PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24477003-2	2014	VKOR and its homologues generate disulphide bonds in organisms ranging from bacteria to humans.	disulphide	33-43	vitamin K epoxide reductase complex subunit 1	Homo sapiens	0-4	
33466919-4	2021	Similarly, hVKORC1 is analysed in its native state, where two pairs of cysteine residues are covalently linked, forming two disulphide bridges, as a target for Trx-fold proteins.	disulphide	124-134	vitamin K epoxide reductase complex subunit 1	Homo sapiens	11-18	
33466919-6	2021	By probing the alternative orientation of PDI with respect to hVKORC1, the functionally related noncovalent complex formed by hVKORC1 and PDI was found, which is proposed to be a first precursor to probe thiol-disulphide exchange reactions between PDI and hVKORC1.	disulphide	210-220	vitamin K epoxide reductase complex subunit 1	Homo sapiens	62-69	
33466919-6	2021	By probing the alternative orientation of PDI with respect to hVKORC1, the functionally related noncovalent complex formed by hVKORC1 and PDI was found, which is proposed to be a first precursor to probe thiol-disulphide exchange reactions between PDI and hVKORC1.	disulphide	210-220	vitamin K epoxide reductase complex subunit 1	Homo sapiens	126-133	
33466919-6	2021	By probing the alternative orientation of PDI with respect to hVKORC1, the functionally related noncovalent complex formed by hVKORC1 and PDI was found, which is proposed to be a first precursor to probe thiol-disulphide exchange reactions between PDI and hVKORC1.	disulphide	210-220	vitamin K epoxide reductase complex subunit 1	Homo sapiens	126-133	
20110994-5	2010	We propose a pathway for how VKOR uses electrons from cysteines of newly synthesized proteins to reduce a quinone, a mechanism confirmed by in vitro reconstitution of vitamin K-dependent disulphide bridge formation.	disulphide	187-197	vitamin K epoxide reductase complex subunit 1	Homo sapiens	29-33