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showing 10 items of 1641 documents

Diverse relations between ABC transporters and lipids: An overview.

2016

It was first discovered in 1992 that P-glycoprotein (Pgp, ABCB1), an ATP binding cassette (ABC) transporter, can transport phospholipids such as phosphatidylcholine, -ethanolamine and -serine as well as glucosylceramide and glycosphingolipids. Subsequently, many other ABC transporters were identified to act as lipid transporters. For substrate transport by ABC transporters, typically a classic, alternating access model with an ATP-dependent conformational switch between a high and a low affinity substrate binding site is evoked. Transport of small hydrophilic substrates can easily be imagined this way, as the molecule can in principle enter and exit the transporter in the same orientation. …

0301 basic medicineModels MolecularATP Binding Cassette Transporter Subfamily BBiophysicsGene ExpressionATP-binding cassette transporterPhosphatidylserinesBiologyBiochemistrySubstrate SpecificitySerine03 medical and health sciencesLipid translocationHumansProtein IsoformsBinding siteLipid bilayerLipid TransportATP-binding domain of ABC transportersBinding SitesPhosphatidylethanolaminesFatty AcidsTransporterBiological TransportCell BiologyCell biology030104 developmental biologyBiochemistryPhosphatidylcholineslipids (amino acids peptides and proteins)Protein BindingBiochimica et biophysica acta. Biomembranes
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On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome

2018

Phytochromes are photoreceptors in plants, fungi, and various microorganisms and cycle between metastable red light-absorbing (Pr) and far-red light-absorbing (Pfr) states. Their light responses are thought to follow a conserved structural mechanism that is triggered by isomerization of the chromophore. Downstream structural changes involve refolding of the so-called tongue extension of the phytochrome-specific GAF-related (PHY) domain of the photoreceptor. The tongue is connected to the chromophore by conserved DIP and PRXSF motifs and a conserved tyrosine, but the role of these residues in signal transduction is not clear. Here, we examine the tongue interactions and their interplay with …

0301 basic medicineModels MolecularCrystallography X-RayBiochemistrybakteeritProtein structurephotoconversionchromophore-binding domainTransferasestructural biologyCRYSTAL-STRUCTURETyrosineDEINOCOCCUS-RADIODURANSbiologyPhytochromeChemistryREARRANGEMENTSProtein Structure and FoldingDeinococcusmutagenesisBinding domainSignal TransductionMODULEPLANT PHYTOCHROMEPhenylalaninefotobiologia03 medical and health sciencesBacterial Proteinsprotein conformationcell signalingprotein structureBACTERIOPHYTOCHROMEMolecular BiologyX-ray crystallographysoluviestintäphytochromeAGP1BINDING DOMAINBinding Sitesta114030102 biochemistry & molecular biologyta1182Deinococcus radioduransCell BiologyChromophorebiology.organism_classificationphotoreceptor030104 developmental biologyStructural biologyFTIRBiophysicsTyrosineproteiinit3111 Biomedicineröntgenkristallografia
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Addition of thiols to the double bond of dipeptide C-terminal dehydroalanine as a source of new inhibitors of cathepsin C.

2017

Addition of thiols to double bond of glycyl-dehydroalanine and phenyl-dehydroalanine esters provided micromolar inhibitors of cathepsin C. The structure-activity studies indicated that dipeptides containing N-terminal phenylalanine exhibit higher affinity towards the enzyme. A series of C-terminal S-substituted cysteines are responsible for varying interaction with S1 binding pocket of cathepsin C. Depending on diastereomer these compounds most likely act as slowly reacting substrates or competitive inhibitors. This was proved by TLC analysis of the medium in which interaction of methyl (S)-phenylalanyl-(R,S)-(S-adamantyl)cysteinate (7i) with the enzyme was studied. Molecular modeling enabl…

0301 basic medicineModels MolecularDouble bondStereochemistryPhenylalanineCysteine Proteinase InhibitorsBiochemistryCathepsin CCathepsin CSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity Relationship0302 clinical medicineDehydroalanineMoietyAnimalsSulfhydryl CompoundsBinding sitechemistry.chemical_classificationDipeptideAlanineBinding SitesDehydropeptidesDiastereomerEnzyme inhibitorsGeneral MedicineDipeptidesKinetics030104 developmental biologychemistryThiol addition030220 oncology & carcinogenesisCattleBiochimie
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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The hydrolysis of 6-phosphogluconolactone in the second step of pentose phosphate pathway occurs via a two-water mechanism.

