Search results for "Biochemistry & Molecular Biology"

showing 10 items of 431 documents

5' tRNA halves are highly expressed in the primate hippocampus and might sequence-specifically regulate gene expression

2020

Fragments of mature tRNAs have long been considered as mere degradation products without physiological function. However, recent reports show that tRNA-derived small RNAs (tsRNAs) play prominent roles in diverse cellular processes across a wide spectrum of species. Contrasting the situation in other small RNA pathways the mechanisms behind these effects appear more diverse, more complex, and are generally less well understood. In addition, surprisingly little is known about the expression profiles of tsRNAs across different tissues and species. Here, we provide an initial overview of tsRNA expression in different species and tissues, revealing very high levels of 5′ tRNA halves (5′ tRHs) pa…

PrimatesUntranslated regionSmall RNANeurogenesisBiologyHippocampusMice03 medical and health sciencesRNA TransferReportGene expressionAnimalsHumansRNA Small InterferingMolecular BiologyGene030304 developmental biologyRegulation of gene expression0303 health sciencesSequence Analysis RNAMechanism (biology)030302 biochemistry & molecular biologyArgonauteRatsCell biologyMicroRNAsHEK293 CellsGene Expression RegulationTransfer RNARNA Small UntranslatedRNA
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Catalyzing transcriptomics research in cardiovascular disease: The CardioRNA COST action CA17129

2019

WOS: 000474931400001

Project Report0301 basic medicinemedicine.medical_specialtyBiochemistry & Molecular BiologyKnowledge managementlcsh:QH426-470BIOMARKERSbest practices and guidelines; cardiovascular disease; personalized medicine; transcriptomics; translational researchContext (language use)Translational researchDisease030204 cardiovascular system & hematologyBiologyBiochemistryLONG NONCODING RNAS03 medical and health sciencestranscriptomics0302 clinical medicine[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemCIRCULATING MICRORNASTARGETScardiovascular diseaseGeneticsmedicineCost actionSet (psychology)Molecular BiologyComputingMilieux_MISCELLANEOUSGenetics & HeredityScience & Technologybusiness.industryCardiovascular system -- DiseasesPublic healthMedicine -- Research -- International cooperationpersonalized medicine3. Good healthlcsh:Genetics030104 developmental biologyAction (philosophy)PERSPECTIVEStranslational researchPersonalized medicineTranslational research biomedicalbest practices and guidelinesbusinessTranscriptomeLife Sciences & Biomedicine
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The N-glycan processing in HT-29 cells is a function of their state of enterocytic differentiation. Evidence for an atypical traffic associated with …

1991

International audience; When the human colon cancer cells HT-29 undergo enterocytic differentiation, they correctly process their N-glycans, whereas their undifferentiated counterpart are unable to process Man9-8-GlcNAc2 species, the natural substrate of alpha-mannosidase I. As this enzyme is fully active in both HT-29 cell populations, we hypothesize that N-glycoproteins are unable to reach the cis Golgi, the site where alpha-mannosidase I has been localized. We have demonstrated this point by using 1-deoxymannojirimycin, leupeptin, and monensin. In the presence of 1-deoxymannojirimycin, a specific inhibitor of alpha-mannosidase I, differentiated HT-29 cells, as expected, accumulate Man9-8…

Proteases1-DeoxynojirimycinColonLeupeptinsCellular differentiationCellIn Vitro TechniquesBiologyBiochemistry03 medical and health sciencessymbols.namesakechemistry.chemical_compoundPolysaccharidesalpha-Mannosidase[ CHIM.ORGA ] Chemical Sciences/Organic chemistryMannosidasesTumor Cells CulturedmedicineHumansMonensinMolecular Biology030304 developmental biologychemistry.chemical_classificationGlucosamine0303 health sciencesMembrane Glycoproteins[CHIM.ORGA]Chemical Sciences/Organic chemistryEndoplasmic reticulum030302 biochemistry & molecular biologyLeupeptinBiological TransportCell DifferentiationCell BiologyCompartment (chemistry)Golgi apparatus[CHIM.ORGA] Chemical Sciences/Organic chemistrymedicine.anatomical_structureBiochemistrychemistryColonic NeoplasmssymbolsGlycoproteinProtein Processing Post-Translational
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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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Disentangling the complexity of low complexity proteins

