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| http://dx.doi.org/10.1172/JCI103246 | DOI Listing |
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Identification of a Novel Stomatal Opening Chemical, PP242, That Inhibits Early Abscisic Acid Signal Transduction in Guard Cells.
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Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa, Nagoya 464-8602, Japan.
Plants control their stomatal apertures to optimize carbon dioxide uptake and water loss. Stomata open in response to light through the phosphorylation of the penultimate residue, Thr, of plasma membrane (PM) H+-ATPase in guard cells. Stomata close in response to drought and the phytohormone abscisic acid (ABA), and ABA suppresses the light-induced activation of PM H+-ATPase.
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January 2025
School of Pharmaceutical Sciences, Hangzhou First People's Hospital, Zhejiang Chinese Medical University, Hangzhou, China.
Background: Nirmatrelvir/ritonavir is licensed for the treatment of mild-to-moderate coronavirus disease (COVID-19) in patients at an increased risk of progression to severe disease. However, data on the real-world plasma exposure to nirmatrelvir/ritonavir remain limited, particularly in Chinese patients. This study aimed to assess the nirmatrelvir/ritonavir trough concentration (Ctrough) and identify its critical factors in hospitalized Chinese patients treated with nirmatrelvir/ritonavir 300 mg/100 mg twice daily over a 5-day course.
View Article and Find Full Text PDFSimultaneous determination of nirmatrelvir, ritonavir, and beta-D-N4-hydroxycytidine in human plasma and epithelial lining fluid using LC-MS/MS and its clinical application to compare rates of achieving effective concentrations.
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January 2025
Department of Pharmacy, Shanghai Changhai Hospital, The First Affiliated Hospital of Naval Medical University, Shanghai, China.
Currently, the trials found that the clinical efficacy of molnupiravir is lower than ritonavir-boosted nirmatrelvir. An explanation for these different efficacies in clinical treatments is still limited. The analysis method was developed and validated to simultaneously quantify nirmatrelvir, ritonavir, and beta-D-N4-hydroxycytidine (NHC) in human plasma and bronchoalveolar lavage fluid (BALF) by electrospray ionization mass spectrometry.
View Article and Find Full Text PDFInteraction and cleavage of cell and plasma proteins by the platelet-aggregating serine protease PA-BJ of Bothrops jararaca venom.
Biochimie
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Laboratory of Applied Toxinology, Center of Toxins, Immune-Response and Cell Signaling (CeTICS), Butantan Institute, São Paulo, Brazil. Electronic address:
PA-BJ is a serine protease present in Bothrops jararaca venom that triggers platelet aggregation and granule secretion by activating the protease-activated receptors PAR-1 and PAR-4, without clotting fibrinogen. These receptors also have a relevant role in endothelial cells, however, the interaction of PA-BJ with other membrane-bound or soluble targets is not known. Here we explored the activity of PA-BJ on endothelial cell receptor, cytoskeleton, and coagulation proteins in vitro, and show the degradation of fibrinogen and protein C, and the limited proteolysis of actin, EPCR, PAR-1, and thrombomodulin.
View Article and Find Full Text PDFCholesterol affects the binding of proteins to phosphatidic acid without influencing its ionization properties.
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Department of Biological Sciences, Kent State University, P.O. Box 5190, Kent, OH 44242, USA. Electronic address:
Phosphatidic acid (PA) through its unique negatively charged phosphate headgroup binds to various proteins to modulate multiple cellular events. To perform such diverse signaling functions, the ionization and charge of PA's headgroup relies on the properties of vicinal membrane lipids and changes in cellular conditions. Cholesterol has conspicuous effects on lipid properties and membrane dynamics.
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