Structure-based design of novel inhibitors of the MDM2-p53 interaction
about
Chemical Variations on the p53 Reactivation ThemeInhibition of nutlin-resistant HDM2 mutants by stapled peptidesIn vitro selection of mutant HDM2 resistant to Nutlin inhibitionStructural characterization and inhibition of the Plasmodium Atg8–Atg3 interactionDiscovery of RG7112: A Small-Molecule MDM2 Inhibitor in Clinical DevelopmentThe structure of an MDM2-Nutlin-3a complex solved by the use of a validated MDM2 surface-entropy reduction mutant8-Triazolylpurines: Towards Fluorescent Inhibitors of the MDM2/p53 InteractionDesign, Synthesis and Evaluation of 2,5-Diketopiperazines as Inhibitors of the MDM2-p53 InteractionDiaryl- and triaryl-pyrrole derivatives: inhibitors of the MDM2-p53 and MDMX-p53 protein-protein interactions†Electronic supplementary information (ESI) available: Experimental details for compound synthesis, analytical data for all compounds and inOrganocatalytic, diastereo- and enantioselective synthesis of nonsymmetric cis-stilbene diamines: a platform for the preparation of single-enantiomer cis-imidazolines for protein-protein inhibition.Discovery of Potent and Simplified Piperidinone-Based Inhibitors of the MDM2-p53 Interaction.MDM2, MDMX and p53 in oncogenesis and cancer therapyTargeting protein-protein interactions as an anticancer strategyDesign, synthesis and biological evaluation of sulfamide and triazole benzodiazepines as novel p53-MDM2 inhibitorsSAR405838: an optimized inhibitor of MDM2-p53 interaction that induces complete and durable tumor regressionA novel drug discovery strategy: mechanistic investigation of an enantiomeric antitumor agent targeting dual p53 and NF-κB pathways.Identification of novel rab27a/melanophilin blockers by pharmacophore-based virtual screening.Small-molecule inhibitors of the MDM2-p53 protein-protein interaction (MDM2 Inhibitors) in clinical trials for cancer treatment.Small-molecule MDM2-p53 inhibitors: recent advances.How To Design a Successful p53-MDM2/X Interaction Inhibitor: A Thorough Overview Based on Crystal Structures.AlphaSpace: Fragment-Centric Topographical Mapping To Target Protein-Protein Interaction Interfaces.Markov models of the apo-MDM2 lid region reveal diffuse yet two-state binding dynamics and receptor poses for computational docking.Diastereomeric spirooxindoles as highly potent and efficacious MDM2 inhibitorsA potent small-molecule inhibitor of the MDM2-p53 interaction (MI-888) achieved complete and durable tumor regression in mice.Capsaicin mediates cell cycle arrest and apoptosis in human colon cancer cells via stabilizing and activating p53.Targeting the ubiquitin-mediated proteasome degradation of p53 for cancer therapy.Resistance acquisition to MDM2 inhibitors.Targeting p53-MDM2-MDMX loop for cancer therapy.Targeting the MDM2-p53 Protein-Protein Interaction for New Cancer Therapy: Progress and Challenges.Coccoquinones A and B, new anthraquinone derivatives produced by Staphylotrichum coccosporum PF1460.Medicinal Chemistry Strategies to Disrupt the p53-MDM2/MDMX Interaction.Pharmacological activation of wild-type p53 in the therapy of leukemia.Pre-clinical evaluation of the MDM2-p53 antagonist RG7388 alone and in combination with chemotherapy in neuroblastoma.Synthesis of spiro[isoindole-1,5'-isoxazolidin]-3(2H)-ones as potential inhibitors of the MDM2-p53 interaction.Microsecond simulations of mdm2 and its