Search results for "Protein multimerization"

showing 10 items of 99 documents

The Greenland shark Somniosus microcephalus—Hemoglobins and ligand-binding properties

2017

A large amount of data is currently available on the adaptive mechanisms of polar bony fish hemoglobins, but structural information on those of cartilaginous species is scarce. This study presents the first characterisation of the hemoglobin system of one of the longest-living vertebrate species (392 +/- 120 years), the Arctic shark Somniosus microcephalus. Three major hemoglobins are found in its red blood cells and are made of two copies of the same a globin combined with two copies of three very similar beta subunits. The three hemoglobins show very similar oxygenation and carbonylation properties, which are unaffected by urea, a very important compound in marine elasmobranch physiology.…

---0301 basic medicinegenetic structuresProtein ConformationGreenlandlcsh:MedicineRESONANCE RAMAN-SPECTRAHETERODONTUS-PORTUSJACKSONISpectrum Analysis RamanBiochemistrychemistry.chemical_compoundHemoglobinsProtein structureAMINO-ACID SEQUENCEAnimal CellsSequence Analysis ProteinRed Blood CellsUreaNOTOTHENIOID FISHESPost-Translational Modificationlcsh:ScienceHemeChondrichthyesMultidisciplinarybiologyChemistryOrganic CompoundsChemical ReactionsVertebrateEukaryotaMOLECULAR ADAPTATIONSMicrocephalusGlobinsChemistryBiochemistryOptical EquipmentVertebratesPhysical SciencesEngineering and TechnologyCellular TypesResearch ArticleEnvironmental MonitoringProtein BindingQUATERNARY STRUCTURESAllosteric regulationEquipmentSTRETCHING FREQUENCIESHeme03 medical and health sciencesOXYGEN-BINDINGbiology.animalAnimals14. Life underwaterGlobinHemoglobinPhotolysisBlood Cells030102 biochemistry & molecular biologyLaserslcsh:ROrganic ChemistryOrganismsChemical CompoundsBiology and Life SciencesProteinsxxxCell Biologybiology.organism_classificationCARTILAGINOUS FISHOxygen030104 developmental biologySomniosusFishSharkslcsh:QHemoglobinProtein MultimerizationELASMOBRANCH HEMOGLOBINElasmobranchiiPLoS ONE
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Jumping on the Edge—First Evidence for a 2 × 6-meric Hemocyanin in Springtails

2019

Hemocyanins are respiratory dioxygen carrier proteins found in many arthropods including ancient terrestrial species such as spiders and scorpions as well as marine horseshoe crabs. As hemocyanins are highly conserved in this lineage, it is possible to observe an evolutionary descent through its subunits and their overall structure. Unfortunately, little is known about the structure and function of hexapod hemocyanins. Using recent springtail taxa (Collembola) as models for basal hexapods, and the help of electron microscopy, light scattering, SDS PAGE, and Western blot, we could demonstrate for the first time the presence of 2 × 6-meric hemocyanins in the hemolymph of hexapods. The quatern…

0106 biological sciences0301 basic medicineLineage (evolution)medicine.medical_treatmentlcsh:QR1-502Zoologychemical and pharmacologic phenomenaSpringtail010603 evolutionary biology01 natural sciencesBiochemistrycomplex mixtureslcsh:MicrobiologyArthropod Proteins03 medical and health sciencesCrustaceaHemolymphmedicineterrestrializationAnimalsProtein Structure QuaternaryMolecular BiologyArthropodsbiologyspringtailsCommunicationHemocyaninbiology.organism_classificationhexapodsCrustaceanHorseshoe crabRespiratory protein030104 developmental biologyHemocyaninsCollembolaProtein quaternary structurehemocyaninProtein MultimerizationBiomolecules
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AMPA receptor complex constituents: Control of receptor assembly, membrane trafficking and subcellular localization