2018

Hydrolysis reaction marks the basis of life yet the mechanism of this crucial biochemical reaction is not completely understood. We recently reported the mechanisms of hydrolysis of nucleoside triphosphate and phosphate monoester. These two reactions hydrolyze P-O-P and P-O-C linkages, respectively. Here, we present the mechanism of hydrolysis of δ-6-phosphogluconolactone, which is an important precursor in the second step of the pentose phosphate pathway. Its hydrolysis requires the cleavage of C-O-C linkage and its mechanism is hitherto unknown. We report three mechanisms of hydrolysis of δ-6-phosphogluconolactone based on density functional computations. In the energetically most favorab…

0301 basic medicineModels MolecularStereochemistryBiophysicsPentose phosphate pathway010402 general chemistryCleavage (embryo)01 natural sciencesBiochemistryGluconatesPentose Phosphate Pathway03 medical and health scienceschemistry.chemical_compoundHydrolysis6-Phosphogluconolactonechemistry.chemical_classificationBinding SitesHydrolysisOrganic ChemistryWaterPhosphate0104 chemical sciencesEcoRV030104 developmental biologyEnzymechemistryNucleoside triphosphateQuantum TheoryThermodynamicsBiophysical chemistry
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Coordination of the biliverdin D-ring in bacteriophytochromes.

2018

Phytochrome proteins translate light into biochemical signals in plants, fungi and microorganisms. Light cues are absorbed by a bilin chromophore, leading to an isomerization and a rotation of the D-ring. This relays the signal to the protein matrix. A set of amino acids, which is conserved across the phytochrome superfamily, holds the chromophore in the binding pocket. However, the functional role of many of these amino acids is not yet understood. Here, we investigate the hydrogen bonding network which surrounds the D-ring of the chromophore in the resting (Pr) state. We use UV/vis spectroscopy, infrared absorption spectroscopy and X-ray crystallography to compare the photosensory domains…

0301 basic medicineModels MolecularStereochemistryProtein ConformationProtein Data Bank (RCSB PDB)General Physics and Astronomyphytochrome proteinsbakteerit03 medical and health scienceschemistry.chemical_compoundProtein structureBacterial ProteinsProteobacteriabiochemical signalsDeinococcusPhysical and Theoretical ChemistryStigmatella aurantiacaBiliverdinBinding SitesbiologyPhytochromeBiliverdineta1182Deinococcus radioduransHydrogen BondingChromophorebiology.organism_classificationPhotochemical ProcessesD-ring030104 developmental biologychemistryproteiinitvalokemiaDeinococcusPhytochromeProtein BindingPhysical chemistry chemical physics : PCCP
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Peptide Processing Is Critical for T-Cell Memory Inflation and May Be Optimized to Improve Immune Protection by CMV-Based Vaccine Vectors.

2016

Cytomegalovirus (CMV) elicits long-term T-cell immunity of unparalleled strength, which has allowed the development of highly protective CMV-based vaccine vectors. Counterintuitively, experimental vaccines encoding a single MHC-I restricted epitope offered better immune protection than those expressing entire proteins, including the same epitope. To clarify this conundrum, we generated recombinant murine CMVs (MCMVs) encoding well-characterized MHC-I epitopes at different positions within viral genes and observed strong immune responses and protection against viruses and tumor growth when the epitopes were expressed at the protein C-terminus. We used the M45-encoded conventional epitope HGI…

0301 basic medicineMuromegalovirusEpitopes T-LymphocyteCD8-Positive T-LymphocytesLymphocyte ActivationPathology and Laboratory MedicineBiochemistryEpitopeMass SpectrometryMiceWhite Blood Cells0302 clinical medicineAnimal CellsMedicine and Health SciencesCytotoxic T celllcsh:QH301-705.5Antigens ViralImmune ResponseStainingVaccines SyntheticbiologyT CellsCell StainingHerpesviridae InfectionsFlow CytometryRecombinant Proteins3. Good healthmedicine.anatomical_structureMedical MicrobiologyViral PathogensVirusesHuman CytomegalovirusCellular TypesPathogensResearch Articlelcsh:Immunologic diseases. AllergyHerpesvirusesT cellImmune CellsAntigen presentationImmunologyCytotoxic T cellsMajor histocompatibility complexResearch and Analysis MethodsMicrobiology03 medical and health sciencesViral ProteinsImmune systemAntigenVirologyGeneticsmedicineAnimalsAntigen-presenting cellMolecular Biology TechniquesMolecular BiologyMicrobial PathogensBlood CellsImmunodominant EpitopesOrganismsBiology and Life SciencesProteinsViral VaccinesCell BiologyVirology030104 developmental biologylcsh:Biology (General)Specimen Preparation and Treatmentbiology.proteinMutagenesis Site-DirectedParasitologylcsh:RC581-607PeptidesDNA virusesImmunologic Memory030215 immunologyChromatography LiquidCloningPLoS pathogens
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Molecular docking-based design and development of a highly selective probe substrate for UDP-glucuronosyltransferase 1A10

