Search results for "Protein Domain"

showing 10 items of 132 documents

Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

2019

JBC papers in press xx, 16604-16619 (2019). doi:10.1074/jbc.RA119.009845

0301 basic medicineendocrine systemCircadian clockTranscription factor complex610BiochemistryProtein Structure SecondaryProtein–protein interaction03 medical and health sciencesTransactivationMiceProto-Oncogene Proteins c-mybProtein DomainsX-Ray DiffractionCircadian ClocksScattering Small AngleAnimalsddc:610Amino Acid SequenceCREB-binding proteinMolecular BiologyTernary complexTranscription factorBinding Sites030102 biochemistry & molecular biologybiologyChemistryARNTL Transcription FactorsCell BiologyHistone-Lysine N-MethyltransferaseSurface Plasmon ResonanceCREB-Binding ProteinRecombinant ProteinsCell biologyProtein Structure Tertiary030104 developmental biologyStructural biologyProtein Structure and Foldingbiology.proteinMutagenesis Site-DirectedMyeloid-Lymphoid Leukemia ProteinProtein Binding
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Phosphorylated immunoreceptor tyrosine-based activation motifs and integrin cytoplasmic domains activate spleen tyrosine kinase via distinct mechanis…

2018

Spleen tyrosine kinase (Syk) is involved in cellular adhesion and also in the activation and development of hematopoietic cells. Syk activation induced by genomic rearrangement has been linked to certain T-cell lymphomas, and Syk inhibitors have been shown to prolong survival of patients with B-cell lineage malignancies. Syk is activated either by its interaction with a double-phosphorylated immunoreceptor tyrosine-based activation motif (pITAM), which induces rearrangements in the Syk structure, or by the phosphorylation of specific tyrosine residues. In addition to its immunoreceptor function, Syk is activated downstream of integrin pathways, and integrins bind to the same region in Syk a…

0301 basic medicinekinaasitCell signalingentsyymitIntegrinsintegrinIntegrinAmino Acid MotifsMutation MissenseSykPeptidechemical and pharmacologic phenomenaBiochemistryspleen tyrosine kinase (Syk)environment and public healthBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesProtein DomainsLääketieteen bioteknologia - Medical biotechnologyenzyme kineticshemic and lymphatic diseasescell signalingHumansSyk KinaseTyrosinePhosphorylationCell adhesionMolecular Biologychemistry.chemical_classificationsoluviestintäintegriinit030102 biochemistry & molecular biologybiologyChemistryta1182hemic and immune systemsCell Biology3. Good healthCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)030104 developmental biologyAmino Acid SubstitutionCytoplasmbiology.proteinPhosphorylationPeptidessurface plasmon resonance (SPR)Signal Transduction
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Do genetic polymorphisms in angiotensin converting enzyme 2 (ACE2) gene play a role in coronavirus disease 2019 (COVID-19)?

2020

Abstract Although some demographic, clinical and environmental factors have been associated with a higher risk of developing coronavirus disease 2019 (COVID-19) and progressing towards severe disease, altogether these variables do not completely account for the different clinical presentations observed in patients with comparable baseline risk, whereby some subjects may remain totally asymptomatic, whilst others develop a very aggressive illness. Some predisposing genetic backgrounds can hence potentially explain the broad inter-individual variation of disease susceptibility and/or severity. It has been now clearly established that severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2…

0301 basic medicinereceptorClinical BiochemistryPopulationPneumonia ViralAdipose tissueInflammationPeptidyl-Dipeptidase AAsymptomaticViruspolymorphism03 medical and health sciencesBetacoronavirus0302 clinical medicineProtein DomainsFibrosismedicineHumans030212 general & internal medicineeducationGenePandemicseducation.field_of_studyPolymorphism Geneticbusiness.industrySARS-CoV-2Biochemistry (medical)COVID-19General Medicineangiotensinmedicine.diseaseenzyme030104 developmental biologyCOVID-19 angiotensin enzyme polymorphism receptorImmunologyAngiotensin-converting enzyme 2Spike Glycoprotein CoronavirusReceptors VirusAngiotensin-Converting Enzyme 2medicine.symptombusinessCoronavirus InfectionsProtein Binding
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Spontaneous domain formation of phospholipase A2 at interfaces: fluorescence microscopy of the interaction of phospholipase A2 with mixed monolayers …

