Evidence map›Paper›PMID 40226990›Full record

ArticleACS chemical biology2025

Identification of Rapaglutin E as an Isoform-Specific Inhibitor of Glucose Transporter 1.

Marnie Kotlyar, Zufeng Guo, A V Subba Rao, Hanjing Peng, Jingxin Wang, Zhongnan Ma, Cordelia Schiene-Fischer, Gunter Fischer, Jun O Liu

Abstract read
In one paragraph

Article in ACS chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Marnie KotlyarChemistry Biology Interface Graduate Program, Johns Hopkins University, Baltimore, Maryland 21218, United States.
Zufeng GuoDepartment of Pharmacology, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, United States.
A V Subba RaoDepartment of Pharmacology, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, United States.
Hanjing PengDepartment of Pharmacology, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, United States.
Jingxin WangDepartment of Pharmacology, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, United States.
Zhongnan MaDepartment of Pharmacology, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, United States.ORCID 0000-0003-1457-0330
Cordelia Schiene-FischerDepartment of Enzymology, Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany.
Gunter FischerMax Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany.
Jun O LiuChemistry Biology Interface Graduate Program, Johns Hopkins University, Baltimore, Maryland 21218, United States.ORCID 0000-0003-3842-9841

Funding

Translational Research Central ServicesP30CA006973 · NCI · JOHNS HOPKINS UNIVERSITY · PI WILLIAM George NELSON · 1985 to 2026
$208.6M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM149382 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI STEVEN E ROKITA · 2023 to 2026
$1.4M
Targeting Glucose Transporters Using RapafucinsR01GM137319 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LIU, JUN O. · 2020 to 2023
$1.3M
Acquisition of a 500 MHz NMR Spectrometer to Support Small-Molecule Chemistry at Johns Hopkins Medical SchoolS10OD034217 · OD · JOHNS HOPKINS UNIVERSITY · PI BHAT, SHRIDHAR · 2024 to 2024
$425k
NCI NIH HHS P30 CA006973NIGMS NIH HHS R01 GM137319NIGMS NIH HHS T32 GM080189NIGMS NIH HHS T32 GM149382NIH HHS S10 OD034217
6 · The paper itself

Abstract

Natural products rapamycin and FK506 are macrocyclic compounds with therapeutic benefits whose unique scaffold inspired the generation and exploration of hybrid macrocycle rapafucins. From this library, a potent inhibitor of the facilitative glucose transporter (GLUT), rapaglutin A (RgA), was previously identified. RgA is a pan-GLUT inhibitor of Class I isoforms GLUT1, GLUT3, and GLUT4. Herein, we report the discovery of rapaglutin E (RgE). Unlike RgA, RgE is highly specific for GLUT1. Further characterization revealed that RgE and RgA likely bound to distinct sites on GLUT1 despite their shared FKBP-binding domain, suggesting that the distinct effector domains of RgE and RgA play key roles in the recognition of GLUTs.

Indexed as

Glucose Transporter Type 1HumansProtein IsoformsGlucose Transporter Type 1Protein Isoforms

Identifiers

PMID40226990
PMCPMC12210310

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Registered trials

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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.