Search results for "Histidine"

showing 10 items of 152 documents

Tuning the pH-Switch of Supramolecular Polymer Carriers for siRNA to Physiologically Relevant pH

2017

The preparation of histidine enriched dendritic peptide amphiphiles and their self-assembly into multicomponent pH-switchable supramolecular polymers is reported. Alternating histidine and phenylalanine peptide synthons allow the assembly/disassembly to be adjusted in a physiologically relevant range of pH 5.3-6.0. Coassembly of monomers equipped with dendritic tetraethylene glycol chains with monomers bearing peripheral primary amine groups leads to nanorods with a tunable cationic surface charge density. These surface functional supramolecular polycations are able to reversibly bind short interfering RNA (siRNA). The nanorod-like supramolecular polymers, their complexation with siRNA, and…

DendrimersCircular dichroismPolymers and PlasticsStereochemistryPhenylalanineStatic ElectricitySupramolecular chemistryBioengineeringPeptide02 engineering and technology010402 general chemistry01 natural sciencesPolyethylene GlycolsBiomaterialschemistry.chemical_compoundCationsAmphiphileMaterials ChemistryHistidineRNA Small Interferingchemistry.chemical_classificationDrug CarriersNanotubesGene Transfer Techniquestechnology industry and agricultureCationic polymerizationHydrogen-Ion Concentration021001 nanoscience & nanotechnologyCombinatorial chemistry0104 chemical sciencesSupramolecular polymersMonomerchemistrySelf-assemblyPeptides0210 nano-technologyBiotechnology
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Expression and purification of polyhistidine-tagged rotavirus NSP4 proteins in insect cells

2003

The rotavirus nonstructural NSP4 protein, a transmembrane endoplasmic reticulum-specific glycoprotein, has been described as the first viral enterotoxin. Purified NSP4 or a peptide corresponding to NSP4 residues 114-135 induces diarrhea in young mice. NSP4 has a membrane-destabilizing activity and causes an increase in intracellular calcium levels and chloride secretion by a calcium-dependent signalling pathway in eucaryotic cells. In this study, four recombinant baculoviruses were generated expressing the rotavirus NSP4 glycoprotein from the human strains Wa and Ito, the porcine strain OSU, and the simian strain SA11, which belong to two different NSP4 genotypes, A and B. The recombinant g…

DiarrheaRotavirusGlycosylationInsectaImmunoprecipitationRecombinant Fusion ProteinsvirusesGenetic VectorsViral Nonstructural ProteinsProtein Engineeringmedicine.disease_causelaw.inventionMicelawRotavirusmedicineAnimalsHumansHistidinePolyacrylamide gel electrophoresisCells CulturedGlycoproteinsToxins Biologicalchemistry.chemical_classificationChemistryEndoplasmic reticulumbiochemical phenomena metabolism and nutritionMolecular biologyTransmembrane proteinBlotGene Expression RegulationRecombinant DNAElectrophoresis Polyacrylamide GelGlycoproteinBiotechnologyProtein Expression and Purification
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Crystal structure of human gamma-butyrobetaine hydroxylase.

2010

Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domai…

EGF-like domainStereochemistrygamma-Butyrobetaine DioxygenaseBiophysicsDrug designBiochemistryHydroxylationchemistry.chemical_compoundDioxygenaseCatalytic DomainHumansEnzyme InhibitorsMolecular BiologyHistidinechemistry.chemical_classificationCrystallographybiologyActive siteCell BiologyRecombinant ProteinsZincEnzymeBiochemistrychemistryCyclic nucleotide-binding domainDrug Designbiology.proteinProtein MultimerizationMethylhydrazinesBiochemical and biophysical research communications
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An Improved Force Field for O2, CO and CN Binding to Metalloporphyrins

2004

Parametrization of a molecular-mechanics program to include terms specific for five- and six-coordinate transition metal complexes is applied to heme complexes. The principal new feature peculiar to five and six coordination is a term that represents the effect of electron-pair repulsion modified by the ligand electronegativity and takes into account the different possible structures of complexes. The model system takes into account the structural differences of the fixing centre in the haemoglobin subunits. The customary proximal histidine is added. The macrocycle heme IX is wholly considered in our model. The calculations show clearly that certain conformations of heme IX–histidine models…

Electronegativitychemistry.chemical_compoundTransition metalchemistryMyoglobinComputational chemistryLigandBent molecular geometryPorphyrinHemeHistidineJournal of Inclusion Phenomena
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Oligomeric Sensor Kinase DcuS in the Membrane of Escherichia coli and in Proteoliposomes: Chemical Cross-linking and FRET Spectroscopy

2010

The DcuSR (dicarboxylate uptake sensor and regulator) system of Escherichia coli is a typical two-component system consisting of a membranous sensor kinase (DcuS) and a cytoplasmic response regulator (DcuR) (11, 26, 48). DcuS responds to C4-dicarboxylates like fumarate, malate, or succinate (19). In the presence of the C4-dicarboxlates, the expression of the genes of anaerobic fumarate respiration (dcuB, fumB, and frdABCD) and of aerobic C4-dicarboxylate uptake (dctA) is activated. DcuS is a histidine protein kinase composed of two transmembrane helices with an intermittent sensory PAS domain in the periplasm (PASP) that was also termed the PDC domain (for PhoQ/DcuS/DctB/CitA domain or fold…

Escherichia coli ProteinsProteolipidsCell MembraneGreen Fluorescent ProteinsHistidine kinaseAutophosphorylationBiologyMicrobiologyLuminescent ProteinsResponse regulatorTransmembrane domainSpectrometry FluorescenceProtein kinase domainBiochemistryPAS domainEscherichia coliFluorescence Resonance Energy TransferKinase activityProtein kinase AProtein KinasesMolecular BiologySignal TransductionJournal of Bacteriology
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Risk Assessment of "Other Substances" – L-Histidine

