Evidence map›Paper›PMID 32333192›Full record

ArticleJournal of biomolecular NMR2020

Achieving pure spin effects by artifact suppression in methyl adiabatic relaxation experiments.

Fa-An Chao, Domarin Khago, R Andrew Byrd

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Complete solution for rotating frame relaxation functions during adiabatic pulses.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. 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

3 authors.

Fa-An ChaoStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702-1201, USA.ORCID http://orcid.org/0000-0001-5215-8545
Domarin KhagoStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702-1201, USA.ORCID http://orcid.org/0000-0001-5676-6804
R Andrew ByrdStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702-1201, USA. byrdra@mail.nih.gov.ORCID http://orcid.org/0000-0003-3625-4232

Funding

Investigation of Protein-Protein Interactions in the ERAD Ubiquitylation PathwayZIABC011131 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$12.0M
Methods DevelopmentZIABC011132 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$4.6M
Intramural NIH HHS ZIA BC011131Intramural NIH HHS ZIA BC011132NCI NIH HHS ZIA BC 011131NCI NIH HHS ZIA BC 011132
6 · The paper itself

Abstract

Recent methyl adiabatic relaxation dispersion experiments provide examination of conformational dynamics across a very wide timescale (10

Indexed as

ArtifactsProtein ConformationAllosteric RegulationBinding SitesModels, MolecularNuclear Magnetic Resonance, BiomolecularPeptide FragmentsPoint MutationProtein FoldingProtonsReceptors, Autocrine Motility FactorRecombinant Fusion ProteinsThermodynamicsUbiquitin-Conjugating EnzymesAMFR protein, humanG2BR peptidePeptide FragmentsProtonsReceptors, Autocrine Motility FactorRecombinant Fusion ProteinsUBE2G2 protein, humanUbiquitin-Conjugating EnzymesAdiabatic relaxation dispersionComposite decouplingConformational dynamicsCross-correlation between DD and CSAMethyl relaxationMethyl TROSY

Identifiers

PMID32333192
PMCPMC7430055

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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.