These authors contributed equally to this work.
Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase
Version of Record online: 31 OCT 2013
© 2013 International Society for Neurochemistry
Journal of Neurochemistry
Volume 128, Issue 2, pages 315–329, January 2014
How to Cite
J. Neurochem. (2014) 128, 315–329.
- Issue online: 6 JAN 2014
- Version of Record online: 31 OCT 2013
- Accepted manuscript online: 30 SEP 2013 09:18AM EST
- Manuscript Accepted: 23 SEP 2013
- Manuscript Revised: 20 SEP 2013
- Manuscript Received: 27 MAY 2013
- National Key Basic Research Program of China. Grant Numbers: 2013CB967700, 2012CB910402
- National Natural Science Foundation of China. Grant Numbers: 81171062, 31100580, 31271505, 31000362, 31270857, 81100836
- Foundation of Program for New Century Excellent Talents in University, China. Grant Number: NCET-09-0531
- Foundation for Excellent Young and Middle-Aged Scientists of Shandong Province, China. Grant Number: BS2011SW020
- Independence Innovation Foundation of Shandong University. Grant Number: 2012TS114
- National Institutes of Health. Grant Numbers: HL095556, HL108922
Vol. 134, Issue 5, 978, Version of Record online: 14 JUL 2015
|jnc12463-sup-0001-FigS1_Methods.pdf||application/PDF||100K||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.|
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