Search results for "carrier protein"

showing 10 items of 361 documents

Investigation on a MMACHC mutant from cblC disease: The c.394C>T variant

2022

The cblC disease is an inborn disorder of the vitamin B12 (cobalamin, Cbl) metabolism characterized by methylmalonic aciduria and homocystinuria. The clinical consequences of this disease are devastating and, even when early treated with current therapies, the affected children manifest symptoms involving vision, growth, and learning. The illness is caused by mutations in the gene codifying for MMACHC, a 282aa protein that transports and transforms the different Cbl forms. Here we present data on the structural properties of the truncated protein p.R132X resulting from the c.394C > T mutation that, along with c.271dupA and c.331C > T, is among the most common mutations in cblC. Althou…

Vitamin B12 (cobalamin)Structure-function relationshipBiophysicsBiochemistryAnalytical ChemistryVitamin B 12MutationMMACHC proteinHumansMethylmalonic aciduria and homocystinuria cblC typeHomocystinuriaCarrier ProteinsChildOxidoreductasesAmino Acid Metabolism Inborn ErrorsMolecular BiologyBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Purification and structural characterisation of lipid transfer protein from red wine and grapes

2012

Lipid transfer proteins (LTP) play a major role in plant defence and are of particular interest due to their known ability to cause allergic reactions. These proteins are expressed in grapes and also remain detectable after vinification, especially in red wine. However, it remains unknown whether the protein undergoes any changes during the vinification process. Here, we present a purification method for LTPs from Dornfelder grapes and wine. By liquid-chromatography-mass spectroscopy (LC-MS/MS) we identified LTPs from two different species (Vitis vinifera and Vitis aestivalis). Additionally, the purified LTPs were characterised using spectrometric methods, confirming their high purity and s…

Vitis aestivalisProtein ConformationChemistryfungifood and beveragesWineFast protein liquid chromatographyGeneral MedicineTandem mass spectrometryAnalytical ChemistryProtein structureBiochemistryTandem Mass SpectrometrywineVitiswine.grape_varietyPurification methodsCarrier ProteinsPlant lipid transfer proteinsPolyacrylamide gel electrophoresisPlant ProteinsFood ScienceFood Chemistry
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Wee1 inhibition potentiates Wip1-dependent p53-negative tumor cell death during chemotherapy

2016

AbstractInactivation of p53 found in more than half of human cancers is often associated with increased tumor resistance to anti-cancer therapy. We have previously shown that overexpression of the phosphatase Wip1 in p53-negative tumors sensitizes them to chemotherapeutic agents, while protecting normal tissues from the side effects of anti-cancer treatment. In this study, we decided to search for kinases that prevent Wip1-mediated sensitization of cancer cells, thereby interfering with efficacy of genotoxic anti-cancer drugs. To this end, we performed a flow cytometry-based screening in order to identify kinases that regulated the levels of γH2AX, which were used as readout. Another criter…

Wip1ApoptosisCell Cycle ProteinsPharmacologyMESH: G2 Phase Cell Cycle CheckpointsHistonesMESH : PhosphorylationMiceMESH : Cell Cycle ProteinsMESH: AnimalsMESH: Tumor Suppressor Protein p53MESH: HistonesKinaseTp53 mutationsMESH : Mice Transgenic3. Good healthProtein Phosphatase 2CSurvival RateMESH : Antineoplastic AgentsH2ax phosphorylationP53 activationMESH: Protein Phosphatase 2CRNA InterferenceMESH : Colorectal NeoplasmsMESH : Carrier ProteinsHistone H2axMESH: MitochondriaImmunologyHuman fibroblastsMESH: Carrier ProteinsAntineoplastic AgentsMESH: Protein-Tyrosine KinasesMESH: Protein-Serine-Threonine KinasesMESH : Cisplatin03 medical and health sciencesMESH: Cell Cycle ProteinsGenotoxic stressMESH : Protein-Tyrosine KinasesHumansMESH : HistonesAnticancer TherapyMESH: DNA DamageCisplatinMESH: HumansMESH: Phosphorylation[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH : HumansMESH : Nuclear Proteins030104 developmental biologyCancer cellMESH: Antineoplastic AgentsCisplatinCarrier ProteinsMESH: Nuclear ProteinsMESH : ApoptosisDna-damage response0301 basic medicineCancer ResearchMESH: Caspase 3MESH : Caspase 3PhosphorylationCytotoxicityMESH : DNA DamageSensitizationmedicine.diagnostic_testCaspase 3Nuclear ProteinsProtein-Tyrosine KinasesMESH : Survival RateMitochondriaG2 Phase Cell Cycle CheckpointsWee1medicine.anatomical_structureMESH : Protein Phosphatase 2COriginal ArticleMESH : MitochondriaColorectal Neoplasmsmedicine.drugMESH : Protein-Serine-Threonine KinasesMESH: Cell Line TumorMESH: Survival RateMESH: Mice TransgenicMESH: RNA InterferencePhosphataseMice Transgenic[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyProtein Serine-Threonine KinasesFlow cytometryCellular and Molecular NeuroscienceCell Line TumorMESH : MicemedicineAnimalsMESH: MiceMESH : Cell Line TumorMESH: ApoptosisCell BiologyMESH : Tumor Suppressor Protein p53MESH: CisplatinCancer researchbiology.proteinMESH : AnimalsMESH : G2 Phase Cell Cycle CheckpointsMESH : RNA InterferenceTumor Suppressor Protein p53MESH: Colorectal NeoplasmsDNA DamageCell Death & Disease
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Interactions in the network of Usher syndrome type 1 proteins

