Evidence map›Paper›PMID 37782045›Full record

ArticleJournal of the American Chemical Society2023

An Analysis of Nucleotide-Amyloid Interactions Reveals Selective Binding to Codon-Sized RNA.

Saroj K Rout, Riccardo Cadalbert, Nina Schröder, Julia Wang, Johannes Zehnder, Olivia Gampp, Thomas Wiegand, Peter Güntert, David Klingler, Christoph Kreutz and 4 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. ATP Hydrolysis by α-Synuclein Amyloids is Mediated by Enclosing β-Strand.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Saroj K RoutInstitute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
Riccardo CadalbertInstitute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
Nina SchröderInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.
Julia WangInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.
Johannes ZehnderInstitute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
Olivia GamppInstitute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
Thomas WiegandInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.
Peter GüntertInstitute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
David KlinglerInstitute of Organic Chemistry and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, 6020 Innsbruck, Austria.ORCID 0000-0003-4056-6810
Christoph KreutzInstitute of Organic Chemistry and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, 6020 Innsbruck, Austria.ORCID 0000-0002-7018-9326
Anna KnörleinInstitute of Pharmaceutical Sciences, ETH Zürich, 8093 Zürich, Switzerland.
Jonathan HallInstitute of Pharmaceutical Sciences, ETH Zürich, 8093 Zürich, Switzerland.ORCID 0000-0003-4160-7135
Jason GreenwaldInstitute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
Roland RiekInstitute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.ORCID 0000-0002-6333-066X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interactions between RNA and proteins are the cornerstone of many important biological processes from transcription and translation to gene regulation, yet little is known about the ancient origin of said interactions. We hypothesized that peptide amyloids played a role in the origin of life and that their repetitive structure lends itself to building interfaces with other polymers through avidity. Here, we report that short RNA with a minimum length of three nucleotides binds in a sequence-dependent manner to peptide amyloids. The 3'-5' linked RNA backbone appears to be well-suited to support these interactions, with the phosphodiester backbone and nucleobases both contributing to the affinity. Sequence-specific RNA-peptide interactions of the kind identified here may provide a path to understanding one of the great mysteries rooted in the origin of life: the origin of the genetic code.

Indexed as

NucleotidesRNAAmyloidAmyloidogenic ProteinsCodonPeptidesAmyloidAmyloidogenic ProteinsCodonNucleotidesPeptidesRNA

Identifiers

PMID37782045
PMCPMC10571083

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.