Evidence map›Paper›PMID 35034173›Full record

ArticleCellular and molecular life sciences : CMLS2022

Ins and outs of AlphaFold2 transmembrane protein structure predictions.

Tamás Hegedűs, Markus Geisler, Gergely László Lukács, Bianka Farkas

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing 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

67 citing papers in PubMed.

  1. Article
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  9. Exploring the Blueprint of Life: The Innovation in Antibody and Protein Design.Combinatorial chemistry & high throughput screening · 2026
    Article
  10. Review
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  12. A tripartite protein complex promotes DNA transport during natural transformation in Firmicutes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Article
  15. Article
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  18. TBM preferred to AlphaFold 3 for functional models of insect odorant receptors.Computational and structural biotechnology journal · 2025
    Article
  19. Article
  20. Article

7 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

4 authors.

Tamás HegedűsDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary. hegedus@hegelab.org.ORCID http://orcid.org/0000-0002-5195-749X
Markus GeislerDepartment of Biology, University of Fribourg, Fribourg, Switzerland.ORCID http://orcid.org/0000-0002-6641-5810
Gergely László LukácsDepartment of Physiology and Biochemistry, McGill University, Montreal, QC, Canada.ORCID http://orcid.org/0000-0003-0900-0675
Bianka FarkasDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.ORCID http://orcid.org/0000-0002-0258-6864

Funding

Cystic Fibrosis Canada LUKACS20G0Cystic Fibrosis Foundation HEGEDU20I0Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K127961Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 310030_197563
6 · The paper itself

Abstract

Transmembrane (TM) proteins are major drug targets, but their structure determination, a prerequisite for rational drug design, remains challenging. Recently, the DeepMind's AlphaFold2 machine learning method greatly expanded the structural coverage of sequences with high accuracy. Since the employed algorithm did not take specific properties of TM proteins into account, the reliability of the generated TM structures should be assessed. Therefore, we quantitatively investigated the quality of structures at genome scales, at the level of ABC protein superfamily folds and for specific membrane proteins (e.g. dimer modeling and stability in molecular dynamics simulations). We tested template-free structure prediction with a challenging TM CASP14 target and several TM protein structures published after AlphaFold2 training. Our results suggest that AlphaFold2 performs well in the case of TM proteins and its neural network is not overfitted. We conclude that cautious applications of AlphaFold2 structural models will advance TM protein-associated studies at an unexpected level.

Indexed as

Protein ConformationProtein FoldingAlgorithmsComputational BiologyComputer SimulationGenomeHumansLipidsMachine LearningMembrane ProteinsMolecular Dynamics SimulationProtein DomainsProtein Structure, SecondaryProteomeProteomicsReproducibility of ResultsLipidsMembrane ProteinsProteomeAlphaFold2BioinformaticsStructure predictionTransmembrane proteins

Identifiers

PMID35034173
PMCPMC8761152

What OpenQuestion holds

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Registered trials

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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.