2018

Fast excitatory transmission at synapses of the central nervous system is mainly mediated by AMPA receptors (AMPARs). Synaptic AMPAR number and function correlates with synaptic strength. AMPARs are thus key proteins of activity-dependent plasticity in neuronal communication. Up- or down-regulation of synaptic AMPAR number is a tightly controlled dynamic process that involves export of receptors from the endoplasmic reticulum (ER) and Golgi apparatus, exocytosis and endocytosis as well as lateral diffusion of the receptors in the cell membrane. The four AMPAR subunits are embedded into a dynamic network of more than 30 interacting proteins. Many of these proteins are known to modulate recep…

0301 basic medicineAMPA receptorBiologyEndocytosisAxonal TransportExocytosis03 medical and health sciencesCellular and Molecular Neurosciencesymbols.namesakeAnimalsHumansReceptors AMPAReceptorMolecular BiologyNeuronsmusculoskeletal neural and ocular physiologyEndoplasmic reticulumCell BiologyGolgi apparatusSubcellular localizationCell biologyTransport proteinProtein Transport030104 developmental biologynervous systemSynapsessymbolsProtein MultimerizationGuanylate KinasesMolecular and Cellular Neuroscience
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Role of pulmonary surfactant protein Sp-C dimerization on membrane fragmentation: An emergent mechanism involved in lung defense and homeostasis.

2020

Surfactant protein C (SP-C) is a protein present in the pulmonary surfactant system that is involved in the biophysical properties of this lipoprotein complex, but it also has a role in lung defense and homeostasis. In this article, we propose that the link between both functions could rely on the ability of SP-C to induce fragmentation of phospholipid membranes and generate small vesicles that serve as support to present different ligands to cells in the lungs. Our results using bimolecular fluorescence complementation and tunable resistive pulse sensing setups suggest that SP-C oligomerization could be the triggering event that causes membrane budding and nanovesiculation. As shown by flu…

0301 basic medicineBiophysicsBiochemistryCell Line03 medical and health sciencesBimolecular fluorescence complementation0302 clinical medicinePulmonary surfactantProtein DomainsHumansAmino Acid SequenceFragmentation (cell biology)Unilamellar LiposomesChemistryVesicleSurfactant protein CCell BiologyMembrane buddingFlow CytometryPulmonary Surfactant-Associated Protein CEndocytosisRecombinant ProteinsCell biology030104 developmental biology030228 respiratory systemMembrane proteinStructural biologyMicroscopy FluorescencePeptidomimeticsProtein MultimerizationDimerizationBiochimica et biophysica acta. Biomembranes
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Specific interaction of IM30/Vipp1 with cyanobacterial and chloroplast membranes results in membrane remodeling and eventually in membrane fusion.

2016

The photosynthetic light reaction takes place within the thylakoid membrane system in cyanobacteria and chloroplasts. Besides its global importance, the biogenesis, maintenance and dynamics of this membrane system are still a mystery. In the last two decades, strong evidence supported the idea that these processes involve IM30, the inner membrane-associated protein of 30kDa, a protein also known as the vesicle-inducing protein in plastids 1 (Vipp1). Even though we just only begin to understand the precise physiological function of this protein, it is clear that interaction of IM30 with membranes is crucial for biogenesis of thylakoid membranes. Here we summarize and discuss forces guiding I…

0301 basic medicineCations DivalentBiophysicsArabidopsisBiologyBiochemistryMembrane FusionThylakoids03 medical and health sciencesBacterial ProteinsPlant CellsMagnesiumPhotosynthesisCytoskeletonPhospholipidsOrganelle BiogenesisMembrane transport proteinArabidopsis ProteinsMembrane structureSynechocystisLipid bilayer fusionMembrane ProteinsCell BiologyCell biology030104 developmental biologyMembraneMembrane proteinThylakoidbiology.proteinOrganelle biogenesisProtein MultimerizationBiogenesisBiochimica et biophysica acta. Biomembranes
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Hetero-oligomerization of Bacillus thuringiensis Cry1A proteins enhance binding to the ABCC2 transporter of Spodoptera exigua

