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ProteomicsBiochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro (XL-MS)
SARS-CoV-2, a human coronavirus, is the causative agent of the COVID-19 pandemic, entailing enormous disruption worldwide. Its ~30 kb RNA genome is translated into two large polyproteins subsequently cleaved by viral papain-like protease and main protease (Mpro/nsp5). Polyprotein processing is essen...
ORGANISM(S): Severe acute respiratory syndrome coronavirus 2 
2022-12-19 | PXD033748 | Pride
Nsp7-8 Xl-ms Nsp7-11 Mpro Sars-cov-2 Polyprotein 
ProteomicsBiochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro (HDX-MS pulse labeling)
SARS-CoV-2, a human coronavirus, is the causative agent of the COVID-19 pandemic, entailing enormous disruption worldwide. Its ~30 kb RNA genome is translated into two large polyproteins subsequently cleaved by viral papain-like protease and main protease (Mpro/nsp5). Polyprotein processing is essen...
ORGANISM(S): Severe acute respiratory syndrome coronavirus 2 
2022-12-19 | PXD033702 | Pride
Pulse labeling Hdx-ms Mpro Sars-cov-2 Polyprotein 
ProteomicsBiochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro (HDX-MS continuous labeling)
SARS-CoV-2, a human coronavirus, is the causative agent of the COVID-19 pandemic, entailing enormous disruption worldwide. Its ~30 kb RNA genome is translated into two large polyproteins subsequently cleaved by viral papain-like protease and main protease (Mpro/nsp5). Polyprotein processing is essen...
ORGANISM(S): Severe acute respiratory syndrome coronavirus 2 
2022-12-19 | PXD033698 | Pride
Hdx-ms Mpro Sars-cov-2 Polyprotein Continuous labeling 
ProteomicsThe kinetics of nsp7-11 polyprotein processing and impact on complexation with nsp16 among human coronaviruses
In coronavirus (CoV) infection, polyproteins (pp1a/pp1ab) are processed into non-structural proteins (nsps), which largely form the replication/transcription complex (RTC). The polyprotein processing and complex formation is critical and offers potential therapeutic targets. However, the interplay o...
ORGANISM(S): Escherichia coli 
2025-07-08 | PXD049009 | Pride
Mass spectrometry Sars-cov-2 Kinetics Native ms Rate constants Complexation 
UnknownHallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes.
Not available
S-EPMC7929516 | biostudies-literature
UnknownHallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes.
Not available
S-EPMC7536876 | biostudies-literature
Unknown1H, 13C, and 15N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7.
Not available
S-EPMC7678775 | biostudies-literature
UnknownBio-Chemoinformatics-Driven Analysis of nsp7 and nsp8 Mutations and Their Effects on Viral Replication Protein Complex Stability.
Not available
S-EPMC10968879 | biostudies-literature
UnknownIn silico analysis of RNA-dependent RNA polymerase of the SARS-CoV-2 and therapeutic potential of existing antiviral drugs.
Not available
S-EPMC8220294 | biostudies-literature
UnknownProcessing of the SARS-CoV pp1a/ab nsp7-10 region.
Not available
S-EPMC7078746 | biostudies-literature
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