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Articles by University of Molise

Surface Plasmon Resonance technology to assess biological interactions

Published on: 25th August, 2017

OCLC Number/Unique Identifier: 7317592002

Molecular interactions between proteins or between proteins and small molecules are pivotal events for selective binding of biological structures and, consequentially, for their correct function. In this scenario, the evaluation of kinetic parameters, characterizing a molecular interactions, is considered a crucial event to reveal the nature of binding processes. The focus on peculiar forces involved in the molecular recognition represents an opportunity to explore biological interactions in real time, and to develop a number of innovative biotechnological methods for diagnosis and/or therapy. Currently, optical biosensors, offering an increasingly effective technology to detect in real time molecular binding, are usually composed by a detector, a sensor surface and a sample delivery system: only definite substances, which are able to interact specifically with the biological part, lead to an optical or electrical signal of the physical transducer. In this review we want to highlight the exponentially-growing interest of Surface Plasmon Resonance (SPR) based optical biosensors for molecular binding analysis in different research fields.
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The master regulator gene PRDM2 controls C2C12 myoblasts proliferation and Differentiation switch and PRDM4 and PRDM10 expression

Published on: 25th September, 2017

OCLC Number/Unique Identifier: 7317606260

The Positive Regulatory Domain (PRDM) protein family gene is involved in a spectrum variety of biological processes, including proliferation, differentiation and apoptosis: its member seem to be transcriptional regulators highly cell type and tissue peculiar, towards histones modifications or recruitment of specific interaction patters to modify the expression of target genes. In this study we analyzed the expression profile of different member of PRDM gene family focusing our attention on the role of PRDM2, PRDM4 and PRDM10 genes in mouse C2C12 cell line, during the differentiation of myoblasts into myotubes and speculate about the role of the protein Retinoblastoma protein-interacting zinc finger protein 1-RIZ1, coded by PRDM2 gene, as a regulator of the proliferation/differentiation switch. Results showed a reduction of PRDM2, PRDM4 and PRDM10 expression level during the commitment of the differentiation of myoblasts into myotubes. The RIZ1 silencing stimulated myoblasts differentiation, similar to the effect of serum deprivation on these cells, associated with an increase of Myogenin expression level, which is considered to be involved in the differentiation of myoblasts into multinucleated myotubes. As demonstrated by chromatin immunoprecipitation experiments, RIZ1 is associated with Myogenin promoter in proliferation condition and after 24h from differentiation induction, negatively controlling therefore Myogenin expression. Moreover RIZ1 silencing induced a reduction in PRDM4 and PRDM10 expression levels leaving us to speculate that the PRDM genes have a redundant role and they are hierarchically organized.
Cite this ArticleCrossMarkPublonsHarvard Library HOLLISGrowKudosResearchGateBase SearchOAI PMHAcademic MicrosoftScilitSemantic ScholarUniversite de ParisUW LibrariesSJSU King LibrarySJSU King LibraryNUS LibraryMcGillDET KGL BIBLiOTEKJCU DiscoveryUniversidad De LimaWorldCatVU on WorldCat
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