Results 1 to 10 of about 23,761 (232)
Copper-transporting ATPase is important for malaria parasite fertility [PDF]
Homeostasis of the trace element copper is essential to all eukaryotic life. Copper serves as a cofactor in metalloenzymes and catalyses electron transfer reactions as well as the generation of potentially toxic reactive oxygen species. Here, we describe
Kenthirapalan, Sanketha +3 more
core +7 more sources
Heme Oxygenase-Like Metalloenzymes. [PDF]
Heme oxygenase (HO)-like metalloenzymes are an emerging protein superfamily diverse in reaction outcome and mechanism. Found primarily in bacterial biosynthetic pathways, members conserve a flexible protein scaffold shared with the heme catabolic enzyme, HO, and a set of metal-binding residues.
Pope SR +6 more
europepmc +4 more sources
identifier:oai:t2r2.star.titech.ac.jp ...
Cathleen Zeymer +2 more
exaly +8 more sources
Targeting Metalloenzymes: The “Achilles’ Heel” of Viruses and Parasites
Metalloenzymes are central to the regulation of a wide range of essential viral and parasitic functions, including protein degradation, nucleic acid modification, and many others.
Dimitrios Moianos +3 more
doaj +1 more source
A series of benzenesulfonamides incorporating pyrazole- and pyridazinecarboxamides decorated with several bulky moieties has been obtained by original procedures.
Andrea Angeli +8 more
doaj +1 more source
Machine Learning Approaches for Metalloproteins
Metalloproteins are a family of proteins characterized by metal ion binding, whereby the presence of these ions confers key catalytic and ligand-binding properties.
Yue Yu, Ruobing Wang, Ruijie D. Teo
doaj +1 more source
Evaluation of Metallo-β-Lactamase Susceptibility Testing in a Physiologic Medium
Research in identifying alternative growth media that better mimic host conditions is gaining ground. Relative to nutrient-rich Mueller-Hinton broth (MHB), data on the influence of physiologic or host-mimicking media on metallo-β-lactamase (MBL ...
Tomefa E. Asempa +4 more
doaj +1 more source
Nitrogenase beyond the Resting State: A Structural Perspective
Nitrogenases have the remarkable ability to catalyze the reduction of dinitrogen to ammonia under physiological conditions. How does this happen? The current view of the nitrogenase mechanism focuses on the role of hydrides, the binding of dinitrogen in ...
Rebeccah A. Warmack, Douglas C. Rees
doaj +1 more source
Selective targeting of proteins by hybrid polyoxometalates: Interaction between a bis-biotinylated hybrid conjugate and avidin [PDF]
The Keggin-type polyoxometalate [\u3b3-SiW10O36]8 12 was covalently modified to obtain a bis-biotinylated conjugate able to bind avidin. Spectroscopic studies such as UV-vis, fluorimetry, circular dichroism, coupled to surface plasmon resonance technique
Alessandra Saccani +12 more
core +2 more sources
Enzymatic functionalization of carbon-hydrogen bonds [PDF]
The development of new catalytic methods to functionalize carbon–hydrogen (C–H) bonds continues to progress at a rapid pace due to the significant economic and environmental benefits of these transformations over traditional synthetic methods.
Arnold, Frances H. +2 more
core +1 more source

