Search results for "binding"

showing 10 items of 3896 documents

The fungal elicitor cryptogein is a sterol carrier protein

1997

AbstractCryptogein is a protein secreted by the phytopathogenic pseudo-fungus, Phytophthora cryptogea. It is a basic 10 kDa hydrophilic protein having a hydrophobic pocket and three disulfide bridges. These common features with sterol carrier proteins led us to investigate its possible sterol transfer activity using the fluorescent sterol, dehydroergosterol. The results show that cryptogein has one binding site with strong affinity for dehydroergosterol. Moreover, this protein catalyzes the transfer of sterols between phospholipidic artificial membranes. This is the first evidence for the existence of an extracellular sterol carrier protein and for a molecular activity of cryptogein. This p…

Phytophthora0106 biological sciencesBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular Biology01 natural sciencesBiochemistryFluorescenceFungal Proteins03 medical and health scienceschemistry.chemical_compoundStructural BiologyErgosterolPhosphatidylcholinepolycyclic compoundsGeneticsExtracellularBinding siteMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesbiologyPhytophthora cryptogeaAlgal ProteinsElicitinCell Biologybiology.organism_classificationElicitinSterolElicitorKineticsCholesterolSpectrometry FluorescenceSterol carrier proteinDehydroergosterolBiochemistrychemistryLiposomeslipids (amino acids peptides and proteins)Carrier Proteins010606 plant biology & botany
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Fatty acids bind to the fungal elicitor cryptogein and compete with sterols

2001

Abstract Cryptogein is a proteinaceous elicitor of plant defense reactions which also exhibits sterol carrier properties. In this study, we report that this protein binds fatty acids. The stoichiometry of the fatty acid–cryptogein complex is 1:1. Linoleic acid and dehydroergosterol compete for the same site, but elicitin affinity is 27 times lower for fatty acid than for sterol. We show that C7 to C12 saturated and C16 to C22 unsaturated fatty acids are the best ligands. The presence of double bonds markedly increases the affinity of cryptogein for fatty acids. A comparison between elicitins and known lipid transfer proteins is discussed.

Phytophthora0106 biological sciencesDouble bondLinoleic acidBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding Competitive01 natural sciencesBiochemistryFungal ProteinsLinoleic AcidLIAISON MOLECULAIREStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundStructural BiologyErgosterolGeneticsPlant defense against herbivoryMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSSterol030304 developmental biologychemistry.chemical_classification0303 health sciencesAlgal ProteinsFatty AcidsProteinsFatty acidLipid–protein interactionElicitinCell BiologyFatty acidElicitinSterol3. Good healthElicitorSterolschemistryBiochemistrylipids (amino acids peptides and proteins)Plant lipid transfer proteinsProtein Binding010606 plant biology & botany
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Modulation of the Biological Activity of a Tobacco LTP1 by Lipid Complexation

2004

Plant lipid transfer proteins (LTPs) are small, cysteine-rich proteins secreted into the extracellular space. They belong to the pathogenesis-related proteins (PR-14) family and are believed to be involved in several physiological processes including plant disease resistance, although their precise biological function is still unknown. Here, we show that a recombinant tobacco LTP1 is able to load fatty acids and jasmonic acid. This LTP1 binds to specific plasma membrane sites, previously characterized as elicitin receptors, and is shown to be involved in the activation of plant defense. The biological properties of this LTP1 were compared with those of LTP1-linolenic and LTP1-jasmonic acid…

Phytophthora0106 biological sciences[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringCyclopentanesPlasma protein bindingBiologyFatty Acid-Binding ProteinsLigands01 natural sciencesMass SpectrometryFatty acid-binding proteinCell membrane03 medical and health scienceschemistry.chemical_compoundTobacco[SDV.IDA]Life Sciences [q-bio]/Food engineeringExtracellularmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringOxylipinsMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesDose-Response Relationship DrugCircular DichroismJasmonic acidCell MembraneFatty AcidsElicitinBiological activityArticlesCell Biology[SDV.IDA] Life Sciences [q-bio]/Food engineeringLipid MetabolismLipidsRecombinant Proteinsmedicine.anatomical_structureBiochemistrychemistryPHYTOPHTORA PARASITICACarrier ProteinsTRANSFERT LIPIDIQUEPlant lipid transfer proteinsChromatography LiquidProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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Reconstitution and Pigment Exchange

2007

PigmentBiochemistryRhodospirillum molischianumChemistryMantoniella squamatavisual_artPigment bindingvisual_art.visual_art_medium
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EXPRESSION OF PIPPIN PROTEIN AND CELL DIFFERENTIATION.

2008

We previously described a CSD-containing protein that seemed to bind mRNAs encoding histone variants and was present both in the nucleus and in the cytoplasm of specific populations of brain cells. Since other CSD-containing proteins have the ability to interact both with RNA and chromatin, we investigated the possibility that PIPPin binds to chromatin and indeed found that about 50% of nuclear PIPPin cannot be extracted from nuclei with salt and is instead extracted with acid, together with histones. Interestingly, a major fraction of chromatin-bound PIPPin is sumoylated and sumoylation seems to be controlled by thyroid hormones, both in vivo and in vitro. In order to study the functions o…

Pippincell differentiationSettore BIO/10 - BiochimicaPC12RNA binding protein
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l-Tyrosine β-naphthylamide is a potent competitive inhibitor of tyramine N-(hydroxycinnamoyl)transferase in vitro

