Related references
Note: Only part of the references are listed.The Differential Regulation of p38α by the Neuronal Kinase Interaction Motif Protein Tyrosine Phosphatases, a Detailed Molecular Study
Dana May Francis et al.
STRUCTURE (2013)
Docking Interactions of Hematopoietic Tyrosine Phosphatase with MAP Kinases ERK2 and p38α
Andrea Piserchio et al.
BIOCHEMISTRY (2012)
Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove
Agnes Garai et al.
SCIENCE SIGNALING (2012)
Resting and Active States of the ERK2:HePTP Complex
Dana M. Francis et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2011)
Structural basis of p38α regulation by hematopoietic tyrosine phosphatase
Dana M. Francis et al.
NATURE CHEMICAL BIOLOGY (2011)
A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38α with the MAPK Binding Domain of the Phosphatase MKP5
Yuan-Yuan Zhang et al.
SCIENCE SIGNALING (2011)
Mechanisms and functions of p38 MAPK signalling
Ana Cuadrado et al.
BIOCHEMICAL JOURNAL (2010)
Pathological roles of MAPK signaling pathways in human diseases
Eun Kyung Kim et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE (2010)
Dual-specificity phosphatases: critical regulators with diverse cellular targets
Kate I. Patterson et al.
BIOCHEMICAL JOURNAL (2009)
Interface Analysis of the Complex between ERK2 and PTP-SL
Mihaela C. Balasu et al.
PLOS ONE (2009)
Differential regulation and properties of MAPKs
M. Raman et al.
ONCOGENE (2007)
Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases
D. M. Owens et al.
ONCOGENE (2007)
Docking interactions induce exposure of activation loop in the MAP kinase ERK2
Tianjun Zhou et al.
STRUCTURE (2006)
PRIMUS:: a Windows PC-based system for small-angle scattering data analysis
PV Konarev et al.
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2003)
Uniqueness of ab initio shape determination in small-angle scattering
VV Volkov et al.
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2003)
Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38α is determined by a kinase specificity sequence and influenced by reducing agents
JJ Muñoz et al.
BIOCHEMICAL JOURNAL (2003)
Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b
CI Chang et al.
MOLECULAR CELL (2002)
Two clusters of residues at the docking groove of mitogen-activated protein kinases differentially mediate their functional interaction with the tyrosine phosphatases PTP-SL and STEP
C Tárrega et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Determination of domain structure of proteins from X-ray solution scattering
DI Svergun et al.
BIOPHYSICAL JOURNAL (2001)
Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: Structural insights into MKP-3 activation by ERK2
A Farooq et al.
MOLECULAR CELL (2001)