PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33539638-1	2021	HLA-C*15:227 differs from HLA-C*15:02:01:01 by a single nonsynonymous change (368A   G Tyrosine 99 to Cysteine).	Cysteine	102-110	major histocompatibility complex, class I, C	Homo sapiens	0-5	
33539638-1	2021	HLA-C*15:227 differs from HLA-C*15:02:01:01 by a single nonsynonymous change (368A   G Tyrosine 99 to Cysteine).	Cysteine	102-110	major histocompatibility complex, class I, C	Homo sapiens	26-31	
15837811-5	2005	Cysteine-to-valine substitution at peptide position 9, while optimizing peptide binding to the MHC, repositions the peptide main chain and generates subtly enhanced interactions between the analogue peptide and the TCR.	Cysteine	0-8	major histocompatibility complex, class I, C	Homo sapiens	95-98	
32571843-0	2020	Impact of Cysteine Residues on MHC Binding Predictions and Recognition by Tumor-Reactive T Cells.	Cysteine	10-18	major histocompatibility complex, class I, C	Homo sapiens	31-34	
32571843-2	2020	Nevertheless, prediction algorithms appear to function poorly for epitopes containing cysteine (Cys) residues, which can oxidize and form disulfide bonds with other Cys residues under oxidizing conditions, thus potentially interfering with their ability to bind to MHC molecules.	Cysteine	86-94	major histocompatibility complex, class I, C	Homo sapiens	265-268	
32571843-2	2020	Nevertheless, prediction algorithms appear to function poorly for epitopes containing cysteine (Cys) residues, which can oxidize and form disulfide bonds with other Cys residues under oxidizing conditions, thus potentially interfering with their ability to bind to MHC molecules.	Cysteine	96-99	major histocompatibility complex, class I, C	Homo sapiens	265-268	
32571843-5	2020	Substitutions of AABA for Cys at putative MHC anchor positions often significantly enhanced T cell recognition, whereas substitutions at non-MHC anchor positions were neutral, except for one epitope where this modification abolished T cell recognition.	Cysteine	26-29	major histocompatibility complex, class I, C	Homo sapiens	42-45	
23849069-4	2013	HLA-C*03:190 was identical to HLA-C*03:02:01 with the exception of a nucleotide change at codon 131 in exon 3 (CGC TGC), and resulted in the amino acid change from Arginine to Cysteine.	Cysteine	176-184	major histocompatibility complex, class I, C	Homo sapiens	0-5	
23849069-4	2013	HLA-C*03:190 was identical to HLA-C*03:02:01 with the exception of a nucleotide change at codon 131 in exon 3 (CGC TGC), and resulted in the amino acid change from Arginine to Cysteine.	Cysteine	176-184	major histocompatibility complex, class I, C	Homo sapiens	30-35	
25135637-2	2014	We have established and interrogated a database of around 70,000 naturally processed MHC-bound peptides and demonstrate that cysteine-containing peptides are presented on the surface of cells in an MHC allomorph-dependent manner and comprise on average 5-10% of the immunopeptidome.	Cysteine	125-133	major histocompatibility complex, class I, C	Homo sapiens	85-88	
25135637-2	2014	We have established and interrogated a database of around 70,000 naturally processed MHC-bound peptides and demonstrate that cysteine-containing peptides are presented on the surface of cells in an MHC allomorph-dependent manner and comprise on average 5-10% of the immunopeptidome.	Cysteine	125-133	major histocompatibility complex, class I, C	Homo sapiens	198-201	
17187819-4	2007	We now report robust preparation of MHC tetramers with small molecule fluorophores, using a recombinant mutant of streptavidin incorporating a carboxy-terminal cysteine in each of the four identical subunits that is conjugated to maleimide derivatives of any of several small molecule fluorophores.	Cysteine	160-168	major histocompatibility complex, class I, C	Homo sapiens	36-39	
12074715-5	2002	The HLA Cw*0105 differs from Cw*0102 at positions 361 and 368 in exon 3 leading to a Trp to Arg and Cys to Ser substitution, respectively.	Cysteine	100-103	major histocompatibility complex, class I, C	Homo sapiens	4-10