Evidence map›Paper›PMID 33645229›Full record

ArticleThe journal of physical chemistry. B2021

Preferential Binding of Lanthanides to Methanol Dehydrogenase Evaluated with Density Functional Theory.

Ran Friedman

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Estimating the Gibbs Hydration Energies of Actinium and Trans-Plutonium Actinides.Chemphyschem : a European journal of chemical physics and physical chemistry · 2023
    Article
  5. 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

1 author at 1 institution in 1 country.

Ran FriedmanDepartment of Chemistry and Biomedical Sciences, Linnaeus University, Kalmar 391 82, Sweden.ORCID 0000-0001-8696-3104
Linnaeus University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methanol dehydrogenase (MDH) is an enzyme used by certain bacteria for the oxidation of methanol to formaldehyde, which is a necessary metabolic reaction. The discovery of a lanthanide-dependent MDH reveals that lanthanide ions (Ln

Indexed as

Lanthanoid Series ElementsAlcohol OxidoreductasesDensity Functional TheoryMethanolalcohol dehydrogenase (acceptor)Alcohol OxidoreductasesLanthanoid Series ElementsMethanol

Identifiers

PMID33645229
PMCPMC8028316
OpenAlexW3135504660

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.