Evidence map›Paper›PMID 41771853›Full record

ArticleNature communications2026

Efficient sampling of large-scale transition pathways and intermediate conformations in sub-mesoscopic protein complexes.

Domenico Scaramozzino, Byung Ho Lee, Laura Orellana

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

3 authors.

Domenico ScaramozzinoProtein Dynamics and Mutation Lab, Department of Oncology-Pathology, Karolinska Institutet, Solna, Sweden.ORCID 0000-0002-6235-8070
Byung Ho LeeProtein Dynamics and Mutation Lab, Department of Oncology-Pathology, Karolinska Institutet, Solna, Sweden.ORCID 0000-0001-6515-7656
Laura OrellanaProtein Dynamics and Mutation Lab, Department of Oncology-Pathology, Karolinska Institutet, Solna, Sweden. laura.orellana@ki.se.ORCID 0000-0003-1927-555X

Funding

Cancerfonden (Swedish Cancer Society) 24 0908 PTCancerfonden (Swedish Cancer Society) CF 21 1471 PjCancerfonden (Swedish Cancer Society) CF 24 3801 PjVetenskapsrådet (Swedish Research Council) VR 2021-02248
6 · The paper itself

Abstract

Protein conformational changes are the cornerstone of biological function. While conformers captured experimentally represent metastable states, the pathways connecting them have been elusive for experiments and simulations alike. Nowadays, cryogenic Electron Microscopy is providing rich structural data on proteins trapped in different states for increasingly large systems, but these are out of scope for most computational methods which exhibit an N

Indexed as

Molecular Dynamics SimulationMultiprotein ComplexesAlgorithmsCryoelectron MicroscopyProtein ConformationMultiprotein Complexes

Identifiers

PMID41771853
PMCPMC12960823

What OpenQuestion holds

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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.