Search results for "HILIC"

showing 10 items of 745 documents

eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences

2017

Abstract eIF5A is an essential protein involved in protein synthesis, cell proliferation and animal development. High eIF5A expression is observed in many tumor types and has been linked to cancer metastasis. Recent studies have shown that eIF5A facilitates the translation elongation of stretches of consecutive prolines. Activated eIF5A binds to the empty E-site of stalled ribosomes, where it is thought to interact with the peptidyl-tRNA situated at the P-site. Here, we report a genome-wide analysis of ribosome stalling in Saccharomyces cerevisiae eIF5A depleted cells using 5Pseq. We confirm that, in the absence of eIF5A, ribosomes stall at proline stretches, and extend previous studies by …

0301 basic medicinePeptidyl transferaseProlineCytoskeleton organizationAmino Acid MotifsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalSaccharomyces cerevisiaeBioinformaticsRibosomeGTP Phosphohydrolases03 medical and health sciences0302 clinical medicinePeptide Initiation FactorsGene Expression Regulation FungalGeneticsProtein biosynthesisHumansMolecular BiologyPolyproline helixBinding SitesbiologyRNA-Binding Proteinsbiology.organism_classificationStop codonCell biology030104 developmental biologybiology.proteinGenome FungalHydrophobic and Hydrophilic InteractionsRibosomesEIF5A030217 neurology & neurosurgeryProtein BindingNucleic Acids Research
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Comparison Study of Two Differently Clicked 18F-Folates—Lipophilicity Plays a Key Role

2018

Within the last decade, several folate-based radiopharmaceuticals for Single Photon Emission Computed Tomography (SPECT) and Positron Emission Tomography (PET) have been evaluated; however, there is still a lack of suitable 18F-folates for clinical PET imaging. Herein, we report the synthesis and evaluation of two novel 18F-folates employing strain-promoted and copper-catalyzed click chemistry. Furthermore, the influence of both click-methods on lipophilicity and pharmacokinetics of the 18F-folates was investigated. 18F-Ala-folate and 18F-DBCO-folate were both stable in human serum albumin. In vitro studies proved their high affinity to the folate receptor (FR). The lipophilic character of …

0301 basic medicinePharmaceutical Sciencelcsh:Medicinelcsh:RS1-441copper-catalyzed clickSingle-photon emission computed tomographyArticlelcsh:Pharmacy and materia medica03 medical and health sciencesfolic acid0302 clinical medicinePharmacokineticsIn vivoDrug Discoverymedicinemedicine.diagnostic_testChemistrylcsh:Rstrain promoted clickHuman serum albumin<sup>18</sup>F-folates; PET; folic acid; folate receptor; click chemistry; copper-catalyzed click; strain promoted click18F-folatesfolate receptor030104 developmental biologyPETPositron emission tomographyFolate receptor030220 oncology & carcinogenesisLipophilicityclick chemistryClick chemistryBiophysicsMolecular Medicinemedicine.drugPharmaceuticals
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Interaction of G protein coupled receptors and cholesterol

2016

G protein coupled receptors (GPCRs) form the largest receptor superfamily in eukaryotic cells. Owing to their seven transmembrane helices, large parts of these proteins are embedded in the cholesterol-rich plasma membrane bilayer. Thus, GPCRs are always in proximity to cholesterol. Some of them are functionally dependent on the specific presence of cholesterol. Over the last years, enormous progress on receptor structures has been achieved. While lipophilic ligands other than cholesterol have been shown to bind either inside the helix bundle or at the receptor-lipid interface, the binding site of cholesterol was either a single transmembrane helix or a groove between two or more transmembra…

0301 basic medicinePlasma protein bindingLigandsBiochemistryReceptors G-Protein-Coupled03 medical and health sciences0302 clinical medicineHumansBinding siteReceptorMolecular BiologyG protein-coupled receptorHelix bundleChemistryOrganic ChemistryCholesterol bindingCell BiologyTransmembrane domainCholesterol030104 developmental biologyBiochemistrylipids (amino acids peptides and proteins)LeucineHydrophobic and Hydrophilic Interactions030217 neurology & neurosurgeryProtein BindingChemistry and Physics of Lipids
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Viral Bcl2s' transmembrane domain interact with host Bcl2 proteins to control cellular apoptosis

2020

© The Author(s) 2020.

