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Structure and spectral characteristics of fervenulin and 2-methylfervenulin-3-one 4-N-oxides: Features of the transformations of fervenulin-3-one and its 4-N-oxide with C-nucleophiles

The structures of crystalline fervenulin, 2-methylfervenulin-3-one (MSD-92), and their 4-N-oxides were studied using x-ray diffraction and ¹H and ¹³C NMR spectroscopy techniques. Acomparative analysis of the spectroscopic data and the chemical reactivity of pyrimidotriazine antibiotics and their analogs allowed the reactive centers of these biologically active compounds, ways of their activation, and mechanisms of transformation to be elucidated. __________ Translated from Khimiko-Farmatsevticheskii Zhurnal, Vol. 40, No. 7, pp. 49–54, July, 2006.     

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Specific features of the interaction of fervenulin and its 4-N-oxide with C-nucleophiles: Structural and spectroscopic characteristics of molecular complexes and covalent adducts with indoles

Experimental data on the chemical transformations of the antibiotic fervenulin and its analogs have been analyzed and compared to the results of recent physicochemical investigations. Crystals of donor-acceptor complexes of fervenulin and its 4-N-oxide with indoles have been obtained, their IR spectra have been studied, and their x-ray structure analysis was performed for the first time. Information concerning the reaction sites of the fervenulin molecule is obtained. __________ Translated from Khimiko-Farmatsevticheskii Zhurnal, Vol. 41, No. 2, pp. 49–53, February, 2007.     

Proteomic Approaches to Dissect Host SUMOylation during Innate Antiviral Immune Responses

SUMOylation is a highly dynamic ubiquitin-like post-translational modification that is essential for cells to respond to and resolve various genotoxic and proteotoxic stresses. Virus infections also constitute a considerable stress scenario for cells, and recent research has started to uncover the diverse roles of SUMOylation in regulating virus replication, not least by impacting antiviral defenses. Here, we review some of the key findings of this virus-host interplay, and discuss the increasingly important contribution that large-scale, unbiased, proteomic methodologies are making to discoveries in this field. We highlight the latest proteomic technologies that have been specifically developed to understand SUMOylation dynamics in response to cellular stresses, and comment on how these techniques might be best applied to dissect the biology of SUMOylation during innate immunity. Furthermore, we showcase a selection of studies that have already used SUMO proteomics to reveal novel aspects of host innate defense against viruses, such as functional cross-talk between SUMO proteins and other ubiquitin-like modifiers, viral antagonism of SUMO-modified antiviral restriction factors, and an infection-triggered SUMO-switch that releases endogenous retroelement RNAs to stimulate antiviral interferon responses. Future research in this area has the potential to provide new and diverse mechanistic insights into host immune defenses.     

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