Associated Papers
Targeting PTPN22 at Nonorthosteric Binding SitesA Fragment Approach.
Di Lello P et al.
Acs Omega, 2026
Phosphatase PTPN22 functions as an adaptor in the mTORC2 complex.
Gupta K et al.
Embo Reports, 2025
Protein tyrosine phosphatase PTPN22 negatively modulates platelet function and thrombus formation.
Wang X et al.
Blood, 2022
Autoimmunity linked protein phosphatase PTPN22 as a target for cancer immunotherapy.
Cubas R et al.
Journal for Immunotherapy of Cancer, 2020
PTPN22 interacts with EB1 to regulate T-cell receptor signaling.
Zhang X et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2020
A molecular signature of preclinical rheumatoid arthritis triggered by dysregulated PTPN22.
Chang HH et al.
Jci Insight, 2016
Autoimmunity-associated protein tyrosine phosphatase PEP negatively regulates IFN-α receptor signaling.
Holmes DA et al.
The Journal of Experimental Medicine, 2015
Altered expression of protein tyrosine phosphatase, non-receptor type 22 isoforms in systemic lupus erythematosus.
Chang HH et al.
Arthritis Research & Therapy, 2014
Tyrosine phosphatase PTPN22: multifunctional regulator of immune signaling, development, and disease.
Bottini N et al.
Annual Review of Immunology, 2014
Autoimmunity-associated LYP-W620 does not impair thymic negative selection of autoreactive T cells.
Wu DJ et al.
Plos One, 2014
The autoimmunity-associated gene PTPN22 potentiates toll-like receptor-driven, type 1 interferon-dependent immunity.
Wang Y et al.
Immunity, 2013
Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate.
Yu X et al.
The Journal of Biological Chemistry, 2011
Distinct functional and conformational states of the human lymphoid tyrosine phosphatase catalytic domain can be targeted by choice of the inhibitor chemotype.
Vidović D et al.
Journal of Computer-aided Molecular Design, 2011
Autoimmune-associated PTPN22 R620W variation reduces phosphorylation of lymphoid phosphatase on an inhibitory tyrosine residue.
Fiorillo E et al.
The Journal of Biological Chemistry, 2010
A loss-of-function variant of PTPN22 is associated with reduced risk of systemic lupus erythematosus.
Orrú V et al.
Human Molecular Genetics, 2009
The lymphoid protein tyrosine phosphatase Lyp interacts with the adaptor molecule Grb2 and functions as a negative regulator of T-cell activation.
Hill RJ et al.
Experimental Hematology, 2002
Characterization of TCR-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP.
Gjörloff-Wingren A et al.
European Journal of Immunology, 1999
Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase.
Cloutier JF et al.
The Journal of Experimental Medicine, 1999