53 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Cyclic Peptides Incorporating Phosphotyrosine Mimetics as Potent and Specific Inhibitors of the Grb7 Breast Cancer Target.
The University of Sydney
Novel inhibitors of a Grb2 SH3C domain interaction identified by a virtual screen.
University of Oxford
Macrocycles are great cycles: applications, opportunities, and challenges of synthetic macrocycles in drug discovery.
Universite£
Discovery of thioether-bridged cyclic pentapeptides binding to Grb2-SH2 domain with high affinity.
Chinese Academy of Sciences
Synthesis and utilization of chiral alpha-methylated alpha-amino acids with a carboxyalkyl side chain in the design of novel Grb2-SH2 peptide inhibitors free of phosphotyrosine.
Chinese Academy of Sciences
Inhibition of protein-protein association by small molecules: approaches and progress.
Pfizer
Actinomycin D, C2 and VII, inhibitors of Grb2-SHC interaction produced by Streptomyces.
Korea Research Institute of Bioscience and Biotechnology
Development of non-peptide ligands of growth factor receptor-bound protein 2-SRC homology 2 domain using molecular modeling and NMR spectroscopy.
Universidad Complutense De Madrid
8-O-Methylsclerotiorinamine, antagonist of the Grb2-SH2 domain, isolated from Penicillium multicolor.
Korea Research Institute of Bioscience & Biotechnology
Examination of acylated 4-aminopiperidine-4-carboxylic acid residues in the phosphotyrosyl+1 position of Grb2 SH2 domain-binding tripeptides.
National Cancer Institute-Frederick
High affinity Grb2-SH3 domain ligand incorporating Cbeta-substituted prolines in a Sos-derived decapeptide.
Université
Application of azide-alkyne cycloaddition 'click chemistry' for the synthesis of Grb2 SH2 domain-binding macrocycles.
Nih
Discovery of a novel nonphosphorylated pentapeptide motif displaying high affinity for Grb2-SH2 domain by the utilization of 3'-substituted tyrosine derivatives.
Graduate School of The Chinese Academy of Sciences
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
Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain.
H. Lee Moffitt Cancer Center and Research Institute
Development of l-3-aminotyrosine suitably protected for the synthesis of a novel nonphosphorylated hexapeptide with low-nanomolar Grb2-SH2 domain-binding affinity.
Institute of Materia Medica
Macrocyclization in the design of non-phosphorus-containing Grb2 SH2 domain-binding ligands.
National Cancer Institute-Frederick
Synthesis of a 5-methylindolyl-containing macrocycle that displays ultrapotent Grb2 SH2 domain-binding affinity.
National Cancer Institute-Frederick
Utilization of a beta-aminophosphotyrosyl mimetic in the design and synthesis of macrocyclic Grb2 SH2 domain-binding peptides.
National Cancer Institute-Frederick
Potent Grb2-SH2 domain antagonists not relying on phosphotyrosine mimics.
National Cancer Institute-Frederick
Structure-based design of thioether-bridged cyclic phosphopeptides binding to Grb2-SH2 domain.
National Cancer Institute-Frederick
Macrocyclization in the design of Grb2 SH2 domain-binding ligands exhibiting high potency in whole-cell systems.
National Cancer Institute-Frederick
Development of a phosphatase-stable phosphotyrosyl mimetic suitably protected for the synthesis of high-affinity Grb2 SH2 domain-binding ligands.
National Institutes of Health
Rational design of cell-permeable cyclic peptides containing a d-Pro-l-Pro motif.
The Ohio State University
Macrocyclization in the design of a conformationally constrained Grb2 SH2 domain inhibitor.
National Institutes of Health
Convergent synthesis of potent peptide inhibitors of the Grb2-SH2 domain by palladium catalyzed coupling of a terminal alkyne.
Novartis Pharma
Structure-based design and synthesis of phosphinate isosteres of phosphotyrosine for incorporation in Grb2-SH2 domain inhibitors. Part 1.
Novartis Pharmaceuticals
Examination of novel non-phosphorus-containing phosphotyrosyl mimetics against protein-tyrosine phosphatase-1B and demonstration of differential affinities toward Grb2 SH2 domains.
National Cancer Institute-Bethesda
Inhibition of the ras-dependent mitogenic pathway by phosphopeptide prodrugs with antiproliferative properties.
University of Paris
Inhibition of Grb2 SH2 domain binding by non-phosphate-containing ligands. 2. 4-(2-Malonyl)phenylalanine as a potent phosphotyrosyl mimetic.
National Cancer Institute-Bethesda
Mapping the X(+1) binding site of the Grb2-SH2 domain with alpha,alpha-disubstituted cyclic alpha-amino acids.
Novartis Pharma
Small peptides containing phosphotyrosine and adjacent alphaMe-phosphotyrosine or its mimetics as highly potent inhibitors of Grb2 SH2 domain.
University of Paris
Significant compensatory role of position Y-2 conferring high affinity to non-phosphorylated inhibitors of Grb2-SH2 domain.
National Cancer Institute-Bethesda
Structure-based design of a non-peptidic antagonist of the SH2 domain of GRB2.
Novartis Pharmaceuticals
Structure-based design, synthesis, and X-ray crystallography of a high-affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic.
Novartis Pharma
Monocarboxylic-based phosphotyrosyl mimetics in the design of GRB2 SH2 domain inhibitors.
National Cancer Institute-Bethesda
Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1).
Novartis Forschungsinstitut
Potent inhibition of Grb2 SH2 domain binding by non-phosphate-containing ligands.
National Cancer Institute-Bethesda
Structure-based design and synthesis of high affinity tripeptide ligands of the Grb2-SH2 domain.
Novartis Pharma
Potent antagonists of the SH2 domain of Grb2: optimization of the X+1 position of 3-amino-Z-Tyr(PO3H2)-X+1-Asn-NH2.
Novartis Pharma
Discovery of 3-aminobenzyloxycarbonyl as an N-terminal group conferring high affinity to the minimal phosphopeptide sequence recognized by the Grb2-SH2 domain.
Novartis Pharma
Protein-ligand interactions: probing the energetics of a putative cation-π interaction.
The University of Texas
L-O-(2-malonyl)tyrosine: a new phosphotyrosyl mimetic for the preparation of Src homology 2 domain inhibitory peptides.
National Cancer Institute-Bethesda
Acquisition of high-affinity, SH2-targeted ligands via a spatially focused library.
The Albert Einstein College of Medicine of Yeshiva University
