Evidence map›Paper›PMID 29097275›Full record

ReviewBiochimica et biophysica acta. Biomembranes2018

Comparison of mechanistic transport cycle models of ABC exporters.

Dániel Szöllősi, Dania Rose-Sperling, Ute A Hellmich, Thomas Stockner

Open access · hybridAbstract readComparative StudyReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Prodrug Approach as a Strategy to Enhance Drug Permeability.Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Interdomain communication in a homodimeric ABC transporter.The Journal of biological chemistry · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. ABCC Transporter GeneJournal of fungi (Basel, Switzerland) · 2023
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 2 countries.

Dániel SzöllősiMedical University of Vienna, Institute of Pharmacology, Waehringerstr. 13A, Vienna 1090, Austria.
Dania Rose-SperlingJohannes Gutenberg-University, Department of Pharmacy and Biochemistry, Johann-Joachim-Becher-Weg 30, Mainz 55128, Germany; Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt, Max von Laue-Str. 9, 60438 Frankfurt am Main, Germany.
Ute A HellmichJohannes Gutenberg-University, Department of Pharmacy and Biochemistry, Johann-Joachim-Becher-Weg 30, Mainz 55128, Germany; Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt, Max von Laue-Str. 9, 60438 Frankfurt am Main, Germany.
Thomas StocknerMedical University of Vienna, Institute of Pharmacology, Waehringerstr. 13A, Vienna 1090, Austria. Electronic address: thomas.stockner@meduniwien.ac.at.
Johannes Gutenberg University Mainz · DEMedical University of Vienna · AT

Funding

Austrian Science Fund FWF F 3524Austrian Science Fund FWF P 23319
6 · The paper itself

Abstract

ABC (ATP binding cassette) transporters, ubiquitous in all kingdoms of life, carry out essential substrate transport reactions across cell membranes. Their transmembrane domains bind and translocate substrates and are connected to a pair of nucleotide binding domains, which bind and hydrolyze ATP to energize import or export of substrates. Over four decades of investigations into ABC transporters have revealed numerous details from atomic-level structural insights to their functional and physiological roles. Despite all these advances, a comprehensive understanding of the mechanistic principles of ABC transporter function remains elusive. The human multidrug resistance transporter ABCB1, also referred to as P-glycoprotein (P-gp), is one of the most intensively studied ABC exporters. Using ABCB1 as the reference point, we aim to compare the dominating mechanistic models of substrate transport and ATP hydrolysis for ABC exporters and to highlight the experimental and computational evidence in their support. In particular, we point out in silico studies that enhance and complement available biochemical data. "This article is part of a Special Issue entitled: Beyond the Structure-Function Horizon of Membrane Proteins edited by Ute Hellmich, Rupak Doshi and Benjamin McIlwain."

Indexed as

Models, BiologicalMolecular Dynamics SimulationProtein ConformationAdenosine TriphosphateAnimalsATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 1Biological TransportHumansProtein BindingAdenosine TriphosphateATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 1ABCB1ABC transporterMechanistic modelsMolecular dynamics simulationsP-glycoproteinTransport cycle

Identifiers

PMID29097275
PMCPMC7610611
OpenAlexW2766922062

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.