Search results for "TP"

showing 10 items of 4688 documents

Poly(hydroxyalkanoate) synthase genes in pseudomonads strains, isolation and heterologous expression

2010

ATP synthasebiologySettore AGR/12 - Patologia VegetaleBioengineeringGeneral MedicineIsolation (microbiology)PolyhydroxyalkanoatePseudomonas corrugataApplied Microbiology and BiotechnologyMicrobiologybiology.proteinHeterologous expressionGenePseudomonas mediterraneaNicotiana BentamianaBiotechnology
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S1/3 The stator stalk of Escherichia coli ATP synthase

2008

ATP synthasebiologyStatorChemistryBiophysicsCell Biologymedicine.disease_causeBiochemistrylaw.inventionStalkBiochemistrylawmedicinebiology.proteinEscherichia coliBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Binding mode analysis of ABCA7 for the prediction of novel Alzheimer's disease therapeutics

2021

Graphical abstract

ATP Adenosine-triphosphateNBD nucleotide binding domainGSH reduced glutathionePolypharmacologyAlzheimer’s disease (AD)ATP-binding cassette transporterHTS high-throughput screeningBiochemistryABCA7Structural BiologyPLIF protein ligand interactionMSD membrane spanning domainPDB protein data bankTM transmembrane helixABC ATP-binding cassetteMultitarget modulation (PANABC)RMSD root mean square distanceABC transporter (ABCA1 ABCA4 ABCA7)Computer Science ApplicationsMOE Molecular Operating EnvironmentPharmacophoreSNP single-nucleotide polymorphismBiotechnologyResearch ArticleBBB blood-brain barrierBiophysicsDrug designComputational biologyBiologyAD Alzheimer’s diseasePET positron emission tomographyIC intracellular helixAPP amyloid precursor proteincryo-EM cryogenic-electron microscopyGeneticsHomology modelingBinding siteRational drug design and developmentComputingMethodologies_COMPUTERGRAPHICSNBD-cholesterol 7-nitro-2-13-benzoxadiazol-4-yl-cholesterolTransporterPSO particle swarm optimizationPET tracer (PETABC)ECD extracellular domainR-domain/region regulatory domain/regionABCA1biology.proteinEH extracellular helixTP248.13-248.65BODIPY-cholesterol 44-difluoro-4-bora-3a4a-diaza-s-indacene-cholesterolComputational and Structural Biotechnology Journal
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P2Y-mediated contractile responses in the longitudinal muscle of mouse distal colon: distinct signaling pathways

2008

ATPMouse distal colonP2Y purinoreceptorIntracellular calcium storeMuscular contractionSettore BIO/09 - Fisiologia
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Activation of P2Y receptors by ATP and by its analogue, ADPbetaS, triggers two calcium signal pathways in the longitudinal muscle of mouse distal col…

2008

Our previous research showed that ATP and adenosine 5'-O-2-thiodiphosphate (ADPbetaS) induce contractile effects in the longitudinal muscle of mouse distal colon via activation of P2Y receptors which are not P2Y(1) or P2Y(12) subtypes. This study investigated the nature of the P2Y receptor subtype(s) and the mechanisms leading to the intracellular calcium concentration increase necessary to trigger muscular contraction. Motor responses of mouse colonic longitudinal muscle to P2Y receptor agonists were examined in vitro as changes in isometric tension. ATP or ADPbetaS induced muscular contraction, which was not affected by P2Y(11) or P2Y(13) selective antagonists. Calcium-free solution or th…

ATPP2Y purinoreceptorIntracellular calcium storeMuscular contractionSettore BIO/09 - Fisiologia
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Agonist-specific Ca2+ signaling at P2Y receptors

2008

ATPP2Y purinoreceptorIntracellular calcium storeMuscular contractionSettore BIO/09 - Fisiologia
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Evidence that ATP or a related purine is an excitatory neurotransmitter in the longitudinal muscle of mouse distal colon

