User contributions for Cara Halseth
From Proteopedia
Results for Cara Halseth talk block log uploads logs
A user with 155 edits. Account created on 3 February 2010.
13 February 2012
- 14:3114:31, 13 February 2012 diff hist −8 m User:Cara Halseth No edit summary current
10 October 2010
- 04:3604:36, 10 October 2010 diff hist +27 N Cara Halseth/Yersinia YopH Cara Halseth/Yersinia YopH moved to Yersinia YopH current
- 04:3604:36, 10 October 2010 diff hist 0 m Yersinia YopH Cara Halseth/Yersinia YopH moved to Yersinia YopH
24 April 2010
- 06:3506:35, 24 April 2010 diff hist −15 Yersinia YopH No edit summary
- 06:3406:34, 24 April 2010 diff hist +12,943 N Yersinia YopH New page: <applet load='1XXV' size='300' frame='true' align='right' caption='Crystal structure showing two YopH protein-tyrosine phosphatase catalytic domains from Yersinia enterocolitica bound to E...
31 March 2010
- 17:1617:16, 31 March 2010 diff hist 0 m File:Catalytic domain of YopH.gif →Summary current
- 04:2504:25, 31 March 2010 diff hist +287 N File:Potential mechanism.gif Possible mechanism with formation of phosphocysteine intermediate for YopH. Derived using information from Stuckey, J.A. et al. Nature. 370:571-575 (1994) and Pannifer et al. The Journal of Biological Chemistry. 273:10454–10462 (1998). current
27 March 2010
- 04:5104:51, 27 March 2010 diff hist 0 File:Key residues at site 2-Arg 278 and Lys 342.gif uploaded a new version of "Image:Key residues at site 2-Arg 278 and Lys 342.gif" current
- 04:4704:47, 27 March 2010 diff hist 0 N File:Key residues at site 2-Arg 278 and Lys 342.gif No edit summary
26 March 2010
- 19:2119:21, 26 March 2010 diff hist 0 File:Catalytic domain of YopH.gif uploaded a new version of "Image:Catalytic domain of YopH.gif": The residue of the catalytic domain of YopH closest to the N-terminal is coloured in blue. The C-terminal residue is red, and the phosphate-binding loop in the active site is green. Pho
- 19:1919:19, 26 March 2010 diff hist +286 N File:Catalytic domain of YopH.gif The catalytic domain of YopH. The C-terminal residues is coloured in red, the residue closest to the N-terminal of the protein is coloured in blue, the phosphate binding loop is coloured green, and the phosphopeptide ligands are purple.
