Evidence map›Paper›PMID 29576935›Full record

ArticlePeerJ2018

Homology modeling and docking studies of a Δ9-fatty acid desaturase from a Cold-tolerant

Lawal Garba, Mohamad Ariff Mohamad Yussoff, Khairul Bariyyah Abd Halim, Siti Nor Hasmah Ishak, Mohd Shukuri Mohamad Ali, Siti Nurbaya Oslan, Raja Noor Zaliha Raja Abd Rahman

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PeerJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Research Progress Regarding PsychrotrophicFoods (Basel, Switzerland) · 2025
    Review
  2. Evaluating Biofilm Inhibitory Potential in Fish Pathogen,Antibiotics (Basel, Switzerland) · 2023
    Article
  3. Article
  4. Review
  5. LeveragingFrontiers in microbiology · 2021
    Review
  6. Article
  7. 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

7 authors at 2 institutions in 2 countries.

Lawal GarbaEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Mohamad Ariff Mohamad YussoffDepartment of Biotechnology, Kulliyyah of Science, International Islamic University Malaysia, Kuantan, Pahang Darul Makmur, Malaysia.
Khairul Bariyyah Abd HalimDepartment of Biotechnology, Kulliyyah of Science, International Islamic University Malaysia, Kuantan, Pahang Darul Makmur, Malaysia.
Siti Nor Hasmah IshakEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Mohd Shukuri Mohamad AliEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Siti Nurbaya OslanEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Raja Noor Zaliha Raja Abd RahmanEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Universiti Putra Malaysia · MYInternational Islamic University Malaysia · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane-bound fatty acid desaturases perform oxygenated desaturation reactions to insert double bonds within fatty acyl chains in regioselective and stereoselective manners. The Δ9-fatty acid desaturase strictly creates the first double bond between C9 and 10 positions of most saturated substrates. As the three-dimensional structures of the bacterial membrane fatty acid desaturases are not available, relevant information about the enzymes are derived from their amino acid sequences, site-directed mutagenesis and domain swapping in similar membrane-bound desaturases. The cold-tolerant

Indexed as

Cold-tolerant Pseudomonas sp. AMS8Homology modelingMolecular dockingPalmitic acidδ9-fatty acid desaturase

Identifiers

PMID29576935
PMCPMC5863719
OpenAlexW2793106426

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.