0301 basic medicineProgrammed cell deathScienceProtein domainGeneral Physics and AstronomyApoptosisBiologyVirus-host interactionsArticleGeneral Biochemistry Genetics and Molecular BiologyFluorescenceCell Line03 medical and health sciences0302 clinical medicineProtein Domainsimmune system diseaseshemic and lymphatic diseasesmedicineHumansAmino Acid SequenceAuthor CorrectionPeptide sequenceneoplasmsMultidisciplinaryVirus–host interactionsQCell MembraneGeneral ChemistryViral proteinsmedicine.diseaseControl cellLymphomaCell biologyVirusTransmembrane domain030104 developmental biologyProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisDoxorubicin030220 oncology & carcinogenesisbiological phenomena cell phenomena and immunityProtein MultimerizationHydrophobic and Hydrophilic InteractionsProteïnesProtein Binding
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The Crystal Structure of Gurmarin, a Sweet Taste–Suppressing Protein: Identification of the Amino Acid Residues Essential for Inhibition

2018

International audience; Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges that form a cystine knot. Here, we report the crystal structure of gurmarin at a 1.45 Å resolution and compare it with previously reported NMR solution structures. The atomic structure at this resolution allowed us to identify a very flexible region consisting of hydrophobic residues. Some of these amino acid residues had been identified as a putative binding site for the rat sweet taste receptor in a previous study. By combining alanine-scanning …

0301 basic medicineProtein ConformationPhysiologyCrystal structureCrystallography X-Ray03 medical and health sciencesBehavioral NeuroscienceGPCRsweet tastetaste receptorPhysiology (medical)goût sucréAnimalsHumansG protein-coupled receptorAmino AcidsBinding siteReceptorNuclear Magnetic Resonance BiomolecularPlant ProteinsGurmarininhibiteur030102 biochemistry & molecular biologybiologyChemistryMutagenesisCystine knotGymnema sylvestreSweet tastebiology.organism_classificationRecombinant ProteinsSensory SystemsRats3. Good healthinhibitorHEK293 Cells030104 developmental biologyBiochemistryGymnema sylvestreknottin[SDV.AEN]Life Sciences [q-bio]/Food and NutritionHydrophobic and Hydrophilic InteractionsChemical Senses
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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

2016

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the inserti…

0301 basic medicineProtein familyCèl·lulesBiologyBiochemistryMitochondrial Proteins03 medical and health sciencesProtein DomainsMembranes (Biologia)Protein-fragment complementation assayMembrane BiologyMicrosomesProto-Oncogene ProteinsHumansMolecular BiologyAdaptor Proteins Signal TransducingGeneticsBcl-2-Like Protein 11030102 biochemistry & molecular biologyCell MembraneBcl-2 familyProteïnes de membranaMembrane ProteinsBiological membraneCell BiologyFusion proteinTransmembrane proteinCell biology030104 developmental biologyMembraneProto-Oncogene Proteins c-bcl-2Membrane proteinB-cell lymphoma 2 (Bcl-2) family BH3-only apoptosis membrane insertion membrane protein mitochondrial apoptosis transmembrane domainApoptosis Regulatory ProteinsHydrophobic and Hydrophilic InteractionsHeLa CellsJournal of Biological Chemistry
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Thermophilic anaerobic conversion of raw microalgae: Microbial community diversity in high solids retention systems

2019

[EN] The potential of microbial communities for efficient anaerobic conversion of raw microalgae was evaluated in this work. A long-term operated thermophilic digester was fed with three different Organic Loading Rates (OLR) (0.2, 0.3 and 0.4¿g·L¿1·d¿1) reaching 32¿41% biodegradability values. The microbial community analysis revealed a remarkable presence of microorganisms that exhibit high hydrolytic capabilities such as Thermotogae (~44.5%), Firmicutes (~17.6%) and Dictyoglomi, Aminicenantes, Atribacteria and Planctomycetes (below ~5.5%) phyla. The suggested metabolic role of these phyla highlights the importance of protein hydrolysis and fermentation when only degrading microalgae. The …

0301 basic medicineRenewable energyFirmicutesBioreactor010501 environmental sciences01 natural sciences03 medical and health sciencesAnaerobic digestionMicrobial communityBioreactorMicroalgaeFood scienceTECNOLOGIA DEL MEDIO AMBIENTE0105 earth and related environmental sciencesbiologyChemistryThermophilic digesterArmatimonadetesBiodegradationbiology.organism_classificationAnaerobic digestion030104 developmental biologyMicrobial population biologyFermentation16S rRNA geneAgronomy and Crop Science
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Exploring Strategies for Labeling Viruses with Gold Nanoclusters through Non-equilibrium Molecular Dynamics Simulations.