2004

International audience; Defects in myosin VIIa, harmonin (a PDZ domain protein), cadherin 23, protocadherin 15 and sans (a putative scaffolding protein), underlie five forms of Usher syndrome type I (USH1). Mouse mutants for all these proteins exhibit disorganization of their hair bundle, which is the mechanotransduction receptive structure of the inner ear sensory cells, the cochlear and vestibular hair cells. We have previously demonstrated that harmonin interacts with cadherin 23 and myosin VIIa. Here we address the extent of interactions between the five known USH1 proteins. We establish the previously suggested sans-harmonin interaction and find that sans also binds to myosin VIIa. We …

[SDV]Life Sciences [q-bio]Hearing Loss SensorineuralStereocilia (inner ear)PDZ domainCadherin Related ProteinsProtocadherinCell Cycle ProteinsNerve Tissue ProteinsCuticular plateMyosinsBiologyMiceTwo-Hybrid System TechniquesHair Cells AuditoryBone plateMyosinotorhinolaryngologic diseasesGeneticsAnimalsHumansProtein PrecursorsMolecular BiologyGenetics (clinical)GeneticsStereociliumDyneinsSyndromeGeneral MedicineCadherinsCell biologyCytoskeletal ProteinsMyosin VIIaMutationsense organsCarrier ProteinsRetinitis PigmentosaPCDH15HeLa CellsProtein BindingHuman Molecular Genetics
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A (1->3)-beta-D-glucan recognition protein from the sponge Suberites domuncula. Mediated activation of fibrinogen-like protein and epidermal growth f…

2004

Sponges (phylum Porifera) live in a symbiotic relationship with microorganisms, primarily bacteria. Until now, molecular proof for the capacity of sponges to recognize fungi in the surrounding aqueous milieu has not been available. Here we demonstrate, for the demosponge Suberites domuncula (Porifera, Demospongiae, Hadromerida), a cell surface receptor that recognizes (1--3)-beta-D-glucans, e.g. curdlan or laminarin. This receptor, the (1--3)-beta-D-glucan-binding protein, was identified and its cDNA analysed. The gene coding for the 45 kDa protein was found to be upregulated in tissue after incubation with carbohydrate. Simultaneously with the increased expression of this gene, two further…

beta-GlucansMolecular Sequence DataPinacodermGene Expression-BiochemistryDemospongeEpidermal growth factorComplementary DNALectinsAnimalsAmino Acid SequencePhosphorylationProtein PrecursorsGlucansHadromeridaPhylogenybiologyEpidermal Growth FactorFibrinogenbiology.organism_classificationRecombinant ProteinsPoriferaSuberites domunculaSpongeBiochemistryCarrier ProteinsTyrosine kinaseSequence Alignment
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Citrate lyases of lactic acid bacteria

1998

Citrate Iyase is a key enzyme of the citrate metabolism which is involved in flavor and texture of many fermented milk products. Citrate Iyase which catalyses the cleavage of citrate into oxaloacetate and acetate is a multienzyme complex composed of three proteins: an acyl carrier protein (ACP); a citrate, acetate-ACP transferase; and a citryl-S-ACP Iyase. The citrate Iyase is active only when the thioester residue of the prosthetic group bound to ACP is acetylated. In the presence of citrate, the transferase mediates the formation of citryl-S-acyl carrier protein by acyl exchange and liberation of acetate. Then the Iyase subunit cleaves the citryl-S-ACP with libe- ration of oxaloacetate an…

biologyATP citrate lyasefood and beverages[SDV.IDA] Life Sciences [q-bio]/Food engineeringbiology.organism_classificationCofactorLactic acidchemistry.chemical_compoundAcyl carrier protein[SDV.AEN] Life Sciences [q-bio]/Food and NutritionBiochemistrychemistryLeuconostoc mesenteroidesbiology.proteinTransferaseLeuconostocCitrate synthaselipids (amino acids peptides and proteins)ComputingMilieux_MISCELLANEOUSFood Science
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Total Synthesis of a Partial Structure from Arabinogalactan and Its Application for Allergy Prevention

