ArticleProceedings of the National Academy of Sciences of the United States of America2014
Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 73 citations in OpenAlex.
- Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotype.Nature communications · 2026Article
- A self-assembled protein β-helix as a self-contained biofunctional motif.Nature communications · 2025Article
- Application of Odd-Order Derivatives in Fourier Transform Nuclear Magnetic Resonance Spectroscopy toward Quantitative Deconvolution.ACS omega · 2024Article
- Delineating the Role of GxxxG Motif in Amyloidogenesis: A New Perspective in Targeting Amyloid-Beta Mediated AD Pathogenesis.ACS bio & med chem Au · 2024Review
- Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023Review
- The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo.Biomolecules · 2023Article
- Trans-seeding of Alzheimer-related tau protein by a yeast prion.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Article
- Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022Review
- Anti-Prion Systems inViruses · 2022Review
- Review
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Article
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- Structural Arrangement within a Peptide Fibril Derived from the Glaucoma-Associated Myocilin Olfactomedin Domain.The journal of physical chemistry. B · 2021Article
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Review
- Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Tautomeric Effect of Histidine on β-Sheet Formation of Amyloid Beta 1-40: 2D-IR Simulations.Biophysical journal · 2020Article
- Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1-42).Journal of molecular biology · 2020Article
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The [PSI+] prion is a self-propagating amyloid of the translation termination factor, Sup35p, of Saccharomyces cerevisiae. The N-terminal 253 residues (NM) of this 685-residue protein normally function in regulating mRNA turnover but spontaneously form infectious amyloid in vitro. We converted the three Ile residues in Sup35NM to Leu and then replaced 16 single residues with Ile, one by one, and prepared Ile-1-(13)C amyloid of each mutant, seeding with amyloid formed by the reference sequence Sup35NM. Using solid-state NMR, we showed that 10 of the residues examined, including six between residues 30 and 90, showed the ∼0.5-nm distance between labels diagnostic of the in-register parallel amyloid architecture. The five scattered N domain residues with wider spacing may be in turns or loops; one is a control at the C terminus of M. All mutants, except Q56I, showed little or no [PSI+] transmission barrier from the reference sequence, suggesting that they could assume a similar amyloid architecture in vitro when seeded with filaments of reference sequence Sup35NM. Infection of yeast cells expressing the reference SUP35 gene sequence with amyloid of several mutants produced [PSI+] transfectants with similar efficiency as did reference sequence Sup35NM amyloid. Our work provides a stringent demonstration that the Sup35 prion domain has the folded in-register parallel β-sheet architecture and suggests common locations of the folds. This architecture naturally suggests a mechanism of inheritance of conformation, the central mystery of prions.
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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.