Evidence map›Paper›PMID 37641402›Full record

ArticleBiophysical journal2023

Native and nonnative reactions in ethanolamine ammonia-lyase are actuated by different dynamics.

Wei Li, Kurt Warncke

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.1field-weighted citation impact, top 16% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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 at 1 institution in 1 country.

Wei LiDepartment of Physics, Emory University, Atlanta, Georgia.
Kurt WarnckeDepartment of Physics, Emory University, Atlanta, Georgia. Electronic address: kwarncke@physics.emory.edu.
Emory University · US

Funding

Co(II) Radical Pair Dynamics in B12 Enzyme CatalysisR01GM142113 · NIGMS · EMORY UNIVERSITY · PI WARNCKE, KURT · 2020 to 2023
$1.3M
Electron Paramagnetic Resonance SpectrometerS10RR017767 · NCRR · EMORY UNIVERSITY · PI WARNCKE, KURT · 2003 to 2003
$261k
NCRR NIH HHS S10 RR017767NIGMS NIH HHS R01 GM142113
6 · The paper itself

Abstract

We address the contribution of select classes of solvent-coupled configurational fluctuations to the complex choreography involved in configurational and chemical steps in an enzyme by comparing native and nonnative reactions conducted at different protein internal sites. The low temperature, first-order kinetics of covalent bond rearrangement of the cryotrapped substrate radical in coenzyme B

Indexed as

Ethanolamine Ammonia-LyaseCysteineElectron Spin Resonance SpectroscopyHydrogen PeroxideKineticsSalmonella typhimuriumSolventsWaterCysteineEthanolamine Ammonia-LyaseHydrogen PeroxideSolventsWater

Identifiers

PMID37641402
PMCPMC10560697
OpenAlexW4386226705

What OpenQuestion holds

Textmetadata
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.