Search results for "sp1"

showing 2 items of 82 documents

Extracellular Vesicle microRNAs Contribute to the Osteogenic Inhibition of Mesenchymal Stem Cells in Multiple Myeloma

2020

Osteolytic bone disease is the major complication associated with the progression of multiple myeloma (MM). Recently, extracellular vesicles (EVs) have emerged as mediators of MM-associated bone disease by inhibiting the osteogenic differentiation of human mesenchymal stem cells (hMSCs). Here, we investigated a correlation between the EV-mediated osteogenic inhibition and MM vesicle content, focusing on miRNAs. By the use of a MicroRNA Card, we identified a pool of miRNAs, highly expressed in EVs, from MM cell line (MM1.S EVs), expression of which was confirmed in EVs from bone marrow (BM) plasma of patients affected by smoldering myeloma (SMM) and MM. Notably,we found that miR-129-5p, whic…

transcription factor sp1.Cancer ResearchBone diseaseosteogenic differentiationexosomeslcsh:RC254-282transcription factor sp1ArticleSettore MED/15 - Malattie Del SangueSettore BIO/13 - Biologia Applicatamedicinemultiple myeloma (MM)ChemistrySettore BIO/16 - Anatomia UmanaMesenchymal stem cellALPLOsteoblastMicroRNAExtracellular vesiclemedicine.diseaselcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensSettore CHIM/08 - Chimica FarmaceuticaCell biologymicroRNAsExosomemedicine.anatomical_structureOncologyCell cultureAlkaline phosphatasebone diseaseBone marrowextracellular vesicles (EVs)Cancers
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Molecular Basis of SARS-CoV-2 Nsp1-Induced Immune Translational Shutdown as Revealed by All-Atom Simulations.

2021

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic represents the most severe global health crisis in modern human history. One of the major SARS-CoV-2 virulence factors is nonstructural protein 1 (Nsp1), which, outcompeting with the binding of host mRNA to the human ribosome, triggers a translation shutdown of the host immune system. Here, microsecond-long all-atom simulations of the C-terminal portion of the SARS-CoV-2/SARS-CoV Nsp1 in complex with the 40S ribosome disclose that SARS-CoV-2 Nsp1 has evolved from its SARS-CoV ortholog to more effectively hijack the ribosome by undergoing a critical switch of Q/E158 and E/Q159 residues that perfects Nsp1's interactions…

virusesSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)VirulenceBiologyMolecular Dynamics SimulationViral Nonstructural ProteinsRibosomeImmune systemHumansGeneral Materials ScienceEukaryotic Small Ribosomal SubunitPhysical and Theoretical Chemistryskin and connective tissue diseasesRibosome Subunits Small EukaryoticMessenger RNANSP1SARS-CoV-2fungivirus diseasesCOVID-19Translation (biology)Hydrogen BondingCell biologybody regionsSettore CHIM/03 - Chimica Generale E InorganicaProtein BindingThe journal of physical chemistry letters
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