ReviewCurrent opinion in structural biology2019
Interpretation of medium resolution cryoEM maps of multi-protein complexes.
Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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.
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Who cites it
14 citing papers in PubMed.
- Quantized neural representation for lossy cryo-EM compression.Bioinformatics (Oxford, England) · 2026Article
- Automated assembly of protein complexes from cryo-EM maps with structure-informed Monte Carlo Tree Search.bioRxiv : the preprint server for biology · 2026Article
- A Novel Machine-Learning Based Method for Resolving Secondary Structure Topology in Medium-Resolution Cryo-EM Density Maps.International journal of molecular sciences · 2026Article
- Structural analysis of uridine modifications in solved RNA structures.NAR genomics and bioinformatics · 2026Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Recognizing amino acid sidechains in a medium-resolution cryo-electron density map.Protein science : a publication of the Protein Society · 2025Article
- Photo-crosslinkers boost structural information from crosslinking mass spectrometry.Current opinion in structural biology · 2025Review
- Multiscale Computational Protocols for Accurate Residue Interactions at the Flexible Insulin-Receptor Interface.Journal of chemical information and modeling · 2025Article
- Advancing structure modeling from cryo-EM maps with deep learning.Biochemical Society transactions · 2025Review
- Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases.Nature communications · 2023Article
- Refinement of AlphaFold2 Models against Experimental Cryo-EM Density Maps at 4-6Å Resolution.Proceedings. IEEE International Conference on Bioinformatics and Biomedicine · 2022Article
- Elucidation of structure-function relationships in Methanocaldococcus jannaschii RNase P, a multi-subunit catalytic ribonucleoprotein.Nucleic acids research · 2022Article
- Refinement of AlphaFold2 models against experimental and hybrid cryo-EM density maps.QRB discovery · 2022Article
- Three-Dimensional Graph Matching to Identify Secondary Structure Correspondence of Medium-Resolution Cryo-EM Density Maps.Biomolecules · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Electron cryo-microscopy (cryoEM) is used to determine structures of biological molecules, including multi-protein complexes. Maps at better than 3.0Å resolution are relatively straightforward to interpret since atomic models of proteins and nucleic acids can be built directly. Still, these resolutions are often difficult to achieve, and map quality frequently varies within a structure. This results in data that are challenging to interpret, especially when crystal structures or suitable homology models are not available. Recent advances in mass spectrometry techniques, computational methods and model building tools facilitate subunit/domain fitting into maps, elucidation of protein contacts, and de novo generation of atomic models. Here, we review techniques for map interpretation and provide examples from recent studies of multi-protein complexes.
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