PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11815609-4	2002	In addition, Tyr-103, Cys-161, Cys-210, and Cys-211, previously identified to contribute to binding IL-2 and IL-7, were also found to be involved in binding IL-4 and IL-15.	Cysteine	22-25	interleukin 2	Mus musculus	100-104	
11815609-4	2002	In addition, Tyr-103, Cys-161, Cys-210, and Cys-211, previously identified to contribute to binding IL-2 and IL-7, were also found to be involved in binding IL-4 and IL-15.	Cysteine	31-34	interleukin 2	Mus musculus	100-104	
11815609-4	2002	In addition, Tyr-103, Cys-161, Cys-210, and Cys-211, previously identified to contribute to binding IL-2 and IL-7, were also found to be involved in binding IL-4 and IL-15.	Cysteine	31-34	interleukin 2	Mus musculus	100-104	
12541508-5	2000	IL-2 has one disulphide bridge (between 58th Cys and 105th Cys) and one free cysteine.	Cysteine	45-48	interleukin 2	Mus musculus	0-4	
12541508-5	2000	IL-2 has one disulphide bridge (between 58th Cys and 105th Cys) and one free cysteine.	Cysteine	59-62	interleukin 2	Mus musculus	0-4	
12541508-5	2000	IL-2 has one disulphide bridge (between 58th Cys and 105th Cys) and one free cysteine.	Cysteine	77-85	interleukin 2	Mus musculus	0-4	
8128610-8	1994	Three Cys residues are conserved in all compared mature IL-2 molecules.	Cysteine	6-9	interleukin 2	Mus musculus	56-60	
9028557-8	1997	Administration of CY 200 mg/kg + GCSF, the most potent regimen for CFC mobilization, led to a marked decrease in proportion of CD3+ cells in day 6 PBSC as compared to controls (17.7% vs 3.9%) and was associated with a significant decrease in generation of cytotoxic cells after IL-2 activation.	Cysteine	18-20	interleukin 2	Mus musculus	278-282	
9028557-10	1997	When IL-2 was combined with CY without G-CSF, the number of CFC mobilized was comparable to that seen with CY + G-CSF and these CY + IL-2 mobilized PBSC generated potent cytotoxic effectors after in vitro IL-2 activation.	Cysteine	28-30	interleukin 2	Mus musculus	133-137	
9028557-10	1997	When IL-2 was combined with CY without G-CSF, the number of CFC mobilized was comparable to that seen with CY + G-CSF and these CY + IL-2 mobilized PBSC generated potent cytotoxic effectors after in vitro IL-2 activation.	Cysteine	28-30	interleukin 2	Mus musculus	133-137	
7591713-3	1995	Thus cysteine, by enhancing GSH production, is able to affect some T-cell functions like IL-2 dependent cell proliferation and the generation of cytotoxic T cells.	Cysteine	5-13	interleukin 2	Mus musculus	89-93	
10464704-7	1999	These results demonstrated that the IL-2 gene modified vaccine could exert more potent anti-metastases effects when it is combined with IL-1 or/and low-dose Cy by activating the specific and non-specific antitumor immune responses more effectively.	Cysteine	157-159	interleukin 2	Mus musculus	36-40	
1445335-0	1992	Analysis of IL-2 functional structure by multiple cysteine substitutions.	Cysteine	50-58	interleukin 2	Mus musculus	12-16	
1445335-1	1992	IL-2 has three cysteine residues.	Cysteine	15-23	interleukin 2	Mus musculus	0-4	
1445335-2	1992	The cysteines at positions 58 and 105 of active IL-2 form an intramolecular disulfide bond while that at position 125 remains as a free form.	Cysteine	4-13	interleukin 2	Mus musculus	48-52	
3259620-11	1988	The combination treatment of IL2 and LAK cells with CY caused additional tumor growth suppression in a manner dependent on the total number of LAK cells transferred.	Cysteine	52-54	interleukin 2	Mus musculus	29-32	
1419069-2	1992	As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2.	Cysteine	20-23	interleukin 2	Mus musculus	38-51	
1419069-2	1992	As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2.	Cysteine	20-23	interleukin 2	Mus musculus	53-57	
1419069-2	1992	As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2.	Cysteine	20-23	interleukin 2	Mus musculus	209-213	
1419069-2	1992	As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2.	Cysteine	20-23	interleukin 2	Mus musculus	209-213	
2832473-8	1988	In contrast, modification of any of the other 10 Cys residues, either singly or in combinations corresponding to the predicted disulfide bonds, greatly reduced the ability of the corresponding protein to bind IL-2 or either of two mAb (anti-Tac and 7G7/B6) which recognize the Tac protein.	Cysteine	49-52	interleukin 2	Mus musculus	209-213	
3286824-6	1988	The combination of IL-2 and CY at 75 or 100 mg/kg, however, dramatically reduced the mortality induced by IL-2 and made it possible to escalate the dose and long-term administration of IL-2.	Cysteine	28-30	interleukin 2	Mus musculus	106-110	
3286824-6	1988	The combination of IL-2 and CY at 75 or 100 mg/kg, however, dramatically reduced the mortality induced by IL-2 and made it possible to escalate the dose and long-term administration of IL-2.	Cysteine	28-30	interleukin 2	Mus musculus	106-110