
doi: 10.1039/c4ob00742e
pmid: 24817343
Evaluating the influence of staple position, azido amino acid side-chain length and point mutation on the activity of ‘double-click’ stapled p53 peptides.
Peptide sequences, Circular Dichroism, Molecular Sequence Data, Fluorescence Polarization, Genes, Reporter, Amino acids, Click Chemistry, Amino Acid Sequence, Tumor Suppressor Protein p53, Peptides
Peptide sequences, Circular Dichroism, Molecular Sequence Data, Fluorescence Polarization, Genes, Reporter, Amino acids, Click Chemistry, Amino Acid Sequence, Tumor Suppressor Protein p53, Peptides
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 46 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