2020

Abstract There are multiple definitions for low complexity regions (LCRs) in protein sequences, with all of them broadly considering LCRs as regions with fewer amino acid types compared to an average composition. Following this view, LCRs can also be defined as regions showing composition bias. In this critical review, we focus on the definition of sequence complexity of LCRs and their connection with structure. We present statistics and methodological approaches that measure low complexity (LC) and related sequence properties. Composition bias is often associated with LC and disorder, but repeats, while compositionally biased, might also induce ordered structures. We illustrate this dichot…

Protein ConformationComputer scienceReview ArticleComputational biologyMeasure (mathematics)Evolution MolecularLow complexity03 medical and health sciencesProtein DomainsAmino Acid Sequencestructure[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Databases ProteinMolecular Biology030304 developmental biologyStructure (mathematical logic)0303 health sciencesSequence[SCCO.NEUR]Cognitive science/Neurosciencecomposition bias030302 biochemistry & molecular biologyProteinsdisorderlow complexity regionsStructure and function[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]AlgorithmsInformation SystemsBriefings in Bioinformatics
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Expression and glycosylation studies of human FGF receptor 4

2001

Fibroblast growth factor receptor subtype 4 (FGFR4) has been shown to have special activation properties and just one splicing form, unlike the other FGFRs. FGFR4 overexpression is correlated with breast cancer and therefore FGFR4 is a target for drug design. Our aim is to overexpress high amounts of homogeneous FGFR4 extracellular domain (FGFR4ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4ed is glycosylated on three (N88, N234, and N266) of the six possible N-glycosylation sites but is not O-glycosylated. The deglycosylated triple mutant was expressed and had binding properties similar to those of glycosylated FGFR4ed, but was still heterogeneous. Large am…

Protein FoldingGlycosylationGlycosylationBlotting WesternImmunoblottingMolecular Sequence DataProtein RenaturationBiologyFibroblast growth factorMass SpectrometryInclusion bodiesCell Line03 medical and health scienceschemistry.chemical_compoundSDG 3 - Good Health and Well-beingEscherichia coliAnimalsHumansReceptor Fibroblast Growth Factor Type 4TrypsinAmino Acid SequenceDisulfidesReceptorChromatography High Pressure Liquid030304 developmental biologyInclusion Bodies0303 health sciencesHeparin030302 biochemistry & molecular biologyFibroblast growth factor receptor 4Fibroblast growth factor receptor 3Receptors Fibroblast Growth FactorMolecular biologyRecombinant Proteins3. Good healthchemistryFibroblast growth factor receptorMutationRNA splicing/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingBaculoviridaeBiotechnology
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Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.

2019

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+ -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore…

Protein FoldingProtein ConformationLipoproteinsBiophysicsBiochemistryMicrobiology03 medical and health sciencesLyme diseaseBacterial ProteinsStructural BiologyOxidoreductaseGeneticsmedicineHumansBinding siteBorrelia burgdorferiMolecular BiologyFerredoxin030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseaseBinding SitesbiologyChemistry030302 biochemistry & molecular biologyCell BiologyPeriplasmic spacebacterial infections and mycosesmedicine.diseasebiology.organism_classificationZincMembrane proteinBorrelia burgdorferiPeriplasmbacteriaNAD+ kinaseSodium-Potassium-Exchanging ATPaseFEBS lettersReferences
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The cytosolic Arabidopsis thaliana cysteine desulfurase ABA3 delivers sulfur to the sulfurtransferase STR18

