Results 21 to 30 of about 125,417 (229)

Should I Stay or Should I Go—Leveraging an Overlooked Feature of Click‐to‐Release Chemistry for Affinity Labeling

Angewandte Chemie, EarlyView.
Click‐to‐release (C2R) chemistry is redirected from payload liberation toward ligand‐directed covalent protein labeling through a transient dihydropyridazine methide (DHP‐methide). This concept opens the way to dual‐functional systems combining covalent target engagement with controlled effector release.
Dóra Kern, Krisztina Németh, Tímea Imre, József Simon, Kitti Meggyes, Gergő Bárdos, László Petri, Márton Bojtár, Attila Kormos, Péter Kele   +9 more
wiley   +2 more sources

DHFR (dihydrofolate reductase) [PDF]

, 2016
Dihydrofolate reductase (DHFR) is a member of the reductase enzyme family, which is ubiquitously expressed in all organisms. Levels of this enzyme peak at the G1/S cell cycle boundary. Autoregulation, through DHFR-RNA interactions, has also been reported.
Krajinovic, Maja, Abaji, Rachid, Sharif-Askari, Bahram   +2 more
core   +1 more source

MOLECULAR SURVEILLANCE OF Plasmodium vivax AND Plasmodium falciparum DHFR MUTATIONS IN ISOLATES FROM SOUTHERN IRAN

Revista do Instituto de Medicina Tropical de São Paulo, 2016
In Iran, both Plasmodium vivax and P. falciparum malaria have been detected, but P. vivax is the predominant species. Point mutations in dihydrofolate reductase (dhfr) gene in both Plasmodia are the major mechanisms of pyrimethamine resistance.
Khojasteh SHARIFI-SARASIABI, Ali HAGHIGHI, Bahram KAZEMI, Niloofar TAGHIPOUR, Ehsan Nazemalhosseini MOJARAD, Latif GACHKAR   +5 more
doaj   +1 more source

A trimethoprim derivative impedes antibiotic resistance evolution

Nature Communications, 2021
The efficacy of the antibiotic trimethoprim, which inhibits bacterial dihydrofolate reductase (DHFR), is limited by the rapid emergence of resistant bacteria. Here, Manna et al.
Madhu Sudan Manna, Yusuf Talha Tamer, Ilona Gaszek, Nicole Poulides, Ayesha Ahmed, Xiaoyu Wang, Furkan C. R. Toprak, DaNae R. Woodard, Andrew Y. Koh, Noelle S. Williams, Dominika Borek, Ali Rana Atilgan, John D. Hulleman, Canan Atilgan, Uttam Tambar, Erdal Toprak   +15 more
doaj   +1 more source

Stretching exercises — flexibility in dihydrofolate reductase catalysis [PDF]

, 1998
As an enzyme, dihydrofolate reductase performs two tasks: transformation of its substrate dihydrofolate or folate to tetrahydrofolate, using NADPH as a cofactor, and regeneration of the enzyme for a subsequent round of catalysis.
Benkovic, Stephen J., Miller, Grover Paul   +1 more
core   +1 more source

A novel bicyclic 2,4-diaminopyrimidine inhibitor of Streptococcus suis dihydrofolate reductase [PDF]

PeerJ, 2021
Streptococcus suis is a Gram-positive bacterial pathogen of pigs and an emerging zoonotic pathogen. It has become increasingly resistant to multiple classes of antibiotics.
Warangkhana Songsungthong, Sunisa Prasopporn, Louise Bohan, Potjanee Srimanote, Ubolsree Leartsakulpanich, Suganya Yongkiettrakul   +5 more
doaj   +2 more sources

A calibration curve for immobilized dihydrofolate reductase activity assay

Data in Brief, 2015
An assay was developed for measuring the active-site concentration, activity, and thereby the catalytic turnover rate (kcat) of an immobilized dihydrofolate reductase model system (Singh et al., (2015), Anal. Biochem).
Priyanka Singh, Holly Morris, Alexei V. Tivanski, Amnon Kohen   +3 more
doaj   +1 more source

High prevalence of dhfr triple mutant and correlation with high rates of sulphadoxine-pyrimethamine treatment failures in vivo in Gabonese children. [PDF]

, 2011
BACKGROUND: Drug resistance contributes to the global malaria burden. Plasmodium falciparum dihydrofolate reductase (dhfr) and dihydropteroate synthase (dhps) polymorphisms confer resistance to sulphadoxine-pyrimethamine (SP). METHODS: The study assessed
Gabor, Julian J., Profanter, K., Grobusch, Martin P., Kurth, F., Grobusch, Martin P, Gabor, J.J., Gabor Julian J, Oyakhirome, Sunny, Oyakhirome, S., Kun, Jürgen FJ, Greutélaers, Benedikt, Jürgen FJ Kun, Grobusch Martin P, Kremsner, P.G., Issifou, Saadou, Kun, Jürgen F. J., Grobusch, M.P., Saadou Issifou, Issifou, S., Roper, C., Ord, Rosalynn, Roper, Cally, Mombo-Ngoma, Ghyslain, Peter G Kremsner, Greutélaers, K.C., Kremsner, Peter G., Katharina Profanter, Martin P Grobusch, Sunny Oyakhirome, Lell, Bertrand, Greutélaers, B., Greutélaers, Katja C., Greutélaers, Katja C, Kurth, Florian, Julian J Gabor, Rosalynn Ord, Mombo-Ngoma, G., Cally Roper, Florian Kurth, Issifou Saadou, Mombo-Ngoma Ghyslain, Ord Rosalynn, Gabor, Julian J, Oyakhirome Sunny, Kremsner, Peter G, Kun Jürgen FJ, Katja C Greutélaers, Ghyslain Mombo-Ngoma, Kurth Florian, Greutélaers Benedikt, Roper Cally, Profanter Katharina, Kun, J.F.J., Kremsner Peter G, Bertrand Lell, Lell Bertrand, Benedikt Greutélaers, Lell, B., Ord, R., Greutélaers Katja C, Profanter, Katharina   +60 more
core   +2 more sources

Trimethoprim: An Old Antibacterial Drug as a Template to Search for New Targets. Synthesis, Biological Activity and Molecular Modeling Study of Novel Trimethoprim Analogs

Molecules, 2019
A new series of trimethoprim (TMP) analogs containing amide bonds (1−6) have been synthesized. Molecular docking, as well as dihydrofolate reductase (DHFR) inhibition assay were used to confirm their affinity to bind dihydrofolate reductase enzyme.
Agnieszka Wróbel, Dawid Maliszewski, Maciej Baradyn, Danuta Drozdowska   +3 more
doaj   +1 more source

Synthesis, Molecular Docking Study, and Biological Evaluation of New 4-(2,5-Dimethyl-1H-pyrrol-1-yl)-N’-(2-(substituted)acetyl)benzohydrazides as Dual Enoyl ACP Reductase and DHFR Enzyme Inhibitors

Antibiotics, 2023
In this study, a new series of 4-(2,5-dimethyl-1H-pyrrol-1-yl)-N’-(2-(substituted)acetyl) benzohydrazides (5a–n) were prepared and new heterocycles underwent thorough characterization and evaluation for antibacterial activity; some of them underwent ...
Mater H. Mahnashi, Pooja Koganole, Prem Kumar S. R., Sami S. Ashgar, Ibrahim Ahmed Shaikh, Shrinivas D. Joshi, Ali S. Alqahtani   +6 more
doaj   +1 more source