complex with p53 yield insight into force field accuracy and conformational dynamics.MDM2 antagonists synergize broadly and robustly with compounds targeting fundamental oncogenic signaling pathways.Spiro-oxindoles as a Promising Class of Small Molecule Inhibitors of p53-MDM2 Interaction Useful in Targeted Cancer Therapy.Reviving the guardian of the genome: Small molecule activators of p53.Efficient synthesis of RITA and its analogues: derivation of analogues with improved antiproliferative activity via modulation of p53/miR-34a pathway.The use of ion mobility mass spectrometry to probe modulation of the structure of p53 and of MDM2 by small molecule inhibitors
P2860
Q26749008-A218C942-6AE5-4DD8-9AAB-4E1F058DE34AQ27301404-A2DB5C0F-9649-4A49-B66D-AE69AE8E42E5Q27322456-C089E43E-347D-42D6-A404-CABD34B5C611Q27673186-3C7035F8-2F5A-4888-A794-F880947FFB61Q27684199-D4C54CE0-8634-4068-9FFE-E9EADA5F1380Q27685287-FE7B6DA7-1F32-4C88-9EDB-71298839703CQ28547009-8F612BB3-758E-45D6-BCA7-64F4E3412A04Q28548694-2FF42DB6-B5E7-4AF9-A232-F81F231543FAQ30670705-1E56B62C-08DE-4179-BE31-D9764CC53445Q33998827-F373D443-A095-445E-8982-0C058938FE8CQ34063712-E16E0513-0FB2-43A9-BED6-6F1C8FB75245Q34166049-50313AD3-0B37-478F-811C-3AA7AEA82D82Q34347892-07D4831B-3A0A-402E-86D3-4B37BD86D07FQ34358585-30ECF89D-1D10-4AB2-9C55-831AAC52B603Q34584722-DEB068FA-B03D-479C-8060-4621048A4ABFQ34786578-FF57AEF2-154D-426F-9013-52FF77B128D7Q35057299-4CDCBFCE-B6FD-4E5A-8853-8CAABEDB905CQ35087851-34B11058-3EED-495C-A1D4-49F541B186AFQ35617077-7D1D9AF0-9E32-405B-92E5-025E08287797Q35871210-A6EA5391-2751-42A9-81B5-0DE18005E088Q35997296-E74FF267-2E6A-451D-92A5-485274DACC76Q37188955-F5835B9F-1472-458B-97FC-EE60ED698AF2Q37249642-E5F2D9EE-99F9-42B4-9D73-917976EB4952Q37432745-DE775BD1-05DE-456F-A687-B39F7A364575Q37642359-FE50BDA6-7BD7-4447-9C06-8776DF260DF0Q38059739-A62B25E0-3E0E-45EE-99F0-52A4427801DFQ38238600-1D178091-61E0-42CE-9859-EED166330302Q38247168-CD29659D-3B46-4AD8-803D-FE554AEE4170Q38749151-0B2D003B-0AD3-4465-95EF-3E2272CC93F8Q38828141-FAB3A1B9-EA29-4F2B-A20E-0BB288AF37A9Q38865504-44A65F0C-4BB7-4146-8080-D4B160C0B609Q38872029-6B69AF1F-88D9-4890-A0DA-5D344B955953Q38890690-FAD63C28-01D0-4809-9895-B2863F00E427Q38987994-1C25AE16-142A-4CB4-8147-E7EBB82B2BB2Q38988816-8FC19CE4-9653-4F48-B630-FC74B30716F9Q38997002-FC1D80E2-A1CA-462F-B9BD-CD3DB6E20822Q39036213-2F5332D1-3A5B-43AB-805A-8D6745FBE794Q39205536-A16413F0-E225-4810-B07F-712285FD1754Q39244957-3A453DE5-D2BF-4401-81B8-A97F511C66BBQ40688335-38AAC6FA-6DDE-49F9-BD8A-DE5F8E70E733
P2860
Structure-based design of novel inhibitors of the MDM2-p53 interaction
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@ast
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@en
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@nl
type
label
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@ast
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@en
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@nl
prefLabel
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@ast
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@en
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@nl
P2093
P3181
P356
P1476
Structure-based design of novel inhibitors of the MDM2-p53 interaction
@en
P2093
Alexander M Long
Anne Y Saiki
Brian M Fox
Daqing Sun
Darin Gustin
David Chow
David J Kopecky
Dongyin Yu
Felix Gonzalez-Lopez De Turiso
P304
P3181
P356
10.1021/JM300354J
P407
P577
2012-06-14T00:00:00Z