Evidence map›Paper›PMID 40001557›Full record

ArticleBiomolecules2025

Enhanced Site-Specific Fluorescent Labeling of Membrane Proteins Using Native Nanodiscs.

Bence Ezsias, Felix Wolkenstein, Nikolaus Goessweiner-Mohr, Rohit Yadav, Christine Siligan, Sandra Posch, Andreas Horner, Carolyn Vargas, Sandro Keller, Peter Pohl

Abstract read
In one paragraph

Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

10 authors.

Bence EzsiasInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.ORCID 0009-0002-8665-4410
Felix WolkensteinInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.ORCID 0009-0001-0202-3383
Nikolaus Goessweiner-MohrInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.ORCID 0000-0002-6572-5606
Rohit YadavInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.
Christine SiliganInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.ORCID 0000-0001-8294-1960
Sandra PoschInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.ORCID 0000-0003-4400-5412
Andreas HornerInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.ORCID 0000-0002-5328-1745
Carolyn VargasBiophysics, Institute of Molecular Biosciences (IMB), NAWI Graz, University of Graz, Humboldtstr. 50/III, 8010 Graz, Austria.
Sandro KellerBiophysics, Institute of Molecular Biosciences (IMB), NAWI Graz, University of Graz, Humboldtstr. 50/III, 8010 Graz, Austria.ORCID 0000-0001-5469-8772
Peter PohlInstitute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria.ORCID 0000-0002-1792-2314

Funding

FWF Austrian Science Fund TAI181
6 · The paper itself

Abstract

Fluorescent labeling of membrane proteins is essential for exploring their functions, signaling pathways, interaction partners, and structural dynamics. Organic fluorophores are commonly used for this purpose due to their favorable photophysical properties and photostability. However, a persistent challenge is the inaccessibility of the surface-exposed cysteine residues required for site-specific labeling, as these residues often become sequestered within detergent micelles during protein extraction. To address this limitation, we developed an approach based on polymer-encapsulated nanodiscs that preserves the protein's native-like lipid-bilayer environment while ensuring the accessibility of surface-exposed cysteine residues. In this method, His-tagged proteins embedded in native nanodiscs are retained on a nickel affinity column, allowing for simultaneous purification and labeling by adding fluorescent dyes. This versatile technique was demonstrated with two challenging-to-label membrane proteins, the potassium channel KvAP and the urea channel

Indexed as

Fluorescent DyesMembrane ProteinsNanostructuresCysteineLipid BilayersStaining and LabelingCysteineFluorescent DyesLipid BilayersMembrane Proteinselectrophysiologyfluorescence correlation spectroscopypotassium channelurea channel

Identifiers

PMID40001557
PMCPMC11852578

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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.