Evidence map›Paper›PMID 40151087›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Functional Ambidexterity of an Ancient Nucleic Acid-Binding Domain.

Orit Weil-Ktorza, Segev Naveh-Tassa, Yael Fridmann-Sirkis, Dragana Despotović, Kesava Phaneendra Cherukuri, Tatsuya Corlett, Yaakov Levy, Norman Metanis, Liam M Longo

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Chirality Makes or Breaks Chemically Driven Self-Assembly.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Functional Ambidexterity of an Ancient Nucleic Acid-Binding Domain.Angewandte Chemie (International ed. in English) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
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

9 authors.

Orit Weil-Ktorza *Institute of Chemistry, The Center for Nanoscience and Nanotechnology, Casali Center of Applied Chemistry, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Segev Naveh-Tassa *Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Yael Fridmann-Sirkis *Department of Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Dragana Despotović *Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Kesava Phaneendra CherukuriDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Tatsuya CorlettInstitute of Science Tokyo, Earth-Life Science Institute, Tokyo, 152-8550, Japan.
Yaakov LevyDepartment of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Norman MetanisInstitute of Chemistry, The Center for Nanoscience and Nanotechnology, Casali Center of Applied Chemistry, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Liam M LongoInstitute of Science Tokyo, Earth-Life Science Institute, Tokyo, 152-8550, Japan.

Funding

Israel Science Foundation 1388/22
6 · The paper itself

Abstract

The helix-hairpin-helix (HhH) motif is an ancient and ubiquitous nucleic acid-binding element that has emerged as a model system for studying the evolution of dsDNA-binding domains from simple peptides that phase separate with RNA. We analyzed the entire putative evolutionary trajectory of the HhH motif - from a flexible peptide to a folded domain - for functional robustness to total chiral inversion. Against expectations, functional "ambidexterity" was observed for both the phase separation of HhH peptides with RNA and binding of the duplicated (HhH)

Indexed as

DNANucleic AcidsRNABinding SitesMolecular Dynamics SimulationPeptidesDNANucleic AcidsPeptidesRNAChemical protein synthesisMirror‐image proteinsNucleic acid‐binding proteinsOrigin of lifeProtein evolution

Identifiers

PMID40151087
PMCPMC12171331

What OpenQuestion holds

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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.