Evidence map›Paper›PMID 33273141›Full record

ArticleActa crystallographica. Section C, Structural chemistry2020

Crystal structure of a calcium(II)-pyrroloquinoline quinone (PQQ) complex outside a protein environment.

Henning Lumpe, Peter Mayer, Lena J Daumann

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section C, Structural chemistry, 2020. 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
0.3field-weighted citation impact, top 45% 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, 8 citations in OpenAlex.

  1. Pyrroloquinoline quinone ameliorates liver injury in mice induced by cyclophosphamide.Environmental science and pollution research international · 2022
    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.

Henning LumpeDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstrasse 5-13, Munich, Bavaria 81377, Germany.
Peter MayerDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstrasse 5-13, Munich, Bavaria 81377, Germany.
Lena J DaumannDepartment of Chemistry, Ludwig-Maximilians-Universität München, Butenandtstrasse 5-13, Munich, Bavaria 81377, Germany.
Ludwig-Maximilians-Universität München · DE

Funding

Deutsche Forschungsgemeinschaft 392552271
6 · The paper itself

Abstract

Pyrroloquinoline quinone (PQQ) is an important cofactor of calcium- and lanthanide-dependent alcohol dehydrogenases, and has been known for over 30 years. Crystal structures of Ca-MDH enzymes (MDH is methanol dehydrogenase) have been known for some time; however, crystal structures of PQQ with biorelevant metal ions have been lacking in the literature for decades. We report here the first crystal structure analysis of a Ca-PQQ complex outside the protein environment, namely, poly[[undecaaquabis(μ-4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylato)tricalcium(II)] dihydrate], {[Ca

Indexed as

Alcohol OxidoreductasesCalciumCatalytic DomainCrystallizationCrystallography, X-RayEuropiumHydrogen BondingModels, MolecularMolecular StructurePQQ Cofactoralcohol dehydrogenase (acceptor)Alcohol OxidoreductasesCalciumEuropiumPQQ Cofactorcalciumcrystal structuremethanol dehydrogenasePQQpyrroloquinoline quinone

Identifiers

PMID33273141
PMCPMC7716187
OpenAlexW3095707102

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.