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    <title>OAR@UM Collection:</title>
    <link>https://www.um.edu.mt/library/oar/handle/123456789/815</link>
    <description />
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        <rdf:li rdf:resource="https://www.um.edu.mt/library/oar/handle/123456789/145906" />
        <rdf:li rdf:resource="https://www.um.edu.mt/library/oar/handle/123456789/145888" />
        <rdf:li rdf:resource="https://www.um.edu.mt/library/oar/handle/123456789/145828" />
        <rdf:li rdf:resource="https://www.um.edu.mt/library/oar/handle/123456789/145825" />
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    <dc:date>2026-04-27T00:54:47Z</dc:date>
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  <item rdf:about="https://www.um.edu.mt/library/oar/handle/123456789/145906">
    <title>Smoking and fibrinogen levels modify the risk of Ml due to FXIII V34L : results from the MAMI study</title>
    <link>https://www.um.edu.mt/library/oar/handle/123456789/145906</link>
    <description>Title: Smoking and fibrinogen levels modify the risk of Ml due to FXIII V34L : results from the MAMI study
Authors: Debattista, J.; Attard, Ritienne; Tabone, C.; Lisman, T.; Cassar, Karen; Doggen, C. J. M.; Bezzina Wettinger, Stephanie; Farrugia, Rosienne
Abstract: Background: Coagulation factor XIII (FXIII), after activation by thrombin cleavage in the final step of the coagulation cascade, participates &#xD;
in cross-linking fibrin to form a stable clot. The Leu34 form of the &#xD;
common FXIII V34L polymorphism (rs5985) accelerates the rate by &#xD;
which thrombin activates FXIII during coagulation.</description>
    <dc:date>2017-01-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="https://www.um.edu.mt/library/oar/handle/123456789/145888">
    <title>Monocyte response to activated platelets : a transcriptional study</title>
    <link>https://www.um.edu.mt/library/oar/handle/123456789/145888</link>
    <description>Title: Monocyte response to activated platelets : a transcriptional study
Authors: Farrugia, Rosienne; Gusnanto, A.; Ellis, P.; Langford, C. F.; Goodall, A. H.; Watkins, N. A.; Ouwehand, W. H.
Abstract: Introduction: Plaque rupture exposes platelets to collagen resulting in their activation via the &#xD;
collagen-GPVI/FcRgamma signalling cascade. This signal is communicated to monocytes via two &#xD;
routes; directly by cell-cell contact, or indirectly by a wide spectrum of soluble factors in the platelet &#xD;
secretome. We used whole-genome expression arrays to define the changes in the monocyte &#xD;
transcriptome in response to CRP-18 (collagen-related peptide), a GPVI specific ligand, and &#xD;
contrasted this with the changes that occur upon activation by LPS (lipopolysaccharide) via the &#xD;
CD14/TLR4 signalling cascade.</description>
    <dc:date>2007-01-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="https://www.um.edu.mt/library/oar/handle/123456789/145828">
    <title>Soluble P-selectin levels are higher in patients with NSTEMI vs STEMI</title>
    <link>https://www.um.edu.mt/library/oar/handle/123456789/145828</link>
    <description>Title: Soluble P-selectin levels are higher in patients with NSTEMI vs STEMI
Authors: Agius, C.; Attard, Ritienne; Dingli, Philip; Lisman, T.; Cassar, Karen; Doggen, C. J. M.; Bezzina Wettinger, Stephanie; Farrugia, Rosienne
Abstract: P-selectin is stored in the α-granules of platelets and the &#xD;
Weibel-Palade bodies of endothelial cells. Upon activation, it is re&#xD;
distributed to the plasma membrane where it participates in binding to &#xD;
its receptor, P-selectin glycoprotein ligand-1, present on the surface &#xD;
of activated leukocytes. Soluble P-selectin (sP-sel) is a cleaved form &#xD;
detected in plasma and is a marker of platelet activation and endothelial dysfunction.</description>
    <dc:date>2017-01-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="https://www.um.edu.mt/library/oar/handle/123456789/145825">
    <title>Tetrahydrobiopterin deficiencies in the Maltese population</title>
    <link>https://www.um.edu.mt/library/oar/handle/123456789/145825</link>
    <description>Title: Tetrahydrobiopterin deficiencies in the Maltese population
Authors: Farrugia, Rosienne; Naudi, R.; Attard Montalto, S.; Parascandolo, Raymond; Scerri, Christian A.; Bartolo, C.; Felice, A. E.
Abstract: A higher than usual frequency of hyperphenylalaninaemia due to &#xD;
tetrahydrobiopterin (BH4) deficiencies, specifically Dihydropteridine &#xD;
Reductase (DHPR) deficiency, is present in the Maltese population. &#xD;
Classical Phenylketonuria due to Phenylalanine Hydroxylase &#xD;
deficiency has not been identified to date.</description>
    <dc:date>2002-01-01T00:00:00Z</dc:date>
  </item>
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