0000000000305272

AUTHOR

Mohammed I. Y. Elmallah

showing 3 related works from this author

Marine Actinomycetes-Derived Secondary Metabolites Overcome TRAIL-Resistance via the Intrinsic Pathway through Downregulation of Survivin and XIAP

2020

Resistance of cancer cells to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis represents the major hurdle to the clinical use of TRAIL or its derivatives. The discovery and development of lead compounds able to sensitize tumor cells to TRAIL-induced cell death is thus likely to overcome this limitation. We recently reported that marine actinomycetes&rsquo

0301 basic medicineAquatic OrganismsProgrammed cell deathCell SurvivalSurvivinDown-RegulationSecondary MetabolismX-Linked Inhibitor of Apoptosis ProteinTRAILJurkat cellsArticleTNF-Related Apoptosis-Inducing LigandJurkat Cells03 medical and health sciences0302 clinical medicinemarine actinomycetesDownregulation and upregulationDrug DiscoveryOxazinesSurvivinHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyFADDBenzopyreneslcsh:QH301-705.5ComputingMilieux_MISCELLANEOUSCaspase 8therapybiologyChemistryProdigiosinQuinonesapoptosisGeneral MedicineHCT116 Cells3. Good healthXIAPActinobacteria030104 developmental biologylcsh:Biology (General)Drug Resistance NeoplasmApoptosis030220 oncology & carcinogenesisCancer cellbiology.proteinCancer researchGene DeletionCells
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Epigenetic Regulation of TRAIL Signaling: Implication for Cancer Therapy

2019

International audience; One of the main characteristics of carcinogenesis relies on genetic alterations in DNA and epigenetic changes in histone and non-histone proteins. At the chromatin level, gene expression is tightly controlled by DNA methyl transferases, histone acetyltransferases (HATs), histone deacetylases (HDACs), and acetyl-binding proteins. In particular, the expression level and function of several tumor suppressor genes, or oncogenes such as c-Myc, p53 or TRAIL, have been found to be regulated by acetylation. For example, HATs are a group of enzymes, which are responsible for the acetylation of histone proteins, resulting in chromatin relaxation and transcriptional activation,…

0301 basic medicineCancer Researchtumor necrosis factor (TNF)TRAILReviewmedicine.disease_causelcsh:RC254-282Chromatin remodelingchromatin remodeling03 medical and health sciences0302 clinical medicinemedicinetumor necrosis factor (TNF).[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biologycancer[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyEpigeneticsHistone Acetyltransferasesbiologyhistone deacetylase (HDAC)lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogens3. Good healthChromatin030104 developmental biologyHistonehistone deacetylase inhibitors (HDACIs)OncologyAcetylation030220 oncology & carcinogenesissilencingCancer researchbiology.proteinHistone deacetylasemethylationCarcinogenesisCancers
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Membrane-anchored heat-shock protein 70 (Hsp70) in cancer.

2020

International audience; Hsp70 is a highly conserved and inducible heat shock protein that belongs to the HSP70 family of molecular chaperones and plays a central role in protein homeostasis. The main function of Hsp70 is to protect cells from physiological, pathological and environmental insults, as it assists an ATP-dependent manner the process of protein folding. Since Hsp70 provides critical cell survival functions, cancer cells are assumed to rely on this chaperone. Strong evidence suggests that Hsp70 is upregulated in different type of cancers and is involved in tumor growth, invasion, migration and resistance to anti-cancer therapy. Interestingly, this Hsp70 upregulation induces Hsp70…

0301 basic medicineCancer ResearchCarcinogenesisCell SurvivalHsp70 translocation[SDV]Life Sciences [q-bio]Antineoplastic AgentsExosomesTargeting Hsp7003 medical and health sciences0302 clinical medicineDownregulation and upregulationHeat shock proteinNeoplasmsExtracellularHumansHSP70 Heat-Shock ProteinsExosomal Hsp70biologyChemistryCell MembraneHsp70Cell biologyUp-Regulation[SDV] Life Sciences [q-bio]030104 developmental biologyMembraneMembrane Hsp70Oncology030220 oncology & carcinogenesisChaperone (protein)Cancer cellbiology.proteinDisease ProgressionProtein foldingCancer letters
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