2018

Intestinal and hepatic glucuronidation by the UDP-glucuronosyltransferases (UGTs) greatly affect the bioavailability of phenolic compounds. UGT1A10 catalyzes glucuronidation reactions in the intestine, but not in the liver. Here, our aim was to develop selective, fluorescent substrates to easily elucidate UGT1A10 function. To this end, homology models were constructed and used to design new substrates, and subsequently, six novel C3-substituted (4-fluorophenyl, 4-hydroxyphenyl, 4-methoxyphenyl, 4-(dimethylamino)phenyl, 4-methylphenyl, or triazole) 7-hydroxycoumarin derivatives were synthesized from inexpensive starting materials. All tested compounds could be glucuronidated to nonfluorescen…

0301 basic medicineMutantGlucuronidationPharmaceutical ScienceUGT1A10030226 pharmacology & pharmacySubstrate Specificity7-hydroxycoumarin derivativechemistry.chemical_compound0302 clinical medicineDrug DiscoveryCRYSTAL-STRUCTUREGlucuronosyltransferaseta116ta317AFFINITYchemistry.chemical_classificationChemistry3. Good healthMolecular ImagingMolecular Docking Simulation7-hydroxycoumarin317 Pharmacyin silicoMolecular MedicinefluorescenceUDP-glucuronosyltransferaseEXPRESSIONENZYMEStereochemistryIn silicoKineticsFLUORESCENT-PROBETriazoleta311103 medical and health sciencesGlucuronidesMicrosomesXENOBIOTICSHumansUmbelliferonesFluorescent DyesGLUCURONIDATIONta1182glucuronidationfluoresenssiSubstrate (chemistry)drug metabolism030104 developmental biologyEnzymeDRUG-METABOLISMDrug DesignMolecular ProbesMutationMutagenesis Site-DirectedORAL BIOAVAILABILITYDrug metabolism
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Archaeology and ichnology at Gombore II-2, Melka Kunture, Ethiopia: everyday life of a mixed age hominin group 700,000 years ago

2018

AbstractWe report the occurrence at 0.7 million years (Ma) of an ichnological assemblage at Gombore II-2, which is one of several archaeological sites at Melka Kunture in the upper Awash Valley of Ethiopia, 2000 m asl. Adults and children potentially as young as 12 months old left tracks in a silty substrate on the shore of a body of water where ungulates, as well as other mammals and birds, congregated. Furthermore, the same layers contain a rich archaeological and palaeontological record, confirming that knapping was taking place in situ and that stone tools were used for butchering hippo carcasses at the site. The site gives direct information on hominin landscape use at 0.7 Ma and may p…

0301 basic medicineOld Left010506 paleontologySciencegrowthtanzanialengthEnvironment01 natural sciencesArticlemultidisciplinary; growth; foot; children; site; footprints; tanzania; height; length; tracks; kenya; ethiopia03 medical and health sciencesIchnologychildrenGroup (stratigraphy)siteAssemblage (archaeology)AnimalsHumansEveryday lifeHistory Ancient0105 earth and related environmental sciencesShoregeography.geographical_feature_categoryKnappingFossilsQRPaleontologyHominidae15. Life on landfootprintstracksArchaeology030104 developmental biologyGeographykenyaArchaeologyfootMedicineethiopiamultidisciplinaryheight
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MicroRNA-30a-5pme: a novel diagnostic and prognostic biomarker for clear cell renal cell carcinoma in tissue and urine samples

2020

Abstract Background The rising incidence of renal cell carcinomas (RCC) constitutes a significant challenge owing to risk of overtreatment. Because aberrant microRNA (miR) promoter methylation contributes to cancer development, we investigated whether altered miR-30a-5p expression associates with DNA promoter methylation and evaluated the usefulness as clear cell RCC (ccRCC) diagnostic and prognostic markers. Methods Genome-wide methylome and RNA sequencing data from a set of ccRCC and normal tissue samples from The Cancer Genome Atlas (TCGA) database were integrated to identify candidate CpG loci involved in cancer onset. MiR-30a-5p expression and promoter methylation were quantitatively a…

0301 basic medicineOncologyClear cell renal cell carcinomaCancer Researchmedicine.medical_specialty610Urinelcsh:RC254-28203 medical and health sciences0302 clinical medicineInternal medicinemicroRNADiagnosisMedicineDNA methylationReceiver operating characteristicmicroRNAbusiness.industryResearchBiomarkermedicine.diseaselcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensPrognosisLog-rank testClear cell renal cell carcinoma030104 developmental biologyOncologyCpG site030220 oncology & carcinogenesisDNA methylationbusinessClear cellJournal of Experimental & Clinical Cancer Research : CR
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