about
BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreStructure of the parallel-stranded DNA quadruplex d(TTAGGGT)4 containing the human telomeric repeat: evidence for A-tetrad formation from NMR and molecular dynamics simulationsDrug recognition and stabilisation of the parallel-stranded DNA quadruplex d(TTAGGGT)4 containing the human telomeric repeatBAX activation is initiated at a novel interaction siteStructure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4GSynthetic Antibodies Inhibit Bcl-2-associated X Protein (BAX) through Blockade of the N-terminal Activation Site.A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers.Correcting mitochondrial fusion by manipulating mitofusin conformations.Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeuticMarinopyrrole derivatives with sulfide spacers as selective disruptors of Mcl-1 binding to pro-apoptotic protein Bim.Chemical modulation of chaperone-mediated autophagy by retinoic acid derivatives.Design, synthesis and evaluation of marinopyrrole derivatives as selective inhibitors of Mcl-1 binding to pro-apoptotic Bim and dual Mcl-1/Bcl-xL inhibitors.Photoreactive stapled BH3 peptides to dissect the BCL-2 family interactome.An interconnected hierarchical model of cell death regulation by the BCL-2 familyDirect and selective small-molecule activation of proapoptotic BAXMultimodal interaction with BCL-2 family proteins underlies the proapoptotic activity of PUMA BH3Identification of Neutrophil Exocytosis Inhibitors (Nexinhibs), Small Molecule Inhibitors of Neutrophil Exocytosis and Inflammation: DRUGGABILITY OF THE SMALL GTPase Rab27a.Progress in targeting the BCL-2 family of proteins.An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway.Inhibition of Pro-apoptotic BAX by a noncanonical interaction mechanism.Chemical genetics: Unraveling cell death mysteries.BH3-triggered structural reorganization drives the activation of proapoptotic BAX.Self-regulation of BAX-induced cell death.Distinct BimBH3 (BimSAHB) stapled peptides for structural and cellular studies.Cystinosin, the small GTPase Rab11, and the Rab7 effector RILP regulate intracellular trafficking of the chaperone-mediated autophagy receptor LAMP2A.Pharmacological inhibition of the transcription factor PU.1 in leukemia.Direct Activation of BAX by BTSA1 Overcomes Apoptosis Resistance in Acute Myeloid Leukemia.New perspectives for targeting RAF kinase in human cancer.Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018.ICBS 2017 in Shanghai-Illuminating Life with Chemical Innovation.MFN2 agonists reverse mitochondrial defects in preclinical models of Charcot-Marie-Tooth disease type 2A.Current Insights of BRAF Inhibitors in Cancer.Editorial overview: Chemical genetics and epigenetics.Pulling the BAX trigger for tumor cell death.Erratum: Corrigendum: Chemical modulation of chaperone-mediated autophagy by retinoic acid derivativesRecognition and Stabilization of Quadruplex DNA by a Potent New Telomerase Inhibitor: NMR Studies of the 2:1 Complex of a Pentacyclic Methylacridinium Cation with d(TTAGGGT)4Optimal targeting of BCL-family proteins in head and neck squamous cell carcinoma requires inhibition of both BCL-xL and MCL-1Chaperone-Mediated Autophagy Upregulation Rescues Megalin Expression and Localization in Cystinotic Proximal Tubule CellsThe structure of FADD and its mode of interaction with procaspase-8Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
P50
Q27002044-466CC0C8-FDC1-4F0B-9975-1E03F9BA26B2Q27641867-054A2899-5DD8-4705-8FEE-3C826997AA0AQ27642482-0C29D94A-CAFA-443C-9B06-B58206974E5EQ27652635-434CEF12-B686-4AF9-82C7-3287444085D6Q27684773-5BBAA43C-8DF8-4869-9BA4-4CD92D70B1BEQ30381337-A5C26C45-7FE7-4198-8989-7E2335522B16Q30466831-24D43F43-441B-47F4-AC1D-AE70C2155A1BQ30839081-2C15A8DE-E9DE-4617-9E17-0D04EC195CDCQ34069846-5444D1ED-7F37-47A3-996D-6E1CDB43EBC3Q34091851-3DE9BC6C-0D74-4F53-946D-D14A908C4EB7Q34339147-684042F4-3F20-4438-A09D-7F65563547B8Q34450265-44519D98-12A2-4DBF-AACB-1BAF9D776E2AQ34621121-E6091C94-504B-4C2B-97D3-59468C685F8DQ36109186-3B918726-4656-4FD6-A471-C479A8272599Q36741892-63E7FAC7-1B7C-4983-9063-3D9EAF333FF2Q37192687-78CB140D-476E-40A5-8551-65281B676F1BQ39323149-45456BD6-981C-4992-93CF-F7CE084D1015Q39452441-DBAB1629-FE62-4A89-BC69-77C4DD771677Q39593727-049CA1B9-2BED-4AC7-BD7C-8334593BF2B6Q41432708-5E2583E1-EE18-4F27-A373-48C744837065Q41696518-B4E4819E-AFFA-4017-83BA-9A14919E7C07Q41884328-97F289A7-79A9-46D4-B5D5-ABE4D436B910Q42317568-6AED75B3-2C51-4F52-B3F5-E5B045DE52E8Q42788323-BB006A48-B383-4D4B-8C0F-835E9C41821BQ46864655-70AF33B0-4DB8-4C87-9014-D170290C3AE5Q46873766-B018F483-F3BD-490E-B760-81BDA7F0CDDDQ47670493-94A0C756-CAA6-452A-AC41-D2483F9DC46BQ47688064-65BB29D0-8041-425D-8025-AE408FF54D72Q47843948-DD5C382F-47D0-4F18-803E-380455216DA9Q52574306-A52A3678-468F-4B3C-A85D-AA8C713427A2Q52576485-D1F24791-E939-44F1-9BAE-EE20BBBD1610Q52692917-81E8EB51-EC34-47E5-B4C2-718F7B843378Q53100240-8DF2EEC5-1EB5-46DC-8EDB-BE90866E4F96Q55234523-DAA3215D-875D-4AF5-82F2-12B3A7D5FBA3Q57082930-11F9FFC6-9259-407B-B75B-9776525F6D86Q58096744-1FEA6768-FECF-424C-AC02-2A57087CF710Q61796819-744FA952-5576-48CE-805D-84152502FC13Q61803757-7FCF310F-1BF2-4735-8727-7BDDFA32C83BQ83953841-B89DA6B7-FD04-4F12-AD89-D0B9E7B3FB27Q87139132-8B56C0E9-6F09-4D87-B0DF-FAB9B4111178
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0001-6319-8331
@en
name
Evripidis Gavathiotis
@ast
Evripidis Gavathiotis
@en
Evripidis Gavathiotis
@es
Evripidis Gavathiotis
@nl
type
label
Evripidis Gavathiotis
@ast
Evripidis Gavathiotis
@en
Evripidis Gavathiotis
@es
Evripidis Gavathiotis
@nl
prefLabel
Evripidis Gavathiotis
@ast
Evripidis Gavathiotis
@en
Evripidis Gavathiotis
@es
Evripidis Gavathiotis
@nl
P106
P1153
6506522837
P31
P496
0000-0001-6319-8331