Search results for "Map"

showing 10 items of 3484 documents

Novel view synthesis for projective texture mapping on real 3D objects

2006

Industrial reproduction, as stereography or lithography, have a lack in texture information, as they only deal with 3D reconstruction. In this paper, we provide a new technique to map texture on real 3D objects, by synthesizing a novel view from two camera images to a projector frame, considered as a camera acting in reverse. No prior information on the pose or the shape of the 3D object is necessary, however hard calibration of the complete system is needed.

Projective texture mappingbusiness.industryComputer scienceEpipolar geometry3D reconstructionComputingMethodologies_IMAGEPROCESSINGANDCOMPUTERVISIONVolume rendering3D modelinglaw.inventionView synthesisProjectorlawTrifocal tensorComputer graphics (images)Computer visionArtificial intelligencebusinessTexture mappingComputingMethodologies_COMPUTERGRAPHICSSPIE Proceedings
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Singular quasisymmetric mappings in dimensions two and greater

2018

For all $n \geq 2$, we construct a metric space $(X,d)$ and a quasisymmetric mapping $f\colon [0,1]^n \rightarrow X$ with the property that $f^{-1}$ is not absolutely continuous with respect to the Hausdorff $n$-measure on $X$. That is, there exists a Borel set $E \subset [0,1]^n$ with Lebesgue measure $|E|>0$ such that $f(E)$ has Hausdorff $n$-measure zero. The construction may be carried out so that $X$ has finite Hausdorff $n$-measure and $|E|$ is arbitrarily close to 1, or so that $|E| = 1$. This gives a negative answer to a question of Heinonen and Semmes.

Property (philosophy)General MathematicsExistential quantificationMathematics::General Topology01 natural sciencesfunktioteoriaCombinatoricsMathematics - Metric Geometry0103 physical sciences30L10FOS: MathematicsMathematics::Metric Geometry0101 mathematicsMathematicsLebesgue measuremetric space010102 general mathematicsHausdorff spaceZero (complex analysis)quasiconformal mappingMetric Geometry (math.MG)Absolute continuity16. Peace & justicemetriset avaruudetMetric spaceabsolute continuity010307 mathematical physicsBorel set
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Quantitative Analysis of Prion-Protein Degradation by Constitutive and Immuno-20S Proteasomes Indicates Differences Correlated with Disease Susceptib…

2004

Abstract The main part of cytosolic protein degradation depends on the ubiquitin-proteasome system. Proteasomes degrade their substrates into small peptide fragments, some of which are translocated into the endoplasmatic reticulum and loaded onto MHC class I molecules, which are then transported to the cell surface for inspection by CTL. A reliable prediction of proteasomal cleavages in a given protein for the identification of CTL epitopes would benefit immensely from additional cleavage data for the training of prediction algorithms. To increase the knowledge about proteasomal specificity and to gain more insight into the relation of proteasomal activity and susceptibility to prion diseas…

Proteasome Endopeptidase ComplexPrionsMolecular Sequence DataImmunologyCellProtein degradationPeptide MappingMultienzyme ComplexesMHC class ImedicineAnimalsHumansImmunology and AllergyAmino Acid SequencePeptide sequenceAllelesCell Line TransformedSheepbiologyHydrolysisMolecular biologyPeptide FragmentsRecombinant ProteinsCell biologyCysteine EndopeptidasesKineticsCytosolCTL*medicine.anatomical_structureProteasomeCell culturebiology.proteinDisease SusceptibilityThe Journal of Immunology
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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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Identification of disulphide bonds in the refolding of bovine pancreatic RNase A

1996

Background: Comprehension of the rules that govern the folding process is still far from satisfactory, though it is nevertheless clear that all the information required to define the folding is encoded in the amino acid sequence. In proteins that contain disulphide bonds, folding is associated with disulphide bond formation. Protein species with different numbers of disulphides tend to accumulate during the process; these species can be trapped in a stable form, by quenching any remaining free SH groups, and then characterized in order to identify the disulphide bonds formed. Results The refolding pathway of reduced and denatured RNase A has been studied using mass spectrometric strategies …

Protein FoldingSh groupsRNase P010402 general chemistryPeptide Mapping01 natural sciencesBiochemistryrefolding03 medical and health sciencesRNase AAnimalsDisulfidesES-MSPeptide sequencedisulphide bonds030304 developmental biology0303 health sciencesQuenching (fluorescence)ChemistryFAB-MSRibonuclease Pancreatic0104 chemical sciencesFolding (chemistry)CrystallographyMolecular MedicineCattlePancreatic RNaseDisulphide bondsCysteineFolding and Design
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A vertebrate globin expressed in the brain.

