Evidence map›Paper›PMID 32079721›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

On the evolution of protein-adenine binding.

Aya Narunsky, Amit Kessel, Ron Solan, Vikram Alva, Rachel Kolodny, Nir Ben-Tal

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
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

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  7. From Catalysis of Evolution to Evolution of Catalysis.Accounts of chemical research · 2024
    Article
  8. Reused Protein Segments Linked to Functional Dynamics.Molecular biology and evolution · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Article
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  15. De novo proteins from random sequences through in vitro evolution.Current opinion in structural biology · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Fuzzle 2.0: Ligand Binding in Natural Protein Building Blocks.Frontiers in molecular biosciences · 2021
    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

6 authors at 3 institutions in 2 countries.

Aya NarunskyDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Ramat Aviv, Israel.ORCID 0000-0002-6830-5690
Amit KesselDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Ramat Aviv, Israel.ORCID 0000-0003-0227-0226
Ron SolanDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Ramat Aviv, Israel.
Vikram AlvaDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.ORCID 0000-0003-1188-473X
Rachel KolodnyDepartment of Computer Science, University of Haifa, Mount Carmel, 3498838 Haifa, Israel trachel@cs.haifa.ac.il bental@tauex.tau.ac.il.ORCID 0000-0001-8523-1614
Nir Ben-TalDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Ramat Aviv, Israel; trachel@cs.haifa.ac.il bental@tauex.tau.ac.il.ORCID 0000-0001-6901-832X
Tel Aviv University · ILCarmel (Israel) · ILMax Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins' interactions with ancient ligands may reveal how molecular recognition emerged and evolved. We explore how proteins recognize adenine: a planar rigid fragment found in the most common and ancient ligands. We have developed a computational pipeline that extracts protein-adenine complexes from the Protein Data Bank, structurally superimposes their adenine fragments, and detects the hydrogen bonds mediating the interaction. Our analysis extends the known motifs of protein-adenine interactions in the Watson-Crick edge of adenine and shows that all of adenine's edges may contribute to molecular recognition. We further show that, on the proteins' side, binding is often mediated by specific amino acid segments ("themes") that recur across different proteins, such that different proteins use the same themes when binding the same adenine-containing ligands. We identify numerous proteins that feature these themes and are thus likely to bind adenine-containing ligands. Our analysis suggests that adenine binding has emerged multiple times in evolution.

Indexed as

Evolution, MolecularProtein ConformationAdenineBinding SitesHydrogen BondingMolecular Docking SimulationProtein BindingSequence Analysis, ProteinSoftwareAdeninecomputational biologyligand bindingmolecular evolutionmolecular recognitionstructural biology

Identifiers

PMID32079721
PMCPMC7060716
OpenAlexW3008861742

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.