0000000000075997

AUTHOR

Maria Chiara Monti

showing 5 related works from this author

Immigrants Psychopathology: Emerging Phenomena and Adaptation of Mental Health Care Setting by Native Language.

2018

Mental health of immigrants is an important social and clinical issue. Immigrants may report higher rates of mental disorders and lower levels of use of mental health service with respect to natives. The aim of the present work is to review recent findings of the psychopathology of immigrants and analyze how to adapt the mental care settings through the use of mother tongues. We searched the literature to individuate and review the most recent scientific articles focused on the psychopathology of immigrants realized in Europe. Moreover, we summarized the guidelines about immigrants mental health care and we focused on the barriers caused by language. We individuated 15 papers reporting data…

medicine.medical_specialtyEpidemiologyFirst languagePsychological interventionEthnic groupLanguage barrier03 medical and health sciences0302 clinical medicineImmigrantsClinical Practice & Epidemiology in Mental Healthmedicine030212 general & internal medicinePsychiatryPsychopathologyMental health serviceImmigrants Mental disorder Mental health service Native Language Psychopathology Risk factorsmedicine.diseaseMental health030227 psychiatryPsychiatry and Mental healthMental disorderRisk factorsNative LanguageAnxietyRisk factormedicine.symptomPsychologySomatizationImmigrantPsychopathologyClinical practice and epidemiology in mental health : CPEMH
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Toward the Standardization of Mitochondrial Proteomics: The Italian Mitochondrial Human Proteome Project Initiative

2017

The Mitochondrial Human Proteome Project aims at understanding the function of the mitochondrial proteome and its crosstalk with the proteome of other organelles. Being able to choose a suitable and validated enrichment protocol of functional mitochondria, based on the specific needs of the downstream proteomics analysis, would greatly help the researchers in the field. Mitochondrial fractions from ten model cell lines were prepared using three enrichment protocols and analyzed on seven different LC-MS/MS platforms. All data were processed using neXtProt as reference database. The data are available for the Human Proteome Project purposes through the ProteomeXchange Consortium with the iden…

Proteomics0301 basic medicineProteomeStandardizationComputational biologyBiologyMitochondrionProteomicsBioinformaticsBiochemistryenrichment protocol; mitochondria; Mitochondrial Human Proteome Project; standardization;Cell LineMitochondrial Proteins03 medical and health sciences0302 clinical medicineTandem Mass SpectrometryHuman proteome projectHumansProtein Interaction MapsSettore BIO/10 - BIOCHIMICAMitochondrial proteinstandardizationChromatographyLiquidNeXtProtChemistry (all)General Chemistrymitochondria030104 developmental biologyItalyenrichment protocolProteomeReference databaseMitochondrial Human Proteome Projectenrichment protocol; mitochondria; Mitochondrial Human Proteome Project; standardization; Cell Line; Chromatography Liquid; Humans; Italy; Mitochondria; Mitochondrial Proteins; Protein Interaction Maps; Proteome; Proteomics; Tandem Mass Spectrometry; Biochemistry; Chemistry (all)030217 neurology & neurosurgeryChromatography Liquid
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Heterodimerization of Two Pathological Mutants Enhances the Activity of Human Phosphomannomutase2

2015

The most frequent disorder of glycosylation is due to mutations in the gene encoding phosphomannomutase2 (PMM2-CDG). For this disease, which is autosomal and recessive, there is no cure at present. Most patients are composite heterozygous and carry one allele encoding an inactive mutant, R141H, and one encoding a hypomorphic mutant. Phosphomannomutase2 is a dimer. We reproduced composite heterozygosity in vitro by mixing R141H either with the wild type protein or the most common hypomorphic mutant F119L and compared the quaternary structure, the activity and the stability of the heterodimeric enzymes. We demonstrated that the activity of R141H/F119L heterodimers in vitro, which reproduces t…

