0000000000699904

AUTHOR

Elisa Monaca

showing 3 related works from this author

Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications

2021

The highly infectious disease COVID-19 caused by the Betacoronavirus SARS-CoV-2 poses a severe threat to humanity and demands the redirection of scientific efforts and criteria to organized research projects. The international COVID19-NMR consortium seeks to provide such new approaches by gathering scientific expertise worldwide. In particular, making available viral proteins and RNAs will pave the way to understanding the SARS-CoV-2 molecular components in detail. The research in COVID19-NMR and the resources provided through the consortium are fully disclosed to accelerate access and exploitation. NMR investigations of the viral molecular components are designated to provide the essential…

Life sciences; biologySARS-COV-2; COVID-19; protein production; structural biology NMR[SDV.BIO]Life Sciences [q-bio]/BiotechnologyBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryAccessory proteinsNMR spectroscopyddc:570[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Molecular Biosciencesddc:610Nonstructural proteinsMolecular BiologyOriginal Research[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]SARS-CoV-2Intrinsically disordered regionnonstructural proteinsCOVID-19structural proteinsCell-free protein synthesisintrinsically disordered regioncell-free protein synthesisaccessory proteins[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyStructural proteins
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Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion

2022

Solution structure of byssal plaque protein Pvfp-5 beta secreted by the Asian green mussel Perna viridis gives molecular insight into mussel adhesion on wet surfaces.Some marine organisms can resist to aqueous tidal environments and adhere tightly on wet surface. This behavior has raised increasing attention for potential applications in medicine, biomaterials, and tissue engineering. In mussels, adhesive forces to the rock are the resultant of proteinic fibrous formations called byssus. We present the solution structure of Pvfp-5 beta, one of the three byssal plaque proteins secreted by the Asian green mussel Perna viridis, and the component responsible for initiating interactions with the…

PernaEpidermal Growth FactorTissue EngineeringArtificial IntelligenceAdhesivesAnimalsMedicine (miscellaneous)Biocompatible MaterialsGeneral Agricultural and Biological SciencesGeneral Biochemistry Genetics and Molecular BiologyCommunications Biology
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Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates

2021

Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial in such diseases. Thus, strategies to increase TIMP-3 bioavailability in the tissue have been sought for development of therapeutics. Nevertheless, high levels of TIMP-3 may lead to mechanism-based …

0301 basic medicineProteomicsADAM15ProteomeCellMatrix metalloproteinaseMass SpectrometryCell membranelcsh:Chemistryanalysis [Proteome]lcsh:QH301-705.5proteomicSpectroscopybiologyChemistrytissue inhibitor of metalloproteases 3 (TIMP-3)General MedicineTransmembrane proteinComputer Science ApplicationsCell biologymedicine.anatomical_structureEctodomainddc:540TIMP3 protein humanmetalloproteinaseectodomain sheddingmetabolism [Tissue Inhibitor of Metalloproteinase-3]Quantitative proteomicsADAM15 protein humanchemistry [Cell Membrane]Catalysismetabolism [Cell Membrane]ArticlemetalloproteinasesInorganic Chemistry03 medical and health sciencestissue inhibitor of metalloproteases 3 (TIMP-3).medicineDisintegrinHumansPhysical and Theoretical ChemistryMolecular BiologyTissue Inhibitor of Metalloproteinase-3030102 biochemistry & molecular biologyOrganic ChemistryCell MembraneMembrane Proteinsmetabolism [Proteome]ADAM Proteins030104 developmental biologyHEK293 Cellslcsh:Biology (General)lcsh:QD1-999metabolism [ADAM Proteins]biology.proteinmetabolism [Membrane Proteins]International Journal of Molecular Sciences
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