Evidence map›Paper›PMID 36048303›Full record

ArticleMolecular diversity2023

Homology modeling of Forkhead box protein C2: identification of potential inhibitors using ligand and structure-based virtual screening.

Mayar Tarek Ibrahim, Jiyong Lee, Peng Tao

Open access · greenAbstract read
In one paragraph

Article in Molecular diversity, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

6 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Novel Allosteric Effectors Targeting Human Transcription Factor TEAD.International journal of molecular sciences · 2023
    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

3 authors at 2 institutions in 1 country.

Mayar Tarek IbrahimDepartment of Chemistry, Center for Research Computing, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, TX, USA.
Jiyong LeeDepartment of Chemistry and Biochemistry, The University of Texas at Tyler, Tyler, TX, USA.ORCID http://orcid.org/0000-0002-4455-3358
Peng TaoDepartment of Chemistry, Center for Research Computing, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, TX, USA. ptao@smu.edu.ORCID http://orcid.org/0000-0002-2488-0239
Southern Methodist University · USThe University of Texas at Tyler · US

Funding

Probing Hidden Conformational Space and Dynamical States of Circadian Clock Proteins through Rigid Residue Scan and Machine LearningR15GM122013 · NIGMS · SOUTHERN METHODIST UNIVERSITY · PI TAO, PENG · 2018 to 2023
$800k
NIGMS NIH HHS R15 GM122013NIGMS NIH HHS R15GM122013
6 · The paper itself

Abstract

Overexpression of Forkhead box protein C2 (FOXC2) has been associated with different types of carcinomas. FOXC2 plays an important role in the initiation and maintenance of the epithelial-mesenchymal transition (EMT) process, which is essential for the development of higher-grade tumors with an enhanced ability for metastasis. Thus, FOXC2 has become a therapeutic target for the development of anticancer drugs. MC-1-F2, the only identified experimental inhibitor of FOXC2, interacts with the full length of FOXC2. However, only the DNA-binding domain (DBD) of FOXC2 has resolved crystal structure. In this work, a three-dimensional (3D) structure of the full-length FOXC2 using homology modeling was developed and used for structure-based drug design (SBDD). The quality of this 3D model of the full-length FOXC2 was evaluated using MolProbity, ERRAT, and ProSA modules. Molecular dynamics (MD) simulation was also carried out to verify its stability. Ligand-based drug design (LBDD) was carried out to identify similar analogues for MC-1-F2 against 15 million compounds from ChEMBL and ZINC databases. 792 molecules were retrieved from this similarity search. De novo SBDD was performed against the full-length 3D structure of FOXC2 through homology modeling to identify novel inhibitors. The combination of LBDD and SBDD helped in gaining a better insight into the binding of MC-1-F2 and its analogues against the full length of the FOXC2. The binding free energy of the top hits was further investigated using MD simulations and MM/GBSA calculations to result in eight promising hits as lead compounds targeting FOXC2.

Indexed as

Antineoplastic AgentsMolecular Dynamics SimulationForkhead Transcription FactorsLigandsAntineoplastic AgentsForkhead Transcription FactorsLigandsDe novo structure-based designForkhead box protein C2Homology modelingMC-1-F2MM/GBSASimilarity search

Identifiers

PMID36048303
PMCPMC9975119
OpenAlexW4294001182

What OpenQuestion holds

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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.