2020

The Norwegian Scientific Committee for Food Safety (Vitenskapskomiteen for mattrygghet, VKM) has, at the request of the Norwegian Food Safety Authority (Mattilsynet; NFSA), assessed the risk of "other substances" in food supplements and energy drinks sold in Norway. VKM has assessed the risk of doses given by NFSA. These risk assessments will provide NFSA with the scientific basis for regulating "other substances" in food supplements.
 "Other substances" are described in the food supplement directive 2002/46/EC as substances other than vitamins or minerals that have a nutritional and / or physiological effect. It is added mainly to food supplements, but also to energy drinks and other …

Food supplementbusiness.industryAdverse health effectEnvironmental healthMedicinebusinessRisk assessmentHistidineEuropean Journal of Nutrition & Food Safety
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RNA-binding activity of the rat calmodulin-binding PEP-19 protein and of the long PEP-19 isoform

2012

Synthesis of H1˚ histone protein, in the developing rat brain, seems to be regulated mainly at the post-transcriptional level. Since regulation of RNA metabolism depends on a series of RNA-binding proteins, we have been searching for RNA-binding proteins involved in the post-transcriptional regulation of the H1˚ gene. We recently reported isolation, from a cDNA expression library, of an insert encoding a novel protein, the C-terminal half of which is identical to that of PEP-19, a brain-specific protein involved in calcium metabolism. The novel protein was called long PEP-19 isoform (LPI). Herein we show that LPI, as well as PEP-19, can bind H1˚ RNA. Moreover, in order to improve production…

Gene isoformCalmodulinCalmodulin binding domainNerve Tissue ProteinsRNA-binding proteinRNA-binding proteins histone variants H1˚ PEP-19 long PEP-19 isoform calmodulinBiologyBinding CompetitiveRats Sprague-DawleyCalmodulinGeneticsAnimalsProtein IsoformsE2F1RNA Processing Post-TranscriptionalGeneHistidineRNA-Binding ProteinsRNAGeneral MedicineMolecular biologyRatsBiochemistrybiology.proteinRNACalmodulin-Binding ProteinsProtein BindingInternational Journal of Molecular Medicine
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An operon for histidine biosynthesis in Streptomyces coelicolor

1973

On the assumption that a cluster of five his genes (eight cistrons) in S. coelicolor corresponds to an operon, a genetic analysis of a constitutive mutant was carried out. This strain has a multi-site mutation localized at the (conventional) right end of the his cluster and is derepressed for at least two enzymes coded by genes of the cluster. The study of suitable heterozygous clones (heteroclones), showed the mutation to be cis-dominant, suggesting that the operator region is affected. Most likely the strain has a deletion connecting the his operon to an adjacent amm (ammonium requirement) operon as demonstrated by its inability to utilize nitrate as nitrogen source and to complement or r…

Genetics MicrobialHeterozygoteOperator (biology)Genetic LinkageOperonBiologyGenetic analysisOperonGeneticsHistidineAminesMolecular BiologyGeneAllelesCrosses GeneticGenes Dominantchemistry.chemical_classificationGeneticsNitratesStrain (chemistry)Streptomyces coelicolorChromosome MappingDrug Resistance Microbialbiology.organism_classificationStreptomycesQuaternary Ammonium CompoundsButyratesEnzymechemistryMutation (genetic algorithm)Molecular and General Genetics MGG
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Further characterization of the histidine gene cluster of Streptomyces coelicolor A3(2): nucleotide sequence and transcriptional analysis of hisD.

1992

We have further characterized the genomic region of Streptomyces coelicolor A3(2) that contains genes involved in the biosynthesis of histidine. A 2,357-base pair fragment contained in plasmid pSCH3328 that complemented hisD mutations has been sequenced. Computer analysis revealed an open reading frame that encodes a protein with significant homology to the Escherichia coli, Salmonella typhimurium and Mycobacterium smegmatis hisD product, Saccharomyces cerevisiae HIS4C, and Neurospora crassa his3 gene products. Two other contiguous open reading frames oriented divergently with respect to hisD did not show significant similarity with any of the his genes or to other sequences included in the…

GeneticsDNA BacterialbiologyBase SequenceTranscription GeneticStreptomyces coelicolorMolecular Sequence DataRestriction MappingNucleic acid sequenceGeneral MedicineIn Vitro Techniquesbiology.organism_classificationMicrobiologyPrimer extensionStreptomycesNeurospora crassaOpen reading frameOpen Reading FramesCistronGenes BacterialGene clusterHistidineMolecular BiologyGene
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Mechanism for polarized recombination in Streptomyces.

1968

Recombination between pairs of mutations in a cluster of seven cistrons controlling histidine biosynthesis is highly polarized. The polarity is opposite at the opposite ends of the region. In experiments involving three his mutations it has been shown that recombination is the result of the transfer, from one parent to the other, of a segment going from the distal selected his+ allele to the end of the region. The rate of transfer is inversely proportional to the distance of the transferred his+ allele from the end of the region, at its side. A model of the process of recombination is discussed.

GeneticsRecombination GeneticPolarity (international relations)biologyStereochemistryChromosome MappingHistidine biosynthesisbiology.organism_classificationStreptomycesModels BiologicalStreptomycesGeneticsHistidineCrossing Over GeneticAlleleMolecular BiologyRecombinationHistidineCrosses GeneticMoleculargeneral genetics : MGG
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