PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20643143-4	2010	We present here a novel structure of human PrxV at 1.45 A resolution that has a dithiothreitol bound in the active site with its diol moiety mimicking the two oxygens of a peroxide substrate.	Dithiothreitol	80-94	peroxiredoxin 5	Homo sapiens	43-47	
1299627-1	1992	E. coli thioredoxin plus thioredoxin reductase have previously been shown to replace dithiothreitol as the electron donor for mammalian liver microsomal vitamin K epoxide reduction in vitro.	Dithiothreitol	85-99	peroxiredoxin 5	Homo sapiens	25-46	
8664271-16	1996	Reduction of C135S-C32S with dithiothreitol (DTT) results in a decrease of epsilon454 to a value similar to that of TrR C135S, and subsequent NH4Cl titration leads to charge transfer complex formation in the nascent TrR C135S.	Dithiothreitol	29-43	peroxiredoxin 5	Homo sapiens	116-119	
8664271-16	1996	Reduction of C135S-C32S with dithiothreitol (DTT) results in a decrease of epsilon454 to a value similar to that of TrR C135S, and subsequent NH4Cl titration leads to charge transfer complex formation in the nascent TrR C135S.	Dithiothreitol	29-43	peroxiredoxin 5	Homo sapiens	216-219	
8664271-16	1996	Reduction of C135S-C32S with dithiothreitol (DTT) results in a decrease of epsilon454 to a value similar to that of TrR C135S, and subsequent NH4Cl titration leads to charge transfer complex formation in the nascent TrR C135S.	Dithiothreitol	45-48	peroxiredoxin 5	Homo sapiens	116-119	
8664271-16	1996	Reduction of C135S-C32S with dithiothreitol (DTT) results in a decrease of epsilon454 to a value similar to that of TrR C135S, and subsequent NH4Cl titration leads to charge transfer complex formation in the nascent TrR C135S.	Dithiothreitol	45-48	peroxiredoxin 5	Homo sapiens	216-219	
35266940-3	2022	Detailed spectroscopic and kinetic studies in an aqueous medium revealed significantly higher reactivity of the probes towards DTT (for TrxR activity) over the well-known cellular abundant biothiol GSH.	Dithiothreitol	127-130	peroxiredoxin 5	Homo sapiens	136-140	
24844612-2	2014	Basically, the alpha,beta-unsaturated ketone moiety in the probe structure could quench the fluorescence of the coumarin, but upon the covalent modification of TrxR, a significant fluorescence could be generated, which has been confirmed to be obviously selective over Trx, GSH, Cys and DTT.	Dithiothreitol	287-290	peroxiredoxin 5	Homo sapiens	160-164	
23751615-6	2013	A bench-scale model using a thioredoxin/thioredoxin reductase regeneration system revealed that reduction susceptibility depended on not only antibody class but also light chain type; the model further demonstrates that the trend in reducibility was identical to DTT reduction sensitivity following the order IgG1lambda > IgG1kappa > IgG2lambda > IgG2kappa.	Dithiothreitol	263-266	peroxiredoxin 5	Homo sapiens	40-61	
31375973-6	2019	By employing an in vitro CoAlation assay, we showed that Prdx5 peroxidase activity is inhibited by covalent interaction with CoA in a dithiothreitol-sensitive manner.	Dithiothreitol	134-148	peroxiredoxin 5	Homo sapiens	57-62