ArticleMethods in molecular biology (Clifton, N.J.)2024
A New Affinity-Based Probe to Profile MMP Active Forms.
Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed, 2 citations in OpenAlex.
- Proximity-Induced Transfer of a Mass Tag Enables Direct Profiling of Active Matrix Metalloproteases.Angewandte Chemie (International ed. in English) · 2026Article
- Covalent Labeling of Matrix Metalloproteases with Affinity-Based Probes Containing Tuned Reactive N-Acyl-N-Alkyl Sulfonamide Cleavable Linkers.Chembiochem : a European journal of chemical biology · 2024Article
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new generation of affinity-based probes (AfBPs) has been developed to label and identity matrix metalloproteinases (MMPs) under their active form in complex proteomes. First, the probe reacts with an active MMP through a proximity-driven reaction that does not require any external trigger. Following this affinity-labeling step, a streptavidin-based enrichment of the resulting biotin-tagged MMP is carried out. Finally, after on-beads proteolytic digestion by trypsin, MMP signature peptides are analyzed and identified by mass spectrometry. Such a "photoactivation-free" labeling can be applied to the detection of several MMPs in a wide variety of biological systems, including in vivo conditions.
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Registered trials
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