𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B

✍ Scribed by Tiago A.S. Brandão; Sean J. Johnson; Alvan C. Hengge

Book ID
116179052
Publisher
Elsevier Science
Year
2012
Tongue
English
Weight
577 KB
Volume
525
Category
Article
ISSN
0003-9861

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Relation between the flexibility of the
Relation between the flexibility of the WPD loop and the activity of the catalytic domain of protein tyrosine phosphatase SHP-1
✍ Jian Yang; Tianqi Niu; Aihua Zhang; Ashwini K. Mishra; Zhizhuang Joe Zhao; G. Wa 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 365 KB 👁 1 views

## Abstract The conserved WPD loop of protein tyrosine phosphatases play an important role in the catalytic activity and the invariant aspartate residue acts as a general acid/base catalyst in the dephosphorylation reaction. In our previous report, we have demonstrated that the catalytic activities

Involvement of the small protein tyrosin
Involvement of the small protein tyrosine phosphatases TC-PTP and PTP1B in signal transduction and diseases: From diabetes, obesity to cell cycle, and cancer
✍ Nadia Dubé; Michel L. Tremblay 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 201 KB

As in other fields of biomedical research, the use of gene-targeted mice by homologous recombination in embryonic stem cells has provided important findings on the function of several members of the protein tyrosine phosphatase (PTP) family. For instance, the phenotypic characterization of knockout