Search results for " Lysine"

showing 6 items of 6 documents

Histone H3 Lysine 4 Mono-methylation does not Require Ubiquitination of Histone H2B

2005

The yeast Set1-complex catalyzes histone H3 lysine 4 (H3K4) methylation. Using N-terminal Edman sequencing, we determined that 50% of H3K4 is methylated and consists of roughly equal amounts of mono, di and tri-methylated H3K4. We further show that loss of either Paf1 of the Paf1 elongation complex, or ubiquitination of histone H2B, has only a modest effect on bulk histone mono-methylation at H3K4. Despite the fact that Set1 recruitment decreases in paf1delta cells, loss of Paf1 results in an increase of H3K4 mono-methylation at the 5' coding region of active genes, suggesting a Paf1-independent targeting of Set1. In contrast to Paf1 inactivation, deleting RTF1 affects H3K4 mono-methylation…

Histone H3 Lysine 4UbiquitinLysineSaccharomyces cerevisiaeBiologyMethylationenvironment and public healthMolecular biologyCell biologyHistonesHistone H1Structural BiologyHistone methyltransferaseHistone H2AHistone methylationHistone H2BHistone codeHistone octamerMolecular BiologyJournal of Molecular Biology
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The amide of galacturonic acid with lysine as an immunodominant component of the lipopolysaccharide core region from Proteus penneri 42 strain

2014

Most Proteus lipopolysaccharides (LPSs) contain uronic acids or their amides with different amino acids, which together with other negatively charged components account for the acidic character of such LPS molecules. Previous studies have shown the significance of an amide of galacturonic acid with lysine [D-GalA(L-Lys)] for serological specificity of O-antigens from few P. mirabilis strains. In this work, the immunodominant role of GalALys was indicated for the P. penneri 42 LPS core region. The studies also showed the serological identity of core oligosaccharides from P. penneri 42 (O71), P. mirabilis 51/57 (O28) and R14/S1959 strains. from P. penneri 42 (O71), P. mirabilis 51/57 (O28) an…

LipopolysaccharidesLipopolysaccharideStereochemistryLysineProteus penneriGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundAmideGalacturonic acidchemistry.chemical_classificationbiologyStrain (chemistry)Immunodominant EpitopesHexuronic AcidsLysineanti-conjugate serumlipopolysaccharideO AntigensProteusbiology.organism_classificationAmidesProteus penneriAmino acidProteusamide of galacturonic acid with lysinecore regionchemistryBiochemistry
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The SGLT2 inhibitor empagliflozin improves the primary diabetic complications in ZDF rats

2017

Hyperglycemia associated with inflammation and oxidative stress is a major cause of vascular dysfunction and cardiovascular disease in diabetes. Recent data reports that a selective sodium-glucose co-transporter 2 inhibitor (SGLT2i), empagliflozin (Jardiance®), ameliorates glucotoxicity via excretion of excess glucose in urine (glucosuria) and significantly improves cardiovascular mortality in type 2 diabetes mellitus (T2DM). The overarching hypothesis is that hyperglycemia and glucotoxicity are upstream of all other complications seen in diabetes. The aim of this study was to investigate effects of empagliflozin on glucotoxicity, β-cell function, inflammation, oxidative stress and endothel…

