PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26439457-0	2015	Cysteine as a Monothiol Reducing Agent to Prevent Copper-Mediated Oxidation of Interferon Beta During PEGylation by CuAAC.	Cysteine	0-8	interferon beta 1	Homo sapiens	79-94	
8910760-3	1996	In the IFN-beta sequence, there are five potential N-glycosylation sites and four cysteine residues.	Cysteine	82-90	interferon beta 1	Homo sapiens	7-15	
12482656-3	2002	In the absence of the viral V protein cysteine-rich C-terminal domain, IFN-beta mRNA is strongly induced and the transcription factors NF-kappaB and IRF-3 are activated significantly.	Cysteine	38-46	interferon beta 1	Homo sapiens	71-79	
12482656-6	2002	Blocking of the induction of IFN-beta by dsRNA requires the C-terminal cysteine-rich domain, a feature that is highly conserved among paramyxoviruses.	Cysteine	71-79	interferon beta 1	Homo sapiens	29-37	
23962003-6	2013	Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity.	Cysteine	74-82	interferon beta 1	Homo sapiens	133-141	
23962003-6	2013	Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity.	Cysteine	74-82	interferon beta 1	Homo sapiens	224-232	
23962003-6	2013	Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity.	Cysteine	113-121	interferon beta 1	Homo sapiens	133-141	
23962003-6	2013	Here we use site-specific PEGylation technology (targeted attachment of a cysteine-reactive-PEG to an engineered cysteine residue in IFN-beta) to identify several additional amino acid positions where PEG can be attached to IFN-beta without appreciable loss of in vitro bioactivity.	Cysteine	113-121	interferon beta 1	Homo sapiens	224-232	
22404596-5	2012	Selective desulfurization followed by deprotection of the two Cys(Acm) residues gave the target full-length polypeptide chain of interferon-beta bearing either a complex-type sialyl biantennary oligosaccharide or its asialo form.	Cysteine	62-65	interferon beta 1	Homo sapiens	129-144	
21170271-5	2010	Cys-64, -148, -292, -309 and the potential C88xxC91 redox motif in MPYS are indispensable for IFNbeta stimulation and IRF3 activation.	Cysteine	0-3	interferon beta 1	Homo sapiens	94-101	
6091102-1	1984	Human fibroblast interferon has three cysteine residues, located at amino acid positions 17, 31, and 141.	Cysteine	38-46	interferon beta 1	Homo sapiens	6-27	
3220830-5	1988	Among the three cysteine residues in E. coli-derived human interferon-beta 1, the 17th cysteine was identified as being unpaired, as in the natural molecule.	Cysteine	16-24	interferon beta 1	Homo sapiens	59-76	
3220830-5	1988	Among the three cysteine residues in E. coli-derived human interferon-beta 1, the 17th cysteine was identified as being unpaired, as in the natural molecule.	Cysteine	87-95	interferon beta 1	Homo sapiens	59-76