Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Diana M, Colleluori"'
Autor:
Frances A. Emig, E. Cama, Diana M. Colleluori, Laura R. Scolnick, Ronald E. Viola, J. David Cox, Kevin Jude, Robert S. Reczkowski, David W. Christianson, Shoufa Han, David E. Ash, K.M. Compher
Publikováno v:
Archives of Biochemistry and Biophysics. 444:15-26
Rat liver arginase (arginase I) is potently inactivated by diethyl pyrocarbonate, with a second-order rate constant of 113M(-1)s(-1) for the inactivation process at pH 7.0, 25 degrees C. Partial protection from inactivation is provided by the product
Autor:
Evis, Cama, Diana M, Colleluori, Frances A, Emig, Hyunshun, Shin, Soo Woong, Kim, Noel N, Kim, Abdulmaged M, Traish, David E, Ash, David W, Christianson
Publikováno v:
Biochemistry. 42:8445-8451
Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea. The X-ray crystal structure of a fully active, truncated form of human arginase II complexed with a boronic acid transition stat
Autor:
David E. Ash, Diana M. Colleluori
Publikováno v:
Biochemistry. 40:9356-9362
Arginases catalyze the hydrolysis of L-arginine to yield L-ornithine and urea. Recent studies indicate that arginases, both the type I and type II isozymes, participate in the regulation of nitric oxide production by modulating the availability of ar
Publikováno v:
Archives of Biochemistry and Biophysics. 389:135-143
Human type II arginase, which is extrahepatic and mitochondrial in location, catalyzes the hydrolysis of arginine to form ornithine and urea. While type I arginases function in the net production of urea for excretion of excess nitrogen, type II argi
Autor:
David E. Ash, J.D. Cox, S. Pethe, Jean-Luc Boucher, David W. Christianson, Daniel Mansuy, E. Cama, Diana M. Colleluori
Publikováno v:
Biochemistry. 40:2689-2701
Arginase is a binuclear Mn2+ metalloenzyme that catalyzes the hydrolysis of l-arginine to l-ornithine and urea. X-ray crystal structures of arginase complexed to substrate analogues Nω-hydroxy-l-arginine and Nω-hydroxy-nor-l-arginine, as well as th
Publikováno v:
Retrovirology, Vol 3, Iss 1, p 34 (2006)
Retrovirology
Retrovirology
BackgroundTo further our understanding of the structure and function of HIV-1 integrase (IN) we developed and characterized a library of monoclonal antibodies (mAbs) directed against this protein. One of these antibodies, mAb33, which is specific for
Autor:
Karyn McFadden, Karen M. Watson, Tara Pagliei, Irwin Chaiken, Ryan Kuss, Diana M. Colleluori, Deborah Tien, Robert W. Buckheit, Feirong Kang, Timothy McCormick, Joseph W. Romano
Publikováno v:
Protein expression and purification. 39(2)
Cyanovirin-N (CV-N) is a prokaryotic protein under development as a topical anti-HIV microbicide, an urgent and necessary approach to prevent HIV transmission in at-risk populations worldwide. We have expressed recombinant CV-N as inclusion bodies in
Autor:
Ramcharan, Joseph1,2 JRamcharan@locuspharma.com, Colleluori, Diana M.1,3 Diana.Colleluori@APPTECLS.com, Merkel, George1 george.merkel@fccc.edu, Andrake, Mark D.1 mark.andrake@fccc.edu, Skalka, Anna Marie1 AM_Skalka@fccc.edu
Publikováno v:
Retrovirology. 2006, Vol. 3, p1-10. 10p. 2 Diagrams, 2 Charts, 1 Graph.
Publikováno v:
Firat Universitesi Saglik Bilimleri Veteriner Dergisi; 2018, Vol. 32 Issue 1, p13-15, 3p