Results 91 to 100 of about 44,257 (116)
Acetate uptake alleviates propionate-mediated growth restriction in <i>Yersinia enterocolitica</i>. [PDF]
Muramatsu MK +3 more
europepmc +1 more source
Paromomycin is a more effective selection agent than kanamycin in Arabidopsis harboring the neomycin phosphotransferase II transgene. [PDF]
Goodman CP +3 more
europepmc +1 more source
Photosystem I-independent oxygenic photosynthesis in cyanobacteria
Leister D +15 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Talanta, 2023
It is of significance to develop efficient methods for detecting the activity of T4 polynucleotide kinase (T4 PNK) due to its essential role in the modulation of different life activities. In this work, we constructed a novel nanozyme using Kanamycin (KANA) as a trigger for the [Fe(CN)6]3- coordinated Cu2(OH)3NO3 (Cu2(OH)3NO3/[Fe(CN)6]3-) nanorods, and
Guangli Wang, Xiuming Wu
exaly +3 more sources
It is of significance to develop efficient methods for detecting the activity of T4 polynucleotide kinase (T4 PNK) due to its essential role in the modulation of different life activities. In this work, we constructed a novel nanozyme using Kanamycin (KANA) as a trigger for the [Fe(CN)6]3- coordinated Cu2(OH)3NO3 (Cu2(OH)3NO3/[Fe(CN)6]3-) nanorods, and
Guangli Wang, Xiuming Wu
exaly +3 more sources
Biochemistry, 1996
Bacterial resistance to the aminoglycoside antibiotics is manifested primarily through the production of enzymes which covalently modify these drugs. The Enterococci and Staphylococci produce an ATP-dependent kinase, APH(3')-IIIa, which phosphorylates such antibiotics as kanamycin, amikacin, and neomycin, and this enzyme shows a Theorell-Chance kinetic
G A, McKay, G D, Wright
openaire +2 more sources
Bacterial resistance to the aminoglycoside antibiotics is manifested primarily through the production of enzymes which covalently modify these drugs. The Enterococci and Staphylococci produce an ATP-dependent kinase, APH(3')-IIIa, which phosphorylates such antibiotics as kanamycin, amikacin, and neomycin, and this enzyme shows a Theorell-Chance kinetic
G A, McKay, G D, Wright
openaire +2 more sources
Crystallographic studies on two structures of a kanamycin kinase: a Mg-AMPPNP and a Mg-ADP complex.
19983',5"-aminoglycoside phosphotransferase type IIIa (APH(3')-IIIa) belongs to a family of bacterial enzymes that phosphorylate the aminoglycoside antibiotics. The modified antibiotics are rendered ineffective due to a lowered affinity for their targets in the bacterial cells.
openaire +1 more source

