490 research outputs found

    Die Zeichnungen Johann Baptist Zimmermanns (1680 -1758)

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    Die Zeichnungen Johann Baptist Zimmermanns (1680 -1758)

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    Leasing in Confrontation with IAS/IFRS and Czech Accounting

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    Import 26/06/2013Diplomová práce „Leasing v konfrontaci s IAS/IFRS a českým účetnictvím“ je rozdělena do dvou hlavních částí - teoretická a praktická část. Teoretická část analyzuje účetní úpravu finančního leasingu v jeho různých stádiích z pohledu nájemce, který účtuje v souladu s českými účetními předpisy a mezinárodními standardy účetního výkaznictví IAS/IFRS. Zabývá se i vybranými daňovými aspekty leasingu a popisuje pohled české právní úpravy na leasing. V praktické části je řešen dopad standardu IFRS 1 na oblast finančního leasingu.The master thesis „Leasing in Confrontation with IAS/IFRS and Czech Accounting“ consist of two main parts - theoretical and practical. The teoretical part analyzes the accounting treatment of financial leases in its various stages from the perspective of the tenant, who is accounted in accordance with Czech Accounting legislation and International Financial Reporting Standards IAS/IFRS. The master thesis also deals with selected tax aspects of leasing and describes the view of Czech law legislation on lease. In the practical part is solved the impact of IFRS 1 on financial lease.117 - Katedra účetnictvívýborn

    Rilkes Vermächtnis für unsere Zeit

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    Digitalisat der Ausgabe von 1947, erschienen 201

    APC/CCdh1-Mediated Degradation of the F-Box Protein NIPA Is Regulated by Its Association with Skp1

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    NIPA (Nuclear Interaction Partner of Alk kinase) is an F-box like protein that targets nuclear Cyclin B1 for degradation. Integrity and therefore activity of the SCFNIPA E3 ligase is regulated by cell-cycle-dependent phosphorylation of NIPA, restricting substrate ubiquitination to interphase. Here we show that phosphorylated NIPA is degraded in late mitosis in an APC/CCdh1-dependent manner. Binding of the unphosphorylated form of NIPA to Skp1 interferes with binding to the APC/C-adaptor protein Cdh1 and therefore protects unphosphorylated NIPA from degradation in interphase. Our data thus define a novel mode of regulating APC/C-mediated ubiquitination

    Linking post-translational modifications and protein turnover by site-resolved protein turnover profiling

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    Proteome-wide measurements of protein turnover have largely ignored the impact of post-translational modifications (PTMs). To address this gap, we employ stable isotope labeling and mass spectrometry to measure the turnover of &gt;120,000 peptidoforms including &gt;33,000 phosphorylated, acetylated, and ubiquitinated peptides for &gt;9,000 native proteins. This site-resolved protein turnover (SPOT) profiling discloses global and site-specific differences in turnover associated with the presence or absence of PTMs. While causal relationships may not always be immediately apparent, we speculate that PTMs with diverging turnover may distinguish states of differential protein stability, structure, localization, enzymatic activity, or protein-protein interactions. We show examples of how the turnover data may give insights into unknown functions of PTMs and provide a freely accessible online tool that allows interrogation and visualisation of all turnover data. The SPOT methodology is applicable to many cell types and modifications, offering the potential to prioritize PTMs for future functional investigations.</p

    Linking post-translational modifications and protein turnover by site-resolved protein turnover profiling

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    Proteome-wide measurements of protein turnover have largely ignored the impact of post-translational modifications (PTMs). To address this gap, we employ stable isotope labeling and mass spectrometry to measure the turnover of &gt;120,000 peptidoforms including &gt;33,000 phosphorylated, acetylated, and ubiquitinated peptides for &gt;9,000 native proteins. This site-resolved protein turnover (SPOT) profiling discloses global and site-specific differences in turnover associated with the presence or absence of PTMs. While causal relationships may not always be immediately apparent, we speculate that PTMs with diverging turnover may distinguish states of differential protein stability, structure, localization, enzymatic activity, or protein-protein interactions. We show examples of how the turnover data may give insights into unknown functions of PTMs and provide a freely accessible online tool that allows interrogation and visualisation of all turnover data. The SPOT methodology is applicable to many cell types and modifications, offering the potential to prioritize PTMs for future functional investigations.</p
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