Tudóstér: Boross Péter publikációi

Tie, Y., Wang, Y., Boross, P., Chiu, T., Ghosh, A., Tőzsér, J., Louis, J., Harrison, R., Weber, I.: Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors.
Protein Sci. 21 (3), 339-350, 2012.

Csősz, É., Boross, P., Csutak, A., Berta, A., Tóth, F., Póliska, S., Török, Z., Tőzsér, J.: Quantitative analysis of proteins in the tear fluid of patients with diabetic retinopathy.
Journal of Proteomics. 75 (7), 2196-2204, 2012.

Boross, P., Bagossi, P., Weber, I., Tőzsér, J.: Drug targets in human T-lymphotropic virus type 1 (HTLV-1) infection.
Inf. Dis. Drug Targets. 9 (2), 159-171, 2009.

Eizert, E., Bander, P., Bagossi, P., Sperka, T., Miklóssy, G., Boross, P., Weber, I., Tőzsér, J.: Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.
J. Virol. 82 (20), 10111-10117, 2008.

Kádas, J., Boross, P., Weber, I., Bagossi, P., Matúz, K., Tőzsér, J.: C-terminal residues of mature human T-lymphotropic virus type 1 protease are critical for dimerization and catalytic activity.
Biochem. J. 416 (3), 357-364, 2008.

Amano, M., Koh, Y., Das, D., Li, J., Leschenko, S., Wang, Y., Boross, P., Weber, I., Ghosh, A., Mitsuya, H.: A novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI), GRL-98065, is potent against multiple-PI-resistant human immunodeficiency virus in vitro.
Antimicrob. Agents Chemother. 51 (6), 2143-2155, 2007.

Tie, Y., Kovalevsky, A., Boross, P., Wang, Y., Ghosh, A., Tőzsér, J., Harrison, R., Weber, I.: Atomic resolution crystal structures of HIV-1 protease and mutants V82A and I84V with saquinavir.
Proteins. 67 (1), 232-242, 2007.

Sperka, T., Miklóssy, G., Tie, Y., Bagossi, P., Zahuczky, G., Boross, P., Matúz, K., Harrison, R., Weber, I., Tőzsér, J.: Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus protease.
J. Gen. Virol. 88 (7), 2052-2063, 2007.

Olivares, I., Mulky, A., Boross, P., Tőzsér, J., Kappes, J., López-Galindez, C., Menéndez-Arias, L.: HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.
J. Mol. Biol. 372 (2), 369-381, 2007.

Wang, Y., Tie, Y., Boross, P., Tőzsér, J., Ghosh, A., Harrison, R., Weber, I.: Potent new antiviral compound shows similar inhibition and structural interactions with drug resistant mutants and wild type HIV-1 protease.
J. Med. Chem. 50 (18), 4509-4515, 2007.

Fehér, A., Boross, P., Sperka, T., Miklóssy, G., Kádas, J., Bagossi, P., Oroszlan, S., Weber, I., Tőzsér, J.: Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease.
J. Gen. Virol. 87 (5), 1321-1330, 2006.

Sperka, T., Boross, P., Eizert, E., Tőzsér, J., Bagossi, P.: Effect of mutations on the dimer stability and the pH optimum of the human foamy virus protease.
Protein Eng. Des. Sel. 19 (8), 369-375, 2006.

Boross, P., Tőzsér, J., Bagossi, P.: Improved purification protocol for wild-type and mutant human foamy virus proteases.
Protein Expr. Purif. 46 (2), 343-347, 2006.

Liu, F., Kovalevsky, A., Louis, J., Wang, Y., Harrison, R., Weber, I., Boross, P.: Mechanism of drug resistance revealed by the crystal structure of the unliganded HIV-1 protease with F53L mutation.
J. Mol. Biol. 358 (5), 1191-1199, 2006.

Fang, B., Boross, P., Tőzsér, J., Weber, I.: Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition.
J. Mol. Biol. 360 (3), 654-666, 2006.

Kovalevsky, A., Tie, Y., Liu, F., Boross, P., Wang, Y., Leschenko, S., Ghosh, A., Harrison, R., Weber, I.: Susceptibility of Potent Antiviral Inhibitor to Highly Drug Resistant Mutations D30N, I50V and L90M of HIV-1 Protease.
J. Med. Chem. 49 (4), 1379-1387, 2006.

Bagossi, P., Sperka, T., Fehér, A., Kádas, J., Zahuczky, G., Miklóssy, G., Boross, P., Tőzsér, J.: Amino Acid Preferences for a Critical Substrate Binding Subsite of Retroviral Proteases in Type 1 Cleavage Sites.
J. Virol. 79 (7), 4213-4218, 2005.

Liu, F., Boross, P., Tőzsér, J., Louis, J., Harrison, R., Weber, I.: Analysis of HIV-1 protease mutants to understand mechanisms of resistance.
FEBS J. 272 (Suppl1), 12, 2005.

Liu, F., Boross, P., Wang, Y., Tőzsér, J., Louis, J., Harrison, R., Weber, I.: Kinetic, Stability, and Structural Changes in High-resolution Crystal Structures of HIV-1 Protease with Drug-resistant Mutations L24I, I50V, and G73S.
J. Mol. Biol. 354 (4), 789-800, 2005.

