53 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
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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-? 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
Design, synthesis, and activity of achiral analogs of 2-quinolones and indoles as non-thiol farnesyltransferase inhibitors.
Abbott Laboratories