ArticleProteins2021
Cryo-EM targets in CASP14.
Article in Proteins, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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.
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Who cites it
10 citing papers in PubMed.
- Cryo-EM Analysis in CASP16.Proteins · 2026Article
- Breaking the conformational ensemble barrier: Ensemble structure modeling challenges in CASP15.Proteins · 2023Article
- CASP15 cryo-EM protein and RNA targets: Refinement and analysis using experimental maps.Proteins · 2023Article
- Article
- Artificial intelligence and the analysis of cryo-EM data provide structural insight into the molecular mechanisms underlying LN-lamininopathies.Scientific reports · 2023Article
- RIBFIND2: Identifying rigid bodies in protein and nucleic acid structures.Nucleic acids research · 2023Article
- Assessment of three-dimensional RNA structure prediction in CASP15.bioRxiv : the preprint server for biology · 2023Article
- Improved AlphaFold modeling with implicit experimental information.Nature methods · 2022Article
- Article
- Cryo-EM targets in CASP14.Proteins · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Structures of seven CASP14 targets were determined using cryo-electron microscopy (cryo-EM) technique with resolution between 2.1 and 3.8 Å. We provide an evaluation of the submitted models versus the experimental data (cryo-EM density maps) and experimental reference structures built into the maps. The accuracy of models is measured in terms of coordinate-to-density and coordinate-to-coordinate fit. A-posteriori refinement of the most accurate models in their corresponding cryo-EM density resulted in structures that are close to the reference structure, including some regions with better fit to the density. Regions that were found to be less "refineable" correlate well with regions of high diversity between the CASP models and low goodness-of-fit to density in the reference structure.
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What OpenQuestion holds
Registered trials
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.