Evidence map›Paper›PMID 26806127›Full record

ArticleCell2016

De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.

Robert G Smock, Itamar Yadid, Orly Dym, Jane Clarke, Dan S Tawfik

Abstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
–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

51 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. ASR gene family: a case of tandem-drive evolution.Frontiers in molecular biosciences · 2025
    Article
  6. A Macrocycle-Mediated Protein Cage.ACS macro letters · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. An evolutionary history of the CoA-binding protein Nat/Ivy.Protein science : a publication of the Protein Society · 2022
    Review
  15. Article
  16. Similar protein segments shared between domains of different evolutionary lineages.Protein science : a publication of the Protein Society · 2022
    Article
  17. Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains.Journal of the American Chemical Society · 2022
    Article
  18. What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022
    Review
  19. Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Robert G SmockDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Itamar YadidMetabolic Pathways and Enzyme Evolution Laboratory, Migal Galilee Research Institute, Kiryat Shmona 11016, Israel.
Orly DymDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Jane ClarkeDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Dan S TawfikDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: dan.tawfik@weizmann.ac.il.

Funding

Medical Research Council MC_U105485808Wellcome TrustWellcome Trust WT 095195
6 · The paper itself

Abstract

Molecular evolution has focused on the divergence of molecular functions, yet we know little about how structurally distinct protein folds emerge de novo. We characterized the evolutionary trajectories and selection forces underlying emergence of β-propeller proteins, a globular and symmetric fold group with diverse functions. The identification of short propeller-like motifs (<50 amino acids) in natural genomes indicated that they expanded via tandem duplications to form extant propellers. We phylogenetically reconstructed 47-residue ancestral motifs that form five-bladed lectin propellers via oligomeric assembly. We demonstrate a functional trajectory of tandem duplications of these motifs leading to monomeric lectins. Foldability, i.e., higher efficiency of folding, was the main parameter leading to improved functionality along the entire evolutionary trajectory. However, folding constraints changed along the trajectory: initially, conflicts between monomer folding and oligomer assembly dominated, whereas subsequently, upon tandem duplication, tradeoffs between monomer stability and foldability took precedence.

Indexed as

Horseshoe CrabsProtein FoldingAmino Acid MotifsAmino Acid SequenceAnimalsArthropod ProteinsEvolution, MolecularGene DuplicationLectinsModels, MolecularMolecular Sequence DataPhylogenySea AnemonesSequence AlignmentArthropod ProteinsLectins

Identifiers

PMID26806127
PMCPMC4735018

What OpenQuestion holds

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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.