2021

The ATP binding cassette (ABC) transporters are membrane proteins that can act as putative receptors for Cry proteins from Bacillus thuringiensis (Bt) in the midgut of different insects. For the beet armyworm, Spodoptera exigua, ABCC2 and ABCC3 have been found to interact with Cry1A proteins, the main insecticidal proteins used in Bt crops, as well as Bt-based pesticides. The ABCC2 has shown to have specific binding towards Cry1Ac and is involved in the toxic process of Cry1A proteins, but the role of this transporter and how it relates with the Cry1A proteins is still unknown. Here, we have characterized the interactions between the SeABCC2 and the main proteins that bind to the receptor. …

0301 basic medicineCell SurvivalBacillus thuringiensisATP-binding cassette transporterSpodopteraSpodopteraBiochemistryHemolysin Proteins03 medical and health sciences0302 clinical medicineBacterial ProteinsProtein DomainsBacillus thuringiensisSf9 CellsAnimalsBinding siteReceptorMolecular BiologyBinding SitesBacillus thuringiensis ToxinsbiologyChemistryfungifood and beveragesTransporterCell Biologybiology.organism_classificationMultidrug Resistance-Associated Protein 2Endotoxins030104 developmental biologyMembrane proteinCry1AcBiochemistryMutationInsect ProteinsMultidrug Resistance-Associated ProteinsProtein Multimerization030217 neurology & neurosurgeryProtein BindingBiochemical Journal
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Toxic Tau Oligomers Modulated by Novel Curcumin Derivatives

2019

AbstractThe pathological aggregation and accumulation of tau, a microtubule-associated protein, is a common feature amongst more than 18 different neurodegenerative diseases that are collectively known as tauopathies. Recently, it has been demonstrated that the soluble and hydrophobic tau oligomers are highly toxic in vitro due to their capacity towards seeding tau misfolding, thereby propagating the tau pathology seen across different neurodegenerative diseases. Modulating the aggregation state of tau oligomers through the use of small molecules could be a useful therapeutic strategy to target their toxicity, regardless of other factors involved in their formation. In this study, we screen…

0301 basic medicineCell biologyCurcuminCell SurvivalNeurotoxinsChemical biologyBiophysicsDrug Evaluation Preclinicallcsh:Medicinetau ProteinsProtein aggregationOligomerBiochemistryArticleBiophysical Phenomena03 medical and health scienceschemistry.chemical_compoundMiceProtein Aggregates0302 clinical medicineCell Line Tumormental disordersAnimalsHumanslcsh:ScienceNeuronsMultidisciplinaryCell DeathDrug discoveryDrug discoverySettore BIO/16 - Anatomia Umanalcsh:RSettore CHIM/06 - Chimica OrganicaSmall moleculeChemical biologyIn vitro3. Good healthTau protein Curcumin030104 developmental biologychemistryCell cultureBiophysicsCurcuminAlzheimerlcsh:QProtein Multimerization030217 neurology & neurosurgeryNeuroscience
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[1,2]Oxazolo[5,4-e]isoindoles as promising tubulin polymerization inhibitors

2016

Abstract A series of [1,2]Oxazolo [5,4- e ]isoindoles has been synthesized through a versatile and high yielding sequence. All the new structures showed in the 1 HNMR spectra, the typical signal in the 8.34–8.47 ppm attributable to the H-3 of the [1,2]oxazole moiety. Among all derivatives, methoxy benzyl substituents at positions 3 and 4 or/and 5 were very effective in reducing the growth of different tumor cell lines, including diffuse malignant peritoneal mesothelioma (DMPM), an uncommon and rapidly malignancy poorly responsive to available therapeutic options. The most active compound 6j was found to impair tubulin polymerization, cause cell cycle arrest at G2/M phase and induce apoptosi…

