Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Kok-Fui Liew"'
Autor:
Saravanan S. R. Sundaramurthy, Kristen E. Allen, Mark A. Fletcher, Kok Fui Liew, Boekhtiar Borhanuddin, Mohammad Ali, Graciela Morales, Bradford Gessner, Jerusha Naidoo, Jo Southern
Publikováno v:
BMC Infectious Diseases, Vol 24, Iss 1, Pp 1-8 (2024)
Abstract Background Pneumococcal disease caused by Streptococcus pneumoniae is an important cause of morbidity and mortality across all ages, particularly in younger children and older adults. Here, we describe pneumococcal disease hospitalizations a
Externí odkaz:
https://doaj.org/article/ba4615a9d3e54778a172e4d8d67fdee4
Publikováno v:
Bioorganic Chemistry. 135:106509
Publikováno v:
Journal of Pharmaceutical Sciences. 106:502-510
Previously, several aurone derivatives were identified with promising neuroprotective activities. In developing these compounds to target the central nervous system (CNS), an assessment of their blood-brain barrier (BBB) permeability was performed us
Autor:
Mingshi Yang, Prajakta Tambe, Yasir Faraz Abbasi, Dongmei Cun, Kok-Fui Liew, Hriday Bera, Abul Kalam Azad, Pramod Kumar, Virendra Gajbhiye
Publikováno v:
Materials Science and Engineering: C. 110:110628
The current study dealt with the synthesis and characterization of carboxymethyl fenugreek galactomannang-g-poly(N-isopropylacrylamide-co-N,N′-methylene-bis-acrylamide)-bentonite [CFG-g-P(NIPA-co-MBA)-BEN] based nanocomposites (NCs) as erlotinib (E
Publikováno v:
Biomedicine & Pharmacotherapy, Vol 110, Iss, Pp 118-128 (2019)
Previously, a series of aurones bearing amine and carbamate functionalities was synthesized and evaluated for their cholinesterase inhibitory activity and drug-like attributes. In the present study, these aurones were evaluated for their multi-target
Publikováno v:
European journal of medicinal chemistry. 94
A series of novel aurones bearing amine and carbamate functionalities at various positions (rings A and/or B) of the scaffold was synthesized and evaluated for their acetylcholinesterase and butyrylcholinesterase inhibitory activities. Structure–ac