Zobrazeno 1 - 10
of 52
pro vyhledávání: '"David E, Ash"'
Publikováno v:
Bioorganic & Medicinal Chemistry. 21:1123-1135
Atherosclerosis, a leading cause of death worldwide, is associated with the excessive proliferation of vascular smooth muscle cells. Nitrogen monoxide, more commonly known as nitric oxide, inhibits this uncontrolled proliferation. Herein we report th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab3802d1c707ad7d098a83a2a9d8471a
https://doi.org/10.1016/j.bmc.2012.12.043
https://doi.org/10.1016/j.bmc.2012.12.043
Autor:
Yajing Ji, Neeraj Vij, Alec R. Badour, Austin Bowersock, Stephen J. Juris, Dillip K. Mohanty, David E. Ash
Excessive proliferation of vascular smooth muscle cells (SMC) is an important contributor to the progression of atherosclerosis. Inhibition of proliferation can be achieved by endogenously produced and exogenously supplied nitrogen monoxide, commonly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cd2025bb9e49021cfcc62cf75dcaded
https://europepmc.org/articles/PMC5253310/
https://europepmc.org/articles/PMC5253310/
Publikováno v:
Archives of Biochemistry and Biophysics. 488:14-22
Porphyromonas gingivalis peptidylarginine deiminase (PAD) catalyzes the deimination of peptidylarginine residues of various peptides to produce peptidylcitrulline and ammonia. P. gingivalis is associated with adult-onset periodontitis and cardiovascu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5fa321c54c319b9c6c2e23441fe2a6b
https://doi.org/10.1016/j.abb.2009.06.010
https://doi.org/10.1016/j.abb.2009.06.010
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:
Thomas M. Sossong, Lopeti T. Lavulo, David E. Ash, J. David Cox, Michael R. Brigham-Burke, David W. Christianson, Michael L. Doyle
Publikováno v:
Journal of Biological Chemistry. 276:14242-14248
The structure of the trimeric, manganese metalloenzyme, rat liver arginase, has been previously determined at 2.1-A resolution (Kanyo, Z. F., Scolnick, L. R., Ash, D. E., and Christianson, D. W., (1996) Nature383, 554–557). A key feature of this st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7cbb9231a47ed459362365ced8e7314a
https://doi.org/10.1074/jbc.m010575200
https://doi.org/10.1074/jbc.m010575200
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:
Biochemistry. 37:8539-8550
Rat liver arginase contains a dimanganese(II,II) center per subunit that is required for catalytic hydrolysis of l-arginine to form urea and l-ornithine. A recent crystallographic study has shown that the Mn2 center consists of two coordinatively ine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75bccde23ad9094ae25c4dd1f8ea9aff
https://doi.org/10.1021/bi972874c
https://doi.org/10.1021/bi972874c