Search results for "binding"

showing 10 items of 3896 documents

Developments in the Synthesis of Glycopeptides Containing Glycosyl l-Asparagine, l-Serine, and l-Threonine

1994

chemistry.chemical_compoundGlycosylationChemistryStereochemistryL-asparagineGlycosylStereoisomerismPlasma protein bindingPeptide sequenceGlycopeptideL-threonine
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Analysis of Invariant Chain Processing in 3 Day Cultured Rat Langerhans Cells

1995

MHC class II molecules, critical peptide binding elements involved in the presentation of exogenous antigen to T helper cells, are expressed constitutively by Langerhans cells (LC) within their epidermal microenvironment. Several studies in mouse and man demonstrated, that short term in vitro culture of LC entails remarkable functional and penotypic alterations, including a profound increase of class II elements exposed at the LC’s surface1. Biosynthetic analysis revealed a downregulation of class II synthesis during the culture period2,3. In recent work on rat LC we described the uncoupling of the coordinately regulated biosynthesis of class II and invariant chain proteins in the course of…

chemistry.chemical_compoundMHC class IIbiologyBiosynthesischemistryExogenous antigenDownregulation and upregulationbiology.proteinPeptide bindingMajor histocompatibility complexIn vitroCell biologyInvariant chain
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Frontispiece: Positive Allosteric Control of Guests Encapsulation by Metal Binding to Covalent Porphyrin Cages

2019

chemistry.chemical_compoundchemistryCovalent bondMetal bindingOrganic ChemistryAllosteric regulationSupramolecular chemistryGeneral ChemistryCombinatorial chemistryPorphyrinCatalysisEncapsulation (networking)Chemistry - A European Journal
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Orchestin, a calcium-binding phosphoprotein, is a matrix component of two successive transitory calcified biomineralizations cyclically elaborated by…

2003

Orchestia cavimana is a crustacean that cyclically replaces its calcified cuticle during molting cycles in order to grow. Its terrestrial way of life requires storage of calcium during each premolt period, as calcareous concretions, in tubular diverticula of the midgut. During the postmolt period the stored calcium is reabsorbed and is translocated through the storage organ epithelium as calcified small spherules. In a previous study, we sequenced and characterized a remarkable component of the organic matrix of the premolt storage structures, Orchestin, which is a calcium-binding phosphoprotein. In this paper, we analyzed the spatiotemporal expression of the orchestin gene by Northern blot…

chemistry.chemical_elementCalciumMatrix (biology)MoltingCalcium in biologyCalcium Carbonatechemistry.chemical_compoundCalcification PhysiologicStructural BiologyCalcium-binding proteinCrustaceaAnimalsRNA MessengerbiologyCalcium-Binding ProteinsAnatomyOrchestiabiology.organism_classificationPhosphoproteinsImmunohistochemistryAmorphous calcium carbonateCell biologychemistryGene Expression RegulationPhosphoproteinCalciumBiomineralizationJournal of structural biology
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ElaC Encodes a Novel Binuclear Zinc Phosphodiesterase

2002

ElaC is a widespread gene found in eubacteria, archaebacteria, and mammals with a highly conserved sequence. Two human ElaC variants were recently associated with cancer (Tavtigian, S. V., Simard, J., Teng, D. H., Abtin, V., Baumgard, M., Beck, A., Camp, N. J., Carillo, A. R., Chen, Y., Dayananth, P., Desrochers, M., Dumont, M., Farnham, J. M., Frank, D., Frye, C., Ghaffari, S., Gupte, J. S., Hu, R., Iliev, D., Janecki, T., Kort, E. N., Laity, K. E., Leavitt, A., Leblanc, G., McArthur-Morrison, J., Pederson, A., Penn, B., Peterson, K. T., Reid, J. E., Richards, S., Schroeder, M., Smith, R., Snyder, S. C., Swedlund, B., Swensen, J., Thomas, A., Tranchant, M., Woodland, A. M., Labrie, F., Sko…

chemistry.chemical_elementZincBiologymedicine.disease_causeBiochemistrybeta-LactamasesHomology (biology)Conserved sequenceGene productEscherichia colimedicineHistidineCloning MolecularBinding siteMolecular BiologyEscherichia coliHistidineCell NucleusIonsBinding SitesModels StatisticalPhosphoric Diester HydrolasesSpectrum AnalysisX-RaysPhosphodiesteraseCell BiologyProtein Structure TertiaryOxygenKineticsZincBiochemistrychemistryChromatography GelProtonsDimerizationProtein BindingJournal of Biological Chemistry
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Removal of Chromophore-proximal Polar Atoms Decreases Water Content and Increases Fluorescence in a Near Infrared Phytofluor

