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001-es BibID:	BIBFORM040736
Első szerző:	Kádas János (molekuláris biológus, biokémikus, kertészmérnök)
Cím:	Narrow Substrate Specificity and Sensitivity toward Ligand-binding Site Mutations of Human T-cell Leukemia Virus Type 1 Protease / Kádas J., Weber I. T., Bagossi P., Miklóssy G., Boross P., Oroszlan S., Tözsér J.
Dátum:	2004
ISSN:	0021-9258
Megjegyzések:	Human T-cell leukemia virus type 1 (HTLV-1) is associated with a number of human diseases; therefore, its protease is a potential target for chemotherapy. To compare the specificity of HTLV-1 protease with that of human immunodeficiency virus type 1 (HIV-1) protease, oligopeptides representing naturally occurring cleavage sites in various retroviruses were tested. The number of hydrolyzed peptides as well as the specificity constants suggested a substantially broader specificity of the HIV protease. Amino acid residues of HTLV-1 protease substrate-binding sites were replaced by equivalent ones of HIV-1 protease. Most of the single and multiple mutants had altered specificity and a dramatically reduced folding and catalytic capability, suggesting that mutations are not well tolerated in HTLV-1 protease. The catalytically most efficient mutant was that with the flap residues of HIV-1 protease. The inhibition profile of the mutants was also determined for five inhibitors used in clinical practice and inhibitor analogs of HTLV-1 cleavage sites. Except for indinavir, the HIV-1 protease inhibitors did not inhibit wild type and most of the mutant HTLV-1 proteases. The wild type HTLV-1 protease was inhibited by the reduced peptide bond-containing substrate analogs, whereas the mutants showed various degrees of weakened binding capability. Most interesting, the enzyme with HIV-1-like residues in the flap region was the most sensitive to the HIV-1 protease inhibitors and least sensitive to the HTLV-1 protease inhibitors, indicating that the flap plays an important role in defining the specificity differences of retroviral proteases.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal Of Biological Chemistry. - 279 : 26 (2004), p. 27148-27157. -
További szerzők:	Weber, Irene T. Bagossi Péter (1966-2011) (biokémikus, vegyész) Miklóssy Gabriella (1979-) (biológus, vegyész) Boross Péter (1972-) (biokémikus, vegyész) Oroszlan, Stephen Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM033276
035-os BibID:	WOS:A1997XR22100042
Első szerző:	Nemes Zoltán (molekuláris biológus, pszichiáter)
Cím:	Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis / Zoltán Nemes, Róza Adány, Margit Balázs, Peter Boross, László Fésüs
Dátum:	1997
Megjegyzések:	A lysine derivative, 3-[N-alpha[N-epsilon-[2',4'-dinitrophenyl]-amino-n-hexanoyl-L-lysylamido]-propane-1-ol, a novel amine substrate of transglutaminases, was synthesized and delivered into intact HL-60 and U937 human leukemia cells to probe the function of the intracellular enzyme. The novel substrate compound was covalently incorporated into intracellular proteins in these cells expressing high levels of tissue transglutaminase and undergoing apoptosis following the induction of their differentiation with dimethyl sulfoxide and retinoic acid. Immunoaffinity purification and microsequencing of labeled proteins identified cytoplasmic actin as the main endogenous glutaminyl substrate in these cells. As shown by confocal image analysis, cells revealed distinct labeling of the microfilament meshwork structures by the novel compound as the result of the intracellular action of transglutaminase.
Tárgyszavak:	Orvostudományok Egészségtudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	The Journal of biological chemistry. - 272 : 33 (1997), p. 20577-20583. -
További szerzők:	Boross Péter (1972-) (biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Ádány Róza (1952-) (megelőző orvostan és népegészségtan szakorvos)
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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