Evidence map›Paper›PMID 35173330›Full record

ArticleNature2022

Visualizing protein breathing motions associated with aromatic ring flipping.

Laura Mariño Pérez, Francesco S Ielasi, Luiza M Bessa, Damien Maurin, Jaka Kragelj, Martin Blackledge, Nicola Salvi, Guillaume Bouvignies, Andrés Palencia, Malene Ringkjøbing Jensen

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
  4. Article
  5. Protein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Visualizing agonist-induced M2 receptor activation regulated by aromatic ring dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Conserved proline residues prevent dimerization and aggregation in the β-lactamase BlaC.Protein science : a publication of the Protein Society · 2024
    Article
  20. 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

10 authors at 1 institution in 3 countries.

Laura Mariño PérezUniversité Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.ORCID http://orcid.org/0000-0003-1658-7179
Francesco S IelasiInstitute for Advanced Biosciences (IAB), Structural Biology of Novel Targets in Human Diseases, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France.ORCID http://orcid.org/0000-0002-5272-0865
Luiza M BessaUniversité Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.ORCID http://orcid.org/0000-0002-1993-3105
Damien MaurinUniversité Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
Jaka KrageljUniversité Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
Martin BlackledgeUniversité Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.ORCID http://orcid.org/0000-0003-0935-721X
Nicola SalviUniversité Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.ORCID http://orcid.org/0000-0003-1515-6908
Guillaume BouvigniesLaboratoire des Biomolécules (LBM), Département de Chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, Paris, France.ORCID http://orcid.org/0000-0003-4398-0320
Andrés PalenciaInstitute for Advanced Biosciences (IAB), Structural Biology of Novel Targets in Human Diseases, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France. andres.palencia@inserm.fr.ORCID http://orcid.org/0000-0002-1805-319X
Malene Ringkjøbing JensenUniversité Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France. malene.ringkjobing-jensen@ibs.fr.ORCID http://orcid.org/0000-0003-0419-2196
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aromatic residues cluster in the core of folded proteins, where they stabilize the structure through multiple interactions. Nuclear magnetic resonance (NMR) studies in the 1970s showed that aromatic side chains can undergo ring flips-that is, 180° rotations-despite their role in maintaining the protein fold

Indexed as

ProteinsTyrosineCrystallography, X-RayMotionNuclear Magnetic Resonance, BiomolecularProtein Conformationsrc Homology DomainsProteinsTyrosine

Identifiers

PMID35173330
PMCPMC8866124
OpenAlexW4213377669

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.