Search results for "1303 Biochemistry"

showing 7 items of 37 documents

Sequence of a novel cytochrome CYP2B cDNA coding for a protein which is expressed in a sebaceous gland, but not in the liver

1992

The major phenobarbital-inducible rat hepatic cytochromes P-450, CYP2B1 and CYP2B2, are the paradigmatic members of a cytochrome P-450 gene subfamily that contains at least seven additional members. Specific oligonucleotide probes for these genomic members of the CYP2B subfamily were used to assess their tissue-specific expression. In Northern-blot analysis a probe specific to gene 4 (which is designated now as CYP2B12) hybridized to a single mRNA present in the preputial gland, an organ which is used as a model for sebaceous glands, but did not hybridize to mRNA isolated from the liver or from five other tissues of untreated or Aroclor 1254-treated rats. The cDNA sequence for the CYP2B12 R…

MaleSubfamily1303 BiochemistryMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiologyBiochemistryRats Sprague-Dawley1307 Cell BiologySebaceous GlandsRapid amplification of cDNA endsCytochrome P-450 Enzyme SystemComplementary DNAMicrosomes1312 Molecular BiologyCoding regionAnimalsAmino Acid SequenceMolecular BiologyBase SequencecDNA librarySingle-Strand Specific DNA and RNA EndonucleasesProtein primary structureNucleic acid sequenceCell BiologyDNARibonuclease PancreaticBlotting NorthernMolecular biologyRatsOpen reading frameBiochemistryLiverMultigene FamilyMicrosomes Liver570 Life sciences; biologyFemaleOligonucleotide ProbesResearch Article
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The predictive role of atherogenic dyslipidemia in subjects with non-coronary atherosclerosis

2009

Abstract Background Recent findings have suggested that subjects with non-coronary atherosclerosis may show elevated prevalence of atherogenic dyslipidemia, including higher triglyceride levels, reduced HDL-cholesterol concentrations and increased levels of small, dense low-density lipoproteins (LDL). These three lipid abnormalities constitute the so-called “atherogenic-lipoprotein-phenotype” (ALP) but its predictive role in these patients still remains to be established. Methods We performed a 2-year follow-up study to assess clinical and biochemical predictors of cardiovascular events in 44 male patients (64 ± 5 years, BMI: 27 ± 3), 26 with peripheral arterial disease and 18 with abdomina…

Malemedicine.medical_specialtyMultivariate analysis1303 BiochemistryClinical Biochemistry10265 Clinic for Endocrinology and Diabetology610 Medicine & health1308 Clinical Biochemistry2704 Biochemistry (medical)Biochemistrychemistry.chemical_compoundRisk Factorsatherogenic dyslipidemiaInternal medicineDiabetes mellitusmedicineHumansFamily historyCoronary atherosclerosisDyslipidemiasPeripheral Vascular DiseasesUnivariate analysisTriglyceridebusiness.industryBiochemistry (medical)Cholesterol LDLGeneral MedicineMiddle AgedAtherosclerosismedicine.diseaseAbdominal aortic aneurysmPeripheralPhenotypechemistryCase-Control StudiesMultivariate AnalysisCardiologyAtherosclerosis HDL-cholesterol Triglycerides Small dense LDL Atherogenic lipoprotein phenotypebusinessAortic Aneurysm AbdominalFollow-Up Studies
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IL-6 Regulates Neutrophil Microabscess Formation in IL-17A-Driven Psoriasiform Lesions

2014

The lack of a generally accepted animal model for human psoriasis has hindered progress with respect to understanding the pathogenesis of the disease. Here we present a model in which transgenic IL-17A expression is targeted to the skin in mice, achievable after crossing our IL-17A(ind) allele to the K14-Cre strain. K14-IL-17A(ind/+) mice invariably develop an overt skin inflammation bearing many hallmark characteristics of human psoriasis including dermal infiltration of effector T cells, formation of neutrophil microabscesses, and hyperkeratosis. IL-17A expression in the skin results in upregulated granulopoiesis and migration of IL-6R-expressing neutrophils into the skin. Neutralization …

Pathologymedicine.medical_specialty1303 BiochemistryNeutrophilsT-LymphocytesHyperkeratosisGene Expression610 Medicine & healthInflammationDermatology10263 Institute of Experimental ImmunologyBiochemistryGranulopoiesis2708 Dermatology1307 Cell BiologyPathogenesisMicePsoriasis1312 Molecular BiologymedicineAnimalsPsoriasisMicroabscessMolecular BiologyMice Knockoutintegumentary systemInterleukin-6business.industryMacrophagesInterleukin-17Cell Biologymedicine.diseaseReceptors Interleukin-6AbscessDisease Models AnimalImmunology570 Life sciences; biologyEpidermismedicine.symptombusinessInfiltration (medical)GranulocytesSignal TransductionEpidermal thickeningJournal of Investigative Dermatology
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Reproducible and Consistent Quantification of the Saccharomyces cerevisiae Proteome by SWATH-mass spectrometry *

