Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids

Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids

10.1371/journal.pone.0189379

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Bibliographic Details
Main Authors:	Chee S.M.Q., Wongsantichon J., Siau J., Thean D., Ferrer F., Robinson R.C., Lane D.P., Brown C.J., Ghadessy F.J.
Other Authors:	BIOCHEMISTRY
Format:	Article
Published:	2019
Subjects:	6 chlorotryptophan protein MDM2 protein MDMX protein p53 tryptophan unclassified drug amino acid MDM2 protein, human MDM4 protein, human nuclear protein oncoprotein peptide protein binding Article binding affinity controlled study enzyme activation Escherichia coli limit of quantitation nonhuman protein expression protein function protein modification protein purification amino acid sequence chemistry human metabolism sequence alignment structure activity relation X ray crystallography Amino Acid Sequence Amino Acids Crystallography, X-Ray Humans Nuclear Proteins Peptides Protein Binding Proto-Oncogene Proteins Proto-Oncogene Proteins c-mdm2 Sequence Alignment Structure-Activity Relationship
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/161243
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Institution:	National University of Singapore

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Summary:	10.1371/journal.pone.0189379