Search results for " Maps"

showing 10 items of 198 documents

Design of large scale sensors in 180 nm CMOS process modified for radiation tolerance

2019

International audience; The last couple of years have seen the development of Depleted Monolithic Active Pixel Sensors (DMAPS) fabricated with a process modification to increase the radiation tolerance. Two large scale prototypes, Monopix with a column drain synchronous readout, and MALTA with a novel asynchronous architecture, have been fully tested and characterized both in the laboratory and in test beams. This showed that certain aspects have to be improved such as charge collection after irradiation and the output data rate. Some improvements resulting from extensive TCAD simulations were verified on a small test chip, Mini-MALTA. A detailed cluster analysis, using data from laboratory…

Nuclear and High Energy PhysicsOn-chip clusteringPhysics::Instrumentation and Detectors01 natural sciencesCMOS sensors ; Tracking detectors ; Monolithic sensors ; MAPS ; On-chip clustering030218 nuclear medicine & medical imaging03 medical and health sciencesTracking detectors0302 clinical medicinesemiconductor detector: pixelRadiation toleranceCMOS sensors0103 physical sciencesMAPSElectronic engineeringIrradiation[PHYS.PHYS.PHYS-INS-DET]Physics [physics]/Physics [physics]/Instrumentation and Detectors [physics.ins-det]numerical calculationsInstrumentationradiation: damagePhysicsPixelirradiation010308 nuclear & particles physicstracking detector: upgradecharge: yieldBandwidth (signal processing)ATLASDigital architectureChipUpgradeAsynchronous communicationMonolithic sensors
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Identification of Distributed Systems with Logical Interaction Structure

2012

This paper focuses on the structure identification problem for a class of networked systems, where the interaction among components or agents is described through logical maps. In particular, agents are heterogeneous cooperating systems, i.e. they may have different individual dynamics and different interaction rules depending on input events. While we assume that the individual agents' dynamics are known, each agent has partial knowledge of the logical map encoding the interaction of another agent with its neighbors. Based on the so-called algebraic normal form for binary functions, we present a technique by which the network structure described by a logical function can be dynamically est…

Partial knowledgeTheoretical computer scienceInteraction ruleDistributed computingBinary numberClass (philosophy)Individual dynamicAlgebraic normal formLogical functionAlgebraic normal forms; Binary functions; Cooperating systems; Distributed systems; Individual agent; Individual dynamics; Interaction rules; Interaction structures; Logical functions; Logical maps; Lower approximation; Network structures; Networked systems; Partial knowledge; Real systems; Structure identification; Truth tablesBinary functionSettore ING-INF/04 - AutomaticaLogical mapMathematicsCooperating systemStructure (mathematical logic)Networked systemStructure identificationTruth tablesTruth tableMobile robotReal systemParameter identification problemAlgebraic normal formIdentification (information)Lower approximationInteraction structureIndividual agentDistributed systemNetwork structure
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Maps in picturebooks: cognitive status and narrative functions

2015

This article focuses on the relation between maps, mental representations, description, and narration in picturebooks. It is shown that maps are cognitively demanding, since they presuppose the development of cognitive abilities and the comprehension of complex visual codes, including recognition of the specific combination of signs and names representing land- and cityscapes, geographical abstraction as well as the symbolization, highlighting, and suppression of information. After a survey of findings from cognitive psychology and geography literacy about children’s map acquisition, the article gives an overview on some types of maps in picturebooks that are interesting from a narrative po…

Point (typography)media_common.quotation_subjectPictorial mapsCognitionLinguisticsLiteracyComprehensionMental representationPharmacology (medical)NarrativeCitationPsychologyHumanitiesmedia_commonBLFT - Nordic Journal of ChildLit Aesthetics
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Methodological approaches for the analysis of transmembrane domain interactions: A systematic review

