Evidence map›Paper›PMID 39283059›Full record

RevieweLife2024

Exploring protein structural ensembles: Integration of sparse experimental data from electron paramagnetic resonance spectroscopy with molecular modeling methods.

Julia Belyaeva, Matthias Elgeti

Abstract readReview
In one paragraph

Review in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Elliptical β-barrel deformation underlies gating in VDAC1.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. 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

2 authors.

Julia BelyaevaInstitute for Drug Discovery, Leipzig University Medical School, Leipzig, Germany.ORCID https://orcid.org/0000-0002-6175-7942
Matthias ElgetiInstitute for Drug Discovery, Leipzig University Medical School, Leipzig, Germany.ORCID https://orcid.org/0000-0002-0550-4852

Funding

Bundesministerium für Bildung und Forschung SECAI 57616814Deutsche Forschungsgemeinschaft SFB 1423 #421152132Deutsche Forschungsgemeinschaft TRR386 #514664767
6 · The paper itself

Abstract

Under physiological conditions, proteins continuously undergo structural fluctuations on different timescales. Some conformations are only sparsely populated, but still play a key role in protein function. Thus, meaningful structure-function frameworks must include structural ensembles rather than only the most populated protein conformations. To detail protein plasticity, modern structural biology combines complementary experimental and computational approaches. In this review, we survey available computational approaches that integrate sparse experimental data from electron paramagnetic resonance spectroscopy with molecular modeling techniques to derive all-atom structural models of rare protein conformations. We also propose strategies to increase the reliability and improve efficiency using deep learning approaches, thus advancing the field of integrative structural biology.

Indexed as

Models, MolecularProtein ConformationProteinsComputational BiologyElectron Spin Resonance SpectroscopyProteinscomputational structural biologyDEEREPR spectroscopyintegrative structural biologymolecular biophysicsmolecular modelingprotein dynamicsstructural biology

Identifiers

PMID39283059
PMCPMC11405019

What OpenQuestion holds

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LicenceCC BY
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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.