PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1600837-4	1992	Stimulation of PDH by DCA increases peripheral oxidation of alanine and lactate, thereby interrupting the Cori and alanine cycles and reducing the availability of three-carbon precursors for gluconeogenesis.	Carbon	169-175	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	15-18	
34264662-6	2021	Density functional theory calculations revealed a mechanism involving PdH formation and migratory insertion into the alkene, followed by C-C bond formation.	Carbon	137-138	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	70-73	
34264662-6	2021	Density functional theory calculations revealed a mechanism involving PdH formation and migratory insertion into the alkene, followed by C-C bond formation.	Carbon	139-140	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	70-73	
26137220-1	2015	BACKGROUND: Pyruvate dehydrogenase (PDH) occupies a central node of intermediary metabolism, converting pyruvate to acetyl-CoA, thus committing carbon derived from glucose to an aerobic fate rather than an anaerobic one.	Carbon	144-150	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	12-34	
26137220-1	2015	BACKGROUND: Pyruvate dehydrogenase (PDH) occupies a central node of intermediary metabolism, converting pyruvate to acetyl-CoA, thus committing carbon derived from glucose to an aerobic fate rather than an anaerobic one.	Carbon	144-150	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	36-39	
26137220-11	2015	CONCLUSIONS: Although PDH suppression substantially alters central carbon metabolism, the data indicate that rapid cell proliferation occurs independently of PDH activity.	Carbon	67-73	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	22-25	
24817487-1	2014	We present the first in silico modeling of the Pd-H-single-walled carbon nanohorn nanocomposites.	Carbon	66-72	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	47-51	
22431524-3	2012	Here we show that when detached from the matrix, untransformed mammary epithelial cells undergo metabolic reprogramming by markedly upregulating pyruvate dehydrogenase (PDH) kinase 4 (PDK4) through estrogen-related receptor gamma (ERRgamma), thereby inhibiting PDH and attenuating the flux of glycolytic carbon into mitochondrial oxidation.	Carbon	304-310	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	169-172	
21769686-4	2011	This phosphorylation inactivates flux of glycolysis-derived carbon through this enzyme complex and implicates the PDH regulatory kinases (PDKs) as a possible drug target.	Carbon	60-66	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	114-117	
21852536-3	2011	However, flux through pyruvate dehydrogenase (PDH) is disproportionally decreased, concomitant with increased expression of the PDH inhibitory kinase, PDH kinase 4 (PDK4), and increased carbon secretion.	Carbon	186-192	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	22-44	
21852536-3	2011	However, flux through pyruvate dehydrogenase (PDH) is disproportionally decreased, concomitant with increased expression of the PDH inhibitory kinase, PDH kinase 4 (PDK4), and increased carbon secretion.	Carbon	186-192	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	46-49	
22105806-7	2011	Additionally, decreased Erk signaling in matrix-detached cells causes a disproportionate decrease in flux through pyruvate dehydrogenase (PDH), leading to decreased entry of glucose carbons into the citric acid cycle.	Carbon	182-189	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	114-136	
22105806-7	2011	Additionally, decreased Erk signaling in matrix-detached cells causes a disproportionate decrease in flux through pyruvate dehydrogenase (PDH), leading to decreased entry of glucose carbons into the citric acid cycle.	Carbon	182-189	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	138-141