Evidence map›Paper›PMID 41879033›Full record

ArticleAngewandte Chemie (International ed. in English)2026

The Isolated Thumb Domain of Acid-Sensing Ion Channels Forms a Minimal Folding Unit Enabling Ligand Binding Studies.

Biswa P Mishra, Ben Cristofori-Armstrong, Elena Budusan, Mimi Golder, Neville J Butcher, Junyu Liu, Theo Crawford, Yanni K-Y Chin, Anneka Pereira Schmidt, Xinying Jia and 5 more

Abstract read
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In one paragraph

Article in Angewandte Chemie (International ed. in English), 2026. 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

15 authors.

Biswa P MishraAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Ben Cristofori-ArmstrongAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Elena BudusanSchool of Biomedical Sciences, The University of Queensland, St Lucia, Queensland, Australia.
Mimi GolderAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Neville J ButcherSchool of Biomedical Sciences, The University of Queensland, St Lucia, Queensland, Australia.
Junyu LiuAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Theo CrawfordAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Yanni K-Y ChinAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Anneka Pereira SchmidtAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Xinying JiaAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.
Taylor B SmallwoodSchool of Biomedical Sciences, The University of Queensland, St Lucia, Queensland, Australia.
Richard J ClarkSchool of Biomedical Sciences, The University of Queensland, St Lucia, Queensland, Australia.
Jan P WurmBruker Biospin, Ettlingen, Germany.
Lachlan D RashSchool of Biomedical Sciences, The University of Queensland, St Lucia, Queensland, Australia.
Mehdi MobliAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, St Lucia, Queensland, Australia.ORCID 0000-0003-2420-4262

Funding

Australian National Health and Medical Research Council APP1067940Australian National Health and Medical Research Council APP1162427Australian National Health and Medical Research Council APP1162597Australian Research Council DP190101177 to M.MDiscovery Early Career Researcher Award (DECRA) DE240101233
6 · The paper itself

Abstract

Proton-gated acid-sensing ion channels (ASICs) are emerging therapeutic targets for ischemia-related conditions such as stroke and myocardial infarction. Although structural data exist for ASIC1a, key aspects of ligand recognition and modulation remain unresolved. Using multidimensional solution-state NMR spectroscopy, we show that the principal ligand-binding region of ASICs, the thumb domain, forms an independently folded unit that at neutral pH adopts a native-like conformation resembling the resting state of the channel. By integrating high-resolution biophysical analyses of ligand binding to the isolated thumb domain with electrophysiological measurements on full-length ASIC1a, we distinguished molecular interactions that determine binding affinity from those governing functional efficacy. This approach revealed that dynorphin A acts as a competitive antagonist of ASIC1a. Furthermore, NMR-based pK

Indexed as

Acid Sensing Ion ChannelsAnimalsBinding SitesHumansHydrogen-Ion ConcentrationLigandsProtein BindingProtein DomainsProtein FoldingAcid Sensing Ion ChannelsLigandsacid‐sensing ion channelselectrophysiologyNMR spectroscopypeptide ligandsprotein structure

Identifiers

PMID41879033
PMCPMC13134594

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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.