PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
23716694-5	2013	These conformational changes are communicated to the lipoyl-binding pocket, which nullifies BDK activity by blocking its binding to the BCKDC core.	Alpha Lipoyl	53-59	branched chain ketoacid dehydrogenase kinase	Mus musculus	92-95
29987032-5	2018	We report that the physiologically relevant LIPT1 enzyme activity is transfer of lipoyl moieties from the H protein of the glycine cleavage system to the E2 subunits of the 2-oxoacid dehydrogenases required for respiration (e.g., pyruvate dehydrogenase) and amino acid degradation.	Alpha Lipoyl	81-87	lipoyltransferase 1	Homo sapiens	44-49
25525879-4	2014	Importantly, SIRT4 catalytic efficiency for lipoyl- and biotinyl-lysine modifications is superior to its deacetylation activity.	Alpha Lipoyl	44-50	sirtuin 4	Mus musculus	13-18
25525879-7	2014	We demonstrate SIRT4-mediated regulation of DLAT lipoyl levels and PDH activity in cells and in vivo, in mouse liver.	Alpha Lipoyl	49-55	sirtuin 4	Mus musculus	15-20
25525879-7	2014	We demonstrate SIRT4-mediated regulation of DLAT lipoyl levels and PDH activity in cells and in vivo, in mouse liver.	Alpha Lipoyl	49-55	dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase complex)	Mus musculus	44-48
17683942-3	2007	We show that the trifluoromethylpropanamide end of AZD7545 projects into the lipoyl-binding pocket of PDK1.	Alpha Lipoyl	77-83	pyruvate dehydrogenase kinase 1	Homo sapiens	102-106
21763105-1	2011	Our laboratory has hypothesized that xenobiotic modification of the native lipoyl moiety of the major mitochondrial autoantigen, the E2 subunit of the pyruvate dehydrogenase complex (PDC-E2), may lead to loss of self-tolerance in primary biliary cirrhosis (PBC).	Alpha Lipoyl	75-81	dihydrolipoamide S-acetyltransferase	Homo sapiens	183-189
21763105-1	2011	Our laboratory has hypothesized that xenobiotic modification of the native lipoyl moiety of the major mitochondrial autoantigen, the E2 subunit of the pyruvate dehydrogenase complex (PDC-E2), may lead to loss of self-tolerance in primary biliary cirrhosis (PBC).	Alpha Lipoyl	75-81	dihydrolipoamide S-acetyltransferase	Homo sapiens	257-260
20018655-5	2010	Mass spectroscopy of SDS/PAGE-resolved protein bands identified the biotin carboxyl carrier protein subunits of the plastidial acetyl-CoA carboxylase (ACCase) and three other proteins containing a similar biotin/lipoyl-binding motif as putative PII targets.	Alpha Lipoyl	212-218	acetyl Co-enzyme a carboxylase biotin carboxylase subunit	Arabidopsis thaliana	127-149
20018655-5	2010	Mass spectroscopy of SDS/PAGE-resolved protein bands identified the biotin carboxyl carrier protein subunits of the plastidial acetyl-CoA carboxylase (ACCase) and three other proteins containing a similar biotin/lipoyl-binding motif as putative PII targets.	Alpha Lipoyl	212-218	acetyl Co-enzyme a carboxylase biotin carboxylase subunit	Arabidopsis thaliana	151-157
17683942-7	2007	Bound DCA promotes local conformational changes that are communicated to both nucleotide-binding and lipoyl-binding pockets of PDK1, leading to the inactivation of kinase activity.	Alpha Lipoyl	101-107	pyruvate dehydrogenase kinase 1	Homo sapiens	127-131
16472075-1	2006	A novel chemically-modified insulin, epsilon-N(B29)-lipoyl insulin, was selectively prepared by the covalent linkage of alpha-lipoic acid (LA) to the epsilon-amino group of Lys(B29) of insulin without any protecting agent and analyzed by PAGE, HPLC, MALDI-TOF-MS. Monolipoyl- insulin maintained the glucose-lowering effect as well as native insulin and showed a longer duration of action than native insulin and an inhibitory effect towards trypsin degradation.	Alpha Lipoyl	52-58	insulin	Homo sapiens	28-35
16849321-7	2006	Alanine substitutions of residues Leu-27, Phe-32, Phe-35, and Phe-48 in the lipoyl-binding pocket of PDK3 similarly nullify L2 binding and L2-stimulated PDK3 activity.	Alpha Lipoyl	76-82	pyruvate dehydrogenase kinase 3	Homo sapiens	101-105
16849321-7	2006	Alanine substitutions of residues Leu-27, Phe-32, Phe-35, and Phe-48 in the lipoyl-binding pocket of PDK3 similarly nullify L2 binding and L2-stimulated PDK3 activity.	Alpha Lipoyl	76-82	pyruvate dehydrogenase kinase 3	Homo sapiens	153-157
16849321-8	2006	Our results indicate that the above residues in L2 and residues in the C-terminal region and the lipoyl-binding pocket of PDK3 are critical determinants for the cross-talk between L2 and PDK3, which up-regulates PDK3 activity.	Alpha Lipoyl	97-103	pyruvate dehydrogenase kinase 3	Homo sapiens	122-126
