Designer macrocyclic organo-peptide hybrids inhibit the interaction between p53 and HDM2/X by accommodating a functional α-helix.
about
Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein-Protein InteractionsDouble Strain-Promoted Macrocyclization for the Rapid Selection of Cell-Active Stapled PeptidesMethods for the creation of cyclic Peptide libraries for use in lead discovery.Side-chain-to-tail cyclization of ribosomally derived peptides promoted by aryl and alkyl amino-functionalized unnatural amino acidsNew Modalities for Challenging Targets in Drug Discovery.Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network.Peptide Macrocycles Developed from Precisely Regulated Multiple Cyclization of Unprotected Peptides.Oxadiazole grafts in peptide macrocycles.
P2860
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P2860
Designer macrocyclic organo-peptide hybrids inhibit the interaction between p53 and HDM2/X by accommodating a functional α-helix.
description
2014 nî lūn-bûn
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年论文
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2014年论文
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2014年论文
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name
Designer macrocyclic organo-pe ...... modating a functional α-helix.
@ast
Designer macrocyclic organo-pe ...... modating a functional α-helix.
@en
type
label
Designer macrocyclic organo-pe ...... modating a functional α-helix.
@ast
Designer macrocyclic organo-pe ...... modating a functional α-helix.
@en
prefLabel
Designer macrocyclic organo-pe ...... modating a functional α-helix.
@ast
Designer macrocyclic organo-pe ...... modating a functional α-helix.
@en
P2860
P356
P1476
Designer macrocyclic organo-pe ...... modating a functional α-helix.
@en
P2093
Jessica M Smith
John R Frost
P2860
P304
P356
10.1039/C4CC01199F
P407
P50
P577
2014-04-07T00:00:00Z