2007

BACKGROUND AND PURPOSE: This study analysed the contribution of the purinergic system to enteric neurotransmission in the longitudinal muscle of mouse distal colon. EXPERIMENTAL APPROACH: Motor responses to exogenous ATP and to nerve stimulation in vitro were assessed as changes in isometric tension. KEY RESULTS: ATP induced a concentration-dependent contraction, reduced by 4-[[4-formyl-5-hydroxy-6-methyl-3-[(phosphonooxy)methyl]-2-pyridinyl]azo]-1,3-benzene disulphonic acid (PPADS), suramin, P2Y purinoreceptor desensitisation with adenosine 5'-O-2-thiodiphosphate (ADPbetaS), and atropine, but unaffected by P2X purinoceptor desensitisation with alpha,beta-methylene ATP (alpha,beta-meATP) an…

ATPcolonenteric excitatory neurotransmissionP2Y receptorlongitudinal muscleSettore BIO/09 - Fisiologiamouse
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1,4-Dihidropiridīnu atvasinājumu nanodaļiņu toksiskuma novērtējums mikroorganismos

2017

1,4 Dihidropiridīnu (1,4 DHP) atvasinājumi ir plaša organisko vielu grupa, kurā arvien tiek sintezēti jauni savienojumi ar plašām pielietojuma iespējām. Jauno savienojumu toksicitātes raksturojums ir nepieciešams, lai paredzētu to pielietojuma iespējas un novērtētu to iedarbību uz vidi un dzīvajiem organismiem. Darbā pielāgota universāla un efektīva atšķaidījumu metode, lai noteiktu deviņu katjono amfifilo 1,4 DHP atvasinājumu toksicitātes robežkoncentrācijas sešām baktērijām un vienam raugam. Papildus noteikta 1,4 DHP atvasinājumu ietekme uz iekššūnas ATP daudzumu, skābekļa patēriņa ātrumu un etīdija bromīda transportu šūnās. Noskaidrojot toksicitātes robežkoncentrācijas un gūstot ieskatu …

ATPnanodaļiņasetīdija bromīda transportstoksicitātes novērtējumsBioloģija14-dihidropiridīna atvasinājumi
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Conversion of the Ca2+-ATPase from Rhodospirillum rubrum into a Mg2+-dependent enzyme by 1,N6-etheno ATP

1980

Nucleoside triphosphate hydrolysis of R.rubrum ATPase complexes can be changed from Ca2+-dependence to Mg2+-dependence by replacing ATP with 1,N6-etheno ATP. Four ATPase complexes which have been prepared by different procedures hydrolyze ATP and 1,N6-etheno ATP at different rates in dependence on the added metal ions. These differences allow an easy distinction of the various enzyme forms.

ATPaseBiophysicsPhotophosphorylationCalcium-Transporting ATPasesRhodospirillum rubrumBiochemistrychemistry.chemical_compoundAdenosine TriphosphateMagnesiumMolecular BiologyEdetic Acidchemistry.chemical_classificationbiologyATP synthaseChemiosmosisCell MembraneRhodospirillum rubrumCell Biologybiology.organism_classificationKineticsEnzymeBiochemistrychemistrybiology.proteinNucleoside triphosphateOligomycinsATP synthase alpha/beta subunitsEthenoadenosine TriphosphateProtein BindingBiochemical and Biophysical Research Communications
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The Arabidopsis heavy metal P-type ATPase HMA5 interacts with metallochaperones and functions in copper detoxification of roots

2005

*† ‡ § Summary Since copper (Cu) is essential in key physiological oxidation reactions, organisms have developed strategies for handling Cu while avoiding its potentially toxic effects. Among the tools that have evolved to cope with Cu is a network of Cu homeostasis factors such as Cu-transporting P-type ATPases that play a key role in transmembrane Cu transport. In this work we present the functional characterization of an Arabidopsis Cutransporting P-type ATPase, denoted heavy metal ATPase 5 (HMA5), and its interaction with Arabidopsis metallochaperones. HMA5 is primarily expressed in roots, and is strongly and specifically induced by Cu in whole plants. We have identified and characteriz…

ATPaseMolecular Sequence DataMutantArabidopsisPlant ScienceGenes PlantPlant RootsMetallochaperonesArabidopsisGeneticsAmino Acid SequenceRNA MessengerDNA PrimersAdenosine TriphosphatasesBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsCell BiologyCompartmentalization (fire protection)biology.organism_classificationTransmembrane proteinCell biologyBiochemistryChaperone (protein)biology.proteinP-type ATPaseCopperMolecular ChaperonesThe Plant Journal
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