17672-26-3Relevant articles and documents
Cross-Coupling between Hydrazine and Aryl Halides with Hydroxide Base at Low Loadings of Palladium by Rate-Determining Deprotonation of Bound Hydrazine
Borate, Kailaskumar,Choi, Kyoungmin,Goetz, Roland,Hartwig, John F.,Shinde, Harish,Wang, Justin Y.,Zuend, Stephan J.
supporting information, p. 399 - 408 (2020/10/29)
Reported here is the Pd-catalyzed C–N coupling of hydrazine with (hetero)aryl chlorides and bromides to form aryl hydrazines with catalyst loadings as low as 100 ppm of Pd and KOH as base. Mechanistic studies revealed two catalyst resting states: an arylpalladium(II) hydroxide and arylpalladium(II) chloride. These compounds are present in two interconnected catalytic cycles and react with hydrazine and base or hydrazine alone to give the product. The selectivity of the hydroxide complex with hydrazine to form aryl over diaryl hydrazine was lower than that of the chloride complex, as well as the catalytic reaction. In contrast, the selectivity of the chloride complex closely matched that of the catalytic reaction, indicating that the aryl hydrazine is derived from this complex. Kinetic studies showed that the coupling process occurs by rate-limiting deprotonation of a hydrazine-bound arylpalladium(II) chloride complex to give an arylpalladium(II) hydrazido complex.
Enhanced selectivity profile of pyrazole-urea based DFG-out p38α inhibitors
Liu, Hu,Kuhn, Cyrille,Feru, Frederic,Jacques, Suzanne L.,Deshmukh, Gayatri D.,Ye, Ping,Rennie, Glen R.,Johnson, Theresa,Kazmirski, Steven,Low, Simon,Coli, Rocco,Ding, Yuan-Hua,Cheng, Alan C.,Tecle, Haile,English, Jessie M.,Stanton, Robert,Wu, Joe C.
experimental part, p. 4885 - 4891 (2010/10/03)
By targeting an extended region of the conventional 'DFG-out' pocket of p38α, while minimizing interactions with the specificity pocket and eliminating interactions with the adenine binding site, we are able to design and synthesize a number of pyrazole-u
Structure-based design of novel guanidine/benzamidine mimics: Potent and orally bioavailable factor Xa inhibitors as novel anticoagulants
Lam, Patrick Y. S.,Clark, Charles G.,Li, Renhua,Pinto, Donald J. P.,Orwat, Michael J.,Galemmo, Robert A.,Fevig, John M.,Teleha, Christopher A.,Alexander, Richard S.,Smallwood, Angela M.,Rossi, Karen A.,Wright, Matthew R.,Bai, Stephen A.,He, Kan,Luettgen, Joseph M.,Wong, Pancras C.,Knabb, Robert M.,Wexler, Ruth R.
, p. 4405 - 4418 (2007/10/03)
As part of an ongoing effort to prepare orally active factor Xa inhibitors using structure-based drug design techniques and molecular recognition principles, a systematic study has been performed on the pharmacokinetic profile resulting from replacing the