2020

Abstract Arabinogalactan, a microheterogeneous polysaccharide occurring in plants, is known for its allergy‐protective activity, which could potentially be used for preventive allergy treatment. New treatment options are highly desirable, especially in a preventive manner, due to the constant rise of atopic diseases worldwide. The structural origin of the allergy‐protective activity of arabinogalactan is, however, still unclear and isolation of the polysaccharide is not feasible for pharmaceutical applications due to a variation of the activity of the natural product and contaminations with endotoxins. Therefore, a pentasaccharide partial structure was selected for total synthesis and subse…

chemistry.chemical_classificationDrug Discovery | Hot PaperNatural productallergy protectionAllergy preventionCommunicationOrganic ChemistrycarbohydratesAirway inflammationTreatment optionsTotal synthesisGeneral Chemistryairway inflammationPolysaccharideCommunicationsCatalysisarabinogalactanchemistry.chemical_compoundchemistryBiochemistryArabinogalactanCarrier proteintotal synthesisChemistry – A European Journal
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Expression, regulation and function of carrier proteins for cationic amino acids.

2001

Different carrier proteins exhibiting distinct transport properties participate in cationic amino acid transport. There are sodium-independent systems, such as b+, y+, y+L and b0,+, and a sodium-dependent system B0,+, most of which have now been identified at the molecular level. In most non-epithelial cells, members of the cationic amino acid transporter (CAT) family mediating system y+ activity seem to be the major entry pathway for cationic amino acids. CAT proteins underlie complex regulation at the transcriptional, post-transcriptional and activity levels. Recent evidence indicates that individual CAT isoforms are necessary for providing the substrate for nitric oxide synthesis, for ex…

chemistry.chemical_classificationGene isoformAmino Acid Transport System y+SodiumCationic polymerizationSubstrate (chemistry)BiologyNitric oxideAmino acidchemistry.chemical_compoundchemistryBiochemistryNephrologyCarrier proteinInternal MedicineAmino Acid Transport Systems BasicAnimalsHumansAmino acid transporterFunction (biology)Current opinion in nephrology and hypertension
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REGULATION OF CATIONIC AMINO ACID TRANSPORT: The Story of the CAT-1 Transporter

2004

▪ Abstract  The discovery of the function of the receptor for the ecotropic retrovirus as a membrane transporter for the essential amino acids lysine and arginine was a landmark finding in the field of molecular nutrition. This finding indicated that cationic amino acid transporters (CATs) act pathologically as viral receptors. The importance of this transporter was further supported by knockout mice that were not viable after birth. CAT-1 was the first amino acid transporter to be cloned; several other CATs were later characterized biochemically and molecularly. These transporters mediate the bidirectional transport of cationic amino acids, thus supporting important metabolic functions, s…

chemistry.chemical_classificationNutrition and DieteticsArginine transportArginineLysineMedicine (miscellaneous)Biological TransportTransporterBiologyAmino acidGene Expression RegulationBiochemistrychemistryAmino Acid Transport Systems BasicAnimalsHumansRNA MessengerAmino acid transporterAmino AcidsCarrier ProteinsReceptorGeneAnnual Review of Nutrition
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Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1

1998

Abstract A cDNA clone encoding a homolog of the yeast (Saccharomyces cerevisiae) gene Anti-oxidant 1(ATX1) has been identified from Arabidopsis. This gene, referred to as CopperCHaperone(CCH), encodes a protein that is 36% identical to the amino acid sequence of ATX1 and has a 48-amino acid extension at the C-terminal end, which is absent from ATX1 homologs identified in animals. ATX1-deficient yeast (atx1) displayed a loss of high-affinity iron uptake. Expression of CCH in the atx1 strain restored high-affinity iron uptake, demonstrating thatCCH is a functional homolog of ATX1. When overexpressed in yeast lacking the superoxide dismutase geneSOD1, both ATX1 and CCHprotected the cell from t…

endocrine systemDNA ComplementarySaccharomyces cerevisiae ProteinsPhysiologyMolecular Sequence DataSaccharomyces cerevisiaeSOD1ArabidopsisGene ExpressionSaccharomyces cerevisiaePlant ScienceFungal ProteinsGene productSuperoxide dismutaseOzoneCopper Transport ProteinsComplementary DNAArabidopsisGene expressionGeneticsHomeostasisAmino Acid SequenceCation Transport ProteinsBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsGenetic Complementation Testbiology.organism_classificationYeastOxidative StressBiochemistrybiology.proteinCarrier ProteinsCopperResearch ArticlePlant Physiology
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