2001

L-Tyrosine beta-naphthylamide, a synthetic substrate designed to measure tyrosine aminopeptidase activity, is a potent inhibitor of hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase (THT) purified from elicited tobacco cell-suspension cultures. The inhibition is competitive, with the inhibitor binding reversibly to the tyramine binding site of the enzyme. Similar results were obtained with THT extracted from elicited potato cell-suspension cultures. Ki values were found to be 0.66 microM for the enzyme from tobacco and 0.3 microM for the enzyme from potato. L-Tyrosine 7-amido-4-methylcoumarin, a fluorogenic substrate for tyrosine aminopeptidases, the structure of which is close …

Plant ScienceNaphthalenesHorticultureBiologyBinding CompetitiveBiochemistryAminopeptidaseStructure-Activity Relationshipchemistry.chemical_compoundNon-competitive inhibitionTyrosine aminotransferaseTobaccoTransferaseEnzyme InhibitorsTyrosineMolecular BiologySolanum tuberosumchemistry.chemical_classificationGeneral MedicineTyramineKineticsPlants ToxicEnzymechemistryBiochemistryEnzyme inhibitorbiology.proteinTyrosineAcyltransferasesPhytochemistry
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On the zopiclone enantioselective binding to human albumin and plasma proteins. An electrokinetic chromatography approach

2011

In this work, a methodology for the chiral separation of zopiclone (ZPC) by electrokinetic chromatography (EKC) using carboxymethylated-β-cyclodextrin as chiral selector has been developed and applied to the evaluation of the enantioselective binding of ZPC enantiomers to HSA and total plasma proteins. Two mathematical approaches were used to estimate protein binding (PB), affinity constants (K(1)) and enantioselectivity (ES) for both enantiomers of ZPC. Contradictory results in the literature, mainly related to plasma protein binding reported data, suggest that this is an unresolved matter and that more information is needed. Discrepancies and coincidences with previous data are highlighte…

Plasma protein bindingBiochemistryPiperazinesAnalytical ChemistryCapillary electrophoresisAlbuminsmedicineHumansLeast-Squares AnalysisChromatography Micellar Electrokinetic Capillarychemistry.chemical_classificationChromatographyCyclodextrinOrganic ChemistryEnantioselective synthesisReproducibility of ResultsStereoisomerismBlood ProteinsGeneral MedicineHuman serum albuminBlood proteinschemistryStability constants of complexesEnantiomerAzabicyclo CompoundsProtein Bindingmedicine.drugJournal of Chromatography A
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Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.

1995

Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the…

PlasminStreptococcus pyogenesMolecular Sequence DataPlasma protein bindingBiologyMicrobiologyKringle domainBacterial ProteinsKringlesmedicineEscherichia coliAmino Acid SequenceBinding siteCloning MolecularMolecular BiologyPeptide sequenceBinding SitesBase SequenceLysinePlasminogenFusion proteinMolecular biologyRecombinant ProteinsPhenotypeBiochemistryCarrier ProteinsPlasminogen activatorSequence AlignmentBinding domainmedicine.drugProtein BindingMolecular microbiology
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The Internal Dynamics of Fibrinogen and Its Implications for Coagulation and Adsorption

2015

Fibrinogen is a serum multi-chain protein which, when activated, aggregates to form fibrin, one of the main components of a blood clot. Fibrinolysis controls blood clot dissolution through the action of the enzyme plasmin, which cleaves fibrin at specific locations. Although the main biochemical factors involved in fibrin formation and lysis have been identified, a clear mechanistic picture of how these processes take place is not available yet. This picture would be instrumental, for example, for the design of improved thrombolytic or anti-haemorrhagic strategies, as well as, materials with improved biocompatibility. Here, we present extensive molecular dynamics simulations of fibrinogen w…

Plasminmedicine.medical_treatmentAllosteric regulationPlasma protein bindingMolecular Dynamics SimulationFibrinogenFibrinCellular and Molecular NeuroscienceFibrinolysisGeneticsmedicineHumanslcsh:QH301-705.5Molecular BiologyBlood CoagulationEcology Evolution Behavior and SystematicsIntegrin bindingEcologybiologyChemistryComputational BiologyFibrinogenlcsh:Biology (General)Computational Theory and MathematicsCoagulationBiochemistryModeling and Simulationbiology.proteinAdsorptionmedicine.drugResearch ArticleProtein BindingPLoS Computational Biology
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Hijacking the human complement inhibitor C4b-binding protein by the sporozoite stage of the Plasmodium falciparum parasite

2022

We thank Anna Blom for donating the C4bpα CCP1-2 expression plasmid (pET26-CCP1-2). The following reagent was obtained through BEI Resources, NIAID, NIH: Plasmid pDS56-32/RBSII-CS27IVC-6XHis, MRA-272, contributed by Photini Sinnis. The complement system is considered the first line of defense against pathogens. Hijacking complement regulators from blood is a common evasion tactic of pathogens to inhibit complement activation on their surfaces. Here, we report hijacking of the complement C4b-binding protein (C4bp), the regulator of the classical and lectin pathways of complement activation, by the sporozoite (SPZ) stage of the Plasmodium falciparum parasite. This was shown by direct binding …

PlasmodiumsporozoiteskomplementtijärjestelmäImmunologylnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4]malarialoisiotCircumsporozoite proteinComplement evasioncomplement evasionlnfectious Diseases and Global Health Radboud Institute for Health Sciences [Radboudumc 4]C4b binding proteinplasmodiumSporozoitesImmunology and Allergy3111 Biomedicinecircumsporozoite proteinFrontiers in Immunology
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