Zobrazeno 1 - 7
of 7
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b5c2acdf5adca5b765d14c927aa2dcc
https://doi.org/10.1016/j.abb.2005.09.009
https://doi.org/10.1016/j.abb.2005.09.009
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c91f64da032c21f85b6daac5b2820034
https://doi.org/10.1021/bi034340j
https://doi.org/10.1021/bi034340j
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5bfb130c03ea83e3d140383ba088369
https://doi.org/10.1021/bi010783g
https://doi.org/10.1021/bi010783g
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef9818fb3e3ea19be22b54cfaffd767b
https://doi.org/10.1006/abbi.2001.2324
https://doi.org/10.1006/abbi.2001.2324
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c27a8c338525fdc8b03652cace35ff24
https://doi.org/10.1021/bi002318+
https://doi.org/10.1021/bi002318+
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::741a99b95f7e569c6fce2d3221bfd6f3
https://doi.org/10.1186/1742-4690-3-34
https://doi.org/10.1186/1742-4690-3-34
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2075e6f84d6a916a663c49533dffeed
https://pubmed.ncbi.nlm.nih.gov/15642474
https://pubmed.ncbi.nlm.nih.gov/15642474