2021

The study of protein-protein interactions (PPI) has proven fundamental for the understanding of the most relevant cell processes. Any protein domain can participate in PPI, including transmembrane (TM) segments that can establish interactions with other TM domains (TMDs). However, the hydrophobic nature of TMDs and the environment they occupy complicates the study of intramembrane PPI, which demands the use of specific approaches and techniques. In this review, we will explore some of the strategies available to study intramembrane PPI in vitro, in vivo, and, in silico, focusing on those techniques that could be carried out in a standard molecular biology laboratory regarding its previous e…

Protein FoldingBacteriaChemistryIn silicoProtein domainBiophysicsMembrane ProteinsCell CommunicationCell BiologyComputational biologyBiochemistryTransmembrane proteinIn vitroProtein–protein interactionTransmembrane domainProtein DomainsMembrane proteinProtein foldingProtein Interaction MapsHydrophobic and Hydrophilic InteractionsBiochimica et Biophysica Acta (BBA) - Biomembranes
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Proteome-Wide Characterization of the RNA-Binding Protein RALY-Interactome Using the in Vivo-Biotinylation-Pulldown-Quant (iBioPQ) Approach

2013

RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No quantitative proteomic analysis of RALY-containing ribonucleoparticles (RNPs) has been performed so far, and the biological role of RALY remains elusive. Here, we present a workflow for the characterization of RALY's interaction partners, termed iBioPQ, that involves in vivo biotinylation of biotin acceptor peptide (BAP)-fused protein in the presence of the prokaryotic biotin holoenzyme synthetase of BirA so that it can be purified using streptavidin-coated magnetic beads, circumventing the need for specific antibodies and providing e…

ProteomeRecombinant Fusion ProteinsMolecular Sequence DataBiotinRNA-binding proteinBiologyHeterogeneous ribonucleoprotein particleProteomicsPoly(A)-Binding Protein IBiochemistryInteractomeELAV-Like Protein 103 medical and health scienceschemistry.chemical_compound0302 clinical medicineNuclear Matrix-Associated ProteinsBiotinProtein Interaction MappingHumansCarbon-Nitrogen LigasesAmino Acid SequenceProtein Interaction MapsPeptide sequence030304 developmental biology0303 health sciencesEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CRNA-Binding ProteinsGeneral ChemistryRepressor ProteinsHEK293 CellsELAV ProteinsGene Expression RegulationBiochemistrychemistryProtein Biosynthesis030220 oncology & carcinogenesisBiotinylationProteomeBiological AssayStreptavidinHeLa CellsProtein BindingJournal of Proteome Research
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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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An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.

2016

Cellular organelles provide opportunities to relate biological mechanisms to disease. Here we use affinity proteomics, genetics and cell biology to interrogate cilia: poorly understood organelles, where defects cause genetic diseases. Two hundred and seventeen tagged human ciliary proteins create a final landscape of 1,319 proteins, 4,905 interactions and 52 complexes. Reverse tagging, repetition of purifications and statistical analyses, produce a high-resolution network that reveals organelle-specific interactions and complexes not apparent in larger studies, and links vesicle transport, the cytoskeleton, signalling and ubiquitination to ciliary signalling and proteostasis. We observe sub…

Proteomics0301 basic medicineSystems AnalysisDNA Mutational Analysislnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4]General Physics and AstronomyDatasets as Topicmethods [Chromatography Affinity]ProteomicsSensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]Chromatography AffinityMass SpectrometryProtein Interaction Mappingtherapy [Ciliopathies]genetics [Ciliopathies]methods [Molecular Targeted Therapy]Molecular Targeted TherapyProtein Interaction MapsMultidisciplinaryCiliumChemistry (all)Qabnormalities [Spine]pathology [Ciliopathies]genetics [Muscle Hypotonia]therapy [Muscle Hypotonia]Metabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]metabolism [Proteins]isolation & purification [Proteins]physiology [Biological Transport]3. Good healthCell biologyVesicular transport proteinpathology [Dwarfism]metabolism [Cilia]Muscle Hypotoniaddc:500pathology [Muscle Hypotonia]pathology [Spine]genetics [Dwarfism]Rare cancers Radboud Institute for Health Sciences [Radboudumc 9]ScienceDwarfismExocystBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyPhysics and Astronomy (all)03 medical and health sciencesIntraflagellar transportCiliogenesisOrganelleHumansCiliaBiochemistry Genetics and Molecular Biology (all)ProteinsBiological TransportGeneral Chemistrytherapy [Dwarfism]Fibroblastsgenetics [Proteins]CiliopathiesSpinemethods [Protein Interaction Mapping]Renal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]030104 developmental biologyProteostasisHEK293 Cellsmethods [Proteomics]
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Osteogenic commitment and differentiation of human mesenchymal stem cells by low‐intensity pulsed ultrasound stimulation

