Evidence map›Paper›PMID 36988846›Full record

ArticleApplied biochemistry and biotechnology2023

Identification of Novel Protein Targets of Prodigiosin for Breast Cancer Using Inverse Virtual Screening Methods.

Tania Paul, Prashant Bhardwaj, Abhijit Mondal, Tarun Kanti Bandyopadhyay, Nibedita Mahata, Biswanath Bhunia

Abstract read
PubMed Publisher
In one paragraph

Article in Applied biochemistry and biotechnology, 2023. 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
1.3field-weighted citation impact, top 20% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  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

6 authors at 3 institutions in 1 country.

Tania PaulDepartment of Chemical Engineering, National Institute of Technology, Agartala, 799046, India.ORCID http://orcid.org/0000-0002-7987-7918
Prashant BhardwajDepartment of Computer Science and Engineering, National Institute of Technology, Agartala, 799046, India.
Abhijit MondalDepartment of Chemical Engineering, Birla Institute of Technology Mesra, Mesra, Jharkhand, 835215, India.
Tarun Kanti BandyopadhyayDepartment of Chemical Engineering, National Institute of Technology, Agartala, 799046, India.ORCID http://orcid.org/0000-0002-5374-421X
Nibedita MahataDepartment of Biotechnology, National Institute of Technology, Durgapur, India.
Biswanath BhuniaDepartment of Bio Engineering, National Institute of Technology, Agartala, 799046, India. bbhunia@gmail.com.ORCID http://orcid.org/0000-0003-1330-1606
National Institute of Technology Agartala · INBirla Institute of Technology, Mesra · INNational Institute of Technology Durgapur · IN

Funding

Department of science and technology SERC/L2012S-167/
6 · The paper itself

Abstract

Prodigiosin (PG) is chemically formulated as 4-methoxy-5-[(5-methyl-4-pentyl-2H-pyrrol-2ylidene)methyl]-2,2'-bi-1H-pyrrole and it is an apoptotic agent. Only a few protein targets for PG have been identified so far for regulating various diseases; nevertheless, finding more PG targets is crucial for novel drug discovery research. A bioinformatics method was applied in this work to find additional potential PG targets. Initially, a text mining analysis was conducted to determine the relationship between PG and a variety of metabolic processes. One hundred sixteen proteins from the KEGG pathway were selected for the docking study. Inverse virtual screening was performed by Discovery Studio software 4.1 using CHARMm-based docking tool. Twelve proteins are screened out of 116 because their CDOCKER interaction energy is larger than - 40.22 kcal/mol. The best docking score with PG was reported to be - 44.25 kcal/mol, - 44.99 kcal/mol, and - 40.91 kcal/mol for three novel proteins, such as human epidermal growth factor-2 (HER-2), mitogen-activated protein kinase (MEK), and S6 kinase protein (S6K) respectively. The interactions in the S6K/PG complex are predominantly hydrophobic; however, hydrogen bond interactions can be identified in the MEK/PG and HER-2/PG complexes. The root-mean-square deviation (RMSD) and key interaction score system (KISS) were further used to validate the docking approach. The docking approach employed in this work has a low RMSD value (2.44 Å) and a high KISS score (0.5), indicating that it is significant.

Indexed as

NeoplasmsProdigiosinEarly Detection of CancerEpidermal Growth FactorHumansMitogen-Activated Protein Kinase KinasesMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingEpidermal Growth FactorMitogen-Activated Protein Kinase KinasesProdigiosinCDOCKER energyInverse virtual screeningProdigiosinText miningValidation

Identifiers

PMID36988846
OpenAlexW4361289836

What OpenQuestion holds

Textmetadata
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.