ReviewCurrent opinion in structural biology2019
Principles and characteristics of biological assemblies in experimentally determined protein structures.
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 11 papers.
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.
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.
Who cites it
11 citing papers in PubMed.
- Comparative evaluation of methods for the prediction of protein-ligand binding sites.Journal of cheminformatics · 2024Article
- PPI3D: a web server for searching, analyzing and modeling protein-protein, protein-peptide and protein-nucleic acid interactions.Nucleic acids research · 2024Article
- X-Ray Crystallography for Macromolecular Complexes.Advances in experimental medicine and biology · 2024Article
- Structural Outlier Detection and Zernike-Canterakis Moments for Molecular Surface Meshes-Fast Implementation in Python.Molecules (Basel, Switzerland) · 2023Article
- Improved Assessment of Globularity of Protein Structures and the Ellipsoid Profile of the Biological Assemblies from the PDB.Biomolecules · 2023Article
- Exploring protein symmetry at the RCSB Protein Data Bank.Emerging topics in life sciences · 2022Article
- PDB-wide identification of physiological hetero-oligomeric assemblies based on conserved quaternary structure geometry.Structure (London, England : 1993) · 2021Article
- QSalignWeb: A Server to Predict and Analyze Protein Quaternary Structure.Frontiers in molecular biosciences · 2021Review
- Challenges in protein docking.Current opinion in structural biology · 2020Review
- ProtCID: a data resource for structural information on protein interactions.Nature communications · 2020Article
- Assessment of protein assembly prediction in CASP13.Proteins · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
More than half of all structures in the PDB are assemblies of two or more proteins, including both homooligomers and heterooligomers. Structural information on these assemblies comes from X-ray crystallography, NMR, and cryo-EM spectroscopy. The correct assembly in an X-ray structure is often ambiguous, and computational methods have been developed to identify the most likely biologically relevant assembly based on physical properties of assemblies and sequence conservation in interfaces. Taking advantage of the large number of structures now available, some of the most recent methods have relied on similarity of interfaces and assemblies across structures of homologous proteins.
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Registered trials
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