Evidence map›Paper›PMID 30698789›Full record

ArticleGenome biology and evolution2019

PDZ Domains Across the Microbial World: Molecular Link to the Proteases, Stress Response, and Protein Synthesis.

Vijaykumar Yogesh Muley, Yusuf Akhter, Sanjeev Galande

Open access · goldAbstract read
In one paragraph

Article in Genome biology and evolution, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. International journal of molecular sciences · 2026
    Article
  2. Article
  3. Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025
    Article
  4. Evolution of the Tri-PDZ Domain in PSD95 (DLG-4 Gene).Molecular biology and evolution · 2025
    Article
  5. Article
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  8. Review
  9. Article
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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 2 institutions in 2 countries.

Vijaykumar Yogesh MuleyInstituto de Neurobiología, Universidad Nacional Autónoma de México, Querétaro, México.
Yusuf AkhterDepartment of Biotechnology, Babasaheb Bhimrao Ambedkar University, Lucknow, India.
Sanjeev GalandeDepartment of Biology, Indian Institute of Science Education and Research, Pune, India.
Indian Institute of Science Education and Research Pune · INBabasaheb Bhimrao Ambedkar University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PSD-95/Dlg-A/ZO-1 (PDZ) domain is highly expanded, diversified, and well distributed across metazoa where it assembles diverse signaling components by virtue of interactions with other proteins in a sequence-specific manner. In contrast, in the microbial world they are reported to be involved in protein quality control during stress response. The distribution, functions, and origins of PDZ domain-containing proteins in the prokaryotic organisms remain largely unexplored. We analyzed 7,852 PDZ domain-containing proteins in 1,474 microbial genomes in this context. PDZ domain-containing proteins from planctomycetes, myxobacteria, and other eubacteria occupying terrestrial and aquatic niches are found to be in multiple copies within their genomes. Over 93% of the 7,852 PDZ domain-containing proteins were classified into 12 families including six novel families based on additional structural and functional domains present in these proteins. The higher PDZ domain encoding capacity of the investigated organisms was observed to be associated with adaptation to the ecological niche where multicellular life might have originated and flourished. Predicted subcellular localization of PDZ domain-containing proteins and their genomic context argue in favor of crucial roles in translation and membrane remodeling during stress response. Based on rigorous sequence, structure, and phylogenetic analyses, we propose that the highly diverse PDZ domain of the uncharacterized Fe-S oxidoreductase superfamily, exclusively found in gladobacteria and several anaerobes and acetogens, might represent the most ancient form among all the existing PDZ domains.

Indexed as

Biological EvolutionGenome, BacterialGenome, FungalMultigene FamilyPDZ DomainsGenes, MicrobialOxidoreductasesPeptide HydrolasesProtein BiosynthesisStress, PhysiologicalOxidoreductasesPeptide HydrolasesevolutionPDZproteaseradical SAMstress responsetranslation

Identifiers

PMID30698789
PMCPMC6411480
OpenAlexW2912290813

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.