17 articles for AM Long
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Discovery of 1H-pyrazol-3(2H)-ones as potent and selective inhibitors of protein kinase R-like endoplasmic reticulum kinase (PERK).

Amgen
Discovery of AM-7209, a potent and selective 4-amidobenzoic acid inhibitor of the MDM2-p53 interaction.

Amgen
Optimization beyond AMG 232: discovery and SAR of sulfonamides on a piperidinone scaffold as potent inhibitors of the MDM2-p53 protein-protein interaction.

Amgen
Novel inhibitors of the MDM2-p53 interaction featuring hydrogen bond acceptors as carboxylic acid isosteres.

Amgen
Selective and potent morpholinone inhibitors of the MDM2-p53 protein-protein interaction.

Amgen
Discovery of AMG 232, a potent, selective, and orally bioavailable MDM2-p53 inhibitor in clinical development.

Amgen
Rational design and binding mode duality of MDM2-p53 inhibitors.

Amgen
Structural basis for the potent and selective inhibition of casein kinase 1 epsilon.

Amgen
Structure-based design of novel inhibitors of the MDM2-p53 interaction.

Amgen
Novel 2,3-dihydro-1,4-benzoxazines as potent and orally bioavailable inhibitors of tumor-driven angiogenesis.

Amgen
Discovery and optimization of chromenotriazolopyrimidines as potent inhibitors of the mouse double minute 2-tumor protein 53 protein-protein interaction.

Amgen
Pyridyl-pyrimidine benzimidazole derivatives as potent, selective, and orally bioavailable inhibitors of Tie-2 kinase.

Amgen
Synthesis, structural analysis, and SAR studies of triazine derivatives as potent, selective Tie-2 inhibitors.

Amgen
IAP antagonists

Bristol-Myers Squibb
Aminoimidazo[1,2-a]pyridines as a new structural class of cyclin-dependent kinase inhibitors. Part 1: Design, synthesis, and biological evaluation.

Avenida De La Industria
Design of benzoic acid inhibitors of influenza neuraminidase containing a cyclic substitution for the N-acetyl grouping.

University of Alabama At Birmingham
Hydrophobic benzoic acids as inhibitors of influenza neuraminidase.

University of Alabama At Birmingham