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<title>National Centre for Biomedical Engineering Science (Conference Papers)</title>
<link>http://hdl.handle.net/10379/82</link>
<description/>
<pubDate>Mon, 30 Oct 2017 00:11:11 GMT</pubDate>
<dc:date>2017-10-30T00:11:11Z</dc:date>
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<title>Surface chemistry and linker effects on lectin-carbohydrate recognition for glycan microarrays</title>
<link>http://hdl.handle.net/10379/3544</link>
<description>Surface chemistry and linker effects on lectin-carbohydrate recognition for glycan microarrays
Kilcoyne, Michelle; Gerlach, Jared Q.; Kane, Marian; Joshi, Lokesh
Glycan microarrays are an increasingly utilised tool for analysis of protein-carbohydrate interactions and a variety of glycan-containing molecules and slide chemistries have been used to array carbohydrates on microarray surfaces. Slide surface chemistry can have significant impact on the ligand presentation, background noise, spot size and morphology and reproducibility of the arrayed molecules, which in turn impacts upon lectin-carbohydrate recognition. The linker used to attach the carbohydrate to the molecular scaffold is another variable in ligand presentation. To evaluate these effects, three different microarray surface chemistries were arrayed with the same mono-and disaccharide neoglycoconjugates and natural glycoproteins and incubated with four well-characterised plant lectins. Analogues of three monosaccharide neoglycoconjugates, with two common linkers each, were included in the test group to evaluate the linker effect on lectin recognition. Based on lowest background noise, expected lectin-ligand interaction, good spot morphology and best reproducibility, the three-dimensional hydrogel slide surface proved most suitable for lectin interrogation of carbohydrate ligands, and the more flexible phenylisothiocyanate linker afforded greater recognition of the carbohydrates by the relevant lectins.
</description>
<pubDate>Sun, 01 Jan 2012 00:00:00 GMT</pubDate>
<guid isPermaLink="false">http://hdl.handle.net/10379/3544</guid>
<dc:date>2012-01-01T00:00:00Z</dc:date>
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<title>Upregulation of PSCDBP, TLR2, TWIST1, FLJ35382, EDNRB, and RGS12 gene expression in human myometrium at labor.</title>
<link>http://hdl.handle.net/10379/693</link>
<description>Upregulation of PSCDBP, TLR2, TWIST1, FLJ35382, EDNRB, and RGS12 gene expression in human myometrium at labor.
O'Brien, Margaret; Morrison, John J.; Smith, Terry
The regulatory mechanisms underlying myometrial smooth muscle contractility during labor are poorly understood. The authors therefore investigated the transcriptional profile of the changes that occur in the human myometrium at term pregnancy when compared with that at labor. Microarray technology was used to identify differentially expressed genes in human myometrium at labor. Real-time fluorescence reversetranscriptase polymerase chain reaction (RT-PCR) was subsequently performed to verify the microarray data. Semiquantitative RT-PCR, Western blotting, and microscopy methodologies were also used. Certain novel genes were found to be upregulated in human myometrium at labor. Of these, PSCDBP, TLR2, TWIST1 , FLJ35382, andRGS12 have not been previously characterized or identified in human myometrium. EDNRB is the other novel labor-associated gene whose reported expression is also upregulated at labor. All 6 genes were expressed on human myometrial smooth muscle cells. These novel upregulated genes are involved in multiple pathways that may be associated with a variety of cellular processes including inflammation, transcriptional regulation, and intracellular signaling.
</description>
<pubDate>Tue, 01 Jan 2008 00:00:00 GMT</pubDate>
<guid isPermaLink="false">http://hdl.handle.net/10379/693</guid>
<dc:date>2008-01-01T00:00:00Z</dc:date>
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