Derivatives of 5'-32P labeled (pU)3 an (pU)6 bearing 4-(N-2-chloroethyl-N-methylamino)benzylmethylamine residue attached to 5'-phosphate via phosphamide bond and (Up)5U[32P]pC and (Up)11U[32P]pC bearing 4-(N-2-chloroethyl-N-methylamino)benzyl residue attached to 3'-end via benzylidene bond were applied for the affinity labeling of 80S ribosomes from human placenta in the presence of a cognate tRNA. The derivatives of 32P-labeled pAUG and pAUGU3 analogous to the 5'-phosphamides of (pU)n were used for affinity labeling of 40S subunits in the presence of ternary complex eIF-2.GTP.Met-tRNA(f). The sites of the reagents' attachment to 18S ribosomal RNA were identified by blot-hybridization of the modified 18S rRNA with restriction fragments of the corresponding rDNA. They were found to be located within positions 976-1057 for (pU)6 and pAUGU3 derivatives and within 976-1164 for (pU)3 and pAUG ones. The sites of 18S rRNA modification with the derivatives of (Up)5UpC and (Up)11UpC were found within positions 1610-1869 at 3'-end of the molecule. All the sites identified here are located presumably within highly conserved parts of the eukaryotic small subunit rRNA secondary structure.
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http://dx.doi.org/10.1016/0300-9084(92)90115-u | DOI Listing |
Anal Chem
January 2025
Center for Advanced Analytical Science, Guangzhou Key Laboratory of Sensing Materials and Devices, Guangdong Engineering Technology Research Center for Sensing Materials and Devices, School of Chemistry and Chemical Engineering, Guangzhou University, Guangzhou 510006, China.
Glycoproteins are of significant value to liquid biopsy of human diseases. Herein, we present a universal electrochemical platform for the amplified detection of glycoproteins, taking advantage of the glycan-matchmade multivalent decoration of enzyme labels for the enzymatic signal amplification. Briefly, the glycan-matchmade multivalent decoration involves two steps, i.
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View Article and Find Full Text PDFPharmaceuticals (Basel)
December 2024
Dipartimento di Scienze della Vita, della Salute e delle Professioni Sanitarie, Università degli Studi "Link Campus University", Via del Casale di S. Pio V 44, I-00165 Rome, Italy.
, , and parasites are responsible for infectious diseases threatening millions of people worldwide. Despite more recent efforts devoted to the search for new antiprotozoal agents, efficacy, safety, and resistance issues still hinder the development of suited therapeutic options. The lack of robustly validated targets and the complexity of parasite's diseases have made phenotypic screening a preferential drug discovery strategy for the identification of new chemical entities.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
Institute of Chemistry, Faculty of Materials and Chemical Engineering, University of Miskolc, 3515 Miskolc, Hungary.
The signature of human serum IgG glycosylation is critical in the defense against pathogens. Alterations of IgG N-glycome were associated with COVID-19 (Coronavirus disease 2019) severity, although knowledge on the response to vaccination is limited. IgG N-glycome was analyzed in this study in post-COVID-19 and post-vaccination patients to reveal potential glycosylation-based alterations using hydrophilic interaction liquid chromatography (HILIC-UPLC) with fluorescence (FLR) and mass-spectrometric (MS) detection.
View Article and Find Full Text PDFCancers (Basel)
January 2025
Department of Biomedical Engineering, Division of Oncological Sciences, Knight Cancer Institute, Oregon Health & Science University, Portland, OR 97201, USA.
Cell surface receptors are pivotal to cancer cell transformation, disease progression, metastasis, early detection, targeted therapy, drug responses, and clinical outcomes. Since they coordinate complex signaling communication networks in the tumor microenvironment, mapping the physical interaction partners of cell surface receptors in vivo is vital for understanding their roles, functional states, and suitability as therapeutic targets. Yet traditional methods like immunoprecipitation and affinity purification-mass spectrometry often fail to detect key but weak or transient receptor-protein interactions.
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