ArticleMolecules (Basel, Switzerland)2018
Analytical Approaches to Improve Accuracy in Solving the Protein Topology Problem.
Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- A Novel Machine-Learning Based Method for Resolving Secondary Structure Topology in Medium-Resolution Cryo-EM Density Maps.International journal of molecular sciences · 2026Article
- LPTD: a novel linear programming-based topology determination method for cryo-EM maps.Bioinformatics (Oxford, England) · 2022Article
- Three-Dimensional Graph Matching to Identify Secondary Structure Correspondence of Medium-Resolution Cryo-EM Density Maps.Biomolecules · 2021Article
- Combining Cryo-EM Density Map and Residue Contact for Protein Secondary Structure Topologies.Molecules (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
To take advantage of recent advances in genomics and proteomics it is critical that the three-dimensional physical structure of biological macromolecules be determined. Cryo-Electron Microscopy (cryo-EM) is a promising and improving method for obtaining this data, however resolution is often not sufficient to directly determine the atomic scale structure. Despite this, information for secondary structure locations is detectable. De novo modeling is a computational approach to modeling these macromolecular structures based on cryo-EM derived data. During de novo modeling a mapping between detected secondary structures and the underlying amino acid sequence must be identified. DP-TOSS (
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