Evidence map›Paper›PMID 39960219›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Target Agnostic Photoaffinity Labelling by Sulfonylhydrazones.

Kristóf Garami, Nikolett Péczka, László Petri, Tímea Imre, Tamás Langó, Zoltán Szabó, Zoltán Orgován, Pál Szabó, György Miklós Keserü, Péter Ábrányi-Balogh

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 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. Review
  2. Target Agnostic Photoaffinity Labelling by Sulfonylhydrazones.Angewandte Chemie (International ed. in English) · 2025
    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.

Kristóf GaramiMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.
Nikolett PéczkaMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.
László PetriMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.ORCID 0000-0001-9881-5096
Tímea ImreMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.
Tamás LangóProtein Bioinformatics Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.
Zoltán SzabóDepartment of Medical Chemistry, Albert Szent-Györgyi Medical School, University of Szeged, Dóm tér 8, H-6720, Szeged, Hungary.
Zoltán OrgovánMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.
Pál SzabóNational Drug Research and Development Laboratory, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.
György Miklós KeserüMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.ORCID 0000-0003-1039-7809
Péter Ábrányi-BaloghMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, 1117, Budapest, Hungary.ORCID 0000-0002-9284-5160

Funding

Innovációs és Technológiai Minisztérium ÚNKP-22-5,ÚNKP-23-5Magyar Tudományos Akadémia János Bolyai Research FellowshipMagyar Tudományos Akadémia NAP 3.0National Research, Development and Innovation Office 2020-1.1.6-JÖVŐ-2021-00004National Research, Development and Innovation Office K135150National Research, Development and Innovation Office RRF-2.3.1-21-2022-00015
6 · The paper itself

Abstract

Photoaffinity labeling is a widely used methodology for interrogating small molecule-protein interactions. However, these applications are limited by the few photo-crosslinkers that typically modify the affinity and the binding mode of the original ligand. Here, we report the development of new target agnostic photoaffinity warheads, sulfohydrazones that form a reactive carbene upon UV irradiation. Careful optimization of the reaction conditions allowed us to effectively label five different amino acid residues in proteins. Our approach turned biologically relevant hydrazones and sulfohydrazones to intrinsically irreversible covalent binders without structural modifications by photoactivation as demonstrated on monoamine oxidase A (MAO-A) enzyme and STAT5b (Signal transducer and activator of transcription 5b) transcription factor. Sulfohydrazones are readily accessible by transforming the corresponding carbonyl group of a ligand or a suitable tag that extends the application domain of the method for any ligands exemplified by conditional labelling of the acetylcholine esterase enzyme and the oncogenic mutant of GTP-ase KRas

Indexed as

HydrazonesPhotoaffinity LabelsAcetylcholinesteraseHumansMolecular StructureMonoamine OxidaseAcetylcholinesteraseHydrazonesMonoamine OxidasePhotoaffinity Labelsacetylcholine esteraseKRasphotoaffinitySTATsulfohydrazone

Identifiers

PMID39960219
PMCPMC12015381

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.