Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Lilian Parra-Gessert"'
Autor:
Lilian Parra-Gessert, Thomas Todaro, Peter Luginbuhl, Mark A Wall, Jeremy H. Lakey, Claire Dumon, May Sun, Carl Morland, Xuqiu Tan, Richard J. Lewis, Grace DeSantis, James E. Flint, Shaun Healey, Harry J. Gilbert, David P. Weiner, Alexander Varvak
Publikováno v:
Journal of Biological Chemistry. 283:22557-22564
Understanding the structural basis for protein thermostability is of considerable biological and biotechnological importance as exemplified by the industrial use of xylanases at elevated temperatures in the paper pulp and animal feed sectors. Here we
Autor:
Eric J. Mathur, Mircea Podar, Xuqiu Tan, Geoffrey P. Hazlewood, Arne Solbak, Kevin A. Gray, Janne S. Kerovuo, Ryan Mccann, Geoff Tomlinson, Dan E. Robertson, Toby Richardson, Peter Luginbuhl, Jay M. Short, Gerhard Frey, Katie Kline, Mark J. Burk, Flash Bartnek, Lilian Parra-Gessert
Publikováno v:
Journal of Biological Chemistry. 280:9431-9438
There is a growing need in the textile industry for more economical and environmentally responsible approaches to improve the scouring process as part of the pretreatment of cotton fabric. Enzymatic methods using pectin-degrading enzymes are potentia
Autor:
Jeffrey W. Smith, Hervé Le Calvez, Nicholas E. Preece, Nuria Assa-Munt, Xin Jia, Lilian Parra-Gessert
Publikováno v:
Journal of Biological Chemistry. 277:10298-10305
Integrins contain a number of divalent cation binding sites that control ligand binding affinity. Ions such as Ca(2+) and Mg(2+) bind to distinct sites on integrin and can have opposing effects on ligand binding. These effects are presumably brought
Publikováno v:
Journal of Biological Chemistry. 273:7972-7980
In Neurospora crassa, the mitochondrial arginine biosynthetic enzymes, N-acetylglutamate kinase (AGK) and N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), are generated by processing of a 96-kDa cytosolic polyprotein precursor (pAGK-AGPR). The pro
Autor:
Jeffrey W, Smith, Herve, Le Calvez, Lilian, Parra-Gessert, Nicholas E, Preece, Xin, Jia, Nuria, Assa-Munt
Publikováno v:
The Journal of biological chemistry. 277(12)
Integrins contain a number of divalent cation binding sites that control ligand binding affinity. Ions such as Ca(2+) and Mg(2+) bind to distinct sites on integrin and can have opposing effects on ligand binding. These effects are presumably brought