The following articles (labelled with PubMed ID or TBD) are for your review
PMID | Data | Article Title | Organization |
26359549 |
16 |
Cyclic Peptides Incorporating Phosphotyrosine Mimetics as Potent and Specific Inhibitors of the Grb7 Breast Cancer Target. |
The University of Sydney |
23182216 |
2 |
Novel inhibitors of a Grb2 SH3C domain interaction identified by a virtual screen. |
University of Oxford |
21381769 |
56 |
Macrocycles are great cycles: applications, opportunities, and challenges of synthetic macrocycles in drug discovery. |
Universite£ |
19362470 |
17 |
Discovery of thioether-bridged cyclic pentapeptides binding to Grb2-SH2 domain with high affinity. |
Chinese Academy of Sciences |
18821748 |
24 |
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 |
11931608 |
17 |
Inhibition of protein-protein association by small molecules: approaches and progress. |
Pfizer |
9873474 |
3 |
Actinomycin D, C2 and VII, inhibitors of Grb2-SHC interaction produced by Streptomyces. |
Korea Research Institute of Bioscience and Biotechnology |
21271718 |
6 |
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 |
19906464 |
2 |
Synthesis of aryl phosphates based on pyrimidine and triazine scaffolds. |
Cnrs Umr 176 |
11000046 |
1 |
8-O-Methylsclerotiorinamine, antagonist of the Grb2-SH2 domain, isolated from Penicillium multicolor. |
Korea Research Institute of Bioscience & Biotechnology |
17371004 |
10 |
Examination of acylated 4-aminopiperidine-4-carboxylic acid residues in the phosphotyrosyl+1 position of Grb2 SH2 domain-binding tripeptides. |
National Cancer Institute-Frederick |
17113302 |
3 |
High affinity Grb2-SH3 domain ligand incorporating Cbeta-substituted prolines in a Sos-derived decapeptide. |
Université |
16908148 |
6 |
Application of azide-alkyne cycloaddition 'click chemistry' for the synthesis of Grb2 SH2 domain-binding macrocycles. |
Nih |
16509576 |
27 |
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 |
16078854 |
4 |
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 |
15943469 |
14 |
Examination of phosphoryl-mimicking functionalities within a macrocyclic Grb2 SH2 domain-binding platform. |
National Cancer Institute-Frederick |
15713392 |
3 |
Utilization of a nitrobenzoxadiazole (NBD) fluorophore in the design of a Grb2 SH2 domain-binding peptide mimetic. |
Nih |
15689160 |
7 |
Design and synthesis of conformationally constrained Grb2 SH2 domain binding peptides employing alpha-methylphenylalanyl based phosphotyrosyl mimetics. |
National Cancer Institute-Frederick |
15149676 |
7 |
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 |
15056012 |
6 |
Macrocyclization in the design of non-phosphorus-containing Grb2 SH2 domain-binding ligands. |
National Cancer Institute-Frederick |
14761181 |
4 |
Synthesis of a 5-methylindolyl-containing macrocycle that displays ultrapotent Grb2 SH2 domain-binding affinity. |
National Cancer Institute-Frederick |
12801226 |
6 |
Utilization of a beta-aminophosphotyrosyl mimetic in the design and synthesis of macrocyclic Grb2 SH2 domain-binding peptides. |
National Cancer Institute-Frederick |
12798329 |
18 |
Potent Grb2-SH2 domain antagonists not relying on phosphotyrosine mimics. |
National Cancer Institute-Frederick |
12617916 |
13 |
Structure-based design of thioether-bridged cyclic phosphopeptides binding to Grb2-SH2 domain. |
National Cancer Institute-Frederick |
12519063 |
5 |
Macrocyclization in the design of Grb2 SH2 domain-binding ligands exhibiting high potency in whole-cell systems. |
National Cancer Institute-Frederick |
12217375 |
6 |
Development of a phosphatase-stable phosphotyrosyl mimetic suitably protected for the synthesis of high-affinity Grb2 SH2 domain-binding ligands. |
National Institutes of Health |
11459654 |
4 |
Macrocyclization in the design of a conformationally constrained Grb2 SH2 domain inhibitor. |
National Institutes of Health |
11354377 |
8 |
Convergent synthesis of potent peptide inhibitors of the Grb2-SH2 domain by palladium catalyzed coupling of a terminal alkyne. |
Novartis Pharma |
11055351 |
6 |
Structure-based design and synthesis of phosphinate isosteres of phosphotyrosine for incorporation in Grb2-SH2 domain inhibitors. Part 1. |
Novartis Pharmaceuticals |
10853661 |
25 |
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 |
10762050 |
4 |
Inhibition of the ras-dependent mitogenic pathway by phosphopeptide prodrugs with antiproliferative properties. |
University of Paris |
10715157 |
16 |
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 |
10571147 |
7 |
Mapping the X(+1) binding site of the Grb2-SH2 domain with alpha,alpha-disubstituted cyclic alpha-amino acids. |
Novartis Pharma |
10479306 |
14 |
Small peptides containing phosphotyrosine and adjacent alphaMe-phosphotyrosine or its mimetics as highly potent inhibitors of Grb2 SH2 domain. |
University of Paris |
10465559 |
8 |
Significant compensatory role of position Y-2 conferring high affinity to non-phosphorylated inhibitors of Grb2-SH2 domain. |
National Cancer Institute-Bethesda |
10450965 |
4 |
Structure-based design of a non-peptidic antagonist of the SH2 domain of GRB2. |
Novartis Pharmaceuticals |
10395476 |
3 |
Structure-based design, synthesis, and X-ray crystallography of a high-affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic. |
Novartis Pharma |
10091682 |
10 |
Monocarboxylic-based phosphotyrosyl mimetics in the design of GRB2 SH2 domain inhibitors. |
National Cancer Institute-Bethesda |
10090780 |
28 |
Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1). |
Novartis Forschungsinstitut |
10021933 |
11 |
Highly potent inhibitors of the Grb2-SH2 domain. |
Novartis Pharma |
9888830 |
14 |
Potent inhibition of Grb2 SH2 domain binding by non-phosphate-containing ligands. |
National Cancer Institute-Bethesda |
9873638 |
6 |
Structure-based design of peptidomimetic ligands of the Grb2-SH2 domain. |
Novartis Pharma |
9719597 |
12 |
Structure-based design and synthesis of high affinity tripeptide ligands of the Grb2-SH2 domain. |
Novartis Pharma |
9599224 |
10 |
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 |
9357522 |
6 |
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 |
24856058 |
3 |
Protein-ligand interactions: probing the energetics of a putative cation-? interaction. |
The University of Texas |
7473554 |
7 |
L-O-(2-malonyl)tyrosine: a new phosphotyrosyl mimetic for the preparation of Src homology 2 domain inhibitory peptides. |
National Cancer Institute-Bethesda |
10072676 |
15 |
Acquisition of high-affinity, SH2-targeted ligands via a spatially focused library. |
The Albert Einstein College of Medicine of Yeshiva University |
15808463 |
35 |
Design, synthesis, and activity of achiral analogs of 2-quinolones and indoles as non-thiol farnesyltransferase inhibitors. |
Abbott Laboratories |
12443771 |
19 |
Optimization of a pyrazolo[1,5-a]pyrimidine class of KDR kinase inhibitors: improvements in physical properties enhance cellular activity and pharmacokinetics. |
Merck Research Laboratories |