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- MiR-155 and other microRNAs downregulate drug metabolizing cytochromes P450 in inflammationSupplementary data tables to paper "MiR-155 and other microRNAs downregulate drug metabolizing cytochromes P450 in inflammation" by Kugler et al., Biochemical Pharmacolgy, 2019
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- Crystal structure of PDE4D catalytic domain complexed with compound 23a
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- Crystal structure of the P2Y12 receptor in complex with the inverse agonist selatogrel.
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- Crystal structure of the first bromodomain of BRD4 in complex with 16D10
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- Dipyridamole binds to the N-terminal domain of human Hsp90A
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- NMR solution structure of leech peptide HSTX-I
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- CRYSTAL STRUCTURE OF HUMAN PROTECTIVE PROTEIN/CATHEPSIN A, DFP-INHIBITED (AGED)
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- Dataset related to the article "Characterization of aspirin esterase activity in health and disease: in vitro and ex vivo studies"This record contains raw data related to the article “Characterization of aspirin esterase activity in health and disease: In vitro and ex vivo studies" ABSTRACT Due to its ability to irreversibly inactivate platelet cyclooxygenase, low-dose aspirin (ASA) is the most widely used antithrombotic agent. Although, studies in specific types of patients with cardiovascular disease (CVD) have shown an incomplete inhibition of platelet’s cyclooxygenase, which may increase the variability in drug response. Some aspects of ASA pharmacokinetics (PK) still need further investigation. In this study, we aimed to characterise the contribution of esterase enzymes to ASA hydrolysis in the peripheral blood and to assess their activity in 36 healthy subjects (Ctrl) and 77 CVD patients. To this aim, an in vitro assay testing esterase activity in parallel to a liquid chromatography-tandem mass spectrometry method simultaneously detecting ASA and its main metabolites salicylic (SA) and gentisic acids, have been developed. Michaelis-Menten constant (Km) calculation, ASA esterase isoforms characterisation, and ASA PK study were then achieved. The calculated Km identified plasma esterases as the enzymes with the higher affinity for the substrate compared to the RBC ones. Both rivastigmine and 4-bis-nitrophenyl phosphate inhibited plasma esterase activities, suggesting that acetylcholinesterase and carboxylesterase largely contribute to ASA hydrolysis. The feasibility of the method here developed has been explored in Ctrl and CVD patients. The effect of ASA treatment on enzyme activity was further evaluated on an age, sex and BMI matched subgroup of patients and Ctrl (n = 10 for each subgroup, on and off ASA). No overall variations were evidenced in both CVD and Ctrl groups, even when the effect of ASA treatment was tested. This result suggests the absence of any influence of disease state, drug treatments, and comorbidities on plasma esterase and the inability of ASA intake to induce esterase function. In conclusion, the method here developed allows a better characterisation of ASA esterase activity and could be helpful to define the PK-related determinants of ASA responsiveness in order to personalise regimen in specific pathological conditions.
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- Data to support: In silico screening of GMQ-like compounds reveals guanabenz and sephin1 as new allosteric modulators of acid-sensing ion channel 3Raw electrophysiology data to support all figures (Excel file), as well as full statistical analysis of all data (Prism file).
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- Solution structure of delta-theraphotoxin-Hm1b from Heteroscodra maculata
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