0301 basic medicineCell cycle checkpointIsoindoles2]Oxazolo[5StereochemistryDiffuse malignant peritoneal mesotheliomaα-hydroxyalkyl ketonesAntineoplastic AgentsApoptosisIsoindoles01 natural sciencesTubulin Polymerization Inhibitors03 medical and health scienceschemistry.chemical_compoundIsomerismTubulinCell Line TumorDrug DiscoveryHumansMoietyProtein Structure QuaternaryOxazole[12]Oxazolo[54-e]isoindolePharmacology010405 organic chemistryChemistryAntitubulin agentsDrug Discovery3003 Pharmaceutical ScienceOrganic ChemistryGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaTubulin Modulators0104 chemical sciencesAntitubulin agentG2 Phase Cell Cycle Checkpointsα-hydroxyalkyl ketone030104 developmental biologyApoptosisActive compound4-e]isoindolesProton NMRM Phase Cell Cycle CheckpointsAntitubulin agents; Diffuse malignant peritoneal mesothelioma; [1; 2]Oxazolo[5; 4-e]isoindoles; α-hydroxyalkyl ketones; Pharmacology; Drug Discovery3003 Pharmaceutical Science; Organic Chemistry[1Drug Screening Assays AntitumorProtein Multimerization
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Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and …

2016

The IM30 (inner membrane-associated protein of 30 kDa), also known as the Vipp1 (vesicle-inducing protein in plastids 1), has a crucial role in thylakoid membrane biogenesis and maintenance. Recent results suggest that the protein binds peripherally to membranes containing negatively charged lipids. However, although IM30 monomers interact and assemble into large oligomeric ring complexes with different numbers of monomers, it is still an open question whether ring formation is crucial for membrane interaction. Here we show that binding of IM30 rings to negatively charged phosphatidylglycerol membrane surfaces results in a higher ordered membrane state, both in the head group and in the inn…

0301 basic medicineChloroplastsMembrane lipids02 engineering and technologyBiologyBiochemistryThylakoids03 medical and health scienceschemistry.chemical_compoundMembrane LipidsBacterial ProteinsMembrane BiologyLipid bilayerProtein Structure QuaternaryMolecular BiologyPhosphatidylglycerolSynechocystisMembrane ProteinsBiological membranePhosphatidylglycerolsCell BiologySurface Plasmon Resonance021001 nanoscience & nanotechnologyKinetics030104 developmental biologyMembranechemistryBiochemistryMembrane proteinThylakoidMembrane biogenesisBiophysicsMutant ProteinsProtein Multimerization0210 nano-technologyProtein BindingThe Journal of biological chemistry
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Transmembrane signaling and cytoplasmic signal conversion by dimeric transmembrane helix 2 and a linker domain of the DcuS sensor kinase

2020

Transmembrane (TM) signaling is a key process of membrane-bound sensor kinases. The C4-dicarboxylate (fumarate) responsive sensor kinase DcuS of Escherichia coli is anchored by TM helices TM1 and TM2 in the membrane. Signal transmission across the membrane relies on the piston-type movement of the periplasmic part of TM2. To define the role of TM2 in TM signaling, we use oxidative Cys cross-linking to demonstrate that TM2 extends over the full distance of the membrane and forms a stable TM homodimer in both the inactive and fumarate-activated state of DcuS. An S186xxxGxxxG194 motif is required for the stability and function of the TM2 homodimer. The TM2 helix further extends on the periplas…

0301 basic medicineCytoplasmGpA glycophorin AC4DC C4-dicarboxylateCL cross-linkingpiston-typeMBP maltose-binding proteinBiochemistry03 medical and health sciencesProtein DomainsDcuSEscherichia coli(Gly)xxx(Gly) motifMolecular Biologysensor kinasefumarate030102 biochemistry & molecular biologyChemistryEscherichia coli ProteinsCell MembraneHistidine kinaseGene Expression Regulation BacterialCell BiologyPeriplasmic spacelinkerTransmembrane proteinoxidative Cys cross-linkingTransmembrane domain030104 developmental biologyMembrane proteinProtein kinase domainHelixBiophysicsProtein MultimerizationProtein Kinasestransmembrane signalingLinkerResearch ArticleTM transmembraneJournal of Biological Chemistry
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