50690-53-4Relevant academic research and scientific papers
Synthesis of lamellarin alkaloids using orthoester-masked α-keto acids
Shirley, Harry J.,Koyioni, Maria,Muncan, Filip,Donohoe, Timothy J.
, p. 4334 - 4338 (2019/04/17)
Pyruvic acid and other α-keto acids are frequently encountered as intermediates in metabolic pathways, yet their application in total synthesis has met with limited success. In this work, we present a bioinspired strategy that utilizes highly functionaliz
Structure-guided optimization of estrogen receptor binding affinity and antagonist potency of pyrazolopyrimidines with basic side chains
Zhou, Hai-Bing,Sheng, Shubin,Compton, Dennis R.,Kim, Younchang,Joachimiak, Andrzej,Sharma, Sanjay,Carlson, Kathryn E.,Katzenellenbogen, Benita S.,Nettles, Kendall W.,Greene, Geoffrey L.,Katzenellenbogen, John A.
, p. 399 - 403 (2007/10/03)
2,3-Diarylpyrazolo[1,5-α]pyrimidines are estrogen receptor (ER) antagonists of modest potency that we have described previously. Guided by the crystal structure of an ER-ligand complex that we have obtained with one of these compounds, we prepared analogs that contain a basic side chain at the 2- or 3-aryl group and quickly found one that, according to the structure-based prediction, shows an increase in binding affinity and antagonist potency and a loss of residual agonist activity.
Design of Inhibitors from the Three-Dimensional Structure of Alcohol Dehydrogenase. Chemical Synthesis and Enzymatic Properties
Freudenreich, Charles,Samama, Jean-Pierre,Biellmann, Jean-Francois
, p. 3344 - 3353 (2007/10/02)
Inhibitors of liver alcohol dehydrogenase were designed from the three-dimensional structure of the enzyme.The ligand to the catalytic zinc ion is an amide group or, better, a formamide group.With the latter function, a hydrogen bond between the NH group and the hydroxyl group of Ser-48 may be formed.The hydrophobic substrate binding site brings structural restraints. α-ω bifunctional molecules show good inhibitory properties possibly due to the interactions with polar residues at the entrance of the substrate binding site.
