ArticleeLife2016
Origin of a folded repeat protein from an intrinsically disordered ancestor.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 52 citations in OpenAlex.
- 14-3-3θ phosphorylation at S232 reduces its interactome and regulates axonal trafficking.Disease models & mechanisms · 2025Article
- Deciphering opening mechanisms of 14-3-3 proteins.Protein science : a publication of the Protein Society · 2025Article
- Wnt/β-catenin Pathway Aggravates Renal Fibrosis by Activating PUM2 Transcription to Repress YME1L-mediated Mitochondrial Homeostasis.Biochemical genetics · 2025Article
- Tandem Repeats Provide Evidence for Convergent Evolution to Similar Protein Structures.Genome biology and evolution · 2025Article
- 14-3-3 proteins-a moonlight protein complex with therapeutic potential in neurological disorder: in-depth review with Alzheimer's disease.Frontiers in molecular biosciences · 2024Review
- Editorial: From the hydrophobic core to the globular-disorder interface: New challenges and insights into protein design.Frontiers in molecular biosciences · 2023Article
- Creative destruction: New protein folds from old.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Short Tale of the Origin of Proteins and Ribosome Evolution.Microorganisms · 2022Review
- The return of the rings: Evolutionary convergence of aromatic residues in the intrinsically disordered regions of RNA-binding proteins for liquid-liquid phase separation.Protein science : a publication of the Protein Society · 2022Article
- Structural insights into the functional roles of 14-3-3 proteins.Frontiers in molecular biosciences · 2022Review
- New β-Propellers Are Continuously Amplified From Single Blades in all Major Lineages of the β-Propeller Superfamily.Frontiers in molecular biosciences · 2022Article
- 14-3-3 Proteins: Novel Pharmacological Targets in Neurodegenerative Diseases.Trends in pharmacological sciences · 2021Review
- The Effect of Mutations in the TPR and Ankyrin Families of Alpha Solenoid Repeat Proteins.Frontiers in bioinformatics · 2021Review
- On the emergence of P-Loop NTPase and Rossmann enzymes from a Beta-Alpha-Beta ancestral fragment.eLife · 2020Article
- The evolution of the huntingtin-associated protein 40 (HAP40) in conjunction with huntingtin.BMC evolutionary biology · 2020Article
- Identification and Analysis of Natural Building Blocks for Evolution-Guided Fragment-Based Protein Design.Journal of molecular biology · 2020Article
- Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control.International journal of molecular sciences · 2020Review
- Structural basis for the dimerization of Gemin5 and its role in protein recruitment and translation control.Nucleic acids research · 2020Article
- Disease related single point mutations alter the global dynamics of a tetratricopeptide (TPR) α-solenoid domain.Journal of structural biology · 2020Article
- Structural diversity of oligomeric β-propellers with different numbers of identical blades.eLife · 2019Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Repetitive proteins are thought to have arisen through the amplification of subdomain-sized peptides. Many of these originated in a non-repetitive context as cofactors of RNA-based replication and catalysis, and required the RNA to assume their active conformation. In search of the origins of one of the most widespread repeat protein families, the tetratricopeptide repeat (TPR), we identified several potential homologs of its repeated helical hairpin in non-repetitive proteins, including the putatively ancient ribosomal protein S20 (RPS20), which only becomes structured in the context of the ribosome. We evaluated the ability of the RPS20 hairpin to form a TPR fold by amplification and obtained structures identical to natural TPRs for variants with 2-5 point mutations per repeat. The mutations were neutral in the parent organism, suggesting that they could have been sampled in the course of evolution. TPRs could thus have plausibly arisen by amplification from an ancestral helical hairpin.
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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.