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Effective Dephosphorylation of Src Substrates by SHP-1
Carsten Frank
, Carmen Burkhardt
, Diana Imhof
, Jens Ringel
, Olaf Zschörnig
, Karin Wieligmann
,
Martin Zacharias
, Frank D. Böhmer
Friedrich Schiller University Jena
Medical University of Vienna
Altana Pharma AG
University of Leipzig
Fritz Lipmann Institute
Jacobs University Bremen
Research output
:
Contribution to journal
›
Article
›
peer-review
82
Scopus citations
Overview
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Neuroscience
Dephosphorylation
100%
Phosphopeptide
75%
Phosphotyrosine
75%
C-Terminus
50%
In Vitro
50%
Phosphoprotein
50%
Enzyme Active Site
50%
Signal Transduction Pathway
25%
Amino Terminal Sequence
25%
Enzyme Specificity
25%
SH2 Domain
25%
Catenin
25%
Chimeric Protein
25%
Protein Tyrosine Phosphatase SHP 1
25%
Molecular Model
25%
Biochemistry, Genetics and Molecular Biology
Dephosphorylation
100%
Phosphopeptide
75%
C-Terminus
50%
Enzyme Active Site
50%
Phosphoprotein
50%
Signal Transduction
25%
N-Terminus
25%
Substrate Interaction
25%
SH2 Domain
25%
Molecular Model
25%
Enzyme Specificity
25%
Catenin
25%
Protein Tyrosine Phosphatase
25%
Chimeric Protein
25%
Keyphrases
Dephosphorylation
100%
SHP-1
100%
Phosphotyrosine
15%
Phosphopeptides
15%
Phosphorylation
10%
Phosphoprotein
10%
Phosphorylation Sites
10%
Substrate Selectivity
10%
Catalytic Domain
10%
HEK293 Cells
5%
Protein Tyrosine Phosphatase 1B (PTP1B)
5%
Molecular Modeling
5%
Multiple Signals
5%
Substrate Interaction
5%
Recombinant
5%
Intact Cells
5%
C-terminus
5%
Fusion Protein
5%
Negative Regulator
5%
Substrate Specificity
5%
Signal Transduction Pathway
5%
Pullout
5%
SH2 Domain
5%
Biochemical Data
5%
P120-catenin
5%
Src Phosphorylation
5%
Complementary Substrate
5%