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- Mkrtchyan, Satenik, et al.
(author)
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Nanocellulose as a Reaction Media and Stoichiometric Reagent for FeCl3-Mediated Reductive Functionalization of Nitro Compounds
- 2023
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In: ACS Sustainable Chemistry and Engineering. - : American Chemical Society (ACS). - 2168-0485. ; 12:1, s. 1-9
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Journal article (peer-reviewed)abstract
- Among a wide array of synthetic amides, N-aryl/alkyl amides are an important class of structural motifs having significant importance in pharmaceutical and agrochemical industries. In this regard, a rapid, low-cost, and environmentally friendly synthesis of N-aryl/alkyl amides still remains in a high demand. Herein, we report a convenient route for the mechanochemical synthesis of N-aryl/alkyl amides via FeCl3-catalyzed reductive amidation of nitro compounds, as well as acylation of aliphatic/aromatic amines with carboxylic acids using nanocellulose as the reaction media/stoichiometric reducing agent. The protocol was found to be simple, efficient, and environmentally benign to obtain a diverse array of the respective amides with good to excellent yields. Furthermore, the use of nitro compounds, amines, and carboxylic acids as cheap and readily available starting materials, FeCl3 as a nontoxic catalyst, and nanocellulose as the biodegradable reaction media as well as the stoichiometric reducing agent makes this protocol in the category of a green chemical transformation.
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| 3. |
- Serwas, N. K., et al.
(author)
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CEBPE-mutant specific granule deficiency correlates with aberrant granule organization and substantial proteome alterations in neutrophils
- 2018
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In: Frontiers in Immunology. - : Frontiers Media SA. - 1664-3224. ; 9:MAR
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Journal article (peer-reviewed)abstract
- Specific granule deficiency (SGD) is a rare disorder characterized by abnormal neutrophils evidenced by reduced granules, absence of granule proteins, and atypical bilobed nuclei. Mutations in CCAAT/enhancer-binding protein-e (CEBPE) are one molecular etiology of the disease. Although C/EBPe has been studied extensively, the impact of CEBPE mutations on neutrophil biology remains elusive. Here, we identified two SGD patients bearing a previously described heterozygous mutation (p.Val218Ala) in CEBPE. We took this rare opportunity to characterize SGD neutrophils in terms of granule distribution and protein content. Granules of patient neutrophils were clustered and polarized, suggesting that not only absence of specific granules but also defects affecting other granules contribute to the phenotype. Our analysis showed that remaining granules displayed mixed protein content and lacked several glycoepitopes. To further elucidate the impact of mutant CEBPE, we performed detailed proteomic analysis of SGD neutrophils. Beside an absence of several granule proteins in patient cells, we observed increased expression of members of the linker of nucleoskeleton and cytoskeleton complex (nesprin-2, vimentin, and lamin-B2), which control nuclear shape. This suggests that absence of these proteins in healthy individuals might be responsible for segmented shapes of neutrophilic nuclei. We further show that the heterozygous mutation p.Val218Ala in CEBPE causes SGD through prevention of nuclear localization of the protein product. In conclusion, we uncover that absence of nuclear C/EBPe impacts on spatiotemporal expression and subsequent distribution of several granule proteins and further on expression of proteins controlling nuclear shape. © 2018 Serwas, Huemer, Dieckmann, Mejstrikova, Garncarz, Litzman, Hoeger, Zapletal, Janda, Bennett, Kain, Kerjaschky and Boztug.
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