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001-es BibID:	BIBFORM108752
035-os BibID:	(Scopus)85148962397 (WoS)000938549700001
Első szerző:	Miltner Noémi (molekuláris biológus)
Cím:	Identification of SARS-CoV-2 Main Protease (Mpro) Cleavage Sites Using Two-Dimensional Electrophoresis and In Silico Cleavage Site Prediction / Noémi Miltner, Gergő Kalló, Éva Csősz, Márió Miczi, Tibor Nagy, Mohamed Mahdi, János András Mótyán, József Tőzsér
Dátum:	2023
ISSN:	1422-0067
Megjegyzések:	The main protease (Mpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) plays a crucial role in its life cycle. The Mpro-mediated limited proteolysis of the viral polyproteins is necessary for the replication of the virus, and cleavage of the host proteins of the infected cells may also contribute to viral pathogenesis, such as evading the immune responses or triggering cell toxicity. Therefore, the identification of host substrates of the viral protease is of special interest. To identify cleavage sites in cellular substrates of SARS-CoV-2 Mpro, we determined changes in the HEK293T cellular proteome upon expression of the Mpro using two-dimensional gel electrophoresis. The candidate cellular substrates of Mpro were identified by mass spectrometry, and then potential cleavage sites were predicted in silico using NetCorona 1.0 and 3CLP web servers. The existence of the predicted cleavage sites was investigated by in vitro cleavage reactions using recombinant protein substrates containing the candidate target sequences, followed by the determination of cleavage positions using mass spectrometry. Unknown and previously described SARS-CoV-2 Mpro cleavage sites and cellular substrates were also identified. Identification of target sequences is important to understand the specificity of the enzyme, as well as aiding the improvement and development of computational methods for cleavage site prediction.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk coronavirus SARS-CoV-2 main protease Mpro COVID-19 two-dimensional gel electrophoresis cleavage site identification cleavage site prediction protease host protein cleavage specificity
Megjelenés:	International Journal Of Molecular Sciences. - 24 : 4 (2023), p. 1-19. -
További szerzők:	Kalló Gergő (1989-) (molekuláris biológus) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Miczi Márió Nagy Tibor (1988-) (vegyész) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs) Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	GINOP-2.3.3-15-2016-00020 GINOP GINOP-2.3.3-15-2016-00021 GINOP
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001-es BibID:	BIBFORM130745
035-os BibID:	(Scopus)105009019976 (wos)001516039100001
Első szerző:	Mótyán János András (biokémikus, molekuláris biológus)
Cím:	Identification of SARS-CoV-2 Main Protease Cleavage Sites in Bovine β-Casein / Mótyán János András, Nagy Tibor, Nagyné Veres Ágota, Golda Mária, Mahdi Mohamed, Tőzsér József
Dátum:	2025
ISSN:	1661-6596 1422-0067
Megjegyzések:	The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the coronavirus disease of 2019 (COVID-19) and has persistently caused infections since its emergence in late 2019. The main protease (Mpro) of SARS-CoV-2 plays a crucial role in its life-cycle; thus, it is an important target for drug development. One of the first virus-specific drugs that has been approved for the treatment of COVID-19 patients is Paxlovid, which contains nirmatrelvir, a covalent inhibitor of Mpro. Screening of inhibitor candidates and specificity studies also rely on efficient substrates and activity assays. Casein is one of the most commonly applied universal substrates that can be used to study a wide range of proteases, including SARS-CoV-2 Mpro. Casein is a known substrate for Mpro in vitro, but the specific casein isoform cleaved by Mpro remained unidentified, and the cleavage sites have yet to be determined. This work studied cleavage of ?-, ?- and ?-isoforms of bovine casein by SARS-CoV-2 Mpro, using in vitro and in silico approaches. The candidate cleavage sites were predicted in silico based on the protein sequences, and the cleavage positions were identified based on mass spectrometric analysis of cleavage fragments. Based on our results, only ?-casein contains cleavage sites for Mpro and thus can be used as its substrate in vitro. The newly identified cleavage site sequences further widen the knowledge about the specificity of SARS-CoV-2 Mpro.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk SARS-CoV-2 main protease coronavirus casein protease cleavage site substrate specificity cleavage site prediction proteolyis
Megjelenés:	International Journal Of Molecular Sciences. - 26 : 12 (2025), p. 1-11. -
További szerzők:	Nagy Tibor (1988-) (vegyész) Veres Ágota (laboráns) Golda Mária (1986-) (molekuláris biológus) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	TKP2021-EGA-20 Egyéb TKP2021-NKTA-34 Egyéb NKFIH Advanced 150532 Egyéb BO/00110/23/5 MTA University of Debrecen (UD) Program for Scientific Publication Egyéb UD Faculty of Medicine Research Fund (Bridging fund) Egyéb UD Scientific Research Bridging Fund (DETKA) Egyéb
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