Evidence map›Paper›PMID 38602394›Full record

ArticleBiochemistry2024

Contribution of a C-Terminal Extension to the Substrate Affinity and Oligomeric Stability of Aldehyde Dehydrogenase from

Wiktoria Brytan, Kim Shortall, Francisco Duarte, Tewfik Soulimane, Luis Padrela

Abstract read
In one paragraph

Article in Biochemistry, 2024. 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
–field-weighted citation impact
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. 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

5 authors.

Wiktoria BrytanDepartment of Chemical Sciences, Bernal Institute, University of Limerick, Limerick V94 T9PX, Ireland.ORCID 0000-0001-8888-4880
Kim ShortallDepartment of Chemical Sciences, Bernal Institute, University of Limerick, Limerick V94 T9PX, Ireland.
Francisco DuarteDepartment of Chemical Sciences, Bernal Institute, University of Limerick, Limerick V94 T9PX, Ireland.ORCID 0000-0001-7550-9504
Tewfik SoulimaneDepartment of Chemical Sciences, Bernal Institute, University of Limerick, Limerick V94 T9PX, Ireland.
Luis PadrelaDepartment of Chemical Sciences, Bernal Institute, University of Limerick, Limerick V94 T9PX, Ireland.ORCID 0000-0002-8632-2320

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldehyde dehydrogenase enzymes (ALDHs) are widely studied for their roles in disease propagation and cell metabolism. Their use in biocatalysis applications, for the conversion of aldehydes to carboxylic acids, has also been recognized. Understanding the structural features and functions of both prokaryotic and eukaryotic ALDHs is key to uncovering novel applications of the enzyme and probing its role in disease propagation. The thermostable enzyme ALDH

Indexed as

Aldehyde DehydrogenaseEnzyme StabilityThermus thermophilusAmino Acid SequenceBacterial ProteinsCatalytic DomainKineticsProtein MultimerizationSubstrate SpecificityAldehyde DehydrogenaseBacterial Proteins

Identifiers

PMID38602394
PMCPMC11080044

What OpenQuestion holds

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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.