Evidence map›Paper›PMID 35008783›Full record

ArticleInternational journal of molecular sciences2021

Structure-Function Relationships in the Human P-Glycoprotein (ABCB1): Insights from Molecular Dynamics Simulations.

Liadys Mora Lagares, Yunierkis Pérez-Castillo, Nikola Minovski, Marjana Novič

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.8field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Designing a Small Molecule for PET Radiotracing: [Molecules (Basel, Switzerland) · 2025
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Evaluation of Antitumor Activity of Xanthones Conjugated with Amino Acids.International journal of molecular sciences · 2024
    Article
  12. Regulation of P-Glycoprotein during Oxidative Stress.Antioxidants (Basel, Switzerland) · 2024
    Review
  13. Article
  14. Review
  15. Second-site suppressor mutations reveal connection between the drug-binding pocket and nucleotide-binding domain 1 of human P-glycoprotein (ABCB1).Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Article
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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

4 authors at 3 institutions in 2 countries.

Liadys Mora LagaresTheory Department, Laboratory for Cheminformatics, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0002-6205-4675
Yunierkis Pérez-CastilloBio-Cheminformatics Research Group and Escuela de Ciencias Físicas y Matemáticas, Universidad de Las Américas, Quito 170513, Ecuador.ORCID 0000-0002-3710-0035
Nikola MinovskiTheory Department, Laboratory for Cheminformatics, National Institute of Chemistry, 1000 Ljubljana, Slovenia.ORCID 0000-0003-0039-2246
Marjana NovičTheory Department, Laboratory for Cheminformatics, National Institute of Chemistry, 1000 Ljubljana, Slovenia.
National Institute of Chemistry · SIJožef Stefan International Postgraduate School · SIUniversidad de Las Américas · EC

Funding

Marie Sklodowska-Curie Action-Innovative Training Network project in3 721975
6 · The paper itself

Abstract

P-Glycoprotein (P-gp) is a transmembrane protein belonging to the ATP binding cassette superfamily of transporters, and it is a xenobiotic efflux pump that limits intracellular drug accumulation by pumping compounds out of cells. P-gp contributes to a reduction in toxicity, and has broad substrate specificity. It is involved in the failure of many cancer and antiviral chemotherapies due to the phenomenon of multidrug resistance (MDR), in which the membrane transporter removes chemotherapeutic drugs from target cells. Understanding the details of the ligand-P-gp interaction is therefore critical for the development of drugs that can overcome the MDR phenomenon, for the early identification of P-gp substrates that will help us to obtain a more effective prediction of toxicity, and for the subsequent outdesign of substrate properties if needed. In this work, a series of molecular dynamics (MD) simulations of human P-gp (

Indexed as

Molecular Dynamics SimulationATP Binding Cassette Transporter, Subfamily BBinding SitesHumansHydrogen BondingLigandsModels, MolecularPrincipal Component AnalysisProtein Structure, SecondarySolventsStructure-Activity RelationshipThermodynamicsABCB1 protein, humanATP Binding Cassette Transporter, Subfamily BLigandsSolventsABC transporterconformational changesmolecular dynamics simulationsmultidrug resistance (MDR)P-Glycoprotein

Identifiers

PMID35008783
PMCPMC8745603
OpenAlexW4200169367

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.