2015

Targeted mass spectrometry by selected reaction monitoring (S/MRM) has proven to be a suitable technique for the consistent and reproducible quantification of proteins across multiple biological samples and a wide dynamic range. This performance profile is an important prerequisite for systems biology and biomedical research. However, the method is limited to the measurements of a few hundred peptides per LC-MS analysis. Recently, we introduced SWATH-MS, a combination of data independent acquisition and targeted data analysis that vastly extends the number of peptides/proteins quantified per sample, while maintaining the favorable performance profile of S/MRM. Here we applied the SWATH-MS t…

ProteomicsOsmosisSaccharomyces cerevisiae Proteins1303 BiochemistryOsmotic shockSaccharomyces cerevisiae610 Medicine & health10071 Functional Genomics Center ZurichSaccharomyces cerevisiaeOsmosisMass spectrometryBiochemistryMass SpectrometryAnalytical Chemistry1312 Molecular BiologyData-independent acquisitionMolecular Biology1602 Analytical ChemistryChromatographybiologySelected reaction monitoringTechnological Innovation and ResourcesReproducibility of Resultsbiology.organism_classificationTargeted mass spectrometryProteomeCarbohydrate Metabolism570 Life sciences; biologyPeptidesMolecular & Cellular Proteomics
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The membrane anchor of microsomal epoxide hydrolase from human, rat, and rabbit displays an unexpected membrane topology.

1997

The microsomal epoxide hydrolase (mEH) and cytochrome P450s catalyze the sequential formation of carcinogenic metabolites. According to one algorithm for predicting the membrane topology of proteins, the human, the rabbit, and the rat mEH should adopt a type II topology. The type II topology is also predicted by a recently established neuronal network which is trained to recognize signal peptides with very high accuracy. In contrast to these predictions we find, based on N-glycosylation analysis in a cell-free and in a cellular system, that the membrane anchor of human, rat, and rabbit mEH displays a type I topology. This result is correctly predicted by the positive inside rule in which ne…

Signal peptide1303 BiochemistryGlycosylationGlycosylationCytochromeStereochemistryRecombinant Fusion ProteinsImmunoblottingMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthProtein Sorting SignalsTransfectionBiochemistry1307 Cell BiologyCell membranechemistry.chemical_compoundSpecies Specificity1312 Molecular BiologymedicineElectrochemistryAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequenceEpoxide HydrolasesbiologyCell MembraneCell BiologyRatsmedicine.anatomical_structurechemistryMutagenesisMicrosomal epoxide hydrolaseMembrane topologyEpoxide HydrolasesCOS Cellsbiology.protein570 Life sciences; biologyRabbits1304 BiophysicsBiochemical and biophysical research communications
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Reaction of an open-chain analogue of Reissert compound hydrofluoroborate salt with ethyl acrylate. A reinvestigation

1998

Abstract The reaction of an open-chain analogue of Reissert compound hydrofluoroborate salt with ethyl acrylate does not give a [4+2] cycloadduct as previously described, but a [3+2] cycloadduct which evolves to a 2-pyridone 15.

chemistry.chemical_classification10120 Department of Chemistry1303 Biochemistry3002 Drug DiscoveryOrganic ChemistrySalt (chemistry)BiochemistryMedicinal chemistrychemistry.chemical_compoundchemistryChain (algebraic topology)Drug Discovery540 ChemistryEthyl acrylateOrganic chemistry1605 Organic Chemistry
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Epoxide Hydrolases: Structure, Function, Mechanism, and Assay

2005

Epoxide hydrolases are a class of enzymes important in the detoxification of genotoxic compounds, as well as in the control of physiological signaling molecules. This chapter gives an overview on the function, structure, and enzymatic mechanism of structurally characterized epoxide hydrolases and describes selected assays for the quantification of epoxide hydrolase activity.

chemistry.chemical_classificationCell signaling1303 BiochemistryStereochemistry10050 Institute of Pharmacology and Toxicology610 Medicine & healthEpoxide hydrolase activityEnzymeBiochemistrychemistryDetoxificationEpoxide Hydrolases1312 Molecular Biology570 Life sciences; biologyProtein foldingEpoxide hydrolaseFunction (biology)
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