Evidence map›Paper›PMID 28536196›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Physicochemical code for quinary protein interactions in

Xin Mu, Seongil Choi, Lisa Lang, David Mowray, Nikolay V Dokholyan, Jens Danielsson, Mikael Oliveberg

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed.

  1. Review
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  6. Language models reveal a complex sequence basis for adaptive convergent evolution of protein functions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
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  18. How it feels in a cell.Trends in cell biology · 2023
    Review
  19. Review
  20. Article

1 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

7 authors.

Xin MuDepartment of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden.
Seongil ChoiDepartment of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden.
Lisa LangDepartment of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden.
David MowrayDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599.
Nikolay V DokholyanDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599.ORCID 0000-0002-8225-4025
Jens DanielssonDepartment of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden; mikael@dbb.su.se jens.danielsson@dbb.su.se.
Mikael OlivebergDepartment of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden; mikael@dbb.su.se jens.danielsson@dbb.su.se.

Funding

Protein Misfolding and AggregationR01GM080742 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOKHOLYAN, NIKOLAY · 2007 to 2015
$2.8M
NIGMS NIH HHS R01 GM080742
6 · The paper itself

Abstract

How proteins sense and navigate the cellular interior to find their functional partners remains poorly understood. An intriguing aspect of this search is that it relies on diffusive encounters with the crowded cellular background, made up of protein surfaces that are largely nonconserved. The question is then if/how this protein search is amenable to selection and biological control. To shed light on this issue, we examined the motions of three evolutionary divergent proteins in the

Indexed as

Amino Acid SubstitutionBiophysical PhenomenaCopper Transport ProteinsEscherichia coliEscherichia coli ProteinsHumansHydrophobic and Hydrophilic InteractionsMetallochaperonesModels, MolecularMolecular ChaperonesMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularProtein Interaction Domains and MotifsProtein TransportRecombinant ProteinsStatic ElectricityATOX1 protein, humanCopper Transport ProteinsEscherichia coli ProteinsMetallochaperonesMolecular ChaperonesRecombinant ProteinsSOD1 protein, humanSuperoxide Dismutase-1in-cell NMRintracellular diffusionprotein surface properties

Identifiers

PMID28536196
PMCPMC5468600

What OpenQuestion holds

Textmetadata
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.