PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26058329-2	2015	N-Substituted conjugates of cyclam and cyclen with bioisosteric phosphonate groups displayed good activities toward T-cell protein tyrosine phosphatase with IC50 values in the micromolar to nanomolar range and showed selectivity over PTP1B, CD45, SHP2, and PTPbeta.	Nitrogen	0-1	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	247-251	
31936901-5	2020	Here, we present a quantitative characterization of the effect of the T42A mutation on the binding of the N-terminal SH2 domain of SHP2 with a peptide mimicking Gab2, a fundamental interaction that triggers the activation of the phosphatase in the cellular environment.	Nitrogen	106-107	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	131-135	
34025932-7	2021	We demonstrate that this allosteric network exists only in N-SH2, which is directly involved in the regulation of SHP2 activity, while the C-terminal SH2 domain (C-SH2) functions primarily to recruit high-affinity bidentate phosphopeptides.	Nitrogen	59-60	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	114-118	
31356638-0	2019	Endocytosis of flavivirus NS1 is required for NS1-mediated endothelial hyperpermeability and is abolished by a single N-glycosylation site mutation.	Nitrogen	26-27	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	46-49	
30773397-4	2019	Furthermore, individual SH2 domains of SHP-2 strongly engage with the unphosphorylated N-ITIM of 3DL1-cyto, while binding of the tandem SHP-2 SH2 domains to the bis-phosphorylated ITIMs results in more extensive conformational changes in segments I and III.	Nitrogen	87-88	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	39-44