dc.creatorMajmudar, Chinmay Y.
dc.creatorHøjfeldt, Jonas W.
dc.creatorArevang, Carl J.
dc.creatorPomerantz, William C.
dc.creatorGagnon, Jessica K.
dc.creatorSchultz, Pamela J.
dc.creatorCesa, Laura C.
dc.creatorDoss, Conor H.
dc.creatorRowe, Steven P.
dc.creatorVásquez Chaves, Víctor
dc.creatorTamayo Castillo, Giselle
dc.creatorCierpicki, Tomasz
dc.creatorBrooks, Charles L. III
dc.creatorSherman, David H.
dc.creatorMapp, Anna K.
dc.date.accessioned2023-01-02T20:03:38Z
dc.date.accessioned2023-03-13T12:50:24Z
dc.date.available2023-01-02T20:03:38Z
dc.date.available2023-03-13T12:50:24Z
dc.date.created2023-01-02T20:03:38Z
dc.date.issued2012-10-08
dc.identifierhttps://onlinelibrary.wiley.com/doi/10.1002/anie.201206815
dc.identifier1521-3757
dc.identifierhttps://hdl.handle.net/10669/87973
dc.identifier10.1002/ange.201206815
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/6118979
dc.description.abstractAlthough there have been recent notable successes in thediscovery of ligands that target stable, high-affinity protein-protein interactions (PPIs), the transient and moderateaffinity PPIs that underpin many fundamental cellularprocesses have proven to be far less tractable for liganddiscovery.[1]Prime examples of this are the dynamic com-plexes formed between DNA-bound transcriptional activa-tors and coactivators that are part of eukaryotic transcriptioninitiation.
dc.languageeng
dc.sourceAngewandte Chemie, vol.51(45), pp.11258-11262.
dc.subjectCoaktivatoren
dc.subjectDepside
dc.subjectInhibitoren
dc.subjectProtein-Protein-Wechselwirkungen
dc.subjectSekikasäure
dc.titleSekikaic Acid and Lobaric Acid Target a Dynamic Interface of the Coactivator CBP/p300
dc.typeartículo científico


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