Evidence map›Paper›PMID 37438132›Full record

ReviewDrug metabolism and disposition: the biological fate of chemicals2023

How Cryo-EM Has Expanded Our Understanding of Membrane Transporters.

Stefanie A Baril, Tomoka Gose, John D Schuetz

Open access · hybridAbstract readReview
In one paragraph

Review in Drug metabolism and disposition: the biological fate of chemicals, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Cadmium transport by mammalian ATP-binding cassette transporters.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Review
  6. Review
  7. Review
  8. Article
  9. 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 1 institution in 1 country.

Stefanie A BarilDepartment of Pharmacy and Pharmaceutical Sciences, St. Jude Children's Research Hospital, Memphis, Tennessee.ORCID 0000-0003-3249-2866
Tomoka GoseDepartment of Pharmacy and Pharmaceutical Sciences, St. Jude Children's Research Hospital, Memphis, Tennessee.
John D SchuetzDepartment of Pharmacy and Pharmaceutical Sciences, St. Jude Children's Research Hospital, Memphis, Tennessee john.schuetz@stjude.org.
St. Jude Children's Research Hospital · US

Funding

The DNA Damage Response and Tumorigenesis in the BrainP01CA096832 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI BAKER, SUZANNE J. · 2003 to 2025
$38.0M
MRP4 IN DRUG SENSITIVITY AND PHYSIOLOGYR01GM060904 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHUETZ, JOHN D · 2000 to 2012
$4.7M
Transporters and MedulloblastomaR01CA194057 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHUETZ, JOHN D · 2015 to 2025
$4.0M
Transporters and hematopoietic toxicityR01CA194206 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHUETZ, JOHN D · 2016 to 2020
$2.4M
MRP4 in Drug Sensitivity and PhysiologyR56GM060904 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHUETZ, JOHN D · 2008 to 2008
$479k
NCI NIH HHS P01 CA096832NCI NIH HHS P30 CA21745NCI NIH HHS P30 CA21865NCI NIH HHS P30 CA96832NCI NIH HHS R01 CA194057NCI NIH HHS R01 CA194206NIGMS NIH HHS R01 GM060904NIGMS NIH HHS R56 GM060904
6 · The paper itself

Abstract

Over the past two decades, technological advances in membrane protein structural biology have provided insight into the molecular mechanisms that transporters use to move diverse substrates across the membrane. However, the plasticity of these proteins' ligand binding pockets, which allows them to bind a range of substrates, also poses a challenge for drug development. Here we highlight the structure, function, and transport mechanism of ATP-binding cassette/solute carrier transporters that are related to several diseases and multidrug resistance: ABCB1, ABCC1, ABCG2, SLC19A1, and SLC29A1. SIGNIFICANCE STATEMENT: ATP-binding cassette transporters and solute carriers play vital roles in clinical chemotherapeutic outcomes. This paper describes the current understanding of the structure of five pharmacologically relevant transporters and how they interact with their ligands.

Indexed as

ATP-Binding Cassette, Sub-Family C ProteinsMembrane Transport ProteinsATP-Binding Cassette TransportersCryoelectron MicroscopyDrug Resistance, MultipleDrug Resistance, NeoplasmATP-Binding Cassette, Sub-Family C ProteinsATP-Binding Cassette TransportersMembrane Transport Proteins

Identifiers

PMID37438132
PMCPMC10353158
OpenAlexW4384007559

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.