ReviewJournal of biomolecular NMR2014
An overview of tools for the validation of protein NMR structures.
Review in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 36 citations in OpenAlex.
- Restraint validation of biomolecular structures determined by NMR in the Protein Data Bank.Structure (London, England : 1993) · 2024Article
- Methods for Structure Determination of SH2 Domain-Phosphopeptide Complexes by NMR.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Core packing of well-defined X-ray and NMR structures is the same.Protein science : a publication of the Protein Society · 2022Article
- Review
- A method for validating the accuracy of NMR protein structures.Nature communications · 2020Article
- Molecular Mechanism by which Cobra Venom Cardiotoxins Interact with the Outer Mitochondrial Membrane.Toxins · 2020Article
- Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans.PloS one · 2017Article
- Resolution ofIUCrJ · 2016Article
- A protocol for the refinement of NMR structures using simultaneously pseudocontact shift restraints from multiple lanthanide ions.Journal of biomolecular NMR · 2016Article
- Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.Protein science : a publication of the Protein Society · 2016Article
- Computational approaches for inferring the functions of intrinsically disordered proteins.Frontiers in molecular biosciences · 2015Review
- Molecular-docking study of malaria drug target enzyme transketolase in Plasmodium falciparum 3D7 portends the novel approach to its treatment.Source code for biology and medicine · 2015Article
- Structure calculation, refinement and validation using CcpNmr Analysis.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Quality assessment of protein NMR structures.Current opinion in structural biology · 2013Review
- Recommendations of the wwPDB NMR Validation Task Force.Structure (London, England : 1993) · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 5 institutions in 2 countries.
Funding
Abstract
Biomolecular structures at atomic resolution present a valuable resource for the understanding of biology. NMR spectroscopy accounts for 11% of all structures in the PDB repository. In response to serious problems with the accuracy of some of the NMR-derived structures and in order to facilitate proper analysis of the experimental models, a number of program suites are available. We discuss nine of these tools in this review: PROCHECK-NMR, PSVS, GLM-RMSD, CING, Molprobity, Vivaldi, ResProx, NMR constraints analyzer and QMEAN. We evaluate these programs for their ability to assess the structural quality, restraints and their violations, chemical shifts, peaks and the handling of multi-model NMR ensembles. We document both the input required by the programs and output they generate. To discuss their relative merits we have applied the tools to two representative examples from the PDB: a small, globular monomeric protein (Staphylococcal nuclease from S. aureus, PDB entry 2kq3) and a small, symmetric homodimeric protein (a region of human myosin-X, PDB entry 2lw9).
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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.