Search results for "Isoform"

showing 10 items of 350 documents

Yeast Translation Elongation Factor eIF5A Expression Is Regulated by Nutrient Availability through Different Signalling Pathways

2020

Translation elongation factor eIF5A binds to ribosomes to promote peptide bonds between problematic amino acids for the reaction like prolines. eIF5A is highly conserved and essential in eukaryotes, which usually contain two similar but differentially expressed paralogue genes. The human eIF5A-1 isoform is abundant and implicated in some cancer types

MitochondrionBiotecnologialcsh:ChemistryPeptide Initiation FactorsGene Expression Regulation Fungalmitochondrial respirationGene expressionExpressió genèticaHap1Protein Isoformshemelcsh:QH301-705.5SpectroscopyChemistryRNA-Binding ProteinsTranslation (biology)Iron DeficienciesGeneral MedicineTORAerobiosisUp-RegulationComputer Science ApplicationsCell biologySnf1EIF5ASignal TransductionGene isoformSaccharomyces cerevisiae ProteinsIronCitric Acid CycleDown-RegulationSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Models BiologicalArticleCatalysisInorganic ChemistryeIF5APhysical and Theoretical ChemistryMolecular BiologyTranscription factorGeneLysineOrganic ChemistryNutrientsMetabolismCarbonMetabolic Flux AnalysisGlucoselcsh:Biology (General)lcsh:QD1-999Fermentationgene expressionInternational Journal of Molecular Sciences
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Characterization and metal-induced gene transcription of two new copper zinc superoxide dismutases in the solitary ascidian Ciona intestinalis

2013

Antioxidant enzymes are known to protect living organisms against the oxidative stress risk, also induced by metals. In the present study, we describe the purification and molecular characterization of two Cu,Zn superoxide dismutases (SODs), referred to as Ci-SODa and Ci-SODb, from Ciona intestinalis, a basal chordate widely distributed in temperate shallow seawater. The putative amino acid sequences were compared with Cu,Zn SODs from other metazoans and phylogenetic analyses indicate that the two putative Ci-SODs are more related to invertebrate SODs than vertebrate ones. Both phylogenetic and preliminary homology modeling analyses suggest that Ci-SODa and Ci-SODb are extracellular and int…

Models MolecularGene isoformHemocytesCiona intestinaliHealth Toxicology and MutagenesisIn silicoSettore BIO/05 - ZoologiaSuperoxide dismutaseAquatic ScienceGene Expression Regulation EnzymologicSuperoxide dismutaseOvarian FollicleConsensus sequenceAnimalsSUPEROXIDE-DISMUTASECiona intestinalisGeneCiona intestinalis; SUPEROXIDE-DISMUTASE; ascidiansPhylogenybiologyEcologyCadmium; Ciona intestinalis; Copper; Reactive oxygen species; Superoxide dismutase; ZincPromoterbiology.organism_classificationProtein Structure TertiaryCiona intestinalisascidiansCionaZincBiochemistryMetalsbiology.proteinReactive oxygen specieFemaleWater Pollutants ChemicalCopperCadmium
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Diversity of Omega Glutathione Transferases in mushroom-forming fungi revealed by phylogenetic, transcriptomic, biochemical and structural approaches

2021

International audience; The Omega class of glutathione transferases (GSTs) forms a distinct class within the cytosolic GST superfamily because most of them possess a catalytic cysteine residue. The human GST Omega 1 isoform was first characterized twenty years ago, but it took years of work to clarify the roles of the human isoforms. Concerning the kingdom of fungi, little is known about the cellular functions of Omega glutathione transferases (GSTOs), although they are widely represented in some of these organisms. In this study, we re-assess the phylogeny and the classification of GSTOs based on 240 genomes of mushroom-forming fungi (Agaricomycetes). We observe that the number of GSTOs is…

Models MolecularGene isoformProtein ConformationCrystallography X-RayMicrobiologyAgaricomycetesstructure-functionFungal ProteinsSerine03 medical and health scienceschemistry.chemical_compoundPhylogeneticsGeneticsPolyporalesflavonoid[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyglutathionePhylogeny[SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/MycologyGlutathione Transferase030304 developmental biologychemistry.chemical_classification0303 health sciencesBinding Sitesbiology030306 microbiologyGene Expression ProfilingGenetic VariationGlutathionebiology.organism_classificationenzymeEnzymeBiochemistrychemistryfungi[SDE.BE]Environmental Sciences/Biodiversity and EcologyAgaricalesCysteine[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/Symbiosis
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Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

