Results 51 to 60 of about 217,358 (308)

Prediction of Inhibition Activity of Dihydrofolate Reductase Inhibitors With Multivariate Adaptive Regression Splines

IEEE Access, 2023
Dihydrofolate reductase (DHFR) enzyme is a crucial component of cell growth and proliferation in the human body, making it an important target for treating cancer diseases.
Zanib Qayyum, Tahir Mehmood, Laila A. Al-Essa   +2 more
doaj   +1 more source

Trypanosoma brucei DHRF-TS revisited:characterisation of a bifunctional and highly unstable recombinant dihydrofolate reductase-thymidylate synthase [PDF]

, 2016
Bifunctional dihydrofolate reductase–thymidylate synthase (DHFR-TS) is a chemically and genetically validated target in African trypanosomes, causative agents of sleeping sickness in humans and nagana in cattle.
A Dawson, A El Fadili, A Khodursky, AJ Wahba, AJ Wahba, AL Jackman, Alan H. Fairlamb, B Nare, BJ Dolnick, C Fraser-Lhostis, C Shih, CJ Allegra, CW Carreras, D Spinks, DC Jones, E Wirtz, EJ Shanks, EL White, F Gamarro, FW Studier, H Zhang, Han B. Ong, HB Ong, J Phan, J Yuvaniyama, JA Frearson, Jayne Raper, JF Morrison, JM Blaney, JR Appleman, K Al Chalabi, KY Han, LM Changchien, LS Torrie, M Berriman, M Hekmat-Nejad, Marc W. Gibson, MM Bradford, N Greig, N Sienkiewicz, N Sienkiewicz, Natasha Sienkiewicz, ND Brunn, P Prapunwattana, P Reche, PH Liang, R Ferone, R Grumont, RA Copeland, RC Jackson, RD Walter, RJ Bonney, RJ Cisneros, S Shallom, SA Margosiak, SE Webber, SF Chowdhury, SI Ahmad, Simon Dewar, SM Lanham, TC Eadsforth, TD Meek, TW Synold, Y Cheng   +63 more
core   +3 more sources

Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase

Biochemistry, 2015
Homotetrameric R67 dihydrofolate reductase possesses 222 symmetry and a single active site pore. This situation results in a promiscuous binding site that accommodates either the substrate, dihydrofolate (DHF), or the cofactor, NADPH. NADPH interacts more directly with the protein as it is larger than the substrate.
Duff, Michael R., Chopra, Shaileja, Strader, Michael Brad, Agarwal, Pratul K., Howell, Elizabeth E.   +4 more
openaire   +2 more sources

Novel 3D‐Printed Biophotonic Scaffold Displaying Luminescence under Near‐Infrared Light for Photopharmacological Activation and Biological Signaling Compound Release

Advanced Healthcare Materials, EarlyView.
Despite significant efforts in developing novel biomaterials to regenerate tissue, only a few of them have successfully reached clinical use. It has become clear that the next generation of biomaterials must be multifunctional. Smart biomaterials can respond to environmental or external stimuli, interact in a spatial‐temporal manner, and trigger ...
Sonya Ghanavati, Ekin Opar, Virginia Alessandra Gobbo, Carlo Matera, Fabio Riefolo, Rossella Castagna, Julien Colombelli, Andrew Draganski, Joshua Baggott, Mika Lastusaari, Pau Gorostiza, Laeticia Petit, Jonathan Massera   +12 more
wiley   +1 more source

Import of honeybee prepromelittin into the endoplasmic reticulum [PDF]

, 1987
Honeybee prepromelittin is correctly processed and imported by dog pancreas microsomes. Insertion of prepromelittin into microsomal membranes, as assayed by signal sequence removal, does not depend on signal recognition particle (SRP) and docking protein.
Müller, Günter, Zimmermann, Richard
core   +2 more sources

Polimorfismo de deleção de 19 pares de bases do gene dihidrofolato redutase (DHFR): risco materno para síndrome de Down e metabolismo do folato [PDF]

, 2010
CONTEXT AND OBJECTIVE: Polymorphisms in genes involved in folate metabolism may modulate the maternal risk of Down syndrome (DS). This study evaluated the influence of a 19-base pair (bp) deletion polymorphism in intron-1 of the dihydrofolate reductase ...
BISELLI, Joice Matos, CARVALHO, Valdemir Melechco, EBERLIN, Marcos Nogueira, GOLONI-BERTOLLO, Eny Maria, HADDAD, Renato, MENDES, Cristiani Cortez, PAVARINO-BERTELLI, Érika Cristina, RICCIO, Maria Francesca, VANNUCCHI, Hélio, ZAMPIERI, Bruna Lancia   +9 more
core   +1 more source

Affinity chromatography of dihydrofolate reductase [PDF]

Biochemical Journal, 1971
1. Dihydrofolate reductase was purified from Lactobacillus casei MTX/R, and studied on affinity columns containing folic acid and methotrexate. Two forms of the enzyme were interconverted by incubation with substrates. 2. Affinity columns were prepared from agarose activated with cyanogen bromide and coupled with 1,6-diaminohexane.
P C, Newbold, N G, Harding
openaire   +2 more sources

Evolution Alters the Enzymatic Reaction Coordinate of Dihydrofolate Reductase

Journal of Physical Chemistry B, 2014
How evolution has affected enzyme function is a topic of great interest in the field of biophysical chemistry. Evolutionary changes from Escherichia coli dihydrofolate reductase (ecDHFR) to human dihydrofolate reductase (hsDHFR) have resulted in ...
J. E. Masterson, S. Schwartz
semanticscholar   +1 more source

Export of honeybee prepromelittin in Escherichia coli depends on the membrane potential but does not depend on proteins secA and secY [PDF]

, 1989
Honeybee prepromelittin (70 amino acid residues), the precursor of an eukaryotic secretory protein, and a hybrid protein between prepromelittin and mouse dihydrofolate reductase (257 amino acid residues) were expressed in Escherichia coli and ...
Cobet, Werner W. E., Mollay, Christa, Müller, Günter, Zimmermann, Richard   +3 more
core  

para-Aminosalicylic Acid Is a Prodrug Targeting Dihydrofolate Reductase in Mycobacterium tuberculosis♦

Journal of Biological Chemistry, 2013
Background: PAS is an antimycobacterial whose mechanism(s) of action remains elusive. Results: PAS is incorporated into the folate pathway by DHPS-DHFS, generating an anti-metabolite. DHFS and RibD are associated with PAS resistance. Conclusion: Hydroxyl
Jun Zheng, E. Rubin, P. Bifani, V. Mathys, Vivian Lim, M. Au, Jichan Jang, Jiyoun Nam, T. Dick, J. Walker, Kevin Pethe, Luis R. Camacho   +11 more
semanticscholar   +1 more source