Search results for "Timer"

showing 10 items of 119 documents

Wild-type Cu/Zn superoxide dismutase (SOD1) does not facilitate, but impedes the formation of protein aggregates of amyotrophic lateral sclerosis cau…

2009

Aggregation of Cu/Zn superoxide dismutase (SOD1) is a hallmark of a subset of familial amyotrophic lateral sclerosis (ALS) cases. The expression of wild-type SOD1 [SOD(hWT)] surprisingly exacerbates the phenotype of mutant SOD1 in vivo. Here we studied whether SOD1(hWT) may affect mutant SOD1 aggregation by employing fluorescence microscopy techniques combined with lifetime-based Förster resonance energy transfer (FRET). Only a very minor fraction of SOD1(hWT) was observed in aggregates induced by mutant SOD1(G37R), SOD1(G85R) or SOD1(G93C). Quite in contrast, co-expression of SOD(hWT) reduced the amount of mutant SOD1 in the aggregate fraction. Furthermore, we did not detect endogenous mou…

Protein Foldinganimal diseasesSOD1HeterodimerizationMice TransgenicEndogenyProtein aggregationCell Linelcsh:RC321-571MiceSuperoxide Dismutase-1In vivoFluorescence microscopeAnimalsHumanslcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySuperoxide DismutaseChemistryWild typenutritional and metabolic diseasesAmyotrophic lateral sclerosisPhenotypeMolecular biologynervous system diseasesFörster resonance energy transferSolubilitynervous systemNeurologyFLIM-based FRETMutationProtein MultimerizationProtein aggregationNeurobiology of Disease
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Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing

2012

The vast majority of membrane proteins are anchored to biological membranes through hydrophobic alpha-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) helices, often with a functional and/or structural role. Here, using as scaffold the hydrophobic TM domain of the model membrane protein glycophorin A (GpA), we address the consequences of replacing specific residues by ionizable amino acids on TM helix insertion and packing, both in detergent micelles and in biological membranes. Our findings demonstrate that ionizable residues are stably inserted in hydrophobic environments, and tolerated in t…

Protein Foldinglcsh:MedicineBiochemistryBiotecnologiaProtein Structure SecondaryCell membraneGlycophorinsAmino Acidslcsh:ScienceMicelleschemistry.chemical_classificationMultidisciplinarybiologySodium Dodecyl SulfateLipidsTransmembrane proteinAmino acidmedicine.anatomical_structureBiochemistryCytochemistryThermodynamicsResearch ArticleProtein StructureBiophysicsCalcium-Transporting ATPasesProtein ChemistryProtein–protein interactionMembranes (Biologia)MicrosomesEscherichia colimedicineGlycophorinProtein InteractionsBiologyCell Membranelcsh:RMembrane ProteinsProteinsComputational BiologyBiological membraneIntracellular MembranesProtein Structure TertiaryTransmembrane ProteinsMembrane proteinchemistryHelixbiology.proteinBiophysicslcsh:QProtein Multimerization
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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Mutational analyses of YqjA, a Tvp38/DedA protein of E. coli

2015

AbstractMembrane proteins of the DedA/Tvp38 protein family are involved in membrane integrity and virulence of pathogenic organisms. However, the structure and exact function of any member of this large protein family are still unclear. In the present study we analyzed the functional and structural properties of a DedA homolog. Purified YqjA variants from Escherichia coli are detectable in different oligomeric states and specific homo-interaction of YqjA monomers in the membrane were confirmed by formation of a disulfide bond in the C-terminal transmembrane helix. Moreover, alanine scanning mutagenesis exhibited different interaction sites crucial for YqjA activity vs. dimer formation.

Protein familyDNA Mutational AnalysisBiophysicsVirulencelac operonmedicine.disease_causeBiochemistryProtein Structure SecondaryTvp38Structural BiologyEscherichia coliGeneticsmedicineOligomerizationFunctionMolecular BiologyEscherichia coliAlanineChemistryEscherichia coli ProteinsCell MembraneMutagenesisMembrane ProteinsGene Expression Regulation BacterialCell BiologyAlanine scanningTransmembrane domainMembrane proteinBiochemistryDedAMembrane proteinMutationProtein MultimerizationFEBS Letters
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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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Human apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensity

2012

Human apolipoprotein A-I (apoA-I)-derived amyloidosis can present with either wild-type (Wt) protein deposits in atherosclerotic plaques or as a hereditary form in which apoA-I variants deposit causing multiple organ failure. More than 15 single amino acid replacement amyloidogenic apoA-I variants have been described, but the molecular mechanisms involved in amyloid-associated pathology remain largely unknown. Here, we have investigated by fluorescence and biochemical approaches the stabilities and propensities to aggregate of two disease-associated apoA-I variants, apoA-IGly26Arg, associated with polyneuropathy and kidney dysfunction, and apoA-ILys107-0, implicated in amyloidosis in severe…

