Zobrazeno 1 - 6
of 6
pro vyhledávání: '"E J, Goldsmith"'
Autor:
S, Ye, A L, Cech, R, Belmares, R C, Bergstrom, Y, Tong, D R, Corey, M R, Kanost, E J, Goldsmith
Publikováno v:
Nature structural biology. 8(11)
Serine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteolysis of the serpin can occur, massive conf
Publikováno v:
Proteins. 24(2)
Trypanosoma brucei ornithine decarboxylase, expressed and purified from E. coli, has been crystallized by the vapor diffusion method using PEG 3350 as a precipitant. The crystals belong to the monoclinic space group P2(1) and have cell constants of a
Publikováno v:
The Journal of biological chemistry. 266(36)
The structure of rat carboxypeptidase A2 (CPA2), which has a unique specificity for tryptophan-containing COOH-terminal peptides, has been determined in an unliganded state at 1.9-A resolution and refined to a crystallographic R-factor of 18.3%. Comp
Publikováno v:
The Journal of biological chemistry. 265(35)
Tissue-type plasminogen activator (t-PA) catalyzes the rate-limiting step in the fibrinolytic cascade: conversion of plasminogen to plasmin. Plasma contains several inhibitors of t-PA that limit its activity and prevent systemic activation of plasmin
Crystal structure of active serpin family: implication fromManduca sextaserpin K at 2.2 Å resolution
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 52:C244-C244
Publikováno v:
The Journal of biological chemistry. 262(4)
Acarbose, a pseudotetrasaccharide with a conduritol ring at the nonreducing terminus, is a naturally occurring inhibitor of amylases. It is shown here to be an inhibitor of glycogen phosphorylase and to bind more tightly to the enzyme than the equiva