17 research outputs found

    On the vanishing of the coefficients of CM eta quotients

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    This work characterizes the vanishing of the Fourier coefficients of all CM (Complex Multiplication) eta quotients. As consequences, we recover Serre’s characterization about that of η(12z)2 and recent results of Chang on the pth coefficients of η(4z)6 and η(6z)4 . Moreover, we generalize the results on the cases of weight 1 to the setting of binary quadratic forms

    Comparative pharmacokinetics of free doxorubicin and a liposomal formulation in cats following intravenous administration

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    Doxorubicin, a potent chemotherapeutic agent used extensively in cancer treatment, displays complex pharmacokinetic behavior, especially across various formulations. With a rising incidence of cancer cases in cats, understanding the drug’s pharmacokinetics in feline subjects remains a critical yet unexplored area. Hence, this study investigated the pharmacokinetic profile of doxorubicin after slow intravenous administration of doxorubicin hydrochloride (DOX·HCl) or doxorubicin hydrochloride pegylated liposome (DOX·HCl-PLI) in twelve cats at a single dose of 20 mg/m2. Blood samples collected at pretreatment time (0 h) and over 192 h were analyzed using ultra-performance liquid chromatography-mass spectrometry (UPLC-MS/MS). The obtained pharmacokinetic parameters of doxorubicin revealed significant differences between the two formulations and were as follows: elimination half-life (T1/2λz) of 5.00 ± 3.20 h (DOX·HCl) and 17.62 ± 8.13 h (DOX·HCl-PLI), area under the concentration/time curve from 0 to last point (AUClast) of 0.67 ± 0.12 μg hr./mL (DOX·HCl) and 783.09 ± 267.29 μg hr./mL (DOX·HCl-PLI), and total body clearance (CL_obs) of 27098.58 ± 5205.19 mL/h/m2 (DOX·HCl) and 28.65 ± 11.09 mL/h/m2 (DOX·HCl-PLI). Additionally, differences were also detected in the apparent volume of distribution (Vz_obs) with 178.56 ± 71.89 L/m2 (DOX·HCl) and 0.64 ± 0.20 L/m2 (DOX·HCl-PLI), and the maximum plasma concentration (Cmax) with 2.25 ± 0.30 μg/mL (DOX·HCl) and 24.02 ± 5.45 μg/mL (DOX·HCl-PLI). Notably, low concentration of doxorubicinol, the metabolite of doxorubicin, was detected in plasma after administration of DOX·HCl, with even less present when DOX·HCl-PLI was administered. This investigation provides valuable insights into the distinct pharmacokinetic behaviors of DOX·HCl and DOX·HCl-PLI in cats, contributing essential groundwork for future studies and potential clinical applications in feline oncology

    The BCL2 gene is regulated by a special AT-rich sequence binding protein 1-mediated long range chromosomal interaction between the promoter and the distal element located within the 3′-UTR

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    The 279-bp major breakpoint region (mbr) within the 3′-untranslated region (3′-UTR) of the BCL2 gene is a binding site of special AT-rich sequence binding protein 1 (SATB1) that is well known to participate in the long-range regulation of gene transcription. Our previous studies have revealed that the mbr could regulate BCL2 transcription over a 200-kb distance and this regulatory function was closely related to SATB1. This study is to explore the underlying mechanism and its relevance to cellular apoptosis. With chromosome conformation capture (3C) and chromatin immunoprecipitation (ChIP) assays we demonstrated that the mbr could physically interact with BCL2 promoter through SATB1-mediated chromatin looping, which was required for epigenetic modifications of the promoter, CREB accessibility and high expression of the BCL2 gene. During early apoptosis, SATB1 was a key regulator of BCL2 expression. Inhibition of SATB1 cleavage by treatment of cells with a caspase-6 inhibitor or overexpression of mutant SATB1 that was resistant to caspase-6, inhibited disassembly of the SATB1-mediated chromatin loop and restored the BCL2 mRNA level in Jurkat cells. These data revealed a novel mechanism of BCL2 regulation and mechanistically link SATB1-mediated long-range interaction with the regulation of a gene controlling apoptosis pathway for the first time

    Tetrakis(dimethoxyboryl)methane

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    The title compound, tetrakis(dimethoxyboryl)methane (systematic name: octamethyl methanetetrayltetraboronate), C9H24B4O8 or C[B(OMe)2]4, is a useful synthetic intermediate. Crystals of this compound at 102 K conform to the orthorhombic space group Pbcn. The molecules, which reside on sites of crystallographic twofold symmetry, have idealized -4 point symmetry like most other CX4 molecules in which each X group bears two non-H substituents at the 1-position. The central C atom has a slightly distorted tetrahedral coordination geometry, with C—B bond lengths of 1.5876 (16) and 1.5905 (16) Å. One of the methoxy groups is disordered over two sets of sites; the major component has an occupancy factor of 0.676 (8)

    Preparation and spectroscopic properties of Ca

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    Various novel Ca2MgTeO6:Tm3+ blue-emitting tellurate materials were synthesized via solid-state reaction. The structure and phase purity of prepared Ca2MgTeO6:xTm3+ (x = 0.0025-0.10 mol) were examined by X-ray powder diffraction. The Ca2MgTeO6:Tm3+ phosphors emit blue emission at 359 nm excitation. The optimum doping concentration was 0.02 mol. The concentration quenching mechanism in the Ca2MgTeO6 host was due to the electric dipole-dipole interaction. The The CIE chromaticity coordinates of Ca2MgTeO6:Tm3+ phosphors located in the blue region. These results validated the Ca2MgTeO6:Tm3+ tellurate phosphor can be used as good blue-emitting candidate for W-LEDs

    Highly Efficient Synthesis of 2,5-Dihydroxypyridine using <i>Pseudomonas</i> sp. ZZ-5 Nicotine Hydroxylase Immobilized on Immobead 150

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    In this report, the use of immobilized nicotine hydroxylase from Pseudomonas sp. ZZ-5 (HSPHZZ) for the production of 2,5-dihydroxypyridine (2,5-DHP) from 6-hydroxy-3-succinoylpyridine (HSP) in the presence of nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FAD) is described. HSPHZZ was covalently immobilized on Immobead 150 (ImmHSPHZZ). ImmHSPHZZ (obtained with 5&#8315;30 mg of protein per gram of support) catalyzed the hydrolysis of HSP to 2,5-DHP. At a protein loading of 15 mg g&#8722;1, ImmHSPHZZ converted 93.6% of HSP to 2,5-DHP in 6 h. The activity of ImmHSPHZZ was compared with that of free HSPHZZ under various conditions, including pH, temperature, enzyme concentration, substrate concentration and stability over time, and kinetic parameters were measured. The results showed that ImmHSPHZZ performed better over wider ranges of pH and temperature when compared with that of HSPHZZ. The optimal concentrations of ImmHSPHZZ and substrate were 30 mg L&#8722;1 and 0.75 mM, respectively. Under optimal conditions, 94.5 mg L&#8722;1 of 2,5-DHP was produced after 30 min with 85.4% conversion. After 8 reaction cycles and 6 days of storage, 51.3% and 75.0% of the initial enzyme activity remained, respectively. The results provide a framework for development of commercially suitable immobilized enzymes that produce 2,5-DHP

    Additional file 1 of Characteristics of human papillomavirus prevalence and infection patterns among women aged 25–64 according to age groups and cytology results in Ordos City, China

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    Additional file 1.  eTable 1. Prevalence of different HPV genotypes infection by age group. eTable 2. Prevalence of different HPV genotypes infection by cytology results
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