Male0301 basic medicineendocrine system diseasesDiabetic CardiomyopathiesFPS-ZM1 RAGE inhibitorClinical BiochemistryAorta ThoracicRAGE receptor for AGEICAM-1 intercellular adhesion molecule-1ECL enhanced chemiluminescence030204 cardiovascular system & hematologyDPP-4 dipeptidyl peptidase-4medicine.disease_causeTNF-α tumor necrosis factor-αBiochemistryeNOS endothelial •NO synthase (type 3)0302 clinical medicineGlucosidesecSOD extracellular superoxide dismutaseInsulin-Secreting CellsCCL-2 see MCP-1HyperlipidemiaHyperinsulinemiaGTN glyceryl trinitrate (nitroglycerin)IFN-γ interferon-γDHE dihydroethidineEndothelial dysfunctionEndothelial dysfunctionIL-6 interleukin-6lcsh:QH301-705.5HO-1 heme oxygenase-1lcsh:R5-920ICAM-1NG normoglycemiaDiabetesNox catalytic subunit of NADPH oxidaseSGLT2 inhibitorβ-cell contentL-012 8-amino-5-chloro-7-phenylpyrido[34-d]pyridazine-14-(2H3H)dione sodium saltChIP chromatin immunoprecipitationC-Reactive ProteinCRP C-reactive proteinAGE advanced glycation end productsHbA1c glycohemoglobinlcsh:Medicine (General)Research PaperZucker diabetic fatty ratsmedicine.medical_specialtyDMSO dimethylsulfoxideMCP-1 monocyte-chemoattractant-protein-1qRT-PCR quantitative reverse transcription polymerase chain reactionZDF Zucker diabetic fatty (rat)Low-grade inflammation03 medical and health sciencesROS reactive oxygen speciesSodium-Glucose Transporter 2Physiology (medical)Internal medicineDiabetes mellitusPKC protein kinase CEmpagliflozinmedicineAnimalsHypoglycemic AgentsBenzhydryl CompoundsCOX2 cyclooxygenase-2SGLT2i SGLT2 inhibitorSodium-Glucose Transporter 2 InhibitorsGlycated HemoglobinACh acetylcholinebusiness.industryOrganic Chemistrynutritional and metabolic diseasesType 2 Diabetes Mellitusmedicine.diseaseH2K9me2 histone3 lysine9 dimethylationRatsRats ZuckerDHFR dihydrofolate reductaseSGLT2 sodium-glucose co-transporter-2Oxidative StresssGC soluable guanylyl cyclaseGlucose030104 developmental biologyEndocrinologylcsh:Biology (General)ALDH-2 mitochondrial aldehyde dehydrogenaseEndothelium VascularAGE/RAGE signalingHG hyperglycemiabusinessOxidative stressRedox Biology
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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Enhancement of lysine acetylation accelerates wound repair

2013

In physiopathological conditions, such as diabetes, wound healing is significantly compromised and chronic complications, including ulcers, may occur. In a mouse model of skin repair, we recently reported that wound treatment with Sirtuin activators and class I HDAC inhibitors induced keratinocyte proliferation and enhanced healing via a nitric oxide (NO) dependent mechanism. We observed an increase in total protein acetylation in the wound area, as determined by acetylation of α-tubulin and histone H3 Lysine 9. We reasoned that this process activated cell function as well as regulated gene expression to foster tissue repair. We report here that the direct activation of P300/CBP-associated …

Skin repairWound HealingepigeneticsActivator (genetics)Short CommunicationkeratinocyteBiologyNitric OxideCell biologyHistone H3medicine.anatomical_structureepigenetics; pathology Wound Healing; lysine acetylation; PCAF; keratinocyte; Nitric OxideBiochemistryPCAFAcetylationPCAFSirtuinmedicinebiology.proteinpathologyGeneral Agricultural and Biological SciencesKeratinocyteWound healinglysine acetylationCommunicative & Integrative Biology
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Persistence of a mixed lactic acid bacterial starter culture during lysine fortification of sourdough breads by addition of pistachio powder

2020

Abstract Pistachio powder was added to flour or semolina to evaluate its contribution to increase the amount of lysine in bread. Bread production was carried out by sourdough technology using a selected 3-species (Lactobacillus sanfranciscensis/Leuconostoc citreum/Weissella cibaria) lactic acid bacterial (LAB) starter culture. All sourdoughs were subjected to a long-time fermentation (21 h) and showed levels of LAB around 109 CFU/g, indicating the suitability of pistachio powder for lactic fermentation. Yeasts were also detected, in particular in semolina trials. MiSeq Illumina technology was applied to investigate the bacterial composition of sourdoughs evidencing a different distribution …

WeissellaFlourSettore AGR/13 - Chimica AgrariaLactobacillus sanfranciscensisBread fortificationmedicine.disease_causeMicrobiology03 medical and health scienceschemistry.chemical_compoundLeuconostoc citreumLactobacillusmedicineLactic acid bacteriaHumansFood scienceVolatile organic compoundsWeissella cibaria030304 developmental biologyPistacia vera0303 health sciencesbiology030306 microbiologyChemistryLysinedigestive oral and skin physiologyfood and beveragesBreadbiology.organism_classificationLactic acidLactobacillusSettore AGR/15 - SCIENZE E TECNOLOGIE ALIMENTARITasteWeissellaSourdoughFermentationFood FortifiedPistaciaFood AdditivesBread fortification Lactic acid bacteria Lysine Pistacia vera Sourdough Volatile organic compoundFermentationLeuconostocLactic acid fermentationSettore AGR/16 - Microbiologia AgrariaFood Science
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