Evidence map›Paper›PMID 35889163›Full record

ArticleMicroorganisms2022

Structure Prediction and Characterization of Thermostable Aldehyde Dehydrogenase from Newly Isolated

Nur Ezzati Rosli, Mohd Shukuri Mohamad Ali, Nor Hafizah Ahmad Kamarudin, Malihe Masomian, Wahhida Latip, Shazleen Saadon, Raja Noor Zaliha Raja Abd Rahman

Open access · goldAbstract read
In one paragraph

Article in Microorganisms, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Structural Insight into the Catalytic Mechanisms of an L-Sorbosone Dehydrogenase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  4. Review
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

7 authors at 1 institution in 1 country.

Nur Ezzati RosliEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), Serdang 43400, Malaysia.
Mohd Shukuri Mohamad AliEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), Serdang 43400, Malaysia.
Nor Hafizah Ahmad KamarudinEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), Serdang 43400, Malaysia.
Malihe MasomianEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), Serdang 43400, Malaysia.
Wahhida LatipEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), Serdang 43400, Malaysia.ORCID 0000-0002-6241-7528
Shazleen SaadonEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), Serdang 43400, Malaysia.
Raja Noor Zaliha Raja Abd RahmanEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), Serdang 43400, Malaysia.ORCID 0000-0002-6316-6177
Universiti Putra Malaysia · MY

Funding

PETRONAS Research Sdn Bhd UPMCS 2019-75/1021Putra Graduate Initiative Grant GP-IPS/ 2021/9698700
6 · The paper itself

Abstract

In nature, aldehyde dehydrogenase (ALDH) is widely distributed and mainly involved in the oxidation of aldehydes. Thermostability is one of the key features for industrial enzymes. The ability of enzymes to withstand a high operating temperature offers many advantages, including enhancing productivity in industries. This study was conducted to understand the structural and biochemical features of ALDH from thermophilic bacterium,

Indexed as

aldehyde dehydrogenasebiochemical characterizationbiophysical characterizationthermophilethermostable enzyme

Identifiers

PMID35889163
PMCPMC9322625
OpenAlexW4285730382

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.