Zobrazeno 1 - 6
of 6
pro vyhledávání: '"James Mottonen"'
Publikováno v:
Biochemistry. 35:16443-16448
The serpin plasminogen activator inhibitor 1 (PAI-1) folds into an active structure and then converts slowly to a more stable, but low-activity, "latent" conformation [Hekman, C. M., & Loskutoff, D. J. (1985) J. Biol. Chem. 260, 11581-11587]. Thus, t
Publikováno v:
Nature Structural & Molecular Biology. 2:442-445
Mutational studies of a serine proteinase inhibitor (serpin) reveal determinants of its structural rearrangements.
Autor:
James Mottonen, Elizabeth J. Goldsmith
Publikováno v:
Structure (London, England : 1993). 2(4)
The structure of active antithrombin, the first active serpin to be solved, sheds new light on the conformational forms of this important class of inhibitor.
Publikováno v:
Journal of molecular biology. 231(4)
The A-isozyme of O -acetylserine sulfhydrylase, a pyridoxal phosphate-dependent enzyme isolated from Salmonella typhimurium catalyzes the synthesis of l -cysteine from O -acetyl- l -serine and sulfide. The pyridoxal form of the enzyme has been crysta
Autor:
Robert M. Sweet, Arne Strand, Kieran F. Geoghegan, Jindrich Symersky, James Mottonen, Dennis E. Danley, Elizabeth J. Goldsmith, Robert D. Gerard
Publikováno v:
Nature. 355(6357)
Human plasminogen activator inhibitor-1 (PAI-1) is the fast-acting inhibitor of tissue plasminogen activator and urokinase and is a member of the serpin family of protease inhibitors. Serpins normally form complexes with their target proteases that d
Autor:
Arne Strand, Chen Sheng-Cheng, Robert D. Gerard, Elizabeth J. Goldsmith, Kieran Francis Geoghegan, James Mottonen, Dennis Edward Danley
Publikováno v:
Proteins. 9(3)
Crystals of bacterially expressed plasminogen activator inhibitor (PAI-1) suitable for X-ray diffraction analysis have been obtained from 8% (w/v) PEG 1500, pH 8.25. The space group is P1, and the lattice constants are a = 82.17 A, b = 47.82 A, c = 6