Evidence map›Paper›PMID 29923716›Full record

ArticleJournal of the American Chemical Society2018

Monitoring

Cyril Charlier, Joseph M Courtney, T Reid Alderson, Philip Anfinrud, Ad Bax

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Chemical Exchange.Methods in enzymology · 2019
    Article
  11. Article
  12. Additive fabrication for NMR probe builders.Progress in nuclear magnetic resonance spectroscopy
    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.

Cyril CharlierLaboratory of Chemical Physics, NIDDK , National Institutes of Health , Bethesda , Maryland 20892-0520 , United States.
Joseph M CourtneyLaboratory of Chemical Physics, NIDDK , National Institutes of Health , Bethesda , Maryland 20892-0520 , United States.
T Reid AldersonLaboratory of Chemical Physics, NIDDK , National Institutes of Health , Bethesda , Maryland 20892-0520 , United States.
Philip AnfinrudLaboratory of Chemical Physics, NIDDK , National Institutes of Health , Bethesda , Maryland 20892-0520 , United States.
Ad BaxLaboratory of Chemical Physics, NIDDK , National Institutes of Health , Bethesda , Maryland 20892-0520 , United States.ORCID 0000-0002-9809-5700

Funding

Methods to accelerate protein structure determination by solution NMRZIADK029046 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2009 to 2025
$12.8M
Study of protein folding and misfolding by NMR spectroscopyZIADK075141 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2017 to 2025
$8.6M
Ultrafast Biophysical Studies Of ProteinsZIADK029031 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2009 to 2025
$7.1M
Intramural NIH HHS ZIA DK029046
6 · The paper itself

Abstract

Pressure-jump hardware permits direct observation of protein NMR spectra during a cyclically repeated protein folding process. For a two-state folding protein, the change in resonance frequency will occur nearly instantaneously when the protein clears the transition state barrier, resulting in a monoexponential change of the ensemble-averaged chemical shift. However, protein folding pathways can be more complex and contain metastable intermediates. With a pseudo-3D NMR experiment that utilizes stroboscopic observation, we measure the ensemble-averaged chemical shifts, including those of exchange-broadened intermediates, during the folding process. Such measurements for a pressure-sensitized mutant of ubiquitin show an on-pathway kinetic intermediate whose

Indexed as

Nuclear Magnetic Resonance, BiomolecularNitrogen IsotopesPressureProtein FoldingNitrogen-15Nitrogen Isotopes

Identifiers

PMID29923716
PMCPMC6119464

What OpenQuestion holds

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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.