Search results for "Protein S"

showing 10 items of 1431 documents

Trehalose effects on α-crystallin aggregates

2007

alpha-Crystallin in its native state is a large, heterogeneous, low-molecular weight (LMW) aggregate that under certain conditions may progressively became part of insoluble high-molecular weight (HMW) systems. These systems are supposed to play a relevant role in eye lens opacification and vision impairment. In this paper, we report the effects of trehalose on alpha-crystallin aggregates. The role of trehalose in alpha-crystallin stress tolerance, chaperone activity and thermal stability is studied. The results show that trehalose stabilizes the alpha-crystallin native structure, inhibits alpha-crystallin aggregation, and disaggregates preformed LMW systems not affecting its chaperone acti…

BiophysicsMicroscopy Atomic ForceBiochemistrythermal stabilitychemistry.chemical_compoundCrystallinNative stateThermal stabilityBenzothiazolesalpha-Crystallinsalpha-crystallinChaperone activityProtein Structure QuaternaryEye lensMolecular BiologyNative structureCircular DichroismTrehalosefood and beveragesCell BiologyTrehaloseeye diseaseschaperone activityThiazolesSpectrometry FluorescencechemistryBiochemistryaggregatesα-Crystallin Trehalose Aggregates Chaperone activity Thermal stabilitysense organsBiochemical and Biophysical Research Communications
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Stitching proteins into membranes, not sew simple

2014

Abstract Most integral membrane proteins located within the endomembrane system of eukaryotic cells are first assembled co-translationally into the endoplasmic reticulum (ER) before being sorted and trafficked to other organelles. The assembly of membrane proteins is mediated by the ER translocon, which allows passage of lumenal domains through and lateral integration of transmembrane (TM) domains into the ER membrane. It may be convenient to imagine multi-TM domain containing membrane proteins being assembled by inserting their first TM domain in the correct orientation, with subsequent TM domains inserting with alternating orientations. However a simple threading model of assembly, with s…

BioquímicaChemistryEndoplasmic reticulumClinical BiochemistryProteïnes de membranaMembrane ProteinsNanotechnologyIntracellular MembranesEndoplasmic ReticulumTransloconBiochemistryTransmembrane proteinProtein Structure TertiaryProtein TransportMembraneMembrane proteinBiophysicsAnimalsHumansEndomembrane systemThreading (protein sequence)Molecular BiologyIntegral membrane proteinBiological Chemistry
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Insertion and Topology of a Plant Viral Movement Protein in the Endoplasmic Reticulum Membrane

2002

Virus-encoded movement proteins (MPs) mediate cell-to-cell spread of viral RNA through plant membranous intercellular connections, the plasmodesmata. The molecular pathway by which MPs interact with viral genomes and target plasmodesmata channels is largely unknown. The 9-kDa MP from carnation mottle carmovirus (CarMV) contains two potential transmembrane domains. To explore the possibility that this protein is in fact an intrinsic membrane protein, we have investigated its insertion into the endoplasmic reticulum membrane. By using in vitro translation in the presence of dog pancreas microsomes, we demonstrate that CarMV p9 inserts into the endoplasmic reticulum without the aid of any addi…

BioquímicaGlycosylationMolecular Sequence DataPlasmodesmaBiologyEndoplasmic ReticulumTopologyBiochemistryProtein Structure SecondaryViral ProteinsAmino Acid SequenceMolecular BiologyEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane ProteinsSTIM1Translation (biology)Cell Biologybiology.organism_classificationVirusCell biologyPlant Viral Movement ProteinsTobacco Mosaic VirusTransmembrane domainCytoplasmMembrane topologyCarmovirusJournal of Biological Chemistry
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Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein

2004

This article is available from: http://www.biomedcentral.com/1472-6807/4/7

BioquímicaSerum Amyloid A Proteinendocrine systemArabidopsis ProteinsProtein ConformationMolecular Sequence DataOsmolar ConcentrationArabidopsisBiological TransportProtein Structure Secondarylcsh:Biology (General)Amino Acid SequencePeptidesProteïneslcsh:QH301-705.5CopperMolecular ChaperonesResearch Article
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An overview of doping in sports

