PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19382745-0	2009	The cataract-associated R14C mutant of human gamma D-crystallin shows a variety of intermolecular disulfide cross-links: a Raman spectroscopic study.	Disulfides	98-107	crystallin gamma D	Homo sapiens	45-63	
10688888-9	2000	We have expressed recombinant wild-type human gammaD crystallin (HGD) and its Arg-14 to Cys mutant (R14C) in Escherichia coli and show that R14C forms disulfide-linked oligomers, which markedly raise the phase separation temperature of the protein solution.	Disulfides	151-160	crystallin gamma D	Homo sapiens	46-63	
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.	Disulfides	123-132	crystallin gamma D	Homo sapiens	142-159	
30251679-3	2018	Here we determined which Cys residues are involved in disulfide-mediated crosslinking of recombinant human gammaD-crystallin (hgammaD).	Disulfides	54-63	crystallin gamma D	Homo sapiens	107-134