PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6094532-8	1984	The C3 alpha chain contains 24 cysteine residues, 10 of these clustered in the C-terminal 175 amino acids of the alpha chain.	Cysteine	31-39	complement C3	Homo sapiens	4-12	
8387092-3	1993	Alkylation of C3b-free cysteine abolished formation of these complexes and only a noncovalent binding of C3b to CR1 was observed, which could be inhibited by mAb to CR1.	Cysteine	23-31	complement C3	Homo sapiens	14-17	
8387092-5	1993	These observations correspond to a novel capacity of C3b to interact covalently through its cysteine 1010 with free SH groups of protein acceptors.	Cysteine	92-100	complement C3	Homo sapiens	53-56	
6872338-2	1983	The dithiothreitol eluate contained C3b fragments which had been labeled covalently by the radioactive cysteine.	Cysteine	103-111	complement C3	Homo sapiens	36-39	
6872338-3	1983	Labeling was postulated to involve the reaction of the amino group of the cysteine with the "labile site," an acylating group which is exposed when C3 is converted to C3b during the operation of the alternative complement-fixing pathway.	Cysteine	74-82	complement C3	Homo sapiens	167-170	
6167582-6	1981	The proposed sequence is: (formula, see text) Manual alignment of the linear structures of human C3a, C4a, and C5a, based primarily on the location of two Cys-Cys sequences in each indicate a 30% homology between C3a and C4a and a 36% homology between C5a and C4a.	Cysteine	155-158	complement C3	Homo sapiens	97-100	
6167582-6	1981	The proposed sequence is: (formula, see text) Manual alignment of the linear structures of human C3a, C4a, and C5a, based primarily on the location of two Cys-Cys sequences in each indicate a 30% homology between C3a and C4a and a 36% homology between C5a and C4a.	Cysteine	155-158	complement C3	Homo sapiens	213-216	
6167582-6	1981	The proposed sequence is: (formula, see text) Manual alignment of the linear structures of human C3a, C4a, and C5a, based primarily on the location of two Cys-Cys sequences in each indicate a 30% homology between C3a and C4a and a 36% homology between C5a and C4a.	Cysteine	159-162	complement C3	Homo sapiens	97-100	
6167582-6	1981	The proposed sequence is: (formula, see text) Manual alignment of the linear structures of human C3a, C4a, and C5a, based primarily on the location of two Cys-Cys sequences in each indicate a 30% homology between C3a and C4a and a 36% homology between C5a and C4a.	Cysteine	159-162	complement C3	Homo sapiens	213-216	
976263-4	1976	The reactivity of a cysteine located on the active site was quite different, showing increasing alkylation when the alkylating substituent of the affinity labels was shifted from C-3 to C-16 of the steroid nucleus.	Cysteine	20-28	complement C3	Homo sapiens	179-182	
32878894-5	2020	Furthermore, analysis of various N-linked glycosylation site and cysteine mutants in gp85 revealed that glycosylation sites (N6 and N11) and cysteines (C3 and C9) were directly involved in receptor-gp85 binding and important for the entry of ALV-J into cells.	Cysteine	65-73	complement C3	Homo sapiens	152-161	
32878894-5	2020	Furthermore, analysis of various N-linked glycosylation site and cysteine mutants in gp85 revealed that glycosylation sites (N6 and N11) and cysteines (C3 and C9) were directly involved in receptor-gp85 binding and important for the entry of ALV-J into cells.	Cysteine	141-150	complement C3	Homo sapiens	152-161	
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Cysteine	126-129	complement C3	Homo sapiens	62-65	
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Cysteine	134-137	complement C3	Homo sapiens	62-65	
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Cysteine	200-209	complement C3	Homo sapiens	62-65	
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Cysteine	134-137	complement C3	Homo sapiens	62-65	
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Cysteine	134-137	complement C3	Homo sapiens	62-65	
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Cysteine	134-137	complement C3	Homo sapiens	62-65	
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Cysteine	134-137	complement C3	Homo sapiens	62-65	
11032742-8	2000	Using a human thioredoxin in which the structural cysteines were mutated to alanine, Trx-C3A, we show that structural cysteines that do not take part in the catalytic functions of the protein are also important for its reactive oxygen scavenging properties.	Cysteine	118-127	complement C3	Homo sapiens	89-92	
10733916-7	2000	Isoelectric focusing of tryptic peptides from autoacylated wild type, His(6)-tagged, and C3A mutant of G(salpha) showed that Cys 160 is the site of in vitro palmitoylation.	Cysteine	125-128	complement C3	Homo sapiens	89-92	
690134-13	1978	Two repeating Cys sequences occur in the linear structure and 6 of the 7 half-cystines in C5a are located at nearly identical positions to those in the human C3a molecule.	Cysteine	14-17	complement C3	Homo sapiens	158-161	
786982-3	1976	The two samples of cysteine formed in this reaction were analyzed for their configuration at C-3.	Cysteine	19-27	complement C3	Homo sapiens	93-96	
10400348-10	1999	The inactivation process is enhanced in the presence of cofactor Mg2+ ions and Cys-361 appears to serve as a base for the removal of the C-3 proton from the natural substrate, (2S,3S)-3-methylaspartic acid.	Cysteine	79-82	complement C3	Homo sapiens	137-140