Studies on the selectivity of the SARS-CoV-2 papain-like protease reveal the importance of the P2' proline of the viral polyprotein
The SARS-CoV-2 papain-like protease (PLpro) is an antiviral drug target that catalyzes the hydrolysis of the viral polyproteins pp1a/1ab, so releasing the non-structural proteins (nsps) 1–3 that are essential for the coronavirus lifecycle. The LXGG↓X motif in pp1a/1ab is crucial for recognition and...
Main Authors: | Chan, HTH, Brewitz, L, Lukacik, P, Strain-Damerell, C, Walsh, MA, Schofield, CJ, Duarte, F |
---|---|
Format: | Journal article |
Language: | English |
Published: |
Royal Society of Chemistry
2023
|
Similar Items
-
Mass spectrometric assays monitoring the deubiquitinase activity of the SARS-CoV-2 papain-like protease inform on the basis of substrate selectivity and have utility for substrate identification
by: Brewitz, L, et al.
Published: (2023) -
Mass spectrometric assays reveal discrepancies in inhibition profiles for the SARS-CoV-2 papain-like protease
by: Brewitz, L, et al.
Published: (2022) -
Penicillin derivatives inhibit the SARS-CoV-2 main protease by reaction with its nucleophilic cysteine
by: Malla, TR, et al.
Published: (2022) -
Insights into the Dynamics and Binding of Two Polyprotein Substrate Cleavage Points in the Context of the SARS-CoV-2 Main and Papain-like Proteases
by: Zainab Kemi Sanusi, et al.
Published: (2022-11-01) -
Mass spectrometry reveals potential of β-lactams as SARS-CoV-2 Mpro inhibitors.
by: Malla, TR, et al.
Published: (2021)