WKB Approximation in Noncommutative Gravity

We consider the quasi-commutative approximation to a noncommutative geometry defined as a generalization of the moving frame formalism. The relation which exists between noncommutativity and geometry is used to study the properties of the high-frequency waves on the flat background.Comment: This is a contribution to the Proc. of the Seventh International Conference ''Symmetry in Nonlinear Mathematical Physics'' (June 24-30, 2007, Kyiv, Ukraine), published in SIGMA (Symmetry, Integrability and Geometry: Methods and Applications) at http://www.emis.de/journals/SIGMA

Identification of late assembly domains of the human endogenous retrovirus-K(HML-2)

Background: Late assembly (L)-domains are protein interaction motifs, whose dysfunction causes characteristic budding defects in enveloped viruses. Three different amino acid motifs, namely PT/SAP, PPXY and YPXnL have been shown to play a major role in the release of exogenous retroviruses. Although the L-domains of exogenous retroviruses have been studied comprehensively, little is known about these motifs in endogenous human retroviruses. Results: Using a molecular clone of the human endogenous retrovirus K113 that had been engineered to reverse the presumed non-synonymous postinsertional mutations in the major genes, we identified three functional L-domains of the virus, all located in the Gag p15 protein. A consensus PTAP tetrapeptide serves as the core of a main L-domain for the virus and its inactivation reduces virus release in HEK 293T cells by over 80%. Electron microscopy of cells expressing the PTAP mutant revealed predominantly late budding structures and budding chains at the plasma membrane. The fact that this motif determines subcellular colocalization with Tsg101, an ESCRT-I complex protein known to bind to the core tetrapeptide, supports its role as an L-domain. Moreover, two YPXnL motifs providing additional L-domain function were identified in the p15 protein. One is adjacent to the PTAP sequence and the other is in the p15 N-terminus. Mutations in either motif diminishes virus release and induces an L-domain phenotype while inactivation of all three L-domains results in a complete loss of particle release in HEK 293T cells. The flexibility of the virus in the use of L-domains for gaining access to the ESCRT machinery is demonstrated by overexpression of Tsg101 which rescues the release of the YPXnL mutants. Similarly, overexpression of Alix not only enhances release of the PTAP mutant by a factor of four but also the release of a triple mutant, indicating that additional cryptic YPXnL domains with a low affinity for Alix may be present. No L-domain activity is provided by the proline-rich peptides at the Gag C-terminus. Conclusions: Our data demonstrate that HERV-K(HML-2) release is predominantly mediated through a consensus PTAP motif and two auxiliary YPXnL motifs in the p15 protein of the Gag precursor

Supplementary data for article: Zianna, A.; Sumar Ristovic, M.; Psomas, G.; Hatzidimitriou, A.; Coutouli-Argyropoulou, E.; Lalia-Kantouri, M. Cadmium(II) Complexes of 5-Nitro-Salicylaldehyde and α -Diimines: Synthesis, Structure and Interaction with Calf-Thymus DNA. Journal of Coordination Chemistry 2015, 68 (24), 4444–4463. https://doi.org/10.1080/00958972.2015.1101075

Supplementary material for: [https://doi.org/10.1080/00958972.2015.1101075]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/2004]Related to accepted version: [http://cherry.chem.bg.ac.rs/handle/123456789/3350

Supplementary material for the article: Ristovic, M. S.; Zianna, A.; Psomas, G.; Hatzidimitriou, A. G.; Coutouli-Argyropoulou, E.; Lalia-Kantouri, M. Interaction of Dinuclear Cadmium(II) 5-Cl-Salicylaldehyde Complexes with Calf-Thymus DNA. Materials Science and Engineering C 2016, 61, 579–590. https://doi.org/10.1016/j.msec.2015.12.054

Supplementary material: [https://doi.org/10.1016/j.msec.2015.12.054]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/2052

6th Golden Helix Pharmacogenomics Day: pharmacogenomics and individualized therapy

