Evidence map›Paper›PMID 29183970›Full record

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

Patterns of coevolving amino acids unveil structural and dynamical domains.

Daniele Granata, Luca Ponzoni, Cristian Micheletti, Vincenzo Carnevale

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 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

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

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Reused Protein Segments Linked to Functional Dynamics.Molecular biology and evolution · 2024
    Article
  6. Decrypting Allostery in Membrane-Bound K-Ras4B Using ComplementaryJournal of the American Chemical Society · 2024
    Article
  7. Functional Protein Dynamics Directly from Sequences.The journal of physical chemistry. B · 2023
    Article
  8. Protein dynamics: The future is bright and complicated!Structural dynamics (Melville, N.Y.) · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Protein ensembles link genotype to phenotype.PLoS computational biology · 2019
    Review
  19. 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

4 authors.

Daniele GranataInstitute for Computational Molecular Science, College of Science and Technology, Temple University, Philadelphia, PA 19122; vincenzo.carnevale@temple.edu daniele.granata@gmail.com ponzoniluca@gmail.com michelet@sissa.it.
Luca PonzoniMolecular and Statistical Biophysics, Scuola Internazionale Superiore di Studi Avanzati (SISSA), 34136 Trieste, Italy vincenzo.carnevale@temple.edu daniele.granata@gmail.com ponzoniluca@gmail.com michelet@sissa.it.
Cristian MichelettiMolecular and Statistical Biophysics, Scuola Internazionale Superiore di Studi Avanzati (SISSA), 34136 Trieste, Italy vincenzo.carnevale@temple.edu daniele.granata@gmail.com ponzoniluca@gmail.com michelet@sissa.it.ORCID 0000-0002-1022-1638
Vincenzo CarnevaleInstitute for Computational Molecular Science, College of Science and Technology, Temple University, Philadelphia, PA 19122; vincenzo.carnevale@temple.edu daniele.granata@gmail.com ponzoniluca@gmail.com michelet@sissa.it.

Funding

X-ray and Neutron Interferometry Studies of Anesthetic Interactions with VoltageP01GM055876 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LOLL, PATRICK J · 1997 to 2017
$22.4M
Regulation of the Intestinal Ca2+ Channels TRPV6R01GM093290 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI CARNEVALE, VINCENZO, ROHACS, TIBOR · 2011 to 2025
$4.9M
Computer Cluster for Computational Biology and BiophysicsS10OD020095 · OD · TEMPLE UNIV OF THE COMMONWEALTH · PI LEVY, RONALD · 2015 to 2015
$442k
NIGMS NIH HHS P01 GM055876NIGMS NIH HHS R01 GM093290NIH HHS S10 OD020095
6 · The paper itself

Abstract

Patterns of interacting amino acids are so preserved within protein families that the sole analysis of evolutionary comutations can identify pairs of contacting residues. It is also known that evolution conserves functional dynamics, i.e., the concerted motion or displacement of large protein regions or domains. Is it, therefore, possible to use a pure sequence-based analysis to identify these dynamical domains? To address this question, we introduce here a general coevolutionary coupling analysis strategy and apply it to a curated sequence database of hundreds of protein families. For most families, the sequence-based method partitions amino acids into a few clusters. When viewed in the context of the native structure, these clusters have the signature characteristics of viable protein domains: They are spatially separated but individually compact. They have a direct functional bearing too, as shown for various reference cases. We conclude that even large-scale structural and functionally related properties can be recovered from inference methods applied to evolutionary-related sequences. The method introduced here is available as a software package and web server (spectrus.sissa.it/spectrus-evo_webserver).

Indexed as

Evolution, MolecularProtein ConformationSoftwareAmino AcidsAnimalsHumansMolecular Dynamics SimulationSequence Analysis, ProteinAmino Acidsallosteric networkscoevolutionprotein domainsspectral clusteringstructural dynamics

Identifiers

PMID29183970
PMCPMC5740617

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.