ArticleJournal of the American Chemical Society2013
Coupling protein engineering with probe design to inhibit and image matrix metalloproteinases with controlled specificity.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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.
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Who cites it
10 citing papers in PubMed, 36 citations in OpenAlex.
- Matrix metalloproteinase profiling and their roles in disease.RSC advances · 2023Review
- Recent advances in activity-based probes (ABPs) and affinity-based probes (AChemical science · 2021Review
- Chemical Tools for Selective Activity Profiling of Endogenously Expressed MMP-14 in Multicellular Models.ACS chemical biology · 2018Article
- Optimization of a MT1-MMP-targeting Peptide and Its Application in Near-infrared Fluorescence Tumor Imaging.Scientific reports · 2018Article
- Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights.The FEBS journal · 2017Review
- Article
- Applications of small molecule probes in dissecting mechanisms of bacterial virulence and host responses.Biochemistry · 2013Review
- Extracellular matrix determinants and the regulation of cancer cell invasion stratagems.Journal of microscopy · 2013Review
- Engineering to find function.Nature methods · 2013Article
- Moving targets: Emerging roles for MMPs in cancer progression and metastasis.Matrix biology : journal of the International Society for Matrix BiologyReview
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
Matrix metalloproteinases (MMPs) are zinc endopeptidases that play roles in numerous pathophysiological processes and therefore are promising drug targets. However, the large size of this family and a lack of highly selective compounds that can be used for imaging or inhibition of specific MMPs members has limited efforts to better define their biological function. Here we describe a protein engineering strategy coupled with small-molecule probe design to selectively target individual members of the MMP family. Specifically, we introduce a cysteine residue near the active-site of a selected protease that does not alter its overall activity or function but allows direct covalent modification by a small-molecule probe containing a reactive electrophile. This specific engineered interaction between the probe and the target protease provides a means to both image and inhibit the modified protease with absolute specificity. Here we demonstrate the feasibility of the approach for two distinct MMP proteases, MMP-12 and MT1-MMP (or MMP-14).
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Registered trials
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.