474843-41-9Relevant articles and documents
Combining in silico and biophysical methods for the development of pseudomonas aeruginosa quorum sensing inhibitors: An alternative approach for structure-based drug design
Sahner, J. Henning,Brengel, Christian,Storz, Michael P.,Groh, Matthias,Plaza, Alberto,Müller, Rolf,Hartmann, Rolf W.
, p. 8656 - 8664 (2013/12/04)
The present work deals with the optimization of an inhibitor of PqsD, an enzyme essential for Pseudomonas aeruginosa quorum sensing apparatus. Molecular docking studies, supported by biophysical methods (surface plasmon resonance, isothermal titration cal
Discovery and SAR of a novel selective and orally bioavailable nonpeptide classical competitive inhibitor class of protein-tyrosine phosphatase 1B
Andersen, Henrik Sune,Olsen, Ole H.,Iversen, Lars F.,S?rensen, Anette L. P.,Mortensen, Steen B.,Christensen, Michael S.,Branner, Sven,Hansen, Thomas K.,Lau, Jesper F.,Jeppesen, Lone,Moran, Edmond J.,Su, Jing,Bakir, Farid,Judge, Luke,Shahbaz, Manou,Collins, Tassie,Vo, Todd,Newman, Michael J.,Ripka, William C.,M?ller, Niels Peter H.
, p. 4443 - 4459 (2007/10/03)
Reversible phosphorylation and dephosphorylation of key proteins on tyrosine residues are important parts of intracellular signaling triggered by hormones and other agents. Recent knock-out studies in mice have identified PTP1B as a potential target for t
