Evidence map›Paper›PMID 26361636›Full record

ArticleApplications of NMR spectroscopy

Protein-Inhibitor Interaction Studies Using NMR.

Rieko Ishima

Abstract read
In one paragraph

Article in Applications of NMR spectroscopy. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation.Protein science : a publication of the Protein Society · 2016
    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

1 author at 1 institution in 1 country.

Rieko IshimaDepartment of Structural Biology, University of Pittsburgh, School of Medicine, Pittsburgh, PA 15260, USA.
University of Pittsburgh · US

Funding

Conformational Dynamics and inhibitor responses of HIV-1 RT RNase H in solutionR01GM105401 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ISHIMA, RIEKO · 2013 to 2016
$1.4M
NIGMS NIH HHS R01 GM105401
6 · The paper itself

Abstract

Solution-state NMR has been widely applied to determine the three-dimensional structure, dynamics, and molecular interactions of proteins. The designs of experiments used in protein NMR differ from those used for small-molecule NMR, primarily because the information available prior to an experiment, such as molecular mass and knowledge of the primary structure, is unique for proteins compared to small molecules. In this review article, protein NMR for structural biology is introduced with comparisons to small-molecule NMR, such as descriptions of labeling strategies and the effects of molecular dynamics on relaxation. Next, applications for protein NMR are reviewed, especially practical aspects for protein-observed ligand-protein interaction studies. Overall, the following topics are described: (1) characteristics of protein NMR, (2) methods to detect protein-ligand interactions by NMR, and (3) practical aspects of carrying out protein-observed inhibitor-protein interaction studies.

Indexed as

DruginhibitorinteractionNMRproteinrelaxationstructure

Identifiers

PMID26361636
PMCPMC4562695
OpenAlexW654319949

What OpenQuestion holds

Textmetadata
LicenceTDM
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.