1992

Abstract Fluorescence microscopy has recently been proven to be an ideal tool to investigated the specific interaction of phospholipase A 2 with oriented substrate monolayers. Using a dual labeling technique, it could be shown that phospholipase A 2 can specifically attack and hydrolyze solid analogous l -α-DPPC domains. After a critical extent of monolayer hydrolysis the enzyme itself starts to aggregate forming regular shaped protein domains (Grainger et al. (1990) Biochim. Biophys. Acta 1023. 365–379). In order to confirm that the existence of hydrolysis products in the mononlayer is necessary for the observed aggregation of phospholipase A 2 , mixed monolayers of d - and l -α-DPPC, l -α…

12-DipalmitoylphosphatidylcholineCarboxylic acidProtein domainBiophysicsPhospholipidBiochemistryPhospholipases Achemistry.chemical_compoundPhospholipase A2MonolayerOrganic chemistryColoring Agentschemistry.chemical_classificationElapid VenomsPhospholipase AbiologyRhodaminesHydrolysisFatty AcidsSubstrate (chemistry)LysophosphatidylcholinesCell BiologyFluoresceinsEnzyme bindingPhospholipases A2chemistryMicroscopy Fluorescencebiology.proteinBiophysicsPhosphatidylcholinesFluoresceinDecanoic AcidsBiochimica et biophysica acta
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Trichuris trichiura egg extract proteome reveals potential diagnostic targets and immunomodulators.

2021

The proteomic analysis was performed at the proteomics facility of SCSIE, University of Valencia (Burjassot, Spain) that belongs to ProteoRed, PRB2-ISCIII, Madrid, Spain. We also thank Dr. Tatiana Corey, Dr. Amy Beierschmitt and Dr. Pompei Bolfa for their support during sample collection.

ADULT WORMSSerum ProteinsProteomePhysiologyProteomesEggsRC955-962Egg proteinBiochemistryHeat Shock ResponseMedical ConditionsReproductive PhysiologyArctic medicine. Tropical medicineINFECTIONChlorocebus aethiopsMedicine and Health SciencesSUPEROXIDE-DISMUTASECellular Stress ResponsesImmune System ProteinsbiologySoil-transmitted helminthiasisHelminth ProteinsNEMATODEBird EggsInfectious DiseasesTrichurisCell ProcessesHelminth InfectionsProteomeFemaleAntibodyPublic aspects of medicineRA1-1270EXCRETORY-SECRETORY PRODUCTSResearch ArticleNeglected Tropical DiseasesTrichuriasisImmunologyMicrobiologyVitellogeninProtein Domainsparasitic diseasesmedicineParasitic DiseasesHEAT-SHOCK PROTEINSAnimalsHumansTrichuriasisPARASITEOvumImmunodiagnosticsMOLECULAR-CLONINGIDENTIFICATIONPublic Health Environmental and Occupational HealthBiology and Life SciencesProteinsMASS-SPECTROMETRYCell Biologymedicine.diseasebiology.organism_classificationTropical DiseasesSoil-Transmitted HelminthiasesAntigens Helminthbiology.proteinTrichuris trichiuraPLoS Neglected Tropical Diseases
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Neutralizing antibodies against SARS-CoV-2 variants of concern elicited by the comirnaty COVID-19 vaccine in nursing home residents.

2022

Immunosenescence may impact the functionality and breadth of vaccine-elicited humoral immune responses. The ability of sera to neutralize the SARS-CoV-2 spike protein (S) from Beta, Gamma, Delta, and Epsilon variants of concern (VOCs) relative to the ancestral Wuhan-Hu-1 strain was compared in Comirnaty COVID-19-vaccinated elderly nursing home residents, either SARS-CoV-2 naïve (n = 22) or experienced (n = 8), or SARS-CoV-2 naïve younger individuals (n = 18) and non-vaccinated individuals who recovered from severe COVID-19 (n = 19). In all groups, except that including SARS-CoV-2-experienced nursing home residents, some participants lacked NtAb against one or more VOCs, mainly the Beta vari…

