Structual Basis of p38 alpha Regulation by Hematopoietic Tyrosine Phosphatase
Journal Article
·
· Nature Chemical Biology
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE SC OFFICE OF SCIENCE (SC)
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1069453
- Report Number(s):
- BNL-100025-2013-JA
- Journal Information:
- Nature Chemical Biology, Vol. 7, Issue 12; ISSN 1552--4450
- Country of Publication:
- United States
- Language:
- English
Similar Records
The Differential Regulation of p38 alpha by the Neuronal Kinase Interaction Motif Protein Tyrosine Phosphatases, a Detailed Molecular Study
Inhibition of Hematopoietic Protein Tyrosine Phosphatase Augments and Prolongs ERK1/2 and p38 Activation
Structural Basis for the Regulation of the MAP Kinase p38 alpha by the Dual Specificity Phosphatase 16 MAP Kinase Binding Domain in Solution
Journal Article
·
Tue Sep 03 00:00:00 EDT 2013
· Structure
·
OSTI ID:1069453
+3 more
Inhibition of Hematopoietic Protein Tyrosine Phosphatase Augments and Prolongs ERK1/2 and p38 Activation
Journal Article
·
Thu Nov 01 00:00:00 EDT 2012
· ACS Chemical Biology
·
OSTI ID:1069453
+6 more
Structural Basis for the Regulation of the MAP Kinase p38 alpha by the Dual Specificity Phosphatase 16 MAP Kinase Binding Domain in Solution
Journal Article
·
Fri Sep 27 00:00:00 EDT 2013
· Journal of Biological Chemistry
·
OSTI ID:1069453
+1 more