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Stereospecific Resistance to N2-Acyl Tetrahydro-β-carboline Antimalarials Is Mediated by a PfMDR1 Mutation That Confers Collateral Drug Sensitivity.
ACS Infect Dis
January 2025
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, United States.
Half the world's population is at risk of developing a malaria infection, which is caused by parasites of the genus . Currently, resistance has been identified to all clinically available antimalarials, highlighting an urgent need to develop novel compounds and better understand common mechanisms of resistance. We previously identified a novel tetrahydro-β-carboline compound, PRC1590, which potently kills the malaria parasite.
View Article and Find Full Text PDFPd-Catalyzed Stereospecific Glycosyl Cross-Coupling of Reversed Anomeric Stannanes for Modular Synthesis of Nonclassical -Glycosides.
Precis Chem
November 2024
Frontiers Science Center for Transformative Molecules (FSCTM), Center for Chemical Glycobiology, Shanghai Key Laboratory for Molecular Engineering of Chiral Drugs, Department of Chemical Biology, School of Chemistry and Chemical Engineering, Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai 200240, P. R. China.
Nonclassical -glycosides, distinguished by their unique glycosidic bond connection mode, represent a promising avenue for the development of carbohydrate-based drugs. However, the accessibility of nonclassical -glycosides hinders broader investigations into their structural features and modes of action. Herein, we present the first example of Pd-catalyzed stereospecific glycosylation of nonclassical anomeric stannanes with aryl or vinyl halides.
View Article and Find Full Text PDFCopper Single-Atom Nanozyme Mimicking Galactose Oxidase with Superior Catalytic Activity and Selectivity.
Small
December 2024
Department of Chemistry, National University of Singapore, 3 Science Drive 3, Singapore, 117543, Singapore.
Due to the low stability and high cost of some natural enzymes, nanozymes have been developed as enzyme-imitating nanomaterials. Single-atom nanozymes are a class of nanozymes with metal centers that mimic the structure of metal-based natural enzymes. Herein, Cu-N-C single-atom nanozyme (SAN) is synthesized with excellent peroxidase- and enhanced oxidase-like activities to mimic the action of natural galactose oxidase.
View Article and Find Full Text PDFThe catalytic action of human d-lactate dehydrogenase is severely inhibited by oxalate and is impaired by mutations triggering d-lactate acidosis.
Arch Biochem Biophys
April 2024
Department of Pharmacy and Biotechnology, University of Bologna, Viale Risorgimento 4, 40136, Bologna, Italy; CSGI, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, FI, Italy. Electronic address:
d-lactate dehydrogenases are known to be expressed by prokaryotes and by eukaryotic invertebrates, and over the years the functional and structural features of some bacterial representatives of this enzyme ensemble have been investigated quite in detail. Remarkably, a human gene coding for a putative d-lactate dehydrogenase (DLDH) was identified and characterized, disclosing the occurrence of alternative splicing of its primary transcript. This translates into the expression of two human DLDH (hDLDH) isoforms, the molecular mass of which is expected to differ by 2.
View Article and Find Full Text PDFEco-friendly approaches to phytochemical production: elicitation and beyond.
Nat Prod Bioprospect
January 2024
Division of Molecular Biology and Genetic Engineering, School of Bioengineering and Biosciences, Lovely Professional University, Phagwara, 144411, India.
Highly ameliorated phytochemicals from plants are recognized to have numerous beneficial effects on human health. However, obtaining secondary metabolites directly from wild plants is posing a great threat to endangered plant species due to their over exploitation. Moreover, due to complicated structure and stereospecificity chemical synthesis of these compounds is a troublesome procedure.
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