2000

Haemoglobins and myoglobins constitute related protein families that function in oxygen transport and storage in humans and other vertebrates. Here we report the identification of a third globin type in man and mouse. This protein is predominantly expressed in the brain, and therefore we have called it neuroglobin. Mouse neuroglobin is a monomer with a high oxygen affinity (half saturation pressure, P50 approximately 2 torr). Analogous to myoglobin, neuroglobin may increase the availability of oxygen to brain tissue. The human neuroglobin gene (NGB), located on chromosome 14q24, has a unique exon-intron structure. Neuroglobin represents a distinct protein family that diverged early in metaz…

Protein familyRecombinant Fusion ProteinsMolecular Sequence DataNeuroglobinNerve Tissue ProteinsBiologyMiceAnimalsHumansGlobinAmino Acid SequenceCloning MolecularChromosomes Human Pair 14Expressed Sequence TagsMice Inbred BALB CMultidisciplinarySequence Homology Amino AcidGene Expression ProfilingCytoglobinOxygen transportNitric oxide dioxygenaseBrainChromosome MappingExonsMolecular biologyIntronsGlobin foldCell biologyGlobinsRespiratory proteinOxygenNeuroglobinNature
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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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7keto-stigmasterol and 7keto-cholesterol induce differential proteome changes to intestinal epitelial (Caco-2) cells

2015

Abstract Recent studies have expanded the appreciation of the roles of oxysterols triggering inflammatory, immune cytotoxic and apoptotic processes, but have not been considered for proteome analysis. A comparative proteomic study in intestinal epithelial cell cultures incubated (60 μM/24 h) with 7keto-cholesterol or 7keto-stigmasterol was performed. The influence of both compounds was studied following the nLC-TripleTOF analysis. Findings were compared to results for control cultures. In the principal component analysis (PCA) of proteome patterns, two components were extracted accounting for 99.8% of the variance in the protein expression. PCA analysis clearly discriminated between the per…

ProteomeStigmasterolInflammationBiologyToxicologyPeptide MappingImmune systemmedicineHumansRNA MessengerKetocholesterolsTranscription factorPrincipal Component AnalysisCell growthGene Expression ProfilingGeneral MedicineOxidantsCell biologyEnterocytesGene Expression RegulationBiochemistryCell cultureApoptosisProteomeMacrophage migration inhibitory factorCaco-2 Cellsmedicine.symptomFood ScienceFood and Chemical Toxicology
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Sub-cellular proteomic analysis of a Medicago truncatula root microsomal fraction

2004

Since the last decade, Medicago truncatula has emerged as one of the model plants particularly investigated in the field of plant-microbe interactions. Several genetic and molecular approaches including proteomics have been developed to increase knowledge about this plant species. To complement the proteomic data, which have mainly focused on the total root proteins from M. truncatula, we carried out a sub-cellular approach to gain access to the total membrane-associated proteins. Following the setting up of the purification process, microsomal proteins were separated on 2-DE. Ninety-six out of the 440 well-resolved proteins were identified by MALDI-TOF peptide mass fingerprinting. A high p…

Proteomics0106 biological sciencesPlant ScienceFractionationHorticultureBiologyProteomicsPeptide MappingPlant Roots01 natural sciencesBiochemistry03 medical and health sciencesSymbiosisPeptide mass fingerprintingBotanyMedicagoElectrophoresis Gel Two-DimensionalSymbiosisMolecular Biology[SDV.BV.PEP] Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyComputingMilieux_MISCELLANEOUSPlant Proteins030304 developmental biology2. Zero hunger0303 health sciencesfungifood and beveragesGeneral Medicinebiology.organism_classificationMedicago truncatula[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyBiochemistryMicrosomePlant speciesProtein identification010606 plant biology & botanyPhytochemistry
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