2019

The history of doping field can be outlined in three major stages: (1) early stage in which drug abuse took place during sports performance and competition and gas chromatography was used for its detection; (2) approximately in the 1970s when androgenic anabolic steroids were introduced; (3) In the recent era when the fields of biochemistry, physiology, toxicology, genomics, genetics, immunology, and molecular biology were integrated and applied routinely. Advanced omics technology and gene doping age may be applied in near future. This review will discuss commonly abused materials, both their adverse and harmful effects, and the alleged benefits in conjunction with the current standards in…

Bioquímicaprotein synthesis[SDV]Life Sciences [q-bio]anabolic androgenic steroidsPharmacologyProtein chemistry01 natural sciencesDopaje03 medical and health sciencesCondensed Matter::Materials SciencePhysics::Popular PhysicsBlood dopingerythropoiesis-stimulating agentsGene dopinghuman urineCondensed Matter::SuperconductivityToxicologíaComputer Science::Multimediaaromatase inhibition030304 developmental biology0303 health sciencesAromatase inhibitionbody compositionChemistryexogenous growth hormone010401 analytical chemistryMedicina deportivaskeletal muscle massAnabolic-Androgenic SteroidsSkeletal muscle massGenética3. Good health0104 chemical sciencesautologous blood transfusionsCondensed Matter::Strongly Correlated Electronshuman activitiesClinical psychology
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Cloning and characterization of Scavidin, a fusion protein for the targeted delivery of biotinylated molecules.

2001

We have constructed a novel fusion protein "Scavidin" consisting of the macrophage scavenger receptor class A and avidin. The Scavidin fusion protein is transported to plasma membranes where the avidin portion of the fusion protein binds biotin with high affinity and forms the basis for the targeted delivery of biotinylated molecules. Subcellular fractionation analysis, immunostaining, and electron microscopy demonstrated endosomal localization of the fusion protein. According to pulse-labeling and cross-linking studies Scavidin is found as monomers (55 kDa), dimers, and multimers, of which the 220-kDa form was the most abundant. The biotin binding capacity and active endocytosis of the bio…

Biotin bindingRecombinant Fusion ProteinsBlotting WesternGenetic VectorsPlasma protein bindingBiologyEndocytosisLigandsBiochemistrychemistry.chemical_compoundProtein structureBiotinTransduction GeneticTumor Cells CulturedAnimalsBiotinylationCloning MolecularReceptors ImmunologicMicroscopy ImmunoelectronMolecular BiologyReceptors ScavengerModels GeneticCell MembraneGene Transfer TechniquesScavenger Receptors Class ACell BiologyGliomaAvidinBlotting NorthernFusion proteinImmunohistochemistryPrecipitin TestsEndocytosisProtein Structure TertiaryRatsCross-Linking ReagentsRetroviridaeBiochemistrychemistryMicroscopy FluorescenceBiotinylationbiology.proteinDimerizationAvidinProtein BindingThe Journal of biological chemistry
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Biotin Induces Tetramerization of a Recombinant Monomeric Avidin

2001

Chicken avidin, a homotetramer that binds four molecules of biotin was converted to a monomeric form by successive mutations of interface residues to alanine. The major contribution to monomer formation was the mutation of two aspartic acid residues, which together account for ten hydrogen bonding interactions at the 1-4 interface. Mutation of these residues, together with the three hydrophobic residues at the 1-3 interface, led to stable monomer formation in the absence of biotin. Upon addition of biotin, the monomeric avidin reassociated to the tetramer, which exhibited properties similar to those of native avidin, with respect to biotin binding, thermostability, and protease resistance. …

Biotin bindingbiologyProtein subunitCell BiologyBiochemistrychemistry.chemical_compoundMonomerchemistryBiotinTetramerBiochemistryBiotinylationbiology.proteinBiophysicsMolecular BiologyAvidinHomotetramerJournal of Biological Chemistry
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Specific expression of a TRIM-containing factor in ectoderm cells affects the skeletal morphogenetic program of the sea urchin embryo

2011

In the indirect developing sea urchin embryo, the primary mesenchyme cells (PMCs) acquire most of the positional and temporal information from the overlying ectoderm for skeletal initiation and growth. In this study, we characterize the function of the novel gene strim1, which encodes a tripartite motif-containing (TRIM) protein, that adds to the list of genes constituting the epithelial-mesenchymal signaling network. We report that strim1 is expressed in ectoderm regions adjacent to the bilateral clusters of PMCs and that its misexpression leads to severe skeletal abnormalities. Reciprocally, knock down of strim1 function abrogates PMC positioning and blocks skeletogenesis. Blastomere tran…

