Evidence map›Paper›PMID 41099617›Full record

ArticleProtein science : a publication of the Protein Society2025

Quantitative analysis of inhibitor-induced assembly disruption in human UDP-GlcNAc 2-epimerase using mass photometry.

Nico Boback, Jacob Gorenflos López, Christian P R Hackenberger, Santiago Di Lella, Daniel C Lauster

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. 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

5 authors.

Nico BobackFreie Universität Berlin, Institute of Pharmacy, Biopharmaceuticals, Berlin, Germany.ORCID 0009-0003-5261-7168
Jacob Gorenflos LópezLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Christian P R HackenbergerLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Santiago Di LellaUniversidad de Buenos Aires-Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales, Ciudad de Buenos Aires, Argentina.
Daniel C LausterFreie Universität Berlin, Institute of Pharmacy, Biopharmaceuticals, Berlin, Germany.ORCID 0000-0003-2009-633X

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
ANPCyT PICT2021GRF-T1-00403Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) 431232613Federal Ministry of Education and Research 13XP511Joachim Herz FoundationNIGMS NIH HHS R01 GM129325PIP CONICET 11220210100256CO
6 · The paper itself

Abstract

Uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) 2-epimerase (GNE)/N-acetylmannosamine kinase is the rate-limiting enzyme in sialic acid biosynthesis and a promising therapeutic target. We applied mass photometry (MP) to investigate GNE oligomerization and its modulation by three small-molecule inhibitors (C5, C13, and C15). Substrate-binding (UDP-GlcNAc) stabilized tetramer formation by increasing dimer-dimer affinity 98-fold. All inhibitors destabilized tetramers in a concentration-dependent manner, with IC

Indexed as

Carbohydrate EpimerasesEnzyme InhibitorsProtein MultimerizationHumansMolecular Docking SimulationCarbohydrate EpimerasesEnzyme InhibitorsUDP acetylglucosamine-2-epimeraseassembly inhibitionmass photometrymolecular dockingprotein assemblysialic acid biosynthesisUDP‐GlcNAc 2‐epimerase

Identifiers

PMID41099617
PMCPMC12529881

What OpenQuestion holds

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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.