Zobrazeno 1 - 10
of 39
pro vyhledávání: '"F. J. KEZDY"'
Publikováno v:
Analytical Biochemistry. 239:20-24
A rapid and simple method for quantitating the reaction product of UDP-GalNAc:polypeptide, N -acetylgalactosaminyltransferase (GalNAc-transferase) by scintillation proximity assay (SPA) was developed. The assay quantitates the radioactivity incorpora
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba3f8da6a2692204bf59546e2f3f7751
https://doi.org/10.1006/abio.1996.0285
https://doi.org/10.1006/abio.1996.0285
Publikováno v:
Analytical Biochemistry. 221:217-230
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbfc8b57091082cb0b2b607478dcc636
https://doi.org/10.1006/abio.1994.1405
https://doi.org/10.1006/abio.1994.1405
Autor:
Martin R. Deibel, M E Busso, L Resnick, Kuo-Chen Chou, Irene W. Althaus, F. J. Kezdy, A G So, James J. Chou, Donna Lee Romero, A. J. Gonzales
Publikováno v:
Journal of Biological Chemistry. 268:14875-14880
The quinoline U-78036 represents a new class of non-nucleoside human immunodeficiency virus (HIV)-1 reverse transcriptase inhibitors. The agent possesses excellent antiviral activity at nontoxic doses in HIV-1-infected lymphocytes grown in tissue cul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4aef2463cbdf083b031d15bcb052be15
https://doi.org/10.1016/s0021-9258(18)82414-0
https://doi.org/10.1016/s0021-9258(18)82414-0
Autor:
Roger A. Poorman, J G Hoogerheide, Maggiora Linda Louise, Erika T. Brown, F. J. Kezdy, Ake P. Elhammer
Publikováno v:
Journal of Biological Chemistry. 268:10029-10038
The acceptor substrate specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) was inferred from the amino acid sequences surrounding 196 O-glycosylation sites extracted from the National Biomedical Research Found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bf7ee35c39a222bbc88cb06783e0dfa9
https://doi.org/10.1016/s0021-9258(18)82168-8
https://doi.org/10.1016/s0021-9258(18)82168-8
Autor:
Kuo-Chen Chou, Fritz Reusser, Paul A. Aristoff, Martin R. Deibel, Donna Lee Romero, W G Tarpley, James J. Chou, F. J. Kezdy, A. J. Gonzales, Irene W. Althaus
Publikováno v:
Journal of Biological Chemistry. 268:6119-6124
The multifunctional HIV-1 RT (human immunodeficiency virus type 1-reverse transcriptase) enzyme possesses three main functions including the RNA- and DNA-directed DNA polymerases and the RNase H. The bisheteroarylpiperazine U-87201E inhibits the two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc7978499374a2f6406dd698b0435424
https://doi.org/10.1016/s0021-9258(18)53227-0
https://doi.org/10.1016/s0021-9258(18)53227-0
Publikováno v:
Journal of Biological Chemistry. 267:18413-18418
The pH dependence of the kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants has been determined. These data have permitted the calculation of two active-site ionization constants in the free enzymes (pKe1 and pK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::adf066d508d14a532ced687fa8197f4f
https://doi.org/10.1016/s0021-9258(19)36978-9
https://doi.org/10.1016/s0021-9258(19)36978-9
Publikováno v:
Journal of Biological Chemistry. 267:27-30
The bisheteroarylpiperazines (BHAPs) are potent inhibitors of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and specifically block HIV-1 replication (Romero, D. L., Busso, M., Tan, C.-K., Reusser, F., Palmer, J. R., Poppe, S.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::671bb9be8aca97a8a014c4533e619044
https://doi.org/10.1016/s0021-9258(18)48451-7
https://doi.org/10.1016/s0021-9258(18)48451-7
Publikováno v:
Journal of Biological Chemistry. 266:24359-24366
Human immunodeficiency virus type 1 (HIV-1) protease optimally catalyzes in the pH range of 4-6 in contrast to nearly all of the other eukaryotic aspartic proteases, which catalyze best in the pH range of 2-4. A possible structural reason for the hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::731565bcf801f81819b451ef078f0e51
https://doi.org/10.1016/s0021-9258(18)54237-x
https://doi.org/10.1016/s0021-9258(18)54237-x
Publikováno v:
Journal of Biological Chemistry. 266:15591-15594
Human immunodeficiency virus 1 (HIV-1) protease is an aspartyl protease composed of two identical protomers linked by a four-stranded antiparallel beta-sheet consisting of the NH2- and COOH-terminal segments (Weber, I.T. (1990) J. Biol. Chem. 265, 10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aaf6cbbb41acaf652b55e4412c54d49c
https://doi.org/10.1016/s0021-9258(18)98445-0
https://doi.org/10.1016/s0021-9258(18)98445-0
Publikováno v:
Journal of Biological Chemistry. 266:14554-14561
Statistical analysis of an expanded data base of regions in viral polyproteins and in non-viral proteins that are sensitive to hydrolysis by the protease from human immunodeficiency virus (HIV) type 1 has generated a model which characterizes the sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd05167decd79df2d7ee2d16f705c432
https://doi.org/10.1016/s0021-9258(18)98722-3
https://doi.org/10.1016/s0021-9258(18)98722-3