Search results for "SoMe"

showing 10 items of 5114 documents

Development and characterization of mouse anti-human LMP2, LMP7, TAP1 and TAP2 monoclonal antibodies.

2008

Low molecular mass polypeptides (LMP) 2 and LMP7 and transporter associated with antigen processing (TAP) subunits TAP1 and TAP2 play a crucial role in antigen processing and cell surface expression of HLA class I molecules. Since monoclonal antibodies (mAb) to these molecules will facilitate the analysis of their expression, structure and function in normal and transformed cells, in the present study we have developed these reagents. Specifically anti-LMP2 and LMP7 mAb were generated from BALB/c mice immunized with specific peptides, and anti-TAP1 and TAP2 mAb from BALB/c mice immunized with respective recombinant proteins. mAb VF101-39F7 and VF101-39G5 were shown to be specific for LMP2, …

Proteasome Endopeptidase Complexmedicine.drug_classRecombinant Fusion ProteinsImmunologyAntigen presentationBiologyMonoclonal antibodyBiochemistrylaw.inventionCell LineMicelawATP Binding Cassette Transporter Subfamily B Member 3Antibody SpecificityHLA AntigensMultienzyme ComplexesGeneticsmedicineImmunology and AllergyAnimalsHumansATP Binding Cassette Transporter Subfamily B Member 2DNA PrimersSkinAntigen PresentationMice Inbred BALB CHybridomasImmunoperoxidaseBase SequenceAntigen processingAntibodies MonoclonalProteinsGeneral MedicineTransporter associated with antigen processingMolecular biologyImmunohistochemistryCysteine EndopeptidasesCell cultureMonoclonalRecombinant DNAATP-Binding Cassette TransportersFemaleIndicators and ReagentsTissue antigens
researchProduct

Thermal Isomerization Mechanism in Dronpa and Its Mutants.

2016

The photoswitching speed of the reversibly switchable fluorescent proteins (RSFPs) from the family of green fluorescent proteins (GFPs) changes upon mutation which is of direct importance for various high-resolution techniques. Dronpa is one of the most used RSFPs. Its point mutants rsFastLime (Dronpa V157G) and rsKame (Dronpa V157L) exhibit a striking difference in their photoswitching speed. Here the QM/MM on-the-fly string method is used in order to explore the details of the thermal isomerization mechanism. The four principal ways in which isomerization may occur have been scrutinized for each of the three proteins. It has been shown that thermal isomerization occurs via a one-bond-flip…

Protein Conformation alpha-HelicalMutantGreen Fluorescent ProteinsGlycineMolecular Dynamics Simulation010402 general chemistryPhotochemistry01 natural sciencesQM/MMDronpaIsomerismLeucine0103 physical sciencesThermalMaterials ChemistryPoint MutationPhysical and Theoretical Chemistrychemistry.chemical_classification010304 chemical physicsChemistryTemperatureValineChromophoreFluorescence0104 chemical sciencesSurfaces Coatings and FilmsAmino acidKineticsThermodynamicsIsomerizationThe journal of physical chemistry. B
researchProduct

Folding and insertion of transmembrane helices at the ER

2021

In eukaryotic cells, the endoplasmic reticulum (ER) is the entry point for newly synthesized proteins that are subsequently distributed to organelles of the endomembrane system. Some of these proteins are completely translocated into the lumen of the ER while others integrate stretches of amino acids into the greasy 30 Å wide interior of the ER membrane bilayer. It is generally accepted that to exist in this non-aqueous environment the majority of membrane integrated amino acids are primarily non-polar/hydrophobic and adopt an α-helical conformation. These stretches are typically around 20 amino acids long and are known as transmembrane (TM) helices. In this review, we will consider how tra…

Protein Conformation alpha-HelicalfoldingProtein FoldingQH301-705.5ReviewEndoplasmic ReticulumRibosomeCatalysisinsertionInorganic Chemistrytransmembrane segmentAnimalsHumansEndomembrane systemmembrane proteinPhysical and Theoretical ChemistryBiology (General)Molecular BiologyQD1-999Spectroscopytransloconchemistry.chemical_classificationEndoplasmic reticulumOrganic ChemistryProteïnes de membranaMembrane ProteinsGeneral MedicineTransloconTransmembrane proteinComputer Science ApplicationsAmino acidTransmembrane domainChemistrychemistryMembrane proteinribosomeBiophysicsHydrophobic and Hydrophilic InteractionsRibosomes
researchProduct

