Evidence map›Paper›PMID 40649897›Full record

ReviewInternational journal of molecular sciences2025

ABCG2 Transporter: From Structure to Function-Current Insights and Open Questions.

Laura Álvarez-Fernández, Alicia Millán-García, Gracia Merino, Esther Blanco-Paniagua

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. 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.

Laura Álvarez-FernándezDepartment of Biomedical Sciences-Physiology, Faculty of Veterinary Medicine, Instituto de Desarrollo Ganadero y Sanidad Animal (INDEGSAL), University of León, Campus de Vegazana s/n, 24071 León, Spain.ORCID 0000-0002-0313-4034
Alicia Millán-GarcíaDepartment of Biomedical Sciences-Physiology, Faculty of Veterinary Medicine, Instituto de Desarrollo Ganadero y Sanidad Animal (INDEGSAL), University of León, Campus de Vegazana s/n, 24071 León, Spain.ORCID 0009-0008-6619-6428
Gracia MerinoDepartment of Biomedical Sciences-Physiology, Faculty of Veterinary Medicine, Instituto de Desarrollo Ganadero y Sanidad Animal (INDEGSAL), University of León, Campus de Vegazana s/n, 24071 León, Spain.ORCID 0000-0002-7620-3475
Esther Blanco-PaniaguaDepartment of Biomedical Sciences-Physiology, Faculty of Veterinary Medicine, Instituto de Desarrollo Ganadero y Sanidad Animal (INDEGSAL), University of León, Campus de Vegazana s/n, 24071 León, Spain.ORCID 0000-0001-8334-1094

Funding

Junta de Castilla y Leon and European Regional Development Fund LE033P24Ministry of Science and Innovation (Spain) PID2021-125660OB-100Ministry of Science, Innovation, and Universities (Spain) FPU23/00153
6 · The paper itself

Abstract

ABCG2 is a crucial ATP-binding cassette (ABC) transporter involved in multidrug resistance and essential physiological and pharmacological processes. In recent years, multiple ABCG2 structures have been resolved using cryo-electron microscopy (cryo-EM), providing significant insights into its conformational states during its transport cycle. However, even more than 25 years after its description, a high-resolution X-ray crystallographic structure is still unavailable, limiting the understanding of its dynamic transitions, as well as leaving aspects of the transport cycle unresolved and open to discussion. Given the complexity of ABCG2, a multidisciplinary approach is essential in order to fully elucidate its mechanism. This review compiles recent advances in ABCG2 structural biology, highlights unresolved controversies, and explores future directions to bridge the gap between structure and function. Moving forward, integrating multiple structural and functional approaches will be key to uncovering the intricate workings of this enigmatic transporter. In particular, detailed structural insights will be crucial to identifying new ABCG2 substrates and designing selective inhibitors, with important implications for therapeutic development.

Indexed as

ATP Binding Cassette Transporter, Subfamily G, Member 2Neoplasm ProteinsAnimalsCryoelectron MicroscopyDrug Resistance, MultipleHumansModels, MolecularProtein ConformationABCG2 protein, humanATP Binding Cassette Transporter, Subfamily G, Member 2Neoplasm ProteinsABCG2conformationstructuretransport

Identifiers

PMID40649897
PMCPMC12250437

What OpenQuestion holds

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LicenceCC BY
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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.