BlastomeresDNA Complementaryanimal structuresTRIM Sea urchin embryo Ectoderm Skeleton biomineralization Morpholino oligonucleotides Primary mesenchyme Cell migration Guidance otp pax2/5/8 sm30MesenchymeMolecular Sequence DataMorphogenesisSettore BIO/11 - Biologia MolecolareEctodermBiologyLigandsModels BiologicalBone and BonesMesodermCell MovementEctodermGene expressionmedicineAnimalsAmino Acid SequenceMolecular BiologyGeneGeneticsBone DevelopmentSequence Homology Amino AcidGene Expression Regulation DevelopmentalEmbryoBlastomereProtein Structure TertiaryCell biologyTransplantationmedicine.anatomical_structureSea Urchinsembryonic structuresCarrier ProteinsDevelopmental BiologyDevelopment
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Induction of CD36 and thrombospondin-1 in macrophages by hypoxia-inducible factor 1 and its relevance in the inflammatory process.

2012

Inflammation is part of a complex biological response of vascular tissue to pathogens or damaged cells. First inflammatory cells attempt to remove the injurious stimuli and this is followed by a healing process mediated principally by phagocytosis of senescent cells. Hypoxia and p38-MAPK are associated with inflammation, and hypoxia inducible factor 1 (HIF-1) has been detected in inflamed tissues. We aimed to analyse the role of p38-MAPK and HIF-1 in the transcriptional regulation of CD36, a class B scavenger receptor, and its ligand thrombospondin (TSP-1) in macrophages and to evaluate the involvement of this pathway in phagocytosis of apoptotic neutrophils. We have also assessed HIF-1α, p…

CD36 AntigensMaleAnatomy and PhysiologyNeutrophilsCD36Digestive Physiologylcsh:MedicineApoptosisp38 Mitogen-Activated Protein KinasesBiochemistryMonocytesThrombospondin 1Intestinal mucosaCrohn DiseaseIntestinal Mucosalcsh:ScienceHypoxiaPromoter Regions GeneticMultidisciplinaryProtein StabilityMiddle AgedOxygen Metabolismmedicine.anatomical_structureMedicineFemaleHypoxia-Inducible Factor 1medicine.symptomProtein BindingSignal TransductionResearch ArticleAdultCell PhysiologyAdolescentPhagocytosisImmune CellsImmunologyInflammationGastroenterology and HepatologyBiologyCell LineYoung AdultPhagocytosismedicineHumansUlcerative ColitisScavenger receptorBiologyInflammationLamina propriaDigestive RegulationMacrophageslcsh:RInflammatory Bowel DiseaseHypoxia (medical)Hypoxia-Inducible Factor 1 alpha SubunitMetabolismApoptosisImmunologyCancer researchbiology.proteinlcsh:QColitis UlcerativeDigestive SystemPloS one
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Matrix-mediated canal formation in primmorphs from the sponge Suberites domuncula involves the expression of a CD36 receptor-ligand system.

2004

Sponges (Porifera), represent the phylogenetically oldest metazoan phylum still extant today. Recently, molecular biological studies provided compelling evidence that these animals share basic receptor/ligand systems, especially those involved in bodyplan formation and in immune recognition, with the higher metazoan phyla. An in vitro cell/organ-like culture system, the primmorphs, has been established that consists of proliferating and differentiating cells, but no canals of the aquiferous system. We show that after the transfer of primmorphs from the demosponge Suberites domuncula to a homologous matrix (galectin), canal-like structures are formed in these 3D-cell aggregates. In parallel …

CD36 AntigensTime FactorsGalectinsRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataGene ExpressionChick EmbryoLigandsEvolution MolecularDemospongeAllantoisSequence Analysis ProteinAnimalsAmino Acid SequenceCloning MolecularReceptorCells CulturedPhylogenyGalectinCell AggregationGlutathione TransferasebiologyDose-Response Relationship DrugMolecular StructureSequence Homology Amino AcidCell growthCell DifferentiationCell BiologyAnatomyChorionLigand (biochemistry)biology.organism_classificationIn vitroCell biologyExtracellular MatrixPoriferaProtein Structure TertiarySuberites domunculaSpongeThrombospondinsCell DivisionNaphthoquinonesJournal of cell science
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