Evidence map›Paper›PMID 26170095›Full record

ArticleMolecular diversity2015

Modelling the molecular mechanism of protein-protein interactions and their inhibition: CypD-p53 case study.

S M Fayaz, G K Rajanikant

Abstract read
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Article in Molecular diversity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
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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

2 authors.

S M FayazSchool of Biotechnology, National Institute of Technology Calicut, Calicut, 673601, India.
G K RajanikantSchool of Biotechnology, National Institute of Technology Calicut, Calicut, 673601, India. rajanikant@nitc.ac.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclophilin D (CypD) is an important regulatory protein involved in mitochondrial membrane permeability transition and cell death. Further, the mitochondrial CypD-p53 axis is an important contributor to necroptosis, a form of programmed necrosis, involved in various cardiovascular and neurological disorders. The CypD ligand, Cyclosporin A (CsA), was identified as an inhibitor of this interaction. In this study, using computational methods, we have attempted to model the CypD-p53 interaction in order to delineate their mode of binding and also to disclose the molecular mechanism, by means of which CsA interferes with this interaction. It was observed that p53 binds at the CsA-binding site of CypD. The knowledge obtained from this modelling was employed to identify novel CypD inhibitors through structure-based methods. Further, the identified compounds were tested by a similar strategy, adopted during the modelling process. This strategy could be applied to study the mechanism of protein-protein interaction (PPI) inhibition and to identify novel PPI inhibitors.

Indexed as

Binding SitesComputational BiologyCyclophilinsCyclosporineDrug DesignMolecular Docking SimulationMolecular Dynamics SimulationPeptidyl-Prolyl Isomerase FProtein BindingStructure-Activity RelationshipTumor Suppressor Protein p53CyclophilinsCyclosporinePeptidyl-Prolyl Isomerase FTumor Suppressor Protein p53Cyclophilin DCyclosporin ANecroptosisNeurological disordersp53Protein–protein interactions

Identifiers

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Registered trials

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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.