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Peptidic mechanism-based inactivators for carboxypeptidase A.
Ghosh SS, Wu YQ, Mobashery S. Ghosh SS, et al. J Biol Chem. 1991 May 15;266(14):8759-64. J Biol Chem. 1991. PMID: 2026592
Effects of Asp-179 mutations in TEMpUC19 beta-lactamase on susceptibility to beta-lactams.
Vakulenko SB, Tóth M, Taibi P, Mobashery S, Lerner SA. Vakulenko SB, et al. Antimicrob Agents Chemother. 1995 Aug;39(8):1878-80. doi: 10.1128/aac.39.8.1878. Antimicrob Agents Chemother. 1995. PMID: 7486939 Free PMC article.
Purification, characterization, and investigation of the mechanism of aminoglycoside 3'-phosphotransferase type Ia.
Siregar JJ, Miroshnikov K, Mobashery S. Siregar JJ, et al. Biochemistry. 1995 Oct 3;34(39):12681-8. doi: 10.1021/bi00039a026. Biochemistry. 1995. PMID: 7548020
Aminoglycoside 3'-phosphotransferases [APH(3')s] are the most common cause of bacterial high-level resistance to aminoglycoside antibiotics in clinical isolates. ...The enzyme phosphorylates its substrates with kcat/Km values of 10(6)-10(8) M-1 s-1, including substr …
Aminoglycoside 3'-phosphotransferases [APH(3')s] are the most common cause of bacterial high-level resistance to aminoglycoside antib …
Purification and characterization of aminoglycoside 3'-phosphotransferase type IIa and kinetic comparison with a new mutant enzyme.
Siregar JJ, Lerner SA, Mobashery S. Siregar JJ, et al. Antimicrob Agents Chemother. 1994 Apr;38(4):641-7. doi: 10.1128/aac.38.4.641. Antimicrob Agents Chemother. 1994. PMID: 8031025 Free PMC article.
Aminoglycoside 3'-phosphotransferase [APH(3')s] provide an important means for high-level resistance to neomycin- and kanamycin-type aminoglycoside antibiotics. ...Modification of the cysteine thiols by S-cyanylation showed essentially no effect on the enzymatic act …
Aminoglycoside 3'-phosphotransferase [APH(3')s] provide an important means for high-level resistance to neomycin- and kanamycin-type …
Reversal of clavulanate resistance conferred by a Ser-244 mutant of TEM-1 beta-lactamase as a result of a second mutation (Arg to Ser at position 164) that enhances activity against ceftazidime.
Imtiaz U, Manavathu EK, Mobashery S, Lerner SA. Imtiaz U, et al. Antimicrob Agents Chemother. 1994 May;38(5):1134-9. doi: 10.1128/aac.38.5.1134. Antimicrob Agents Chemother. 1994. PMID: 8067751 Free PMC article.
S. Bakken, and J. P. Quinn, J. Infect. Dis. 162:460-465, 1990). The doubly mutated derivative of the TEM-1 enzyme (Ser-164/Ser-244) retains the characteristics of the Ser-164 mutant enzyme, i.e., enhanced activity against ceftazidime and sensitivity to inactivation by clav
S. Bakken, and J. P. Quinn, J. Infect. Dis. 162:460-465, 1990). The doubly mutated derivative of the TEM-1 enzyme (Ser-164/Ser-244) r
Critical hydrogen bonding by serine 235 for cephalosporinase activity of TEM-1 beta-lactamase.
Imtiaz U, Manavathu EK, Lerner SA, Mobashery S. Imtiaz U, et al. Antimicrob Agents Chemother. 1993 Nov;37(11):2438-42. doi: 10.1128/aac.37.11.2438. Antimicrob Agents Chemother. 1993. PMID: 8285630 Free PMC article.
Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2.
Olson MW, Gervasi DC, Mobashery S, Fridman R. Olson MW, et al. J Biol Chem. 1997 Nov 21;272(47):29975-83. doi: 10.1074/jbc.272.47.29975. J Biol Chem. 1997. PMID: 9368077
The kinetic parameters for the onset of inhibition are fast (kon approximately 10(5) M-1 s-1) with slow off rates (koff approximately 10(-3) s-1). ...
The kinetic parameters for the onset of inhibition are fast (kon approximately 10(5) M-1 s-1) with slow off rates (koff approximately …
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