Evidence map›Paper›PMID 41424949›Full record

ArticleFrontiers in bioinformatics2025

Uncovering human kinase substrates in nipah proteome.

Vineetha Shaji, Akash Anil, Ayisha A Jabbar, Althaf Mahin, Ahmad Rafi, Amjesh Revikumar, Sowmya Soman, Ganesh Prasad, Sneha M Pinto, Yashwanth Subbannayya and 2 more

Abstract read
In one paragraph

Article in Frontiers in bioinformatics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

12 authors.

Vineetha ShajiCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Akash AnilCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Ayisha A JabbarCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Althaf MahinCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Ahmad RafiCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Amjesh RevikumarCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Sowmya SomanCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Ganesh PrasadDepartment of Biochemistry, Yenepoya Medical College, Yenepoya (Deemed to be University), Mangalore, India.
Sneha M PintoSchool of Biosciences, Faculty of Health and Medical Sciences, University of Surrey, Guildford, United Kingdom.
Yashwanth SubbannayyaSchool of Biosciences, Faculty of Health and Medical Sciences, University of Surrey, Guildford, United Kingdom.
Abhithaj JayanandanCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.
Rajesh RajuCentre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nipah virus (NiV) is a zoonotic pathogen that causes recurrent outbreaks with considerable implications for public health. Viruses engage host kinases to phosphorylate viral proteins, aiding replication and host disruption. Identifying NiV phosphoproteins and their host kinases is therefore critical for understanding the mechanism of infection and developing therapeutics. We performed kinase-substrate phosphomotif analysis based on prior studies and employed computational tools to identify putative phosphosites in NiV proteins and corresponding host kinases. Redundancy analysis highlighted key kinases capable of phosphorylating multiple NiV proteins and high-potential viral substrates. Integration with human-viral protein-protein interaction data revealed human kinase substrate proteins in human that interact with NiV proteins, while conservation analysis assessed phosphosites across nine NiV proteins in various strains. The functional significance of the identified and predicted viral substrates and their corresponding host kinases was further validated through

Indexed as

computational prediction toolshost–virus interactionskinase-substrate phosphomotif searchmolecular dynamics simulationNipah virusphosphorylationprotein–protein docking

Identifiers

PMID41424949
PMCPMC12715814

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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.