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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:	BIBFORM091549
035-os BibID:	(cikkazonosító)127
Első szerző:	Kassay Norbert (biotechnológus)
Cím:	Biochemical Characterization, Specificity and Inhibition Studies of HTLV-1, HTLV-2, and HTLV-3 Proteases / Kassay Norbert, Mótyán János András, Matúz Krisztina, Golda Mária, Tőzsér József
Dátum:	2021
ISSN:	2075-1729
Megjegyzések:	The human T-lymphotropic viruses (HTLVs) are causative agents of severe diseases including adult T-cell leukemia. Similar to human immunodeficiency viruses (HIVs), the viral protease (PR) plays a crucial role in the viral life-cycle via the processing of the viral polyproteins. Thus, it is a potential target of anti-retroviral therapies. In this study, we performed in vitro comparative analysis of human T-cell leukemia virus type 1, 2, and 3 (HTLV-1, -2, and -3) proteases. Amino acid preferences of S4 to S1· subsites were studied by using a series of synthetic oligopeptide substrates representing the natural and modified cleavage site sequences of the proteases. Biochemical characteristics of the different PRs were also determined, including catalytic efficiencies and dependence of activity on pH, temperature, and ionic strength. We investigated the effects of different HIV-1 PR inhibitors (atazanavir, darunavir, DMP-323, indinavir, ritonavir, and saquinavir) on enzyme activities, and inhibitory potentials of IB-268 and IB-269 inhibitors that were previously designed against HTLV-1 PR. Comparative biochemical analysis of HTLV-1, -2, and -3 PRs may help understand the characteristic similarities and differences between these enzymes in order to estimate the potential of the appearance of drug-resistance against specific HTLV-1 PR inhibitors.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk human T-lymphotropic virus human T-cell leukemia virus HTLV HTLV-1 HTLV-2 HTLV-3 protease retroviral protease protease inhibitor inhibitor HIV protease inhibitor
Megjelenés:	Life. - 11 : 2 (2021), p. 1-21. -
További szerzők:	Mótyán János András (1981-) (biokémikus, molekuláris biológus) Matúz Krisztina (1980-) (vegyész, biokémikus) Golda Mária (1986-) (molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00044 GINOP 125238 OTKA TÁMOP 4.2.2.A-11/1/KONV-2012-0023 TÁMOP TÁMOP-4.2.2.D-15/1/KONV-2015-0016 TÁMOP TKP2020-IKA-04 Egyéb
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