PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21866214-5	2011	RESULTS: Sequencing of the coding regions of CRYGD showed the presence of a heterozygous A G transversion at c.401 position, which results in the substitution of a tyrosine to a cysteine (Y134C).	Cysteine	178-186	crystallin gamma D	Homo sapiens	45-50	
30251679-0	2018	Reactive cysteine residues in the oxidative dimerization and Cu2+ induced aggregation of human gammaD-crystallin: Implications for age-related cataract.	Cysteine	9-17	crystallin gamma D	Homo sapiens	95-112	
30251679-3	2018	Here we determined which Cys residues are involved in disulfide-mediated crosslinking of recombinant human gammaD-crystallin (hgammaD).	Cysteine	25-28	crystallin gamma D	Homo sapiens	107-134	
18618005-6	2008	RESULTS: Sequencing of the coding regions of CRYGC and CRYGD showed the presence of a heterozygous C>A transversion at c.327 of the coding sequence in exon 3 of CRYGC (c.327C>A), which results in the substitution of a wild type cysteine to a nonsense codon (C109X).	Cysteine	234-242	crystallin gamma D	Homo sapiens	55-60	
34537240-0	2021	Surface exposed free cysteine suppresses crystallization of human gammaD-crystallin.	Cysteine	21-29	crystallin gamma D	Homo sapiens	66-83	
35549281-4	2022	Here, we use single-molecule spectroscopy AFM and molecular dynamics simulations to capture both intra- and intermolecular disulfide bonds in gammaD-crystallin, a cysteine-rich, structural human lens protein involved in age-related eye cataracts.	Cysteine	163-171	crystallin gamma D	Homo sapiens	142-159