2017

Biocompatible gold nanoclusters can be utilized as contrast agents in virus imaging. The labeling of viruses can be achieved noncovalently but site-specifically by linking the cluster to the hydrophobic pocket of a virus via a lipid-like pocket factor. We have estimated the binding affinities of three different pocket factors of echovirus 1 (EV1) in molecular dynamics simulations combined with non-equilibrium free-energy calculations. We have also studied the effects on binding affinities with a pocket factor linked to the Au102pMBA44 nanocluster in different protonation states. Although the absolute binding affinities are over-estimated for all the systems, the trend is in agreement with r…

0301 basic medicineStereochemistryBiomedical EngineeringPalmitic AcidPharmaceutical ScienceMetal NanoparticlesBioengineeringProtonationMolecular Dynamics SimulationLigandsAntiviral AgentsNanoclusters03 medical and health sciencesMolecular dynamicschemistry.chemical_compoundCapsidCluster (physics)Moleculeta116OxazolesBinding affinitiesEnterovirusPharmacologyOxadiazolesBinding Sitesta114labeling virusesChemistryOrganic ChemistryBiocompatible materialCrystallography030104 developmental biologyThermodynamicsnon-equilibrium molecular dynamicsGoldgold nanoclustersHydrophobic and Hydrophilic InteractionsDerivative (chemistry)BiotechnologyBioconjugate chemistry
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Membrane insertion and topology of the translocon-associated protein (TRAP) gamma subunit

2017

Translocon-associated protein (TRAP) complex is intimately associated with the ER translocon for the insertion or translocation of newly synthesised proteins in eukaryotic cells. The TRAP complex is comprised of three single-spanning and one multiple-spanning subunits. We have investigated the membrane insertion and topology of the multiple-spanning TRAP-γ subunit by glycosylation mapping and green fluorescent protein fusions both in vitro and in cell cultures. Results demonstrate that TRAP-γ has four transmembrane (TM) segments, an Nt/Ct cytosolic orientation and that the less hydrophobic TM segment inserts efficiently into the membrane only in the cellular context of full-length protein.

0301 basic medicineVesicle-associated membrane protein 8Receptors PeptideProtein subunitBiophysicsReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumTopologyBiochemistryGreen fluorescent protein03 medical and health sciencesN-linked glycosylationMembranes (Biologia)Membrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsProteïnes de membranaMembrane ProteinsCell BiologyTransloconTransmembrane proteinProtein Subunits030104 developmental biologyHydrophobic and Hydrophilic InteractionsGamma subunit
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Draft genomic sequence of Nereida ignava CECT 5292T, a marine bacterium of the family Rhodobacteraceae

2016

Nereida ignava strain 2SM4T (= CECT 5292T = DSM 16309T = CIP 108404T = CCUG 49433T) is a marine bacterium belonging to the Roseobacter group of the family Rhodobacteraceae within the class Alphaproteobacteria. The strain was isolated from sea water surrounding cultivated oysters 2–3 miles off the Mediterranean coast near Valencia (Spain) and was phylogenetically related to uncultured clones of gall symbiont bacteria of some species of Prionitis alga. Here we describe the genome sequence and annotation of this organism, the type strain of the single species of this genus. The genome comprised 2,888,349 bp, 2,872 protein-coding genes and 52 RNA genes. The annotation revealed the capacity to p…

0301 basic medicineWhole genome sequencingGeneticsbiologyNereida ignavaSlightly halophilicStrain (biology)Marine bacteria030106 microbiologyRoseobacterbiology.organism_classificationGenomeShort Genome ReportMicrobiology03 medical and health sciences030104 developmental biologyMarine bacteriophageBacteriocinStrictly aerobicMediterranean SeaGeneticsRhodobacteraceaeRhodobacteraceaeGeneStandards in Genomic Sciences
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