PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12149524-10	2002	CONCLUSIONS: Sputum processing with DTT significantly reduces the detectable concentration of TNFalpha, LTB(4) and MPO, and produces a small but significant increase in median alpha(1)-AT levels.	Dithiothreitol	36-39	serpin family A member 1	Homo sapiens	176-187	
2002060-10	1991	These changes are reversed by dithiothreitol and are consistent with a conformational change which transforms the inhibitory activity from a rapid, irreversible mode in native alpha 1-PI to a dissociable competitive mode in the mixed disulfide derivatives.	Dithiothreitol	30-44	serpin family A member 1	Homo sapiens	176-186	
9409285-3	1997	The synthesis of total apoB (apoB100 plus nascent chains), as well as a number of control proteins, such as albumin and alpha 1-antitrypsin, was decreased significantly in DTT-treated cells.	Dithiothreitol	172-175	serpin family A member 1	Homo sapiens	120-139	
8397210-8	1993	alpha 1-Antitrypsin contains no disulfide bonds; in the continuous presence of DTT it acquires a normal complement of complex oligosaccharides and is secreted at an only slightly reduced rate.	Dithiothreitol	79-82	serpin family A member 1	Homo sapiens	0-19	
1740441-11	1992	Exposure to dithiothreitol reduced albumin export while affecting alpha 1-antitrypsin export minimally.	Dithiothreitol	12-26	serpin family A member 1	Homo sapiens	66-85	
2787317-7	1989	The inactivated alpha 1-PI as the result of peroxidized lipid could be reactivated by dithiothreitol and methionine sulfoxide peptide reductase, suggesting oxidation of methionine residue at the elastase inhibitory site.	Dithiothreitol	86-100	serpin family A member 1	Homo sapiens	16-26	
6206967-1	1984	In this technique for determining the electrophoretic phenotype of alpha 1-antitrypsin in dried blood or serum specimens, the adsorbed material is eluted with a concentrated solution of dithiothreitol, focused on polyacrylamide thin-layer gel, and made visible with silver stain.	Dithiothreitol	186-200	serpin family A member 1	Homo sapiens	67-86	
2841359-3	1988	Cleavage of alpha 1-antitrypsin by cell supernatants was inhibited by EDTA, o-phenanthroline, and DTT, but not by inhibitors of serine or thiol proteinases.	Dithiothreitol	98-101	serpin family A member 1	Homo sapiens	12-31	
3488702-3	1986	Inactivation of alpha 1-PI is likely due to its oxidation by methylene blue, as suggested by the in vitro protective effect of dithiothreitol, a reducing agent.	Dithiothreitol	127-141	serpin family A member 1	Homo sapiens	16-26	
32087961-8	2020	Mechanistically, thiol reductant DTT treatment or C192S mutation prevented SO2-induced AAT1 sulfenylation and the subsequent inhibition of AAT activity in purified AAT1 protein and primary HUVECs.	Dithiothreitol	33-36	serpin family A member 1	Homo sapiens	87-90	
6981613-1	1982	The single disulfide bond of purified human alpha 1-protease inhibitor was reduced with dithiothreitol in the absence of denaturant and the resultant sulfhydryl groups were alkylated with iodoacetamide-1-C14.	Dithiothreitol	88-102	serpin family A member 1	Homo sapiens	44-70