ArticleScientific reports2018
Determination of extended substrate specificity of the MALT1 as a strategy for the design of potent substrates and activity-based probes.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A robust fluorogenic substrate for chikungunya virus protease (nsP2) activity.Protein science : a publication of the Protein Society · 2025Article
- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Lessons in Organic Fluorescent Probe Discovery.Chembiochem : a European journal of chemical biology · 2021Review
- Evaluation of the effects of phosphorylation of synthetic peptide substrates on their cleavage by caspase-3 and -7.The Biochemical journal · 2021Article
- Coumarin as a structural component of substrates and probes for serine and cysteine proteases.Biochimica et biophysica acta. Proteins and proteomics · 2020Review
- Leveraging Peptide Substrate Libraries to Design Inhibitors of Bacterial Lon Protease.ACS chemical biology · 2019Article
- Peptide-based covalent inhibitors of MALT1 paracaspase.Bioorganic & medicinal chemistry letters · 2019Article
- Optical Molecular Imaging of Inflammatory Cells in Interventional Medicine-An Emerging Strategy.Frontiers in oncology · 2019Review
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Authors and funding
8 authors.
Funding
Abstract
Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (MALT1) belongs to the CD clan of cysteine proteases. MALT1 is a unique enzyme among this clan because it recognizes the basic amino acid arginine in the P1 pocket. Previous studies carried out with natural amino acids revealed the substrate specificity of the P4-P1 pockets of MALT1 but have provided only limited information about the catalytic preferences of this enzyme. In this study, we exploited Hybrid Combinatorial Substrate Library and Internally Quenched Fluorescence substrate technologies to interrogate the extended substrate specificity profile of the S5-S2' active site pockets using unnatural amino acids. This strategy resulted in the design of a peptide-based fluorogenic substrate, which exhibited significant activity toward MALT1. Subsequently, the substrate sequence was further utilized to develop potent, irreversible activity-based probes.
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