Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Tara, Mezzasalma Haarlander"'
Autor:
Tara Mezzasalma Haarlander, Karen Carroll, Sharon L. Burke, Shariff Bayoumy, Ingrid Christa Deckman, Cuifen Huo, Richard Alexander, Monica Singer, Matthew J. Todd, Yue-Mei Zhang, Kristi A. Leonard, Cindy Milligan, Robyn Williams, Kenneth J. Rhodes, Robert H. Scannevin, Keli Dzordzorme, John Spurlino, Brett A. Tounge, Diane M. Maguire, Paul F. Jackson, Celine Schalk-Hihi, Lawrence C. Kuo, Eric Devine, Frank A. Lewandowski
Publikováno v:
The Journal of biological chemistry. 292(43)
Aberrant activation of matrix metalloproteinases (MMPs) is a common feature of pathological cascades observed in diverse disorders, such as cancer, fibrosis, immune dysregulation, and neurodegenerative diseases. MMP-9, in particular, is highly dynami
Autor:
Frank A. Lewandowski, Li Liu, Jose Clemente, Charles H. Reynolds, Bruce L. Grasberger, Renee L. DesJarlais, Mark J. Macielag, Celine Schalk-Hihi, Christopher M. Flores, Mcdonnell Mark E, Richard S. Alexander, Shariff Bayoumy, Hongchang Ma, Ingrid Deckman, Diane M. Maguire, Keli C. Dzordzorme, Robyn L. Miller, Tara Mezzasalma Haarlander, Carsten Schubert, Lawrence C. Kuo, James K. Kranz, Cindy Milligan
Publikováno v:
Protein Science. 20:670-683
A high-resolution structure of a ligand-bound, soluble form of human monoglyceride lipase (MGL) is presented. The structure highlights a novel conformation of the regulatory lid-domain present in the lipase family as well as the binding mode of a pha
Autor:
Céline, Schalk-Hihi, Carsten, Schubert, Richard, Alexander, Shariff, Bayoumy, Jose C, Clemente, Ingrid, Deckman, Renee L, DesJarlais, Keli C, Dzordzorme, Christopher M, Flores, Bruce, Grasberger, James K, Kranz, Frank, Lewandowski, Li, Liu, Hongchang, Ma, Diane, Maguire, Mark J, Macielag, Mark E, McDonnell, Tara, Mezzasalma Haarlander, Robyn, Miller, Cindy, Milligan, Charles, Reynolds, Lawrence C, Kuo
Publikováno v:
Protein science : a publication of the Protein Society. 20(4)
A high-resolution structure of a ligand-bound, soluble form of human monoglyceride lipase (MGL) is presented. The structure highlights a novel conformation of the regulatory lid-domain present in the lipase family as well as the binding mode of a pha