Evidence map›Paper›PMID 41698924›Full record

ArticleNature communications2026

Amino acid and viral binding by the high-affinity Cationic Amino acid Transporter 1 (CAT1) from Mus musculus.

Mingda Ye, Zhu Liang, Daming Zhou, Ashley C W Pike, SiYi Wang, Dong Wang, Souvika Bakshi, Laurent Brooke, Eleanor P Williams, Jonathan M Elkins and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

13 authors.

Mingda YeCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-6324-4238
Zhu LiangCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-8223-5003
Daming ZhouChinese Academy of Medical Sciences Oxford Institute, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Ashley C W PikeCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-9661-2607
SiYi WangCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Dong WangCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-7379-357X
Souvika BakshiCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Laurent BrookeCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0009-0003-7425-4978
Eleanor P WilliamsCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-1331-9518
Jonathan M ElkinsCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Benedikt M KesslerCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-8160-2446
David I StuartChinese Academy of Medical Sciences Oxford Institute, Nuffield Department of Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3426-4210
David B SauerCentre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK. david.sauer@cmd.ox.ac.uk.ORCID http://orcid.org/0000-0001-9291-4640

Funding

Chinese Academy of Medical Sciences (CAMS) 2024-I2M-2-001-1Innovative Medicines Initiative (IMI) 807015Innovative Medicines Initiative (IMI) 875510
6 · The paper itself

Abstract

Arginine, lysine, and ornithine are critical to several fundamental aspects of organismal physiology, including protein structure and function, the urea cycle, and intracellular signaling. These cationic amino acids are imported by several membrane transporters, most notably the Cationic Amino acid Transporters (CATs) in the SLC7 family. Of these, CAT1 is also the receptor for two orthoretroviruses, and determines the host tropism for these viruses. Here, using a combination of CryoEM and in vitro biochemical techniques, we characterize the substrate recognition and transport of CAT1 from Mus musculus. Further, by determining the structures of MmCAT1 in complex with the receptor binding domain from the Friend Murine Leukemia Virus, we identify the key structural interactions that determine the virus' rodent-specific tropism.

Indexed as

Amino AcidsCationic Amino Acid Transporter 1AnimalsCryoelectron MicroscopyLeukemia Virus, MurineMiceProtein BindingAmino AcidsCationic Amino Acid Transporter 1

Identifiers

PMID41698924
PMCPMC13022406

What OpenQuestion holds

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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.