136831-13-5Relevant articles and documents
A Bu4N[Fe(CO)3(NO)]-Catalyzed Hemetsberger–Knittel Indole Synthesis
Baykal, Aslihan,Plietker, Bernd
supporting information, (2020/02/20)
The nucleophilic Fe complex Bu4N[Fe(CO)3(NO)] (TBA[Fe]) catalyzes the direct intramolecular amination of aryl vinyl azides to give the corresponding indole derivatives in good to excellent yields.
Intramolecular C-H amination reactions: Exploitation of the Rh 2(II)-catalyzed decomposition of azidoacrylates
Stokes, Benjamin J.,Dong, Huijun,Leslie, Brooke E.,Pumphrey, Ashley L.,Driver, Tom G.
, p. 7500 - 7501 (2008/02/09)
Rhodium(II) perfluorobutyrate-mediated decomposition of vinyl azides provides a new, mild entry into Rh2(II) nitrenoid chemistry. This methodology allows rapid access to a variety of complex, functionalized N-heterocycles in two steps from commercially available starting materials. Copyright
Probing the subpockets of factor Xa reveals two binding modes for inhibitors based on a 2-carboxyindole scaffold: A study combining structure-activity relationship and X-ray crystallography
Nazaré, Marc,Will, David W.,Matter, Hans,Schreuder, Herman,Ritter, Kurt,Urmann, Matthias,Essrich, Melanie,Bauer, Armin,Wagner, Michael,Czech, J?rg,Lorenz, Martin,Laux, Volker,Wehner, Volkmar
, p. 4511 - 4525 (2007/10/03)
Structure-activity relationships within a series of highly potent 2-carboxyindole-based factor Xa inhibitors incorporating a neutral P1 ligand are described with particular emphasis on the structural requirements for addressing subpockets of the factor Xa enzyme. Interactions with the subpockets were probed by systematic substitution of the 2-carboxyindole scaffold, in combination with privileged P1 and P4 substituents. Combining the most favorable substituents at the indole nucleus led to the discovery of a remarkably potent factor Xa inhibitor displaying a Ki value of 0.07 nM. X-ray crystallography of inhibitors bound to factor Xa revealed substituent-dependent switching of the inhibitor binding mode and provided a rationale for the SAR obtained. These results underscore the key role played by the P1 ligand not only in determining the binding affinity of the inhibitor by direct interaction but also in modifying the binding mode of the whole scaffold, resulting in a nonlinear SAR.