Genetics and Molecular Biology (all)HeterozygoteProtein StructureGlycosylationMutantlcsh:MedicineGlucose-6-PhosphateBiologymedicine.disease_causeBiochemistryQuaternaryCongenital Disorders of GlycosylationProtein structuremedicineAlleles; Congenital Disorders of Glycosylation; Dimerization; Glucose-6-Phosphate; Glycosylation; Heterozygote; Humans; Mutation; Phosphorylation; Phosphotransferases (Phosphomutases); Protein Structure Quaternary; Agricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)HumansPhosphorylationAlleleProtein Structure Quaternarylcsh:ScienceGeneAllelesMutationMultidisciplinaryMedicine (all)lcsh:RWild typeMolecular biologyEnzyme structureProteostasisAgricultural and Biological Sciences (all)heterodimresPhosphotransferases (Phosphomutases)Mutationlcsh:QCDG-PMM2DimerizationResearch ArticlePLOS ONE
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PLA2-mediated catalytic activation of its inhibitor 25-acetyl-petrosaspongiolide M: serendipitous identification of a new PLA2 suicide inhibitor.

2004

Abstract25-Acetyl-petrosaspongiolide M (PMAc) (1), a mild non-covalent PLA2 inhibitor, unexpectedly recovers, after incubation with bvPLA2, the ability to covalently modify the enzyme target. This study demonstrates the catalytic effect of bvPLA2 in converting 1 in its deacetylated congener petrosaspongiolide M (PM) (2), a strong covalent PLA2 inhibitor whose molecular mechanism of inhibition has already been clarified. Moreover, our findings outline the potential role of PMAc as anti-inflammatory pro-drug, by virtue of its ability of delivering the active PM agent at the site of inflammation, functioning as a suicide inhibitor.

Protein ConformationMarine natural productLigandsBiochemistryMass SpectrometryProtein Structure SecondaryCIRCULAR-DICHROISMchemistry.chemical_compoundProtein structureStructural BiologyBINDINGEnzyme InhibitorsChromatography High Pressure Liquidchemistry.chemical_classificationbiologyMolecular StructureChemistryCircular DichroismHydrolysisTemperatureAcetylationHydrogen-Ion ConcentrationBEE VENOM PHOSPHOLIPASE-A2PoriferaPETROSASPONGIOLIDES M-RBiochemistryCovalent bondINACTIVATIONMANOALIDESpectrometry Mass Electrospray IonizationCYTOSOLIC PHOSPHOLIPASE A(2); BEE VENOM PHOSPHOLIPASE-A2; FLUORESCENCE DISPLACEMENT ASSAY; PETROSASPONGIOLIDES M-R; CIRCULAR-DICHROISM; NATURAL-PRODUCTS; INACTIVATION; MANOALIDE; POTENT; BINDINGStereochemistryBiophysicsGroup II Phospholipases A2CatalysisPhospholipases AAnti-inflammatory compoundManoalidePhospholipase A2NATURAL-PRODUCTSGeneticsTrifluoroacetic acidAnimalsBinding siteOleanolic AcidMolecular BiologyBinding SitesPOTENTCYTOSOLIC PHOSPHOLIPASE A(2)Cell BiologyMolecular WeightKineticsPhospholipases A2EnzymeAcetylationbiology.proteinFLUORESCENCE DISPLACEMENT ASSAYPhospholipase A2 inhibitionFEBS letters
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Chemical Proteomics-Guided Identification of a Novel Biological Target of the Bioactive Neolignan Magnolol

2019

Understanding the recognition process between bioactive natural products and their specific cellular receptors is of key importance in the drug discovery process. In this outline, some potential targets of Magnolol, a natural bioactive compound, have been identified by proteomic approaches. Among them, Importin-β1 has been considered as the most relevant one. A direct binding between Magnolol and this nuclear chaperone has been confirmed by DARTS and molecular docking, while its influence on Importin-β1 translocation has been evaluated by in vitro assays.

bioactive neolignans02 engineering and technologyComputational biology010402 general chemistryProteomics01 natural scienceslcsh:Chemistrychemistry.chemical_compoundchemical proteomicsdrug affinity responsive target stabilityOriginal Researchbioactive neolignans; chemical proteomics; drug affinity responsive target stability; molecular docking; nuclear importbiologyChemistryDrug discoveryIn vitro toxicologyGeneral Chemistrymolecular docking021001 nanoscience & nanotechnologynuclear importMagnololBioactive compound0104 chemical sciencesChemistrylcsh:QD1-999Biological targetChaperone (protein)Direct bindingbiology.protein0210 nano-technologyFrontiers in Chemistry
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