Search results for " Translationally-Controlled 1"

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AMG900 as novel inhibitor of the translationally controlled tumor protein

2020

Abstract Introduction Cancer is one of the leading causes of death worldwide. Classical cytotoxic chemotherapy exerts high side effects and low tumor selectivity. Translationally controlled tumor protein (TCTP) is a target for differentiation therapy, a promising, new therapeutic approach, which is expected to be more selective and less toxic than cytotoxic chemotherapy. The aim of the present investigation was to identify novel TCTP inhibitors. Methods We performed in silico screening and molecular docking using a chemical library of more than 31,000 compounds to identify a novel inhibitor of TCTP. We tested AMG900 in vitro for binding to TCTP by microscale thermophoresis and co-immunoprec…

0301 basic medicineApoptosisCell Cycle ProteinsToxicologyResting Phase Cell CycleFlow cytometry03 medical and health sciences0302 clinical medicineCyclin D1Differentiation therapyCell Line TumorNeoplasmsTranslationally-controlled tumor proteinBiomarkers TumormedicineHumansCyclin D3medicine.diagnostic_testbiologyChemistryG1 PhaseTumor Protein Translationally-Controlled 1General MedicineMolecular Docking SimulationBlot030104 developmental biologyProtein Biosynthesis030220 oncology & carcinogenesisCancer cellMCF-7 CellsCancer researchbiology.proteinPhthalazinesCyclin-dependent kinase 6Chemico-Biological Interactions
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Molecular interaction of artemisinin with translationally controlled tumor protein (TCTP) of Plasmodium falciparum

2012

Malaria causes millions of death cases per year. Since Plasmodium falciparum rapidly develops drug resistance, it is of high importance to investigate potential drug targets which may lead to novel rational therapy approaches. Here we report on the interaction of translationally controlled tumor protein of P. falciparum (PfTCTP) with the anti-malarial drug artemisinin. Furthermore, we investigated the crystal structure of PfTCTP. Using mass spectrometry, bioinformatic approaches and surface plasmon resonance spectroscopy, we identified novel binding sites of artemisinin which are in direct neighborhood to amino acids 19-46, 108-134 and 140-163. The regions covered by these residues are know…

Drugmedia_common.quotation_subjectPlasmodium falciparumProtozoan ProteinsDrug resistanceBiologyCrystallography X-RayBiochemistryAntimalarialsparasitic diseasesTranslationally-controlled tumor proteinBiomarkers TumormedicineHumansComputer SimulationBinding siteArtemisininmedia_commonPharmacologychemistry.chemical_classificationBinding SitesMolecular StructureTumor Protein Translationally-Controlled 1Plasmodium falciparumSurface Plasmon Resonancebiology.organism_classificationArtemisininsRecombinant ProteinsAmino acidMolecular Docking SimulationchemistryBiochemistryFunction (biology)Protein Bindingmedicine.drugBiochemical Pharmacology
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