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Substrate profiling of mitochondrial caseinolytic protease P via a site‐specific photocrosslinking approach
TA Nguyen, TF Gronauer, T Nast‐Kolb… - Angewandte Chemie …, 2022 - Wiley Online Library
Approaches for profiling protease substrates are critical for defining protease functions, but
remain challenging tasks. We combine genetic code expansion, photocrosslinking and …
remain challenging tasks. We combine genetic code expansion, photocrosslinking and …
Acyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state
B Eyermann, M Meixner, H Brötz‐Oesterhelt… - …, 2020 - Wiley Online Library
Caseinolytic protease P (ClpP) is a tetradecameric peptidase that assembles with
chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) are small …
chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) are small …