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001-es BibID:	BIBFORM086709
035-os BibID:	(WoS)000557707400001 (Scopus)85087574382
Első szerző:	Golda Mária (molekuláris biológus)
Cím:	Biochemical characterization of human retroviral-like aspartic protease 1 (ASPRV1) / Mária Golda, János András Mótyán, Katalin Nagy, Krisztina Matúz, Tibor Nagy, József Tőzsér
Dátum:	2020
ISSN:	2218-273X
Megjegyzések:	The human retroviral-like aspartic protease 1 (ASPRV1) is a mammalian retroviral-like enzyme that catalyzes a critical proteolytic step during epidermal differentiation; therefore, it is also referred as skin-specific aspartic protease (SASPase). Neutrophil granulocytes were also found recently to express ASPRV1 that is involved in the progression of acute chronic in?ammation in the central nervous system, especially in autoimmune encephalomyelitis. Thus, investigation of ASPRV1 is important due to its therapeutic or diagnostic potential. We investigated the structural characteristics of ASPRV1 by homology modeling; analysis of the proposed structure was used for interpretation of in vitro specificity studies. For in vitro characterization, activities of SASP28 and SASP14 enzyme forms were measured using synthetic oligopeptide substrates. We demonstrated that self-processing of SASP28 precursor causes autoactivation of the protease. Highest activity was measured for GST-SASP14 at neutral pH and at high ionic strength, and we proved that pepstatin A and acetyl-pepstatin can also inhibit the protease. In agreement with the structural characteristics, the relatively lower urea dissociation constant implied lower dimer stability of SASP14 compared to that of HIV-1 protease. The obtained structural and biochemical characteristics help better understanding of ASPRV1 function in skin and central nervous system
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk ASPRV1 SASPase protease retroviral-like protease retroviral-like aspartic protease 1 skin-specific aspartic protease homology modeling protease inhibitor
Megjelenés:	Biomolecules. - 10 : 7 (2020), p. 1-25. -
További szerzők:	Mótyán János András (1981-) (biokémikus, molekuláris biológus) Nagy Katalin Matúz Krisztina (1980-) (vegyész, biokémikus) Nagy Tibor (1988-) (vegyész) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00044 GINOP TÁMOP 4.2.2.A-11/1/KONV-2012-0023 TÁMOP TÁMOP-4.2.2.D-15/1/KONV-2015-0016 TÁMOP GINOP-2.3.3-15-2016-00021 GINOP NKFIH-1150-6/2019 Egyéb K-101591 OTKA
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM089970
035-os BibID:	(wos)000602881500001 (scopus)85098234996
Első szerző:	Miczi Márió
Cím:	Identification of Host Cellular Protein Substrates of SARS-COV-2 Main Protease / Márió Miczi, Mária Golda, Balázs Kunkli, Tibor Nagy, József Tőzsér, János András Mótyán
Dátum:	2020
ISSN:	1661-6596 1422-0067
Megjegyzések:	The novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease-19 (COVID-19) being associated with severe pneumonia. Like with other viruses, the interaction of SARS-CoV-2 with host cell proteins is necessary for successful replication, and cleavage of cellular targets by the viral protease also may contribute to the pathogenesis, but knowledge about the human proteins that are processed by the main protease (3CLpro) of SARS-CoV-2 is still limited. We tested the prediction potentials of two different in silico methods for the identification of SARS-CoV-2 3CLpro cleavage sites in human proteins. Short stretches of homologous host-pathogen protein sequences (SSHHPS) that are present in SARS-CoV-2 polyprotein and human proteins were identified using BLAST analysis, and the NetCorona 1.0 webserver was used to successfully predict cleavage sites, although this method was primarily developed for SARS-CoV. Human C-terminal-binding protein 1 (CTBP1) was found to be cleaved in vitro by SARS-CoV-2 3CLpro, the existence of the cleavage site was proved experimentally by using a His6-MBP-mEYFP recombinant substrate containing the predicted target sequence. Our results highlight both potentials and limitations of the tested algorithms. The identification of candidate host substrates of 3CLpro may help better develop an understanding of the molecular mechanisms behind the replication and pathogenesis of SARS-CoV-2.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk host protein cleavage cleavage site prediction cleavage site identification SSHHPS NetCorona COVID-19 SARS SARS-CoV-2 protease 3CL protease coronavirus main protease
Megjelenés:	International Journal Of Molecular Sciences. - 21 : 24 (2020), p. 1-19. -
További szerzők:	Golda Mária (1986-) (molekuláris biológus) Kunkli Balázs (1990-) (bioinformatikus, biokémikus) Nagy Tibor (1988-) (vegyész) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus)
Pályázati támogatás:	GINOP-2.3.3-15-2016-00021 GINOP NKFIH-1150-6/2019 Egyéb
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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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