Evidence map›Paper›PMID 27960325›Full record

ArticleJournal of the American Chemical Society2016

Probing Hydronium Ion Histidine NH Exchange Rate Constants in the M2 Channel via Indirect Observation of Dipolar-Dephased

Riqiang Fu, Yimin Miao, Huajun Qin, Timothy A Cross

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. 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
1.6field-weighted citation impact, top 17% 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, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article
  4. Article
  5. Review
  6. Review
  7. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  8. 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

4 authors at 2 institutions in 1 country.

Riqiang FuNational High Magnet Field Lab , 1800 East Paul Dirac Drive, Tallahassee, Florida 32310, United States.
Yimin MiaoDepartment of Chemistry and Biochemistry, Florida State University , Tallahassee, Florida 32306, United States.
Huajun QinDepartment of Chemistry and Biochemistry, Florida State University , Tallahassee, Florida 32306, United States.
Timothy A CrossNational High Magnet Field Lab , 1800 East Paul Dirac Drive, Tallahassee, Florida 32310, United States.
Florida State University · USNational High Magnetic Field Laboratory · US

Funding

DYNAMIC AND STRUCTURAL ELUCIDATION OF GRAMICIDIN A'R01AI023007 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 1987 to 2014
$5.1M
Membrane Protein Structures and Interactions in the M. tuberculosis DivisomeR01AI119178 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2015 to 2019
$3.6M
NIAID NIH HHS R01 AI023007NIAID NIH HHS R01 AI119178
6 · The paper itself

Abstract

Water-protein chemical exchange in membrane-bound proteins is an important parameter for understanding how proteins interact with their aqueous environment, but has been difficult to observe in membrane-bound biological systems. Here, we demonstrate the feasibility of probing specific water-protein chemical exchange in membrane-bound proteins in solid-state MAS NMR. By spin-locking the

Indexed as

Nuclear Magnetic Resonance, BiomolecularHistidineNitrogen IsotopesOnium CompoundsProtonsViral Matrix ProteinsViroporin ProteinsHistidinehydronium ionM2 protein, Influenza A virusNitrogen IsotopesOnium CompoundsProtonsViral Matrix ProteinsViroporin Proteins

Identifiers

PMID27960325
PMCPMC5368641
OpenAlexW2553182955

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.