2001

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionali…

Models MolecularPhytophthora0106 biological sciencesTime FactorsProtein Conformation[SDV]Life Sciences [q-bio]Receptors Cell SurfaceBiologyModels Biological01 natural sciencesArticleHost-Parasite InteractionsFungal Proteins03 medical and health sciencesTobaccoProtein IsoformsBinding siteReceptorMolecular BiologyComputingMilieux_MISCELLANEOUSCells CulturedPlant DiseasesPlant Proteins030304 developmental biology0303 health sciencesBinding SitesAlgal ProteinsCell MembraneProteinsElicitinCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Receptor–ligand kineticsSterolElicitor[SDV] Life Sciences [q-bio]SterolsBiochemistryTyrosineCalciumSterol bindingProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptors.

2010

AMPA receptors (AMPARs) are tetrameric ion channels that mediate rapid glutamate signaling in neurons and many non-neuronal cell types. Endoplasmic reticulum (ER) quality control mechanisms permit only correctly folded functional receptors to be delivered to the cell surface. We analyzed the biosynthetic maturation and transport of all 12 GluA1–4 subunit splice variants as homomeric receptors and observed robust isoform-dependent differences in ER exit competence and surface expression. In contrast to inefficient ER exit of both GluA3 splice forms and the flop variants of GluA1 and GluA4, prominent plasma membrane expression was observed for the other AMPAR isoforms. Surprisingly, deletion …

Models MolecularProtein ConformationImmunoblottingMolecular Sequence DataAMPA receptorBiologymedicine.disease_causeEndoplasmic ReticulumLigandsBiochemistryCell membrane03 medical and health sciences0302 clinical medicineNeurobiologyProtein targetingChlorocebus aethiopsmedicineHomomericAnimalsHumansProtein IsoformsAmino Acid SequenceReceptors AMPAReceptorMolecular BiologyIon channel030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidEndoplasmic reticulumCell MembraneCell BiologyCell biologyTransport proteinProtein Structure TertiaryAlternative SplicingProtein SubunitsProtein Transportmedicine.anatomical_structureHEK293 CellsMicroscopy FluorescenceCOS CellsProtein Multimerization030217 neurology & neurosurgeryThe Journal of biological chemistry
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Cockroach allergens Per a 3 are oligomers

2009

Allergens from cockroaches cause major asthma-related health problems worldwide. Among them Per a 3 belongs to the most potent allergens. Although the sequences of some members of the Per a 3-family are known, their biochemical and biophysical properties have not been investigated. Here we present for the first time a thorough structural characterization of these allergens, which have recently been tested to induce an increase of allergy specific indicators in blood of Europeans. We isolated two Per a 3 isoforms, which occur freely dissolved in the hemolymph as hexamers with molecular masses of 465+/-25kDa (P II) and 512+/-25kDa (P I). Their sedimentation coefficients (S(20,W)) were determi…

Models MolecularSequence analysismedicine.medical_treatmentProtein subunitMolecular Sequence DataImmunologySequence alignmentRandom hexamermedicine.disease_causeMass SpectrometryAllergenmedicineAnimalsPeriplanetaProtein IsoformsAmino Acid SequencePeptide sequenceBase SequencebiologyCircular DichroismHemocyaninSequence Analysis DNAAllergensbiology.organism_classificationMicroscopy ElectronMicroscopy FluorescenceBiochemistryImmunologyInsect ProteinsElectrophoresis Polyacrylamide GelAmerican cockroachSequence AlignmentUltracentrifugationDevelopmental BiologyDevelopmental & Comparative Immunology
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The Sequence of a Gastropod Hemocyanin (HtH1 from Haliotis tuberculata)

2000

The eight functional units (FUs), a-h, of the hemocyanin isoform HtH1 from Haliotis tuberculata (Prosobranchia, Archaeogastropoda) have been sequenced via cDNA, which provides the first complete primary structure of a gastropod hemocyanin subunit. With 3404 amino acids (392 kDa) it is the largest polypeptide sequence ever obtained for a respiratory protein. The cDNA comprises 10,758 base pairs and includes the coding regions for a short signal peptide, the eight different functional units, a 3'-untranslated region of 478 base pairs, and a poly(A) tail. The predicted protein contains 13 potential sites for N-linked carbohydrates (one for HtH1-a, none for HtH1-c, and two each for the other si…

