14 research outputs found

    General information, peripheral white blood cell count, outcome, karyotype, and survival time of 15 AML patients with complex karyotype.

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    1<p>WBC were detected at the time of diagnosis;</p>2<p>CR: complete remission;</p>3<p>NT: no treatment;</p>4<p>PR: partial remission;</p>5<p>NR: no remission;</p>6<p>Mon: Month.</p><p>General information, peripheral white blood cell count, outcome, karyotype, and survival time of 15 AML patients with complex karyotype.</p

    Prometaphase and mitotic of MDM4FL and MDM4S-expressing cells.

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    <p>A: Chromosome spread of a prometaphase vector control cell. B: Premature sister chromatid separation in an MDM4S prometaphase cell (indicated by arrows). C: Polyploidy in a MDM4S cell. D: Endoreduplication of a MDM4FL cell.</p

    Cell cycle and cell proliferation analysis.

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    <p>A: DNA content detected by flow cytometry in MDM4FL, MDM4S-expressing or control cells. B: The proportion of G0/G1 phase cells at different time points after Nocodazole treatment. C: Cell proliferation assay. The average percentage of proliferating cells was increased in MDM4FL and MDM4S-expressing cells. *<i>P</i><0.05.</p

    Synthetic Polymer Affinity Ligand for <i>Bacillus thuringiensis</i> (<i>Bt</i>) Cry1Ab/Ac Protein: The Use of Biomimicry Based on the <i>Bt</i> Protein–Insect Receptor Binding Mechanism

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    We report a novel strategy for creating abiotic Bacillus thuringiensis (<i>Bt</i>) protein affinity ligands by biomimicry of the recognition process that takes place between <i>Bt</i> Cry1Ab/Ac proteins and insect receptor cadherin-like Bt-R<sub>1</sub> proteins. Guided by this strategy, a library of synthetic polymer nanoparticles (NPs) was prepared and screened for binding to three epitopes <sup>280</sup>FRGS­AQGI­EGS<sup>290</sup>, <sup>368</sup>RRPF­NIGI­NNQQ<sup>379</sup> and <sup>436</sup>FRSG­FSNS­SVSIIR<sup>449</sup> located in loop α8, loop 2 and loop 3 of domain II of <i>Bt</i> Cry1Ab/Ac proteins. A negatively charged and hydrophilic nanoparticle (NP12) was found to have high affinity to one of the epitopes, <sup>368</sup>RRPF­NIGIN­NQQ<sup>379</sup>. This same NP also had specific binding ability to both <i>Bt</i> Cry1Ab and <i>Bt</i> Cry1Ac, proteins that share the same epitope, but very low affinity to <i>Bt</i> Cry2A, <i>Bt</i> Cry1C and <i>Bt</i> Cry1F closely related proteins that lack epitope homology. To locate possible NP-<i>Bt</i> Cry1Ab/Ac interaction sites, NP12 was used as a competitive inhibitor to block the binding of <sup>865</sup>NITI­HITD­TNNK<sup>876</sup>, a specific recognition site in insect receptor Bt-R<sub>1</sub>, to <sup>368</sup>RRPF­NIGIN­NQQ<sup>379</sup>. The inhibition by NP12 reached as high as 84%, indicating that NP12 binds to <i>Bt</i> Cry1Ab/Ac proteins mainly via <sup>368</sup>RRPF­NIGIN­NQQ<sup>379</sup>. This epitope region was then utilized as a “target” or “bait” for the separation and concentration of <i>Bt</i> Cry1Ac protein from the extract of transgenic <i>Bt</i> cotton leaves by NP12. This strategy, based on the antigen-receptor recognition mechanism, can be extended to other biotoxins and pathogen proteins when designing biomimic alternatives to natural protein affinity ligands
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