Zobrazeno 1 - 5
of 5
pro vyhledávání: '"J. L. Rios Steiner"'
Autor:
B. J. Bell, Leandra Watanabe, Lukasz Lebioda, J. L. Rios-Steiner, Raghuvir K. Arni, Alexander Tulinsky
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:1454-1458
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida is a key enzyme in the Entner-Doudoroff pathway which catalyses the cleavage of KDPG via a class I Schiff-base mechanism. The crystal structure of this enzyme has been refined
Autor:
Emil B. Lobkovsky, John L. Occolowitz, Jon Clardy, Jonathan W. Paschal, Stephen H. Larsen, Lawrence C. Creemer, Herbert A. Kirst, J. L. Rios Steiner
Publikováno v:
ChemInform. 27
Autor:
Jon S. Mynderse, James W. Martin, Jon Clardy, Patrick J. Baker, Jonathan W. Paschal, J. L. Rios Steiner, Emil B. Lobkovsky, Herbert A. Kirst
Publikováno v:
ChemInform. 27
Autor:
J. L. Rios-Steiner, S.E. Weaver, Alexander Tulinsky, James H. Geiger, Raghuvir K. Arni, Mário T. Murakami
Publikováno v:
Journal of molecular biology. 366(2)
NAPc2, an anticoagulant protein from the hematophagous nematode Ancylostoma caninum evaluated in phase-II/IIa clinical trials, inhibits the extrinsic blood coagulation pathway by a two step mechanism, initially interacting with the hitherto uncharact
Publikováno v:
Journal of molecular biology. 308(4)
The X-ray crystal structure of a complex of a modified recombinant kringle-2 domain of human plasminogen, K2Pg[C4G/E56D/L72Y] (mK2Pg), containing an upregulated lysine-binding site, bound to a functional 30 residue internal peptide (VEK-30) from an M