TY  - JOUR
AU  - Kuzikov, Maria
AU  - Reinshagen, Jeanette
AU  - Wycisk, Krzysztof
AU  - Corona, Angela
AU  - Esposito, Francesca
AU  - Malune, Paolo
AU  - Manelfi, Candida
AU  - Iaconis, Daniela
AU  - Beccari, Andrea
AU  - Tramontano, Enzo
AU  - Nowotny, Marcin
AU  - Windshügel, Björn
AU  - Gribbon, Philip
AU  - Zaliani, Andrea
TI  - Drug repurposing screen to identify inhibitors of the RNA polymerase (nsp12) and helicase (nsp13) from SARS-CoV-2 replication and transcription complex
JO  - Virus research / Supplement
VL  - 343
SN  - 0168-1702
CY  - Amsterdam
PB  - Elsevier
M1  - PUBDB-2024-05775
SP  - 199356
PY  - 2024
N1  - ISSN 0168-1702 not unique: **2 hits**.
AB  - Coronaviruses contain one of the largest genomes among the RNA viruses, coding for 14–16 non-structural proteins (nsp) that are involved in proteolytic processing, genome replication and transcription, and four structural proteins that build the core of the mature virion. Due to conservation across coronaviruses, nsps form a group of promising drug targets as their inhibition directly affects viral replication and, therefore, progression of infection. A minimal but fully functional replication and transcription complex was shown to be formed by one RNA-dependent RNA polymerase (nsp12), one nsp7, two nsp8 accessory subunits, and two helicase (nsp13) enzymes. Our approach involved, targeting nsp12 and nsp13 to allow multiple starting point to interfere with virus infection progression. Here we report a combined in-vitro repurposing screening approach, identifying new and confirming reported SARS-CoV-2 nsp12 and nsp13 inhibitors. 
LB  - PUB:(DE-HGF)16
C6  - pmid:38490582
UR  - <Go to ISI:>//WOS:001214419000001
DO  - DOI:10.1016/j.virusres.2024.199356
UR  - https://bib-pubdb1.desy.de/record/614235
ER  -