ArticleMolecular and cellular biology2004
Scrambled prion domains form prions and amyloid.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
103 citing papers in PubMed.
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins.International journal of molecular sciences · 2025Article
- Prion-like Proteins in Plants: Key Regulators of Development and Environmental Adaptation via Phase Separation.Plants (Basel, Switzerland) · 2024Review
- Phase separation is regulated by post-translational modifications and participates in the developments of human diseases.Heliyon · 2024Review
- Reviewing the Structure-Function Paradigm in Polyglutamine Disorders: A Synergistic Perspective on Theoretical and Experimental Approaches.International journal of molecular sciences · 2024Review
- The origin recognition complex requires chromatin tethering by a hypervariable intrinsically disordered region that is functionally conserved from sponge to man.Nucleic acids research · 2024Article
- Protein intrinsically disordered regions have a non-random, modular architecture.Bioinformatics (Oxford, England) · 2023Article
- In planta expression of human polyQ-expanded huntingtin fragment reveals mechanisms to prevent disease-related protein aggregation.Nature aging · 2023Article
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
- Article
- Electrostatics tunes protein interactions to context.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Evolution of sequence traits of prion-like proteins linked to amyotrophic lateral sclerosis (ALS).PeerJ · 2022Article
- From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.International journal of molecular sciences · 2021Review
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Spin Label Scanning Reveals Likely Locations of β-Strands in the Amyloid Fibrils of the Ure2 Prion Domain.ACS omega · 2020Article
- Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes.BMC genomics · 2020Article
- Article
- Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior.The Journal of biological chemistry · 2019Review
- Aggregation and degradation scales for prion-like domains: sequence features and context weigh in.Current genetics · 2019Review
43 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The [URE3] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Ure2p. The amino-terminal prion domain of Ure2p is necessary and sufficient for prion formation and has a high glutamine (Q) and asparagine (N) content. Such Q/N-rich domains are found in two other yeast prion proteins, Sup35p and Rnq1p, although none of the many other yeast Q/N-rich domain proteins have yet been found to be prions. To examine the role of amino acid sequence composition in prion formation, we used Ure2p as a model system and generated five Ure2p variants in which the order of the amino acids in the prion domain was randomly shuffled while keeping the amino acid composition and C-terminal domain unchanged. Surprisingly, all five formed prions in vivo, with a range of frequencies and stabilities, and the prion domains of all five readily formed amyloid fibers in vitro. Although it is unclear whether other amyloid-forming proteins would be equally resistant to scrambling, this result demonstrates that [URE3] formation is driven primarily by amino acid composition, largely independent of primary sequence.
Indexed as
Identifiers
What OpenQuestion holds
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.