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81100836 to Dr T.X), the Foundation of Program for New Century
Excellent Talents in University, China (NCET-09-0531 to X.Y.),
Foundation for Excellent Young and Middle-Aged Scientists of
Shandong Province, China (BS2011SW020 to Dr JP.S), the
Independence Innovation Foundation of Shandong University
(2012TS114 to Dr JP.S) and the grants from the National Institutes
of Health (HL095556 and HL108922 to Y.H). The authors declare
no conflict of interest.
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Supporting information
Liu J., Chen M., Li R. et al. (2012a) Biochemical and functional studies
of lymphoid-specific tyrosine phosphatase (Lyp) variants S201F
and R266W. PLoS ONE 7, e43631.
Liu J. J., Horst R., Katritch V., Stevens R. C. and Wuthrich K. (2012b)
Biased signaling pathways in beta2-adrenergic receptor
characterized by 19F-NMR. Science 335, 1106–1110.
Luechapanichkul R., Chen X., Taha H. A., Vyas S., Guan X., Freitas M.
A., Hadad C. M. and Pei D. (2013) Specificity profiling of
dual specificity phosphatase vaccinia VH1-related (VHR) reveals
two distinct substrate binding modes. J. Biol. Chem. 288, 6498–
6510.
Additional supporting information may be found in the online
version of this article at the publisher's web-site:
Figure S1. Bar graph and statistical analysis of the relative
catalytic activity of STEP active-site mutants for four different
substrates, pNPP, the phospho-peptides derived from phospho-
ERK2-pT202pY204 and pp-p38-pT 180pY182, and full-length
phospho-ERK protein, compared to wild-type STEP.
Morooka T. and Nishida E. (1998) Requirement of p38 mitogen-
activated protein kinase for neuronal differentiation in PC12 cells.
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