Literature for RXP407 (M02.001 inhibitor)

(Topics flags: S Structure, I Inhibitor. To select only the references relevant to a single topic, click the link above. See explanation.)

2012
1. Anthony,C.S., Masuyer,G., Sturrock,E.D. and Acharya,K.R.
   Structure based drug design of angiotensin-I converting enzyme inhibitors
   Curr Med Chem19, 845-855. PubMed  Europe PubMed DOI  I
2010
2. Anthony,C.S., Corradi,H.R., Schwager,S.L., Redelinghuys,P., Georgiadis,D., Dive,V., Acharya,K.R. and Sturrock,E.D.
   The N domain of human angiotensin-I-converting enzyme: the role of N-glycosylation and the crystal structure in complex with an N domain-specific phosphinic inhibitor, RXP407
   J Biol Chem285, 35685-35693. PubMed  Europe PubMed DOI  S  I
2009
3. Kroger,W.L., Douglas,R.G., O'Neill,H.G., Dive,V. and Sturrock,E.D.
   Investigating the domain specificity of phosphinic inhibitors RXPA380 and RXP407 in angiotensin-converting enzyme
   Biochemistry48, 8405-8412. PubMed  Europe PubMed DOI  I
2001
4. Junot,C., Gonzales,M.F., Ezan,E., Cotton,J., Vazeux,G., Michaud,A., Azizi,M., Vassiliou,S., Yiotakis,A., Corvol,P. and Dive,V.
   RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis
   J Pharmacol Exp Ther297, 606-611. PubMed  Europe PubMed  I
5. [YEAR:1-4-2001]Vazeux,G., Cotton,J., Cuniasse,P. and Dive,V.
   Potency and selectivity of RXP407 on human, rat, and mouse angiotensin-converting enzyme
   Biochem Pharmacol61, 835-841. PubMed  Europe PubMed DOI  I
1999
6. [YEAR:13-4-1999]Dive,V., Cotton,J., Yiotakis,A., Michaud,A., Vassiliou,S., Jiracek,J., Vazeux,G., Chauvet,M.T., Cuniasse,P. and Corvol,P.
   RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites
   Proc Natl Acad Sci U S A96, 4330-4335. PubMed  Europe PubMed DOI  I