14 articles for RJ Fisher
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Discovery of thioether-bridged cyclic pentapeptides binding to Grb2-SH2 domain with high affinity.
Chinese Academy of Sciences
Protected aminooxyprolines for expedited library synthesis: application to Tsg101-directed proline-oxime containing peptides.
Nih
Elucidation of New Binding Interactions with the Tumor Susceptibility Gene 101 (Tsg101) Protein Using Modified HIV-1 Gag-p6 Derived Peptide Ligands.
Nci-Frederick
4-Pregnen-21-ol-3,20-dione-21-(4-bromobenzenesulfonate) (NSC 88915) and related novel steroid derivatives as tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors.
National Cancer Institute-Bethesda
Application of ring-closing metathesis macrocyclization to the development of Tsg101-binding antagonists.
National Cancer Institute-Frederick
Identification of Shc Src homology 2 domain-binding peptoid-peptide hybrids.
National Cancer Institute-Frederick
Examination of acylated 4-aminopiperidine-4-carboxylic acid residues in the phosphotyrosyl+1 position of Grb2 SH2 domain-binding tripeptides.
National Cancer Institute-Frederick
Application of azide-alkyne cycloaddition 'click chemistry' for the synthesis of Grb2 SH2 domain-binding macrocycles.
Nih
Design and synthesis of 4-(alpha-hydroxymalonyl)phenylalanine as a new phosphotyrosyl mimetic and its use in growth factor receptor bound 2 src-homology 2 (Grb2 SH2) domain-binding peptides.
National Cancer Institute-Frederick
Examination of phosphoryl-mimicking functionalities within a macrocyclic Grb2 SH2 domain-binding platform.
National Cancer Institute-Frederick
Utilization of a nitrobenzoxadiazole (NBD) fluorophore in the design of a Grb2 SH2 domain-binding peptide mimetic.
Nih
Design and synthesis of conformationally constrained Grb2 SH2 domain binding peptides employing alpha-methylphenylalanyl based phosphotyrosyl mimetics.
National Cancer Institute-Frederick
Macrocyclization in the design of non-phosphorus-containing Grb2 SH2 domain-binding ligands.
National Cancer Institute-Frederick