Evidence map›Paper›PMID 29101782›Full record

ReviewCurrent opinion in structural biology2018

Frustration, function and folding.

Diego U Ferreiro, Elizabeth A Komives, Peter G Wolynes

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing 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

69 citing papers in PubMed.

  1. Article
  2. Article
  3. How to frustrate a plant pathogen.The Plant journal : for cell and molecular biology · 2026
    Review
  4. Article
  5. Probing the dark energy in the functional protein universe.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Predicting Protein Folding Dynamics Using Sequence Information.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. An AlphaFold guided model for the evolution of the CaMKII interactome.bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. Article
  19. Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025
    Review
  20. Article

9 more citing papers are in PubMed but not listed here.

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

3 authors.

Diego U FerreiroProtein Physiology Lab, FCEyN-Universidad de Buenos Aires, IQUIBICEN/CONICET, Intendente Güiraldes 2160, Ciudad Universitaria, C1428EGA Buenos Aires, Argentina.
Elizabeth A KomivesDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92092-0378, USA.
Peter G WolynesCenter for Theoretical Biological Physics, Rice University, Houston, TX, USA; Department of Chemistry, Rice University, Houston, TX, USA; Department of Physics, Rice University, Houston, TX, USA; Department of Biosciences, Rice University, Houston, TX, USA.

Funding

STRUCTURE AND STABILITY OF IKB/NF-KB COMPLEXESP01GM071862 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2006 to 2016
$14.9M
CONCEPTUAL ASPECTS OF THE PROTEIN FOLDING PROBLEMR01GM044557 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WOLYNES, PETER GUY · 1990 to 2018
$4.2M
NIGMS NIH HHS P01 GM071862NIGMS NIH HHS R01 GM044557
6 · The paper itself

Abstract

Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information.

Indexed as

Molecular Dynamics SimulationAmino AcidsAmino Acid SequenceAnimalsBiocatalysisEvolution, MolecularHumansKineticsProtein BindingProtein FoldingProteinsStructure-Activity RelationshipThermodynamicsAmino AcidsProteins

Identifiers

PMID29101782
PMCPMC6005193

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.