Evidence map›Paper›PMID 32580303›Full record

ArticleBiomolecules2020

CoRNeA: A Pipeline to Decrypt the Inter-Protein Interfaces from Amino Acid Sequence Information.

Kriti Chopra, Bhawna Burdak, Kaushal Sharma, Ajit Kembhavi, Shekhar C Mande, Radha Chauhan

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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.

Kriti ChopraNational Centre for Cell Science, Pune 411007, Maharashtra, India.ORCID 0000-0002-9788-9218
Bhawna BurdakNational Centre for Cell Science, Pune 411007, Maharashtra, India.
Kaushal SharmaInter-University Centre for Astronomy and Astrophysics, Pune 411007, Maharashtra, India.ORCID 0000-0001-7196-1659
Ajit KembhaviInter-University Centre for Astronomy and Astrophysics, Pune 411007, Maharashtra, India.
Shekhar C MandeCouncil of Scientific and Industrial Research (CSIR), New Delhi 110001, India.ORCID 0000-0002-6634-0820
Radha ChauhanNational Centre for Cell Science, Pune 411007, Maharashtra, India.ORCID 0000-0003-1632-1637
National Centre for Cell Science · INInter-University Centre for Astronomy and Astrophysics · INCouncil of Scientific and Industrial Research · IN

Funding

Department of Biotechnology, Ministry of Science and Technology, India DBT/PR26398/BRB/10/1637/2017Science and Engineering Research Board SERB/EMR/2017/000272
6 · The paper itself

Abstract

Decrypting the interface residues of the protein complexes provides insight into the functions of the proteins and, hence, the overall cellular machinery. Computational methods have been devised in the past to predict the interface residues using amino acid sequence information, but all these methods have been majorly applied to predict for prokaryotic protein complexes. Since the composition and rate of evolution of the primary sequence is different between prokaryotes and eukaryotes, it is important to develop a method specifically for eukaryotic complexes. Here, we report a new hybrid pipeline for predicting the protein-protein interaction interfaces in a pairwise manner from the amino acid sequence information of the interacting proteins. It is based on the framework of Co-evolution, machine learning (Random Forest), and Network Analysis named CoRNeA trained specifically on eukaryotic protein complexes. We use Co-evolution, physicochemical properties, and contact potential as major group of features to train the Random Forest classifier. We also incorporate the intra-contact information of the individual proteins to eliminate false positives from the predictions keeping in mind that the amino acid sequence of a protein also holds information for its own folding and not only the interface propensities. Our prediction on example datasets shows that CoRNeA not only enhances the prediction of true interface residues but also reduces false positive rates significantly.

Indexed as

Computational BiologyMachine LearningAmino Acid SequenceDatabases, ProteinHumansProtein BindingProteinsProteinsco-evolutioninter-protein interfacesmachine learning

Identifiers

PMID32580303
PMCPMC7356028
OpenAlexW3036272762

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.