Evidence map›Paper›PMID 29151213›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.

Vincenzo Venditti, Nicolas L Fawzi

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. 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. Quantifying Ligand-to-Protein Distances in Complex Environments Using IntermolecularChembiochem : a European journal of chemical biology · 2026
    Article
  2. Review
  3. Exploration of the interaction between dynein intermediate chain and dynactin p150Protein science : a publication of the Protein Society · 2025
    Article
  4. Review
  5. A Chemical Biology Primer for NMR Spectroscopists.Journal of magnetic resonance open · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. A Double-Armed, Hydrophilic Transition Metal Complex as a Paramagnetic NMR Probe.Angewandte Chemie (International ed. in English) · 2019
    Review
  10. Article
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

2 authors.

Vincenzo VendittiDepartment of Chemistry, Iowa State University, 0219 Hach Hall, 2438 Pammel Drive, Ames, IA, 50011, USA. venditti@iastate.edu.
Nicolas L FawziDepartment of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Box G-E, 171 Meeting Street, Providence, RI, 02912, USA. Nicolas_Fawzi@brown.edu.

Funding

Turning off the molecular switch for pathological self-assembly of FUSR01GM118530 · NIGMS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX · 2016 to 2020
$1.6M
NIGMS NIH HHS R01 GM118530
6 · The paper itself

Abstract

Important biological processes, including enzyme catalysis, signaling, and protein folding, proceed through lowly populated (<5%) states that elude structural characterization by conventional techniques. Here, we describe the steps required for visualization of these sparsely populated conformations and transient protein-protein interactions using paramagnetic relaxation enhancement solution NMR. We describe experimental design, sample preparation, data acquisition and processing, and the basics of data analysis of structural ensembles.

Indexed as

Models, MolecularProtein ConformationMagnetic Resonance SpectroscopyProtein BindingDark statesEncounter complexLowly populated statesNMR spectroscopyProtein-protein interactionsSite-directed spin-labelingTransient interactions

Identifiers

PMID29151213
PMCPMC5823026

What OpenQuestion holds

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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.