AdultMaleCOVID-19 VaccinesCoronavirus disease 2019 (COVID-19)Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Antibodies ViralImmune systemProtein DomainsNeutralization TestsMedicineHumansBeta (finance)AgedRetrospective StudiesAged 80 and overMultidisciplinarybiologybusiness.industrySARS-CoV-2COVID-19ImmunosenescenceMiddle AgedAntibodies NeutralizingFold changeImmunity HumoralNursing HomesTiterImmunologySpike Glycoprotein Coronavirusbiology.proteinFemaleAntibodybusinessScientific reports
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Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrin…

2013

First generation of insect-protected transgenic corn (Bt-corn) was based on the expression of Cry1Ab or Cry1Fa proteins. Currently, the trend is the combination of two or more genes expressing proteins that bind to different targets. In addition to broadening the spectrum of action, this strategy helps to delay the evolution of resistance in exposed insect populations. One of such examples is the combination of Cry1A.105 with Cry1Fa and Cry2Ab to control O. nubilalis and S. frugiperda. Cry1A.105 is a chimeric protein with domains I and II and the C-terminal half of the protein from Cry1Ac, and domain III almost identical to Cry1Fa. The aim of the present study was to determine whether the c…

Agricultural BiotechnologyApplied MicrobiologyCoated vesiclePlant SciencePlasma protein bindingMothsBiochemistryOstriniaPlagues ControlBacillus thuringiensisBiomacromolecule-Ligand InteractionsPlant PestsMultidisciplinaryMicrovillibiologyGenetically Modified OrganismsQRAgricultureRecombinant ProteinsBiochemistryLarvaMedicineDisease SusceptibilityAgrochemicalsResearch ArticleBiotechnologyProtein BindingScienceProtein domainBiotecnologia agrícolaBacillus thuringiensisCoated VesiclesCerealsCropsSpodopteraSpodopteraMicrobiologyBinding CompetitiveZea maysBacterial ProteinsBotanyAnimalsPesticidesBinding siteProtein InteractionsBiologyTransgenic PlantsfungiProteinsPlant Pathologybiology.organism_classificationFusion proteinMaizeGastrointestinal TractKineticsPlant BiotechnologyPest ControlProteïnes
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Assessment of determinants affecting the dual topology of hepadnaviral large envelope proteins

2004

For functional diversity, the large (L) envelope protein of hepatitis B virus (HBV) acquires a dual transmembrane topology via co-translational membrane integration of the S region and partial post-translational translocation of the preS subdomain. Because each process requires the second transmembrane segment (TM2), we explored the action of this determinant by using protease protection analysis of mutant L proteins. We demonstrated that neither the disruption of a leucine zipper-like motif by multiple alanine substitutions nor the flanking charges of TM2 affected the topological reorientation of L. The dispensability of both putative subunit interaction modules argues against a link betwe…

AlanineHepatitis B virusHepatitis B virusVirus AssemblyAmino Acid MotifsMolecular Sequence DataProtein domainPhenotype mixingBiological TransportBiologyEndoplasmic Reticulummedicine.disease_causeVirologyTransmembrane domainDual topologyAmino Acid SubstitutionViral Envelope ProteinsVirologyMembrane topologymedicineHepadnavirusAmino Acid SequenceProtein Processing Post-TranslationalJournal of General Virology
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Specific Zn(II)-binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus

2022

Abstract Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn(II) and deliver it to a transmembrane zinc transporter, ZrfC. In this work, we focus on the thermodynamics of Zn(II) complexes with unstructured regions of Aspf2; basing on a variety of spectrometric and potentiometric data, we show that the C-terminal part has the highest Zn(II)-binding affinity among the potential binding sites, and Ni(II) does not compete with Zn(II) binding to this region. The 14 amino acid Aspf2 C-terminus coordinates Zn(II) via two Cys thiolates and two His imidazoles and…

Binding SitesAspergillus fumigatusZn(II)- and Ni(II)-binding peptidesMetals and AlloysBiophysicsBiochemistryBiomaterialsZincthermodynamicsProtein DomainsChemistry (miscellaneous)zincophorepotentiometryHumansAmino AcidsMetallomics
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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