The Golden Helix Pharmacogenomics Days are international scientific meetings aiming to educate healthcare professionals and biomedical scientists about pharmacogenomics and personalized medicine. In this meeting report, we provide an overview of the scientific lectures and the topics discussed during the 6th Golden Helix Pharmacogenomics Day that was held in Belgrade, Serbia last June 5, 2012. The scientific program included lectures by the local and international speakers from Europe and the United States

6th Golden Helix Pharmacogenomics Day: pharmacogenomics and individualized therapy

The Golden Helix Pharmacogenomics Days are international scientific meetings aiming to educate healthcare professionals and biomedical scientists about pharmacogenomics and personalized medicine. In this meeting report, we provide an overview of the scientific lectures and the topics discussed during the 6th Golden Helix Pharmacogenomics Day that was held in Belgrade, Serbia last June 5, 2012. The scientific program included lectures by the local and international speakers from Europe and the United States

Die COVID-19-Pandemie in Steglitz-Zehlendorf – sozialräumliche Betrachtung des Infektionsgeschehens

Die laborbestätigten SARS-CoV-2-Falldaten des Berliner Bezirks Steglitz-Zehlendorf im Zeitraum 01.03.2020 bis 30.09.2021 wurden mit dem Ziel ausgewertet, genauere Erkenntnisse über den zeitlichen Verlauf und die kleinräumige Verteilung des Infektionsgeschehens zu gewinnen. Es wurde außerdem geprüft, ob Zusammenhänge zwischen dem Infektionsgeschehen und der Verteilung soziodemografischer Merkmale über die verschiedenen Sozialräume erkennbar sind.Peer Reviewe

Identification of the protease cleavage sites in a reconstituted Gag polyprotein of an HERV-K(HML-2) element

<p>Abstract</p> <p>Background</p> <p>The human genome harbors several largely preserved HERV-K(HML-2) elements. Although this retroviral family comes closest of all known HERVs to producing replication competent virions, mutations acquired during their chromosomal residence have rendered them incapable of expressing infectious particles. This also holds true for the HERV-K113 element that has conserved open reading frames (ORFs) for all its proteins in addition to a functional LTR promoter. Uncertainty concerning the localization and impact of post-insertional mutations has greatly hampered the functional characterization of these ancient retroviruses and their proteins. However, analogous to other betaretroviruses, it is known that HERV-K(HML-2) virions undergo a maturation process during or shortly after release from the host cell. During this process, the subdomains of the Gag polyproteins are released by proteolytic cleavage, although the nature of the mature HERV-K(HML-2) Gag proteins and the exact position of the cleavage sites have until now remained unknown.</p> <p>Results</p> <p>By aligning the amino acid sequences encoded by the <it>gag-pro-pol </it>ORFs of HERV-K113 with the corresponding segments from 10 other well-preserved human specific elements we identified non-synonymous post-insertional mutations that have occurred in this region of the provirus. Reversion of these mutations and a partial codon optimization facilitated the large-scale production of maturation-competent HERV-K113 virus-like particles (VLPs). The Gag subdomains of purified mature VLPs were separated by reversed-phase high-pressure liquid chromatography and initially characterized using specific antibodies. Cleavage sites were identified by mass spectrometry and N-terminal sequencing and confirmed by mutagenesis. Our results indicate that the <it>gag </it>gene product Pr74^Gagof HERV-K(HML-2) is processed to yield p15-MA (matrix), SP1 (spacer peptide of 14 amino acids), p15, p27-CA (capsid), p10-NC (nucleocapsid) and two C-terminally encoded glutamine- and proline-rich peptides, QP1 and QP2, spanning 23 and 19 amino acids, respectively.</p> <p>Conclusions</p> <p>Expression of reconstituted sequences of original HERV elements is an important tool for studying fundamental aspects of the biology of these ancient viruses. The analysis of HERV-K(HML-2) Gag processing and the nature of the mature Gag proteins presented here will facilitate further studies of the discrete functions of these proteins and of their potential impact on the human host.</p