PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34203497-0	2021	Molecular Insight into the Regulation of Vimentin by Cysteine Modifications and Zinc Binding.	Cysteine	53-61	vimentin	Homo sapiens	41-49	
34203497-2	2021	The vimentin network undergoes marked reorganizations in response to oxidative stress, in which modifications of vimentin single cysteine residue, Cys328, play an important role, and is modulated by zinc availability.	Cysteine	129-137	vimentin	Homo sapiens	4-12	
34203497-2	2021	The vimentin network undergoes marked reorganizations in response to oxidative stress, in which modifications of vimentin single cysteine residue, Cys328, play an important role, and is modulated by zinc availability.	Cysteine	129-137	vimentin	Homo sapiens	113-121	
34203497-8	2021	Moreover, zinc selectively protects vimentin from crosslinking using short-spacer cysteine-reactive but not amine-reactive agents.	Cysteine	82-90	vimentin	Homo sapiens	36-44	
34203497-12	2021	Moreover, they provide a molecular standpoint for vimentin regulation through the interplay between cysteine modifications and zinc availability.	Cysteine	100-108	vimentin	Homo sapiens	50-58