISPR and Genetic Engineering
- Biochemical and biochemical processes
- Fungal Infections and Studies
- Neuroscience and Neuropharmacology Research
- Enzyme Structure and Function
- Amyotrophic Lateral Sclerosis Research
- Heat shock proteins research
- Insects and Parasite Interactions
- Microtubule and mitosis dynamics
- Alzheimer's disease research and treatments
- Protein Structure and Dynamics
- Nail Diseases and Treatments
- Fermentation and Sensory Analysis
- DNA Repair Mechanisms
University of Nevada, Reno
2023-2024
Columbia University
2013-2016
University of Illinois Chicago
1996-2014
Howard Hughes Medical Institute
2004-2013
New York Proton Center
2013
New York University
2004-2010
University Medical Center
2007
University of Chicago
2004
Whitehead Institute for Biomedical Research
2004
St Petersburg University
1996-2001
We have previously shown that multicopy plasmids containing the complete SUP35 gene are able to induce appearance of non-Mendelian factor [PSI]. This result was later interpreted by others as a crucial piece evidence for model postulating [PSI] is self-modified, prion-like conformational derivative Sup35 protein. Here we support this interpretation proving it overproduction protein, and not excess DNA or mRNA causes also show "prion-inducing domain" Sup35p in N-terminal region, which, like...
It has previously been shown that yeast prion [PSI+] is cured by GuHCl, although reports on reversibility of curing were contradictory. Here we show GuHCl treatment both and [psi-] strains results in two classes derivatives: Pin+, which can be reinduced Sup35p overproduction, Pin-, overexpression the complete SUP35 gene does not lead to appearance. However, Pin+ Pin- derivatives overproduction a short N-terminal fragment, thus, principle, remains reversible cases. Neither suppression nor...
Prions are infectious protein conformations that generally ordered aggregates. In the absence of prions, newly synthesized molecules these same proteins usually maintain a conventional soluble conformation. However, prions occasionally arise even without homologous prion template. The conformational switch results in de novo appearance yeast with glutamine/aspargine (Q/N)-rich domains (e.g., [ PSI + ]), is promoted by heterologous similar domain RNQ ], also known as PIN or overexpression...
Highlights•CPEB3 is a functional prion with tripartite domain architecture•CPEB3 interacts the actin cytoskeleton in yeast and at mouse synapses•Actin filaments are essential for CPEB3 prionization mRNA target•Actin constitute positive feedback loop important functionSummaryThe cytoplasmic polyadenylation element-binding protein 3 (CPEB3) translational regulator implicated long-term memory maintenance. Invertebrate orthologs of Aplysia Drosophila prions that physiologically active aggregated...
Overproduced fusions of Sup35 or its prion domain with green fluorescent protein (GFP) have previously been shown to form frequent dots in [PSI + ] cells. Rare foci seen [psi − cells were hypothesized indicate the de novo induction caused by overproduced domain. Here, we describe novel ring‐type aggregates that also appear cultures upon overproduction and show directly dot ring only become . The formation either type aggregate requires [PIN , an element needed for Although are visible...
Four mutant strains from Saccharomyces cerevisiae were used to study ribosome structure and function. They included a strain carrying deletions of the two genes encoding ribosomal protein L24, mutation spb2 in gene for L39, deletion lacking both L24 L39. The only showed just 25% normal polyphenylalanine-synthesizing activity followed by decrease P-site binding, suggesting possibility that is involved kinetics translation. Each L39 mutants displayed 4-fold increase their error frequencies...
Prions are self-propagating protein conformations usually existing as amyloid aggregates. [PIN+], a prion form of the Rnq1 frequently found in wild and laboratory yeast strains, facilitates both de novo formation destabilization other prions, affects aggregation toxicity human misfolding disease proteins expressed yeast. consists short N-terminal domain with no confirmed function (the non-prion domain, NPD) C-terminal QN-rich sufficient for [PIN+] maintenance (prion PD). The carries four...
Prions are self-propagating conformations of proteins that can cause heritable phenotypic traits. Most yeast prions contain glutamine (Q)/asparagine (N)-rich domains facilitate the accumulation protein into amyloid-like aggregates. Efficient transmission these infectious aggregates to daughter cells requires chaperones, including Hsp104 and Sis1, continually sever smaller "seeds." We previously identified 11 with Q/N-rich that, when overproduced, de novo aggregation Sup35 [PSI +] prion...
[PSI + ] , a non-Mendelian element found in some strains of Saccharomyces cerevisiae is presumed to be the manifestation self-propagating prion conformation eRF3 (Sup35p). Translation termination factor enhances activity release eRF1 (Sup45p). As predicted by model, overproduction Sup35p induces de novo appearance . However, another determinant, [PIN required for this induction. We now show that SUP45 overexpression inhibits induction strains, but has no effect on propagation or [PIN] status...
Prions are self-propagating protein conformations. Transmission of the prion state between non-identical proteins, e.g. homologous proteins from different species, is frequently inefficient. barriers attributed to sequence differences in but their underlying mechanisms not clear. Here we use a yeast Rnq1/[PIN+]-based experimental system explore nature transmission barriers. [PIN+], form Rnq1, common wild and laboratory strains, where it facilitates appearance other prions. Rnq1's domain...
Summary Background Onychomycosis affects almost 6% of the world population. Topical azoles and systemic antifungal agents are low efficacy can have undesirable side effects. An effective, non‐invasive therapy for onychomycosis is an unmet clinical need. Objective Determine threshold non‐thermal atmospheric plasma (NTAP) to treat in vitro model. Methods A novel toe/nail‐plate model using cadaver nails agarose media inoculated with Candida albicans was exposed a range NTAP doses. Results...
The laminin receptor (LamR) is a cell surface for extracellular matrix laminin, whereas the same protein within interacts with ribosomes, nuclear proteins and cytoskeletal fibers. LamR has been shown to be several bacteria viruses. Furthermore, both cellular infectious forms of prion protein, PrP(C) PrP(Sc). Indeed, PrP(C). Whether PrP(Sc) exclusively in capacity PrP receptor, or specifically recognizes determinants PrP(Sc), unclear. In order explore whether propensity interact prions...