PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20361855-7	2010	Reversible oxidation of thiols in serine threonine protein phosphatase PP2A and in protein tyrosin phosphatases SHP1, SHP2 and CD45 leads to their inactivation generally by formation of intramolecular disulfides.	Disulfides	201-211	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	118-122	
29214238-10	2017	The structure shows that the catalytic Cys459 residue forms a disulfide bond with Cys367, which confirms that Cys367 functions as the "backdoor" cysteine in SHP2.	Disulfides	62-71	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	157-161	
34674683-9	2021	The N-SH2 domain of SHP-2 as a protein chaperone may be potentially favorable to produce other proteins with disulfide bonds.	Disulfides	109-118	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	20-25	
22411627-3	2012	Using complementary approaches, we provide evidence here that endogenous SHP-2 can dimerize through the formation of disulfide bonds that may also involve the catalytic cysteine.	Disulfides	117-126	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	73-78