16849321-8	2006	Our results indicate that the above residues in L2 and residues in the C-terminal region and the lipoyl-binding pocket of PDK3 are critical determinants for the cross-talk between L2 and PDK3, which up-regulates PDK3 activity.	Alpha Lipoyl	97-103	pyruvate dehydrogenase kinase 3	Homo sapiens	187-191
16849321-8	2006	Our results indicate that the above residues in L2 and residues in the C-terminal region and the lipoyl-binding pocket of PDK3 are critical determinants for the cross-talk between L2 and PDK3, which up-regulates PDK3 activity.	Alpha Lipoyl	97-103	pyruvate dehydrogenase kinase 3	Homo sapiens	187-191
16472075-1	2006	A novel chemically-modified insulin, epsilon-N(B29)-lipoyl insulin, was selectively prepared by the covalent linkage of alpha-lipoic acid (LA) to the epsilon-amino group of Lys(B29) of insulin without any protecting agent and analyzed by PAGE, HPLC, MALDI-TOF-MS. Monolipoyl- insulin maintained the glucose-lowering effect as well as native insulin and showed a longer duration of action than native insulin and an inhibitory effect towards trypsin degradation.	Alpha Lipoyl	52-58	insulin	Homo sapiens	59-66
16472075-1	2006	A novel chemically-modified insulin, epsilon-N(B29)-lipoyl insulin, was selectively prepared by the covalent linkage of alpha-lipoic acid (LA) to the epsilon-amino group of Lys(B29) of insulin without any protecting agent and analyzed by PAGE, HPLC, MALDI-TOF-MS. Monolipoyl- insulin maintained the glucose-lowering effect as well as native insulin and showed a longer duration of action than native insulin and an inhibitory effect towards trypsin degradation.	Alpha Lipoyl	52-58	CD79b molecule	Homo sapiens	173-180
16472075-1	2006	A novel chemically-modified insulin, epsilon-N(B29)-lipoyl insulin, was selectively prepared by the covalent linkage of alpha-lipoic acid (LA) to the epsilon-amino group of Lys(B29) of insulin without any protecting agent and analyzed by PAGE, HPLC, MALDI-TOF-MS. Monolipoyl- insulin maintained the glucose-lowering effect as well as native insulin and showed a longer duration of action than native insulin and an inhibitory effect towards trypsin degradation.	Alpha Lipoyl	52-58	insulin	Homo sapiens	59-66
16472075-1	2006	A novel chemically-modified insulin, epsilon-N(B29)-lipoyl insulin, was selectively prepared by the covalent linkage of alpha-lipoic acid (LA) to the epsilon-amino group of Lys(B29) of insulin without any protecting agent and analyzed by PAGE, HPLC, MALDI-TOF-MS. Monolipoyl- insulin maintained the glucose-lowering effect as well as native insulin and showed a longer duration of action than native insulin and an inhibitory effect towards trypsin degradation.	Alpha Lipoyl	52-58	insulin	Homo sapiens	59-66
16472075-1	2006	A novel chemically-modified insulin, epsilon-N(B29)-lipoyl insulin, was selectively prepared by the covalent linkage of alpha-lipoic acid (LA) to the epsilon-amino group of Lys(B29) of insulin without any protecting agent and analyzed by PAGE, HPLC, MALDI-TOF-MS. Monolipoyl- insulin maintained the glucose-lowering effect as well as native insulin and showed a longer duration of action than native insulin and an inhibitory effect towards trypsin degradation.	Alpha Lipoyl	52-58	insulin	Homo sapiens	59-66
16472075-1	2006	A novel chemically-modified insulin, epsilon-N(B29)-lipoyl insulin, was selectively prepared by the covalent linkage of alpha-lipoic acid (LA) to the epsilon-amino group of Lys(B29) of insulin without any protecting agent and analyzed by PAGE, HPLC, MALDI-TOF-MS. Monolipoyl- insulin maintained the glucose-lowering effect as well as native insulin and showed a longer duration of action than native insulin and an inhibitory effect towards trypsin degradation.	Alpha Lipoyl	52-58	insulin	Homo sapiens	59-66
32444142-0	2020	Structural basis for the inhibition of PDK2 by novel ATP- and lipoyl-binding site targeting compounds.	Alpha Lipoyl	62-68	pyruvate dehydrogenase kinase 2	Homo sapiens	39-43
15491156-8	2004	Further investigation demonstrated that this cytochrome c(551) possesses two lipoyl moieties, which presumably function to anchor it to the membrane.	Alpha Lipoyl	77-83	cytochrome c, somatic	Homo sapiens	45-57
15157071-8	2004	Herein, we show that the octanoylated derivative of the lipoyl-bearing subunit of the glycine cleavage system (H-protein) is also a substrate for LipA, providing further evidence that the cofactor is synthesized on its target protein.	Alpha Lipoyl	56-62	myosin binding protein H	Homo sapiens	111-120
15861126-5	2005	These structures disclose that the C-terminal tail from one subunit of PDK3 dimer constitutes an integral part of the lipoyl-binding pocket in the N-terminal domain of the opposing subunit.	Alpha Lipoyl	118-124	pyruvate dehydrogenase kinase 3	Homo sapiens	71-75