2015

Genetically encoded fluorescent markers have revolutionized cell and molecular biology due to their biological compatibility, controllable spatiotemporal expression, and photostability. To achieve in vivo imaging in whole animals, longer excitation wavelength probes are needed due to the superior ability of near infrared light to penetrate tissues unimpeded by absorbance from biomolecules or autofluorescence of water. Derived from near infrared-absorbing bacteriophytochromes, phytofluors are engineered to fluoresce in this region of the electromagnetic spectrum, although high quantum yield remains an elusive goal. An invariant aspartate residue is of utmost importance for photoconversion in…

chromophore binding domain (CBD)Analytical chemistryQuantum yieldPhotochemistryBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryFluorescence spectroscopychemistry.chemical_compoundDeinococcus radioduransWiPhy2Side chainMolecular Biologylcsh:QH301-705.5Wisconsin infrared phytofluor (WiPhy2)Original ResearchBiliverdinta114Physicsta1182Excitation-emission matrix (EEM)ChromophorePhotobleachingFluorescenceexcitation-emission matrix (EEM)chemistrylcsh:Biology (General)Excited statetetrapyrroleFrontiers in Molecular Biosciences
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The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

2020

Please check the README file for more information about the dataset.

chromophore-binding domains of Bacterial phytochromeX-ray Free-electorn LasersXFELData_FILESBL3: EH2Serial Femtosecond CrystallographyGeneralLiterature_MISCELLANEOUSComputingMethodologies_COMPUTERGRAPHICSSACLA
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Prevention of Dominant IgG Adsorption on Nanocarriers in IgG‐Enriched Blood Plasma by Clusterin Precoating

2019

Abstract Nanocarriers for medical applications must work reliably within organisms, independent of the individual differences in the blood proteome. Variation in the blood proteome, such as immunoglobulin levels, is a result of environmental, nutrition, and constitution conditions. This variation, however, should not influence the behavior of nanocarriers in biological media. The composition of the protein corona is investigated to understand the influence varying immunoglobulin levels in the blood plasma have on the interactions with nanocarriers. Specifically, the composition of the nanocarriers' coronas is analyzed after incubation in plasma with normal or elevated immunoglobulin G (IgG)…

clusterinGeneral Chemical Engineeringmedia_common.quotation_subjectGeneral Physics and AstronomyMedicine (miscellaneous)Protein Corona02 engineering and technology010402 general chemistry01 natural sciencesBiochemistry Genetics and Molecular Biology (miscellaneous)Immunoglobulin Gimmunoglobulin Gprotein coronaBlood plasmaGeneral Materials ScienceReceptorInternalizationlcsh:Sciencemedia_commonstealth effectbiologyFull PapernanocarriersChemistryGeneral EngineeringFull Papers021001 nanoscience & nanotechnology0104 chemical sciencesIgG bindingBiophysicsbiology.proteinlcsh:QNanocarriersAntibody0210 nano-technologyAdvanced Science
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Can Physiological and Psychological Factors Predict Dropout from Intense 10-Day Winter Military Survival Training?

2020

Background: In the military context, high levels of physiological and psychological stress together can compromise individual&rsquo

combat readinessHealth Toxicology and MutagenesisPhysical fitnesslcsh:Medicinesotilaskoulutuskeskeyttäminen0302 clinical medicineSex hormone-binding globulintalviMedicineDropout (neural networks)resilienssibiologyHazard ratiofood and beveragesfyysinen kuntovarusmiehetMilitary PersonnelkylmyysBody CompositionattritionAdolescenteducationContext (language use)ArticleYoung Adult03 medical and health sciencessoldierscold environmentHumansAerobic exerciseMuscle StrengthExerciseresiliencebusiness.industryProportional hazards modellcsh:RfungiPublic Health Environmental and Occupational Health030229 sport scienceswinterSelf ConceptHardiness (psychological)physical fitnessbiology.proteinbusinessStress Psychological030217 neurology & neurosurgeryDemographyInternational Journal of Environmental Research and Public Health
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Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity

2002

Mismatch repair (MMR) is involved in the removal of mispaired bases from DNA and thus plays an important role in the maintenance of genomic stability and the prevention of mutations and cancer. Moreover, MMR triggers genotoxicity and apoptosis upon processing of DNA lesions such as O6-methylguanine. Whereas the enzymology of MMR has been elucidated in great detail, only limited data are available concerning its regulation. Here we show that the major mismatch-binding proteins MSH2 and MSH6, forming the MutSalpha complex, are phosphorylated in vitro by protein kinase C and casein kinase II, but not by protein kinase A. Phosphorylation of MSH2 and MSH6 was also found within the cell, with MSH…

congenital hereditary and neonatal diseases and abnormalitiesDNA RepairDNA repairBase Pair MismatchMacromolecular SubstancesActive Transport Cell NucleusBiologyProtein Serine-Threonine KinasesArticleProto-Oncogene ProteinsGeneticsHumansProtein phosphorylationPhosphorylationProtein kinase ACasein Kinase IIneoplasmsProtein kinase CProtein Kinase CCell Nucleusnutritional and metabolic diseasesdigestive system diseasesDNA-Binding ProteinsMutS Homolog 2 ProteinBiochemistryMSH2PhosphorylationDNA mismatch repairCasein kinase 2HeLa Cells
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