The Closed/Open Model for Lipase Activation. Addressing Intermediate Active Forms of Fungal Enzymes by Trapping of Conformers in Water-Restricted Env…

2001

The behavior of prototypic fungal lipases in a water-restricted environment has been investigated by exploiting the reported experimental strategy that allows the trapping (freeze-drying) of the enzyme in the conformation present in aqueous solution and to subsequently assay it in nonaqueous media [Mingarro, I., Abad, C., and Braco, L. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 3308-3312]. We now report, using simple esterification as well as acidolysis (triglycerides as substrates) as nonaqueous model reactions, that the presence of a detergent (n-octyl-beta-glucopyranoside) in the freeze-drying buffer, at concentrations below the critical micellar concentration, generates different catalyti…

Protein ConformationStereochemistryThioglucosidesDetergentsTrappingBuffersBiochemistryFungal ProteinsAscomycotaEnzyme StabilityMoleculeLipaseConformational isomerismMicellesTriglyceridesCandidachemistry.chemical_classificationAqueous solutionbiologyWaterLipaseGeotrichumEnzyme ActivationSolutionsFreeze DryingEnzymeModels ChemicalchemistryCritical micelle concentrationbiology.proteinFungal enzymesRhizopusBiochemistry
researchProduct

The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One

2017

Show your metal: l-Tyrosine is converted into the protective antioxidative polymer melanin in a sequence of reactions. In humans, the catalytic pathway starts with the tyrosinase HsTYR and two tyrosinase-related proteins HsTYRP1 and HsTYRP2. All three enzymes have the same active site but the latter two contain two zinc ions instead of copper ions.

Protein ConformationTyrosinasechemistry.chemical_elementNanotechnologyZincCrystallography X-Ray010402 general chemistry01 natural sciencesAntioxidantsCatalysisMelaninProtein structureCatalytic DomainHumansTYRP1MelanosomeMelaninschemistry.chemical_classificationMembrane Glycoproteinsbiology010405 organic chemistryActive siteGeneral ChemistryCombinatorial chemistry0104 chemical sciencesZincEnzymechemistrybiology.proteinTyrosineOxidoreductasesCopperAngewandte Chemie International Edition
researchProduct

Inhibition of prolyl hydroxylation and procollagen processing in chick-embryo calvaria by a derivative of pyridine-2,4-dicarboxylate. Characterizatio…

1991

The biochemical and morphological consequences of procollagen prolyl 4-hydroxylase inhibition by pyridine-2,4-dicarboxylic acid (2,4-PDCA) and its diethyl ester (diethyl-2,4-PDC) were studied in chick-embryo calvaria, which predominantly synthesize type I collagen. Half-maximal inhibition of tissue hydroxyproline formation required 650 microM-2,4-PDCA, whereas the Ki with respect to chicken prolyl 4-hydroxylase in vitro was 2 microM. In contrast, half-maximal inhibition was caused by 10 microM-diethyl-2,4-PDC in the intact calvaria, although chicken prolyl 4-hydroxylase in vitro was not inhibited even at 1 mM. The collagenous material produced in the presence of diethyl-2,4-PDC showed an al…

Protein DenaturationProtein ConformationPyridinesProcollagen-Proline DioxygenaseCalvariaChick EmbryoEndoplasmic ReticulumModels BiologicalBiochemistryBone and BonesHydroxylationHydroxyprolinechemistry.chemical_compoundmedicineAnimalsMolecular BiologyCells CulturedEndoplasmic reticulumCell BiologyIn vitroKineticsProcollagen peptidasemedicine.anatomical_structurechemistryBiochemistryMicrosomeCollagenProcollagenType I collagenResearch ArticleBiochemical Journal
researchProduct

Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: basis for a virus-like particle ELISA.

2004

In this article, we demonstrate that interaction of human papillomavirus-like particles (HPV-VLPs) with the putative glucosaminoglycan binding receptor is strictly dependent on conformational integrity. Such conformations are present on VLPs and capsomeres but not on monomers of the major capsid protein, L1, confirming reports that capsomeres can induce virus-neutralizing antibodies. Furthermore, we show the suitability of this specific interaction for development of VLP-based enzyme-linked immunosorbent assays (ELISAs), using heparin for indirect coupling of VLPs to microtiter plates, which may add an intrinsic quality control. This avoids presentation of linear, often highly cross-reactiv…

Protein DenaturationProtein ConformationvirusesEnzyme-Linked Immunosorbent AssayPlasma protein bindingCross ReactionsAntibodies ViralEpitopeEpitopesProtein structureVirus-like particleNeutralization TestsVirologyCentrifugation Density GradientHumansPapillomaviridaeGlycosaminoglycansbiologyHeparinCapsomerevirus diseasesOncogene Proteins ViralVirologyInfectious DiseasesProteoglycanCapsidbiology.proteinReceptors VirusCapsid ProteinsHeparan Sulfate ProteoglycansConformational epitopeProtein BindingJournal of medical virology
researchProduct

Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex.

