Evidence map›Paper›PMID 26965640›Full record

ArticleJournal of proteome research2016

NMRmix: A Tool for the Optimization of Compound Mixtures in 1D (1)H NMR Ligand Affinity Screens.

Jaime L Stark, Hamid R Eghbalnia, Woonghee Lee, William M Westler, John L Markley

Abstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Applications of Solution NMR in Drug Discovery.Molecules (Basel, Switzerland) · 2021
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Jaime L StarkNational Magnetic Resonance Facility at Madison, University of Wisconsin , Madison, Wisconsin 53706, United States.
Hamid R EghbalniaNational Magnetic Resonance Facility at Madison, University of Wisconsin , Madison, Wisconsin 53706, United States.
Woonghee LeeNational Magnetic Resonance Facility at Madison, University of Wisconsin , Madison, Wisconsin 53706, United States.
William M WestlerNational Magnetic Resonance Facility at Madison, University of Wisconsin , Madison, Wisconsin 53706, United States.
John L MarkleyNational Magnetic Resonance Facility at Madison, University of Wisconsin , Madison, Wisconsin 53706, United States.

Funding

TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BUTCHER, SAMUEL E · 2012 to 2019
$9.4M
The BMRB as an evolving resource for biomolecular structure-function researchR01GM109046 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HOCH, JEFFREY C · 2014 to 2022
$6.6M
NIGMS NIH HHS P41 GM103399NIGMS NIH HHS P41GM103399NIGMS NIH HHS R01 GM109046NIGMS NIH HHS R01GM109046
6 · The paper itself

Abstract

NMR ligand affinity screening is a powerful technique that is routinely used in drug discovery or functional genomics to directly detect protein-ligand binding events. Binding events can be identified by monitoring differences in the 1D (1)H NMR spectrum of a compound with and without protein. Although a single NMR spectrum can be collected within a short period (2-10 min per sample), one-by-one screening of a protein against a library of hundreds or thousands of compounds requires a large amount of spectrometer time and a large quantity of protein. Therefore, compounds are usually evaluated in mixtures ranging in size from 3 to 20 compounds to improve the efficiency of these screens in both time and material. Ideally, the NMR signals from individual compounds in the mixture should not overlap so that spectral changes can be associated with a particular compound. We have developed a software tool, NMRmix, to assist in creating ideal mixtures from a large panel of compounds with known chemical shifts. Input to NMRmix consists of an (1)H NMR peak list for each compound, a user-defined overlap threshold, and additional user-defined parameters if default settings are not used. NMRmix utilizes a simulated annealing algorithm to optimize the composition of the mixtures to minimize spectral peak overlaps so that each compound in the mixture is represented by a maximum number of nonoverlapping chemical shifts. A built-in graphical user interface simplifies data import and visual evaluation of the results.

Indexed as

High-Throughput Screening AssaysSoftwareAlgorithmsLigandsMagnetic Resonance SpectroscopyProtein BindingProteinsSmall Molecule LibrariesLigandsProteinsSmall Molecule Librariesmixture optimizationNMR-based small molecule screeningprotein−ligand interactionssoftware tools

Identifiers

PMID26965640
PMCPMC4820789

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.