ArticleCurrent genetics2018
Screening for amyloid proteins in the yeast proteome.
Article in Current genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Pathological and Functional Brain Amyloids: A New Concept Explaining the Differences.International journal of molecular sciences · 2025Review
- Amyloid fibrils of the myelin basic protein are an integral component of myelin in the vertebrate brain.Scientific reports · 2025Article
- Leveraging structure-informed machine learning for fast steric zipper propensity prediction across whole proteomes.PLoS computational biology · 2025Article
- Amyloid Fibrils of the s36 Protein Modulate the Morphogenesis ofInternational journal of molecular sciences · 2024Article
- GPI-anchored Gas1 protein regulates cytosolic proteostasis in budding yeast.G3 (Bethesda, Md.) · 2024Article
- Sodium Dodecyl Sulfate Analogs as a Potential Molecular Biology Reagent.Current issues in molecular biology · 2024Review
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Search and Identification of Amyloid Proteins.Methods and protocols · 2023Article
- A New Function for Amyloid-Like Interactions: Cross-Beta Aggregates of Adhesins form Cell-to-Cell Bonds.Pathogens (Basel, Switzerland) · 2021Review
- Functional amyloids of eukaryotes: criteria, classification, and biological significance.Current genetics · 2020Review
- Functional Mammalian Amyloids and Amyloid-Like Proteins.Life (Basel, Switzerland) · 2020Review
- Accumulation of storage proteins in plant seeds is mediated by amyloid formation.PLoS biology · 2020Article
- Amyloidogenic Peptides in Human Neuro-Degenerative Diseases and in Microorganisms: A Sorrow Shared Is a Sorrow Halved?Molecules (Basel, Switzerland) · 2020Review
- RNA-binding protein FXR1 is presented in rat brain in amyloid form.Scientific reports · 2019Article
- Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule BacteriumBiomolecules · 2019Article
- More than just a phase: the search for membraneless organelles in the bacterial cytoplasm.Current genetics · 2019Review
- Aggregation and degradation scales for prion-like domains: sequence features and context weigh in.Current genetics · 2019Review
- Article
- A reversible liquid drop aggregation controls glucose response in yeast.Current genetics · 2018Review
- Overproduction of Sch9 leads to its aggregation and cell elongation in Saccharomyces cerevisiae.PloS one · 2018Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative disorders such as Alzheimer's, Parkinson's Huntington's diseases. At the same time, a set of amyloids regulates vital processes in archaea, prokaryotes and eukaryotes. Our knowledge of the prevalence and biological significance of amyloids is limited due to the lack of universal methods for their identification. Here, using our original method of proteomic screening PSIA-LC-MALDI, we identified a number of proteins that form amyloid-like detergent-resistant aggregates in Saccharomyces cerevisiae. We revealed in yeast strains of different origin known yeast prions, prion-associated proteins, and a set of proteins whose amyloid properties were not shown before. A substantial number of the identified proteins are cell wall components, suggesting that amyloids may play important roles in the formation of this extracellular protective sheath. Two proteins identified in our screen, Gas1 and Ygp1, involved in biogenesis of the yeast cell wall, were selected for detailed analysis of amyloid properties. We show that Gas1 and Ygp1 demonstrate amyloid properties both in vivo in yeast cells and using the bacteria-based system C-DAG. Taken together, our data show that this proteomic approach is very useful for identification of novel amyloids.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.