ArticleRSC advances2026
Bidirectional crosstalk between the catalytic and moonlighting functions of human dipeptidyl peptidase 3: potential physiological implications.
Article in RSC advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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10 authors.
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Abstract
Dipeptidyl peptidase 3 (DPP3) is a ubiquitously expressed zinc-exopeptidase involved in oligopeptide degradation. Beyond its catalytic role, DPP3 exhibits a moonlighting role in the Keap1-Nrf2 signalling pathway, where it promotes Nrf2-dependent gene transcription through an ETGE motif-mediated interaction with the Kelch domain of Keap1. This highlights its role in oxidative stress and cancer, as persistent pathway activation supports tumour cell survival, oxidative stress resistance, and proliferation. While DPP3's catalytic activity is not required for Keap1 binding, the effects of enzyme inactivation on this interaction, and
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