Evidence map›Paper›PMID 29329228›Full record

ReviewMolecules (Basel, Switzerland)2018

Current NMR Techniques for Structure-Based Drug Discovery.

Toshihiko Sugiki, Kyoko Furuita, Toshimichi Fujiwara, Chojiro Kojima

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.8field-weighted citation impact, top 3% of its field
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

47 citing papers in PubMed, 121 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Perspectives on Applications ofMolecules (Basel, Switzerland) · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Quantitative lipid composition characterization of intact liposomes viaAnalytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024
    Article
  11. Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023
    Review
  12. Review
  13. Review
  14. Review
  15. RSC medicinal chemistry · 2022
    Article
  16. Evolving Experimental Techniques for Structure-Based Drug Design.The journal of physical chemistry. B · 2022
    Review
  17. Review
  18. The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022
    Review
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Toshihiko SugikiInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan. sugiki@protein.osaka-u.ac.jp.
Kyoko FuruitaInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan. k-furuit@protein.osaka-u.ac.jp.
Toshimichi FujiwaraInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan. tfjwr@protein.osaka-u.ac.jp.
Chojiro KojimaInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan. kojima-chojiro-xk@ynu.ac.jp.ORCID 0000-0003-2723-8249
Protein Research Foundation · JPYokohama National University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A variety of nuclear magnetic resonance (NMR) applications have been developed for structure-based drug discovery (SBDD). NMR provides many advantages over other methods, such as the ability to directly observe chemical compounds and target biomolecules, and to be used for ligand-based and protein-based approaches. NMR can also provide important information about the interactions in a protein-ligand complex, such as structure, dynamics, and affinity, even when the interaction is too weak to be detected by ELISA or fluorescence resonance energy transfer (FRET)-based high-throughput screening (HTS) or to be crystalized. In this study, we reviewed current NMR techniques. We focused on recent progress in NMR measurement and sample preparation techniques that have expanded the potential of NMR-based SBDD, such as fluorine NMR (

Indexed as

Drug DiscoveryIsotope LabelingMagnetic Resonance SpectroscopyMolecular StructurePharmaceutical PreparationsProteinsPharmaceutical PreparationsProteinsfluorine-19 (19F) NMRligand-based NMRNMR-based fragment screeningNMR-based lead optimizationnuclear magnetic resonance (NMR)protein-based NMRprotein-protein interaction (PPI) breaker/stabilizersite-specific isotope labeling

Identifiers

PMID29329228
PMCPMC6017608
OpenAlexW2784156712

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.