2002

Folding and post-translational modification of the thyroid hormone precursor, thyroglobulin (Tg), in the endoplasmic reticulum (ER) of the thyroid epithelial cells is facilitated by several molecular chaperones and folding enzymes, such as BiP, GRP94, calnexin, protein disulfide isomerase, ERp72, and others. They have been shown to associate simultaneously and/or sequentially with Tg in the course of its maturation, thus forming large heterocomplexes in the ER of thyrocytes. Here we present evidence that such complexes include a novel member, an ER-resident lumenal protein, ERp29, which is present in all mammalian tissues with exceptionally high levels of expression in the secretory cells. …

Protein DenaturationProtein FoldingImmunoprecipitationmedicine.medical_treatmentBlotting WesternThyroid GlandThyrotropinBiologyEndoplasmic ReticulumLigandsBiochemistryThyroglobulinRats Sprague-DawleyCalnexinmedicineCentrifugation Density GradientAnimalsUreaSecretionProtein disulfide-isomeraseMolecular BiologyCells CulturedHeat-Shock ProteinsThyroid Epithelial CellsChromatographyEndoplasmic reticulumCell BiologyPrecipitin TestsRatsCross-Linking ReagentsBiochemistryLiverMicroscopy FluorescenceMicrosomes LiverProtein foldingThyroglobulinProtein BindingThe Journal of biological chemistry
researchProduct

Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics

2015

Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we present an in vitro and in silico characterization of native neuroserpin and its dysfunctional conformation isoforms: the proteolytically cleaved conformer, the inactive latent conformer, and the polymeric species. Based on circular dichroism and fluorescence spectroscopy, we present an experimental validation of the latent model and highlight the main structural features of the different conformers. In particular, emission spectra of aromatic res…

Protein FoldingCircular dichroismSerine Proteinase InhibitorsProtein ConformationStereochemistryNeuroserpinBiophysicsEpilepsies MyoclonicMolecular Dynamics SimulationSerpinMolecular DynamicsBiochemistryProtein Structure SecondaryArticleFluorescenceAnalytical ChemistryMolecular dynamicsProtein structureNeuroserpinmedicineHumansProtein IsoformsFluorescence emission spectra; circular dichroism; neuroserpin latent conformationneuroserpin latent conformationFamilial encephalopathy with neuroserpin inclusion bodiesMolecular BiologyConformational isomerismSerpinsFluorescence emission spectraSerpinChemistryCircular DichroismConformational diseaseNeuropeptidesHydrogen Bondingmedicine.diseaseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Heredodegenerative Disorders Nervous SystemProtein foldingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
researchProduct

Disulfide stress: a novel type of oxidative stress in acute pancreatitis.

2013

Glutathione oxidation and protein glutathionylation are considered hallmarks of oxidative stress in cells because they reflect thiol redox status in proteins. Our aims were to analyze the redox status of thiols and to identify mixed disulfides and targets of redox signaling in pancreas in experimental acute pancreatitis as a model of acute inflammation associated with glutathione depletion. Glutathione depletion in pancreas in acute pancreatitis is not associated with any increase in oxidized glutathione levels or protein glutathionylation. Cystine and homocystine levels as well as protein cysteinylation and γ-glutamyl cysteinylation markedly rose in pancreas after induction of pancreatitis…

Protein FoldingFree RadicalsCystineProtein Disulfide-IsomerasesProtein glutathionylationmedicine.disease_causeBiochemistrychemistry.chemical_compoundStress PhysiologicalPhysiology (medical)medicineAnimalsCysteineDisulfidesSulfhydryl CompoundsProtein disulfide-isomeraseGlutathione DisulfideProtein phosphatase 2GlutathioneKEAP1Oxidative StressBiochemistrychemistryPancreatitisOxidation-ReductionOxidative stressCysteineFree radical biologymedicine
researchProduct