PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8676895-3	1996	Peptide mapping of the epitopes recognized by these Fab indicated that three of the anti-Tat Fab were directed to the functional domain between amino acid residues 22-33 of the Tat molecule, and that binding was inhibited by reduction of this cysteine-rich region with dithiothreitol.	Dithiothreitol	269-283	FA complementation group B	Homo sapiens	93-96	
9135700-6	1997	The Fd fragment (or fragment containing Fd) was prepared from Fab(kappa) by DTT reduction followed by Protein L column.	Dithiothreitol	76-79	FA complementation group B	Homo sapiens	62-65	
11798873-2	2001	METHODS: Monoclonal antibody Fab" fragment was obtained by enzymolysis with pepsin and DTT reduction.	Dithiothreitol	87-90	FA complementation group B	Homo sapiens	29-32	
10780482-1	1999	Crystal structures of the 64M-2 antibody Fab fragment complexed with DNA photoproducts of dT(6-4)T and dTT(6-4)TT, and of the 64M-3 Fab fragment complexed with dT(6-4)T were determined.	Dithiothreitol	103-106	FA complementation group B	Homo sapiens	41-44	
10780482-8	1999	In the 64M-2 Fab complex with dTT(6-4)TT, 5"- and 3"-side phosphate groups are also involved in interaction with Fab residues.	Dithiothreitol	30-33	FA complementation group B	Homo sapiens	13-16	
10780482-8	1999	In the 64M-2 Fab complex with dTT(6-4)TT, 5"- and 3"-side phosphate groups are also involved in interaction with Fab residues.	Dithiothreitol	30-33	FA complementation group B	Homo sapiens	113-116	
9246561-4	1997	When Fab(kappa) was reduced with dithiothreitol (DTT), the Fd fragment in the UF could be separated from the free kappa-chain and the unreduced Fab(kappa) in the BF with a Protein L-Sepharose column.	Dithiothreitol	33-47	FA complementation group B	Homo sapiens	5-8	
9246561-4	1997	When Fab(kappa) was reduced with dithiothreitol (DTT), the Fd fragment in the UF could be separated from the free kappa-chain and the unreduced Fab(kappa) in the BF with a Protein L-Sepharose column.	Dithiothreitol	49-52	FA complementation group B	Homo sapiens	5-8	
9246561-4	1997	When Fab(kappa) was reduced with dithiothreitol (DTT), the Fd fragment in the UF could be separated from the free kappa-chain and the unreduced Fab(kappa) in the BF with a Protein L-Sepharose column.	Dithiothreitol	49-52	FA complementation group B	Homo sapiens	144-147	
8676895-3	1996	Peptide mapping of the epitopes recognized by these Fab indicated that three of the anti-Tat Fab were directed to the functional domain between amino acid residues 22-33 of the Tat molecule, and that binding was inhibited by reduction of this cysteine-rich region with dithiothreitol.	Dithiothreitol	269-283	FA complementation group B	Homo sapiens	52-55	
1875954-5	1991	Fab/c made by cyanylysis of sulfite-reduced IgG was also active in these assays, but Fab/c made by cyanylysis of dithiothreitol-reduced IgG was not.	Dithiothreitol	113-127	FA complementation group B	Homo sapiens	0-3	
22349224-0	2012	Structure of the DNA (6-4) photoproduct dTT(6-4)TT in complex with the 64M-2 antibody Fab fragment implies increased antibody-binding affinity by the flanking nucleotides.	Dithiothreitol	40-43	FA complementation group B	Homo sapiens	86-89	
22349224-2	2012	The crystal structure of the dTT(6-4)TT photoproduct in complex with the Fab fragment of the antibody 64M-2 that is specific for (6-4) photoproducts was determined at 2.4 A resolution.	Dithiothreitol	29-32	FA complementation group B	Homo sapiens	73-76