2020

ABSTRACTThe biosynthesis of many sulfur-containing molecules depends on cysteine as a sulfur source. Cysteine desulfurase (CD) and rhodanese (Rhd) domain-containing protein families participate in the trafficking of sulfur for various metabolic pathways in bacteria and human, but their connection is not yet described in plants. The existence of natural chimeric proteins, however, containing both CD and Rhd domains in specific bacterial genera suggests a general interaction between both proteins. We report here the biochemical relationships between two cytosolic proteins from Arabidopsis thaliana, a Rhd domain containing protein, the sulfurtransferase 18 (STR18), and a CD isoform referred to…

Protein familyArabidopsisSulfurtransferaseRhodaneseBiochemistry03 medical and health scienceschemistry.chemical_compoundCytosolProtein DomainsArabidopsis thalianaCysteineMolecular Biology030304 developmental biology0303 health sciencesbiologyArabidopsis ProteinsCysteine desulfurase030302 biochemistry & molecular biologyCell Biologybiology.organism_classificationFusion proteinThiosulfate SulfurtransferaseCarbon-Sulfur LyasesBiochemistrychemistrySulfurtransferasesMolybdenum cofactorSulfurCysteine
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A novel approach to investigate the evolution of structured tandem repeat protein families by exon duplication.

2020

Tandem Repeat Proteins (TRPs) are ubiquitous in cells and are enriched in eukaryotes. They contributed to the evolution of organism complexity, specializing for functions that require quick adaptability such as immunity-related functions. To investigate the hypothesis of repeat protein evolution through exon duplication and rearrangement, we designed a tool to analyze the relationships between exon/intron patterns and structural symmetries. The tool allows comparison of the structure fragments as defined by exon/intron boundaries from Ensembl against the structural element repetitions from RepeatsDB. The all-against-all pairwise structural alignment between fragments and comparison of the t…

Protein familyStructural alignmentBiological data visualizationExonComputational biologyBiologyEvolution Molecular03 medical and health sciencesExonProtein structureTandem repeatStructural BiologyGene duplicationAnimalsHumans030304 developmental biology0303 health sciences030302 biochemistry & molecular biologyIntronProteinsExonsProtein superfamilyClassificationIntronsBiological data visualization; Classification; Exon; Protein evolution; Protein structure; Repeat proteinTandem Repeat SequencesRepeat proteinProtein structureProtein evolutionJournal of structural biology
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Assessing the low complexity of protein sequences via the low complexity triangle.

2020

Background Proteins with low complexity regions (LCRs) have atypical sequence and structural features. Their amino acid composition varies from the expected, determined proteome-wise, and they do not follow the rules of structural folding that prevail in globular regions. One way to characterize these regions is by assessing the repeatability of a sequence, that is, calculating the local propensity of a region to be part of a repeat. Results We combine two local measures of low complexity, repeatability (using the RES algorithm) and fraction of the most frequent amino acid, to evaluate different proteomes, datasets of protein regions with specific features, and individual cases of proteins…

ProteomeProteomesComputer scienceProtein SequencingBiochemistryDatabase and Informatics MethodsSequence Analysis ProteinProtein methodsPeptide sequencechemistry.chemical_classification0303 health sciencesSequenceMultidisciplinary030302 biochemistry & molecular biologyQRGenomicsAmino acidTandem RepeatsProteomeAmino Acid AnalysisMedicineSequence AnalysisResearch ArticleRepetitive Sequences Amino AcidBioinformaticsSequence analysisScienceResearch and Analysis MethodsGenome Complexity03 medical and health sciencesProtein DomainsAmino Acid Sequence AnalysisTandem repeatGeneticsHumansFraction (mathematics)Repeated SequencesAmino Acid SequenceMolecular Biology TechniquesSequencing TechniquesRepresentation (mathematics)Molecular Biology030304 developmental biologyMolecular Biology Assays and Analysis Techniquesbusiness.industryBiology and Life SciencesProteinsComputational BiologyPattern recognitionchemistryGlobular ProteinsArtificial intelligencebusinessPLoS ONE
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