Evidence map›Paper›PMID 37540029›Full record

ArticleThe journal of physical chemistry letters2023

Reactivity Tracking of an Enzyme Progress Coordinate.

Wei Li, Meghan Kohne, Kurt Warncke

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 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
0.2field-weighted citation impact, top 41% 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, 1 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

3 authors at 1 institution in 1 country.

Wei LiDepartment of Physics, Emory University, Atlanta, Georgia 30322, United States.
Meghan KohneDepartment of Physics, Emory University, Atlanta, Georgia 30322, United States.
Kurt WarnckeDepartment of Physics, Emory University, Atlanta, Georgia 30322, United States.ORCID 0000-0002-3587-3720
Emory University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reactivity of individual solvent-coupled protein configurations is used to track and resolve the progress coordinate for the core reaction sequence of substrate radical rearrangement and hydrogen atom transfer in the ethanolamine ammonia-lyase (EAL) enzyme from

Indexed as

CobamidesEthanolamine Ammonia-LyaseCatalysisKineticsSalmonella typhimuriumSolventsCobamidesEthanolamine Ammonia-LyaseSolvents

Identifiers

PMID37540029
PMCPMC10440813
OpenAlexW4385564580

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.