ArticleBioinformatics (Oxford, England)2012
CheShift-2: graphic validation of protein structures.
Article in Bioinformatics (Oxford, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- PyVibMS: a PyMOL plugin for visualizing vibrations in molecules and solids.Journal of molecular modeling · 2020Article
- Assessing the One-Bond CThe journal of physical chemistry. B · 2020Article
- My 65 years in protein chemistry.Quarterly reviews of biophysics · 2015Review
- Factors affecting the computation of the 13C shielding in disaccharides.Journal of computational chemistry · 2014Article
- Accounting for a mirror-image conformation as a subtle effect in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Physics-based method to validate and repair flaws in protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Quality assessment of protein NMR structures.Current opinion in structural biology · 2013Review
- CheShift-2 resolves a local inconsistency between two X-ray crystal structures.Journal of biomolecular NMR · 2012Article
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
unlabelledThe differences between observed and predicted (13)C(α) chemical shifts can be used as a sensitive probe with which to detect possible local flaws in protein structures. For this reason, we previously introduced CheShift, a Web server for protein structure validation. Now, we present CheShift-2 in which a graphical user interface is implemented to render such local flaws easily visible. A series of applications to 15 ensembles of conformations illustrate the ability of CheShift-2 to locate the main structural flaws rapidly and accurately on a per-residue basis. Since accuracy plays a central role in CheShift predictions, the treatment of histidine (His) is investigated here by exploring which form of His should be used in CheShift-2. AVAILABILITY: CheShift-2 is free of charge for academic use and can be accessed from www.cheshift.com
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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.