ProteomicsProtein Foldinglcsh:MedicineProtein aggregationpolymyxinsBiochemistryProtein Structure SecondaryMiceProtein structureneutrophilsMolecular Cell Biologypolycyclic compoundslcsh:ScienceCellular Stress ResponsesMultidisciplinaryProtein StabilityAmyloidosisCiencias QuímicasfluorescenseCell biologymacrophagesBiochemistryToxicityMedicineProtein foldinglipids (amino acids peptides and proteins)medicine.symptomPolyneuropathyResearch ArticleProtein StructureMedicinaLipoproteinsImmunologyBiophysicsInflammationAmyloidogenic ProteinsBiologyProtein ChemistryMicrobiologyCell Lineprotein aggregationmacrophage activationmedicineAnimalsHumansoligomersProtein InteractionsBiologyInflammationamyloidosisApolipoprotein A-IMacrophageslcsh:RImmunityProteinsnutritional and metabolic diseasesmedicine.diseaseApolipoproteinsAmino Acid SubstitutionCell cultureinflammationCiencias Médicaslcsh:QClinical ImmunologyMutant ProteinspolyneuropathyProtein Multimerization
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Cryopreservation of MHC Multimers: Recommendations for Quality Assurance in Detection of Antigen Specific T Cells

2015

Fluorescence-labeled peptide-MHC class I multimers serve as ideal tools for the detection of antigen-specific T cells by flow cytometry, enabling functional and phenotypical characterization of specific T cells at the single cell level. While this technique offers a number of unique advantages, MHC multimer reagents can be difficult to handle in terms of stability and quality assurance. The stability of a given fluorescence-labeled MHC multimer complex depends on both the stability of the peptide-MHC complex itself and the stability of the fluorochrome. Consequently, stability is difficult to predict and long-term storage is generally not recommended. We investigated here the possibility of…

Quality ControlHistologyT-LymphocytesSerum albuminquality assuranceBiologyrecommendations for MHC multimer storageMajor histocompatibility complexcryopreservationEpitopeCryopreservationPathology and Forensic MedicineFlow cytometryCryoprotective AgentsAntigen specificQuantum DotsmedicineHumansFluorescent Dyesmedicine.diagnostic_testStaining and LabelingcryoprotectantHistocompatibility Antigens Class IReproducibility of ResultsCell BiologyMHC multimerFlow CytometryMolecular biologyMHC multimerBiochemistrybiology.proteinSpecial Section : Improving Methods for Blood Cell AnalysisIndicators and Reagentsglycerol in T cell stainingProtein MultimerizationPeptidesCytometry
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Latviešu karavīra stāsts: Roberts Dāvīds Timermanis (1909–1945)

2019

Grāmata tapusi ar mecenāta Eigita Dāvja Timermaņa atbalstu. Mecenāta ziedojumus administrē Latvijas Universitātes fonds.

Roberts Dāvīds Timermanis:HUMANITIES and RELIGION::History and philosophy subjects::History subjects::History [Research Subject Categories]Nacionālā bruņotā pretestība Latvijā (1944–1957)Latvijas vēstureAtmiņasLatvijas Universitāte - vēstureLatvijas armija - vēsture
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A new Scheme for RPL to handle Mobility in Wireless Sensor Networks

2017

Mobile wireless sensor networks (WSNs) are characterised by dynamic changes in the network topology leading to route breaks and disconnections. The IPv6 routing protocol for low power and lossy networks (RPL), which has become a standard, uses the Trickle timer algorithm to handle changes in the network topology. However, neither RPL nor Trickle timer are well adapted to mobility. This paper investigates the problem of supporting mobility when using RPL. It enhances RPL to fit with sensors' mobility by studying two cases. Firstly, it proposes to modify RPL in order to fit with a dynamic and hybrid topology in the context of medical applications. Secondly, it investigates a more general case…

Routing protocol020203 distributed computingComputer Networks and CommunicationsComputer sciencebusiness.industryNetwork packetComputerSystemsOrganization_COMPUTER-COMMUNICATIONNETWORKS020206 networking & telecommunicationsContext (language use)02 engineering and technologyNetwork topologyIPv6Key distribution in wireless sensor networksHardware and Architecture0202 electrical engineering electronic engineering information engineeringTimerbusinessWireless sensor networkSoftwareComputer networkInternational Journal of Ad Hoc and Ubiquitous Computing
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An adaptive timer for RPL to handle mobility in wireless sensor networks

2016

This paper focuses on the performance of wireless sensor networks characterized by a hybrid topology composed of mobile and static sensor nodes. The Routing Protocol for Low power and lossy networks (RPL), which is standardized as an IPv6 routing protocol for low power and lossy networks, uses the trickle timer algorithm to handle changes in the network topology. However, this algorithm is not well adapted to dynamic environments. This paper enhances the trickle timer in order to fit with mobility requirements. Most of previous works have improved this algorithm without considering the random movement of nodes. In this work, the proposed timer algorithm takes into consideration the random t…

Routing protocolbusiness.industryComputer scienceNode (networking)ComputerSystemsOrganization_COMPUTER-COMMUNICATIONNETWORKSReal-time computing020206 networking & telecommunications02 engineering and technologyNetwork topologyIPv6Key distribution in wireless sensor networks0202 electrical engineering electronic engineering information engineeringMobile wireless sensor network020201 artificial intelligence & image processingTimerbusinessWireless sensor networkComputer network2016 International Wireless Communications and Mobile Computing Conference (IWCMC)
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