ArticleCurrent opinion in systems biology2018
Organizing biochemistry in space and time using prion-like self-assembly.
Article in Current opinion in systems biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Measuring prion propagation in single bacteria elucidates a mechanism of loss.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- N-terminal region of Drosophila melanogaster Argonaute2 forms amyloid-like aggregates.BMC biology · 2023Article
- Measuring prion propagation in single bacteria elucidates mechanism of loss.bioRxiv : the preprint server for biology · 2023Article
- FUS and TDP-43 Phases in Health and Disease.Trends in biochemical sciences · 2021Review
- The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements.Molecular biology and evolution · 2021Article
- Protein assembly systems in natural and synthetic biology.BMC biology · 2020Review
- Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma.The Journal of biological chemistry · 2019Article
- Molecular Origins of Complex Heritability in Natural Genotype-to-Phenotype Relationships.Cell systems · 2019Article
- Review
- It Pays To Be in Phase.Biochemistry · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Prion-like proteins have the capacity to adopt multiple stable conformations, at least one of which can recruit proteins from the native conformation into the alternative fold. Although classically associated with disease, prion-like assembly has recently been proposed to organize a range of normal biochemical processes in space and time. Organisms from bacteria to mammals use prion-like mechanisms to (re)organize their proteome in response to intracellular and extracellular stimuli. Prion-like behavior is an economical means to control biochemistry and gene regulation at the systems level, and prions can act as protein-based genes to facilitate quasi-Lamarckian inheritance of induced traits. These mechanisms allow individual cells to express distinct heritable traits using the same complement of polypeptides. Understanding and controlling prion-like behavior is therefore a promising strategy to combat diverse pathologies and organize engineered biological systems.
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.