ArticleJournal of biomolecular NMR2000
Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations.
Article in Journal of biomolecular NMR, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Article
- Automation of peak-tracking analysis of stepwise perturbed NMR spectra.Journal of biomolecular NMR · 2017Article
- An NMR-Guided Screening Method for Selective Fragment Docking and Synthesis of a Warhead Inhibitor.Molecules (Basel, Switzerland) · 2016Article
- Protein-ligand structure guided by backbone and side-chain proton chemical shift perturbations.Journal of biomolecular NMR · 2014Article
- Comparing binding modes of analogous fragments using NMR in fragment-based drug design: application to PRDX5.PloS one · 2014Article
- Article
- Application of NMR and molecular docking in structure-based drug discovery.Topics in current chemistry · 2012Review
- Article
- Automated evaluation of chemical shift perturbation spectra: New approaches to quantitative analysis of receptor-ligand interaction NMR spectra.Journal of biomolecular NMR · 2004Article
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
No grant is acknowledged in the PubMed record.
Abstract
Structural studies of protein-ligand complexes are often limited by low solubility, poor affinity, and interfacial motion and, in NMR structures, by the lack of intermolecular NOEs. In the absence of other structural restraints, we use a procedure that compares simulated chemical shift perturbations to observed perturbations to better define the binding orientation of ligands with respect to protein surfaces.
Indexed as
Identifiers
11142509What OpenQuestion holds
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.