Models MolecularSignal peptideDNA ComplementaryProtein subunitmedicine.medical_treatmentMolecular Sequence DataOctopodiformesBiologyBiochemistryEvolution MolecularArchaeogastropodaComplementary DNAmedicineAnimalsProtein IsoformsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencePhylogenyGene LibrarySequence Homology Amino AcidProtein primary structureHemocyaninCell BiologyAnatomybiology.organism_classificationRespiratory proteinBiochemistryMolluscaHemocyaninsProtein BindingJournal of Biological Chemistry
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International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G Protein–Coupled Receptors

2015

The Adhesion family forms a large branch of the pharmacologically important superfamily of G protein-coupled receptors (GPCRs). As Adhesion GPCRs increasingly receive attention from a wide spectrum of biomedical fields, the Adhesion GPCR Consortium, together with the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification, proposes a unified nomenclature for Adhesion GPCRs. The new names have ADGR as common dominator followed by a letter and a number to denote each subfamily and subtype, respectively. The new names, with old and alternative names within parentheses, are: ADGRA1 (GPR123), ADGRA2 (GPR124), ADGRA3 (GPR125), ADGRB1 (BAI1…

Models MolecularSocieties ScientificSubfamilyComputational biologyBiologyGPR110PharmacologyLigandsGPR113Second Messenger SystemsReceptors G-Protein-CoupledCell MovementTerminology as TopicCell AdhesionCyclic AMPAnimalsHumansProtein IsoformsReceptorNomenclatureG protein-coupled receptorPharmacologyCell MembraneInternational AgenciesAdhesionQPGPR56Pharmacology ClinicalIUPHAR Nomenclature ReportsMolecular MedicineQP517Cell Adhesion MoleculesSignal TransductionPharmacological Reviews
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Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor

2020

The P2X7 receptor (P2X7R) possesses a unique structure associated to an as yet not fully understood mechanism of action that facilitates cell permeability to large ionic molecules through the receptor itself and/or nearby membrane proteins. High extracellular adenosine triphosphate (ATP) levels—inexistent in physiological conditions—are required for the receptor to be triggered and contribute to its role in cell damage signaling. The inconsistent data on its activation pathways and the few studies performed in natively expressed human P2X7R have led us to review the structure, activation pathways, and specific cellular location of P2X7R in order to analyze its biological relevance. The ATP-…

Models MolecularTranscription GeneticP2X7 receptor physiological rolechannel membrane proteinsAllosteric regulationReviewModels BiologicalCatalysislcsh:ChemistryInorganic ChemistryTransduction (genetics)chemistry.chemical_compoundAdenosine Triphosphateallosteric modulationsmedicineExtracellularAnimalsHumansPhysical and Theoretical ChemistryProtein Structure QuaternaryReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyhuman P2X7 receptor isoformsPolymorphism GeneticCell MembraneOrganic ChemistryGeneral MedicineComputer Science ApplicationsCell biologyATPlcsh:Biology (General)lcsh:QD1-999Mechanism of actionchemistryMembrane proteinP2X7 receptorReceptors Purinergic P2X7medicine.symptomAdenosine triphosphateIntracellularSignal TransductionInternational Journal of Molecular Sciences
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Ramucirumab and its use in gastric cancer treatment

2014

Abstract: The inhibition of the mechanisms of tumor neo-angiogenesis represents a milestone that in the last 10 years has seen the advent of numerous molecules to target action against the vascular endothelial growth factor (VEGF). More recently, new molecules have been developed that inhibit tumor spread by the blockade of specific VEGF receptors (VEGFRs), thereby preventing the binding of a ligand to its receptor and the cascade of proliferative events downstream. Ramucirumab is a fully humanized IgG1 monoclonal antibody that performs its action by blocking the isoform 2 of the VEGF receptor (VEGFR-2). Numerous preclinical and clinical studies have demonstrated its activity in several sol…

Monoclonal antibodyGene isoformmedicine.drug_classAngiogenesisAngiogenesis; Gastroesophageal junction cancer; Metastatic gastric cancer; Monoclonal antibody; Ramucirumab; VEGF receptors; Pharmacology; Pharmacology (medical)Antineoplastic AgentsPharmacologyAntibodies Monoclonal HumanizedGastroesophageal junction cancerMonoclonal antibodyRamucirumabRamucirumabchemistry.chemical_compoundStomach NeoplasmsmedicineHumansPharmacology (medical)ReceptorVEGF receptorsPharmacologyClinical Trials as Topicbusiness.industryPharmacology. TherapyVEGF receptorAntibodies MonoclonalLigand (biochemistry)Vascular Endothelial Growth Factor Receptor-2BlockadeVascular endothelial growth factorAngiogenesichemistryAngiogenesisbusinessMetastatic gastric cancerDrugs of Today
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