Unlabelled: The enzymes in the Embden-Meyerhof-Parnas pathway of Plasmodium falciparum trophozoites were kinetically characterized and their integrated activities analyzed in a mathematical model. For validation of the model, we compared model predictions for steady-state fluxes and metabolite concentrations of the hexose phosphates with experimental values for intact parasites. The model, which is completely based on kinetic parameters that were measured for the individual enzymes, gives an accurate prediction of the steady-state fluxes and intermediate concentrations. This is the first detailed kinetic model for glucose metabolism in P. falciparum, one of the most prolific malaria-causing protozoa, and the high predictive power of the model makes it a strong tool for future drug target identification studies. The modelling workflow is transparent and reproducible, and completely documented in the SEEK platform, where all experimental data and model files are available for download.
Database: The mathematical models described in the present study have been submitted to the JWS Online Cellular Systems Modelling Database (http://jjj.bio.vu.nl/database/penkler). The investigation and complete experimental data set is available on SEEK (10.15490/seek.1.
Investigation: 56).
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http://dx.doi.org/10.1111/febs.13237 | DOI Listing |
Micromachines (Basel)
December 2024
School of Physics, Changchun University of Science and Technology, Changchun 130012, China.
Tungsten oxide (WO) electrochromic devices are obtaining increasing interest due to their color change and thermal regulation. However, most previous work focuses on the absorption or transmission spectra of materials, rather than the optical parameters evolution in full spectrum in the electrochromic processes. Herein, we developed a systematic protocol of ex situ methods to clarify the evolutions of subtle structure changes, Raman vibration modes, and optical parameters of WO thin films in electrochromic processes as stimulated by dosage-dependent Li insertion.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory, 119991 Moscow, Russia.
Proton-translocating NADH-ubiquinone oxidoreductase (complex I) catalyzes the oxidation of NADH by ubiquinone accompanied by the transmembrane transfer of four protons, thus contributing to the formation of a proton motive force () across the coupling membranes of mitochondria and bacteria, which drives ATP synthesis in oxidative phosphorylation. In recent years, great progress has been achieved in resolving complex I structure by means of X-ray crystallography and high-resolution cryo-electron microscopy, which has led to the formulation of detailed hypotheses concerning the molecular mechanism of coupling of the redox reaction to vectorial proton translocation. To test and probe proposed mechanisms, a comprehensive study of complex I using other methods including molecular dynamics and a variety of biochemical studies such as kinetic and inhibitory analysis is required.
View Article and Find Full Text PDFEntropy (Basel)
December 2024
Istituto Nazionale di Alta Matematica (INdAM), 00185 Rome, Italy.
The status of the Second Law of Thermodynamics, even in the 21st century, is not as certain as when Arthur Eddington wrote about it a hundred years ago. It is not only about the truth of this law, but rather about its strict and exhaustive formulation. In the previous article, it was shown that two of the three most famous thermodynamic formulations of the Second Law of Thermodynamics are non-exhaustive.
View Article and Find Full Text PDFUnlabelled: Eastern equine encephalitis virus (EEEV) is an arthropod-borne, positive-sense RNA alphavirus posing a substantial threat to public health. Unlike similar viruses such as SARS-CoV-2, EEEV replicates efficiently in neurons, producing progeny viral particles as soon as 3-4 hours post-infection. EEEV infection, which can cause severe encephalitis with a human mortality rate surpassing 30%, has no licensed, targeted therapies, leaving patients to rely on supportive care.
View Article and Find Full Text PDFBiotechnol Bioeng
January 2025
Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.
The enzymatic reaction kinetics on cellulose and other solid substrates is limited by the access of the enzyme to the reactive substrate sites. We introduce a general model in which the reaction rate is determined by the active surface area, and the resulting kinetics consequently reflects the evolving relationship between the exposed substrate surface and the remaining substrate volume. Two factors influencing the overall surface-to-volume ratio are considered: the shape of the substrate particles, characterized by a single numerical parameter related to its dimensionality, and the distribution of the particle sizes.
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