Tie, Y., Boross, P., Wang, Y., Gaddis, L., Liu, F., Chen, X., Tőzsér, J., Harrison, R., Weber, I.: Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 A angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.
FEBS J. 272 (20), 5265-5277, 2005.

Vana, M., Chen, A., Boross, P., Weber, I., Colman, D., Barklis, E., Leis, J.: Mutations affecting cleavage at the p10-capsid protease cleavage site block Rous sarcoma virus replication.
Retrovirology. 2 (1), 58, 2005.

Mahalingam, B., Wang, Y., Boross, P., Tőzsér, J., Louis, J., Harrison, R., Weber, I.: Crystal structures of HIV protease V82A and L90M mutants reveal changes in the indinavir-binding site.
Eur. J. Biochem. 271 (8), 1516-1524, 2004.

Bagossi, P., Kádas, J., Miklóssy, G., Boross, P., Weber, I., Tőzsér, J.: Development of a microtiter plate fluorescent assay for inhibition studies on the HTLV-1 and HIV-1 proteinases.
J. Virol. Methods. 119 (2), 87-93, 2004.

Fehér, A., Boross, P., Sperka, T., Oroszlan, S., Tőzsér, J.: Expression of the murine leukemia virus protease in fusion with maltose-binding protein in Escherichia coli.
Protein Expr. Purif. 35 (1), 62-68, 2004.

Kádas, J., Weber, I., Bagossi, P., Miklóssy, G., Boross, P., Oroszlan, S., Tőzsér, J.: Narrow Substrate Specificity and Sensitivity toward Ligand-binding Site Mutations of Human T-cell Leukemia Virus Type 1 Protease.
J. Biol. Chem. 279 (26), 27148-27157, 2004.

Tőzsér, J., Shulenin, S., Kádas, J., Boross, P., Bagossi, P., Copeland, T., Nair, B., Sarngadharan, M., Oroszlan, S.: Human immunodeficiency virus type 1 capsid protein is a substrate of the retroviral proteinase while integrase is resistant toward proteolysis.
Virology. 310 (1), 16-23, 2003.

Mahalingam, B., Boross, P., Wang, Y., Louis, J., Fischer, C., Tőzsér, J., Harrison, R., Weber, I.: Combining mutations in HIV-1 protease to understand mechanisms of resistance.
Proteins. 48 (1), 107-116, 2002.

Fehér, A., Weber, I., Bagossi, P., Boross, P., Mahalingam, B., Louis, J., Copeland, T., Torshin, I., Harrison, R., Tőzsér, J.: Effect of sequence polymorphism and drug resistance on two HIV-1 Gag processing sites.
Eur. J. Biochem. 269 (16), 4114-4120, 2002.

Zahuczky, G., Boross, P., Bagossi, P., Emri, G., Copeland, T., Oroszlan, S., Louis, J., Tőzsér, J.: Cloning of the bovine leukemia virus proteinase in Escherichia coli and comparison of its specificity to that of human T-cell leukemia virus proteinase.
Biochim. Biophys. Acta Prot. Struct. Mol. Enzym. 1478 (1), 1-8, 2000.

Tőzsér, J., Bagossi, P., Boross, P., Louis, J., Majerova, E., Oroszlan, S., Copeland, T.: Effect of serine and tyrosine phosphorylation on retroviral proteinase substrates.
Eur. J. Biochem. 265 (1), 423-429, 1999.

Boross, P., Bagossi, P., Copeland, T., Oroszlan, S., Louis, J., Tőzsér, J.: Effect of substrate residues on the P2' preference of retroviral proteinases.
Eur. J. Biochem. 264 (3), 921-929, 1999.

Fenyőfalvi, G., Bagossi, P., Copeland, T., Oroszlan, S., Boross, P., Tőzsér, J.: Expression and characterization of human foamy virus proteinase.
FEBS Lett. 462 (3), 397-401, 1999.

Takács, L., Boross, P., Tőzsér, J., Módis, L., Berta, A.: Transforming growth factor-beta induced protein, betaIG-H3, is present in degraded form and altered localization in lattice corneal dystrophy type I..
Exp. Eye Res. 66 (6), 739-745, 1998.

Nemes, Z., Boross, P., Fésüs, L., Balázs, M., Ádány, R.: Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis.
J. Biol. Chem. 272 (33), 20577-20583, 1997.

Bogáti, M., Pócsi, I., Maticsek, J., Boross, P., Tőzsér, J., Szentirmai, A.: NADP-specific glutamate dehydrogenase of Penicillium chrysogenum has a homohexamer structure.
J. Basic Microbiol. 36 (5), 371-375, 1996.

Nógrády, N., Pócsi, I., Katona, É., Jeney, V., Boross, P., Tőzsér, J., Fachet, J., Szentirmai, A.: Soluble cell-bound and extracellular cyclodextrin glycosyltransferases of Bacillus macerans show identical enzymological characteristics and antigenicity.
J. Basic Microbiol. 36 (5), 335-340, 1996.