PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31513388-0	2019	Kinetic Studies on the Oxoiron(IV) Complex with Tetradentate Aminopyridine Ligand PDP*: Restoration of Catalytic Activity by Reduction with H2O2.	Hydrogen Peroxide	140-144	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	82-86	
34052343-1	2021	Our group has previously observed that protein S-glutathionylation serves as an integral feedback inhibitor for the production of superoxide (O2 -)/hydrogen peroxide (H2O2) by alpha-ketoglutarate dehydrogenase (KGDH), pyruvate dehydrogenase (PDH), and complex I in muscle and liver mitochondria, respectively.	Hydrogen Peroxide	148-165	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	218-240	
34052343-1	2021	Our group has previously observed that protein S-glutathionylation serves as an integral feedback inhibitor for the production of superoxide (O2 -)/hydrogen peroxide (H2O2) by alpha-ketoglutarate dehydrogenase (KGDH), pyruvate dehydrogenase (PDH), and complex I in muscle and liver mitochondria, respectively.	Hydrogen Peroxide	148-165	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	242-245	
34052343-1	2021	Our group has previously observed that protein S-glutathionylation serves as an integral feedback inhibitor for the production of superoxide (O2 -)/hydrogen peroxide (H2O2) by alpha-ketoglutarate dehydrogenase (KGDH), pyruvate dehydrogenase (PDH), and complex I in muscle and liver mitochondria, respectively.	Hydrogen Peroxide	167-171	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	218-240	
34052343-1	2021	Our group has previously observed that protein S-glutathionylation serves as an integral feedback inhibitor for the production of superoxide (O2 -)/hydrogen peroxide (H2O2) by alpha-ketoglutarate dehydrogenase (KGDH), pyruvate dehydrogenase (PDH), and complex I in muscle and liver mitochondria, respectively.	Hydrogen Peroxide	167-171	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	242-245	
31513388-1	2019	Oxoiron(IV) is a common catalytic byproduct observed in the oxidation of alkenes by the combination of H2O2 and nonheme iron catalysts including complex 1, FeIIPDP* (where PDP* = bis(3,5-dimethyl-4-methoxypyridyl-2-methyl)-(R,R)-2,2"-bipyrrolidine).	Hydrogen Peroxide	103-107	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	160-164	
27394173-8	2016	Finally, we also observed that DTT directly stimulated O2( -)/H2O2 formation by purified Pdh and Ogdh and in cardiac or liver mitochondria in the absence of substrates and cofactors.	Hydrogen Peroxide	62-66	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	89-92	
12641442-12	2003	Treatment with H(2)O(2) plus Fenton metals also decreased the PDH activity in HL60 cells.	Hydrogen Peroxide	15-23	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	62-65	
24515115-3	2014	However, the 2-oxoglutarate dehydrogenase (OGDH), branched-chain 2-oxoacid dehydrogenase (BCKDH), and pyruvate dehydrogenase (PDH) complexes are also capable of considerable superoxide/H2O2 production.	Hydrogen Peroxide	185-189	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	102-124	
24515115-3	2014	However, the 2-oxoglutarate dehydrogenase (OGDH), branched-chain 2-oxoacid dehydrogenase (BCKDH), and pyruvate dehydrogenase (PDH) complexes are also capable of considerable superoxide/H2O2 production.	Hydrogen Peroxide	185-189	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	126-129	
24515115-6	2014	At optimal conditions for each system, superoxide/H2O2 was produced by the OGDH complex at about twice the rate from the PDH complex, four times the rate from the BCKDH complex, and eight times the rate from site IF of complex I.	Hydrogen Peroxide	50-54	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	121-124	
27394173-2	2016	O2( -)/H2O2 formation by Pdh and Ogdh from porcine heart were compared when operating under forward or reverse electron transfer conditions.	Hydrogen Peroxide	7-11	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	25-28	
24515115-7	2014	Depending on the substrates present, the dominant sites of superoxide/H2O2 production at the level of NADH may be the OGDH and PDH complexes, but these activities may often be misattributed to complex I.	Hydrogen Peroxide	70-74	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	127-130	
12641442-13	2003	Therefore, it seems that As(2)O(3) elevates H(2)O(2) production in mitochondria and this may produce hydroxyl through the Fenton reaction and result in oxidative damage to the protein of PDH.	Hydrogen Peroxide	44-52	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	187-190	
8954577-10	1996	A hydroxyl radical-generating system (hydrogen peroxide irradiated with ultraviolet radiation) effectively inactivated PDH.	Hydrogen Peroxide	38-55	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	119-122	
35063808-7	2022	After H2O2 exposure, the activity of pyruvate dehydrogenase (PDH) was decreased, the content of glycogen was reduced, and the contents of adenosine monophosphate (AMP) and lactate were increased in breast muscle.	Hydrogen Peroxide	6-10	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	37-59	
35063808-7	2022	After H2O2 exposure, the activity of pyruvate dehydrogenase (PDH) was decreased, the content of glycogen was reduced, and the contents of adenosine monophosphate (AMP) and lactate were increased in breast muscle.	Hydrogen Peroxide	6-10	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	61-64