Zobrazeno 1 - 10
of 29
pro vyhledávání: '"D W, Christianson"'
Autor:
L T, Lavulo, T M, Sossong, M R, Brigham-Burke, M L, Doyle, J D, Cox, D W, Christianson, D E, Ash
Publikováno v:
The Journal of biological chemistry. 276(17)
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) Nature 383, 554-557). A key feature of this str
Autor:
T, Stams, D W, Christianson
Publikováno v:
EXS. (90)
Publikováno v:
EXS. (90)
Autor:
J D, Cox, E, Cama, D M, Colleluori, S, Pethe, J L, Boucher, D, Mansuy, D E, Ash, D W, Christianson
Publikováno v:
Biochemistry. 40(9)
Arginase is a binuclear Mn(2+) metalloenzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. X-ray crystal structures of arginase complexed to substrate analogues N(omega)-hydroxy-L-arginine and N(omega)-hydroxy-nor-L-arginine, a
Publikováno v:
Metal ions in biological systems. 37
Publikováno v:
Nature structural biology. 6(11)
The crystal structure of the complex between the binuclear manganese metalloenzyme arginase and the boronic acid analog of L-arginine, 2(S)-amino-6-boronohexanoic acid (ABH), has been determined at 1.7 A resolution from a crystal perfectly twinned by
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 290(3)
An increase in arginase activity has been associated with the pathophysiology of a number of conditions, including an impairment in nonadrenergic and noncholinergic (NANC) nerve-mediated relaxation of the gastrointestinal smooth muscle. An arginase i
Publikováno v:
The Journal of biological chemistry. 271(2)
The three-dimensional structure of human carbonic anhydrase II (CAII) complexed with the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide (dansylamide) has been determined to 2.1-A resolution by x-ray crystallographic methods. Unlike
Autor:
J A, Ippolito, D W, Christianson
Publikováno v:
Biochemistry. 33(51)
In order to probe the structural importance of zinc ligands in the active site of human carbonic anhydrase II (CAII), we have determined the three-dimensional structures of H94C (in metal-bound form), H94C-BME (i.e., disulfide-linked with beta-mercap
Autor:
G M, Smith, R S, Alexander, D W, Christianson, B M, McKeever, G S, Ponticello, J P, Springer, W C, Randall, J J, Baldwin, C N, Habecker
Publikováno v:
Protein science : a publication of the Protein Society. 3(1)
The 3-dimensional structure of human carbonic anhydrase II (HCAII; EC 4.2.1.1) complexed with 3 structurally related inhibitors, 1a, 1b, and 1c, has been determined by X-ray crystallographic methods. The 3 inhibitors (1a = C8H12N2O4S3) vary only in t