2018

Low-intensity pulsed ultrasound (LIPUS) as an adjuvant therapy in in vitro and in vivo bone engineering has proven to be extremely useful. The present study aimed at investigating the effect of 30 mW/cm(2) LIPUS stimulation on commercially available human mesenchymal stem cells (hMSCs) cultured in basal or osteogenic medium at different experimental time points (7d, 14d, 21d). The hypothesis was that LIPUS would improve the osteogenic differentiation of hMSC and guarantying the maintenance of osteogenic committed fraction, as demonstrated by cell vitality and proteomic analysis. LIPUS stimulation (a) regulated the balance between osteoblast commitment and differentiation by specific network…

Proteomics0301 basic medicineTime FactorsUltrasonic WaveTranscription FactorPhysiologyCellular differentiationClinical BiochemistryLow-intensity pulsed ultrasoundOsteogenesisProtein Interaction MapsStem Cell Nichemesenchymal stem cellCells CulturedProtein metabolic processproteomic analysiMesenchymal Stromal CellReverse Transcriptase Polymerase Chain ReactionOsteogenesiIntracellular Signaling Peptides and ProteinsCell DifferentiationOsteoblastproteomic analysisFlow CytometryCell biologyRUNX2Phenotypemedicine.anatomical_structureUltrasonic Wavesosteoblast differentiationosteogenic commitmentProtein Interaction MapHumanSignal TransductionHomeobox protein NANOGlow-intensity pulsed ultrasoundTime FactorCell SurvivalEnzyme-Linked Immunosorbent AssayBiology03 medical and health sciencesSOX2medicineHumansCell LineageMesenchymal stem cellProteomicMesenchymal Stem CellsCell Biology030104 developmental biologyGene Expression RegulationIntracellular Signaling Peptides and ProteinImmunologyTranscription FactorsJournal of Cellular Physiology
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Comparative Quantitative Analysis of Porcine Optic Nerve Head and Retina Subproteomes

2019

Optic nerve head (ONH) and retina (RET) are the main sites of damage in neurodegenerative optic neuropathies including glaucoma. Up to date, little is known about the molecular interplay between these two adjoining ocular components in terms of proteomics. To close this gap, we investigated ONH and RET protein extracts derived from porcine eyes (n = 12) (Sus scrofa domestica Linnaeus 1758) using semi-quantitative mass spectrometry (MS)-based proteomics comprising bottom-up LC&ndash

Proteomics0301 basic medicineretinaProteomegenetic structuresSus scrofaGlaucomaProteomicslcsh:ChemistrySus scrofa domestica0302 clinical medicineTandem Mass SpectrometryProtein Interaction Mapslcsh:QH301-705.5Spectroscopybiologyoptic nerve headGeneral MedicineComputer Science ApplicationsCell biologymedicine.anatomical_structureProteomeOptic nerveProtein Binding<i>Sus scrofa domestica</i>Optic DiskArticleCatalysisInorganic Chemistry03 medical and health sciencesmedicineMALDI-TOF MSAnimalsHumansPhysical and Theoretical ChemistryEndoplasminMolecular BiologyRetinaClusterinOrganic Chemistrymedicine.diseaseeye diseasesLC-MSglaucomaGene Ontology030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Spectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinsense organsCeruloplasmin030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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