Associated Papers
The pathogenic E139D mutation stabilizes a non-canonical active state of the multi-domain phosphatase SHP2.
van Vlimmeren AE et al.
Protein Science : a Publication of the Protein Society, 2025
The pathogenic E139D mutation stabilizes a non-canonical active state of the multi-domain phosphatase SHP2.
van Vlimmeren AE et al.
Biorxiv : the Preprint Server for Biology, 2025
JAK2V617F-dependent down regulation of SHP-1 expression participates in the selection of myeloproliferative neoplasm cells in the presence of TGF-β.
Aoun C et al.
Journal of Cellular and Molecular Medicine, 2024
Regulation of PPARγ2 Stability and Activity by SHP-1.
Kumar A et al.
Molecular and Cellular Biology, 2024
SHP-1 phosphatase acts as a coactivator of PCK1 transcription to control gluconeogenesis.
Kumar A et al.
The Journal of Biological Chemistry, 2023
SHP-1 dephosphorylates histone H2B to facilitate its ubiquitination during transcription.
Tathe P et al.
The Embo Journal, 2022
Protein tyrosine phosphatases in skeletal development and diseases.
Yang H et al.
Bone Research, 2022
A specific amino acid context in EGFR and HER2 phosphorylation sites enables selective binding to the active site of Src homology phosphatase 2 (SHP2).
Hartman Z et al.
The Journal of Biological Chemistry, 2020
Moesin and myosin IIA modulate phagolysosomal biogenesis in macrophages.
Gomez CP et al.
Biochemical and Biophysical Research Communications, 2018
Discovery of novel Src homology region 2 domain-containing phosphatase 1 agonists from sorafenib for the treatment of hepatocellular carcinoma.
Tai WT et al.
Hepatology (baltimore, Md.), 2014
Regulation of hERG and hEAG channels by Src and by SHP-1 tyrosine phosphatase via an ITIM region in the cyclic nucleotide binding domain.
Schlichter LC et al.
Plos One, 2014
SHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound states.
Alicea-Velazquez NL et al.
Protein and Peptide Letters, 2013
Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition.
Alicea-Velázquez NL et al.
Journal of Structural Biology, 2013
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation.
Wang W et al.
Journal of Cellular Biochemistry, 2011
SHP-1 inhibits β-catenin function by inducing its degradation and interfering with its association with TATA-binding protein.
Simoneau M et al.
Cellular Signalling, 2011
Protein tyrosine phosphatase SHP-1 positively regulates TLR-induced IL-12p40 production in macrophages through inhibition of phosphatidylinositol 3-kinase.
Zhou D et al.
Journal of Leukocyte Biology, 2010
The SHP-1 protein tyrosine phosphatase negatively modulates glucose homeostasis.
Dubois MJ et al.
Nature Medicine, 2006
Shp-1 mediates the antiproliferative activity of tissue inhibitor of metalloproteinase-2 in human microvascular endothelial cells.
Seo DW et al.
The Journal of Biological Chemistry, 2006
The membrane-proximal immunoreceptor tyrosine-based inhibitory motif is critical for the inhibitory signaling mediated by Siglecs-7 and -9, CD33-related Siglecs expressed on human monocytes and NK cells.
Avril T et al.
Journal of Immunology (baltimore, Md. : 1950), 2004
KIR2DL5 can inhibit human NK cell activation via recruitment of Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2).
Yusa S et al.
Journal of Immunology (baltimore, Md. : 1950), 2004
The protein-tyrosine phosphatase SHP-1 regulates the phosphorylation of alpha-actinin.
Lin SY et al.
The Journal of Biological Chemistry, 2004
Src family protein-tyrosine kinases alter the function of PTEN to regulate phosphatidylinositol 3-kinase/AKT cascades.
Lu Y et al.
The Journal of Biological Chemistry, 2003
Role of the protein tyrosine phosphatase SHP-1 (Src homology phosphatase-1) in the regulation of interleukin-3-induced survival, proliferation and signalling.
Paling NR et al.
The Biochemical Journal, 2002
SHP-1- and phosphotyrosine-independent inhibitory signaling by a killer cell Ig-like receptor cytoplasmic domain in human NK cells.
Yusa S et al.
Journal of Immunology (baltimore, Md. : 1950), 2002
Molecular cloning of MIS, a myeloid inhibitory siglec, that binds protein-tyrosine phosphatases SHP-1 and SHP-2.
Ulyanova T et al.
The Journal of Biological Chemistry, 2001
Impaired natural killing of MHC class I-deficient targets by NK cells expressing a catalytically inactive form of SHP-1.
Lowin-Kropf B et al.
Journal of Immunology (baltimore, Md. : 1950), 2000
Src homology region 2 (SH2) domain-containing phosphatase-1 dephosphorylates B cell linker protein/SH2 domain leukocyte protein of 65 kDa and selectively regulates c-Jun NH2-terminal kinase activation in B cells.
Mizuno K et al.
Journal of Immunology (baltimore, Md. : 1950), 2000
Positive regulation of c-Jun N-terminal kinase and TNF-alpha production but not histamine release by SHP-1 in RBL-2H3 mast cells.
Xie ZH et al.
Journal of Immunology (baltimore, Md. : 1950), 2000
The sialoadhesin CD33 is a myeloid-specific inhibitory receptor.
Ulyanova T et al.
European Journal of Immunology, 1999
Murine SHP-1 splice variants with altered Src homology 2 (SH2) domains. Implications for the SH2-mediated intramolecular regulation of SHP-1.
Martin A et al.
The Journal of Biological Chemistry, 1999
Expression of dominant-negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation.
Dustin LB et al.
Journal of Immunology (baltimore, Md. : 1950), 1999
Specificity of the SH2 domains of SHP-1 in the interaction with the immunoreceptor tyrosine-based inhibitory motif-bearing receptor gp49B.
Wang LL et al.
Journal of Immunology (baltimore, Md. : 1950), 1999
Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22.
Blasioli J et al.
The Journal of Biological Chemistry, 1999
The major SHP-1-binding, tyrosine-phosphorylated protein in macrophages is a member of the KIR/LIR family and an SHP-1 substrate.
Berg KL et al.
Oncogene, 1998
Recruitment and activation of SHP-1 protein-tyrosine phosphatase by human platelet endothelial cell adhesion molecule-1 (PECAM-1). Identification of immunoreceptor tyrosine-based inhibitory motif-like binding motifs and substrates.
Hua CT et al.
The Journal of Biological Chemistry, 1998
Regulation of mouse PECAM-1 tyrosine phosphorylation by the Src and Csk families of protein-tyrosine kinases.
Cao MY et al.
The Journal of Biological Chemistry, 1998
Characterization of SHP-1 protein tyrosine phosphatase transcripts, protein isoforms and phosphatase activity in epithelial cancer cells.
Evren S et al.
Genomics, 0