PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
28886479-2	2017	Build-up of fibrous tissue occurs through the cross-linking of collagen or elastin monomers, which is initiated through the oxidation of lysine residues to form alpha-aminoadipic-delta-semialdehyde (allysine).	alpha-aasa	199-207	elastin	Mus musculus	75-82
28471663-1	2017	LOXL2 catalyzes the oxidative deamination of epsilon-amines of lysine and hydroxylysine residues within collagen and elastin, generating reactive aldehydes (allysine).	alpha-aasa	157-165	lysyl oxidase-like 2	Mus musculus	0-5
28471663-1	2017	LOXL2 catalyzes the oxidative deamination of epsilon-amines of lysine and hydroxylysine residues within collagen and elastin, generating reactive aldehydes (allysine).	alpha-aasa	157-165	elastin	Mus musculus	117-124
23375722-3	2013	METHODS: Small peptides containing reactive allysine residues based on sequences of cross-linking domains of human elastin were incubated in vitro to form cross-links characteristic of mature elastin.	alpha-aasa	44-52	elastin	Homo sapiens	115-122
26260980-1	2015	Aldehyde dehydrogenase 7A1 (ALDH7A1) is part of lysine catabolism and catalyzes the NAD(+)-dependent oxidation of alpha-aminoadipate semialdehyde to alpha-aminoadipate.	alpha-aasa	114-145	aldehyde dehydrogenase 7 family member A1	Homo sapiens	0-26
26260980-1	2015	Aldehyde dehydrogenase 7A1 (ALDH7A1) is part of lysine catabolism and catalyzes the NAD(+)-dependent oxidation of alpha-aminoadipate semialdehyde to alpha-aminoadipate.	alpha-aasa	114-145	aldehyde dehydrogenase 7 family member A1	Homo sapiens	28-35
23350806-5	2013	METHODS: The disease was confirmed based on the presence of alpha-aminoadipic semialdehyde (alpha-AASA) in urine measured by liquid chromatography tandem mass spectrometry (LC-MS/MS) and pipecolic acid (PA) in plasma and/or cerebrospinal fluid (CSF) measured by high performance liquid chromatography (HPLC)/MS/MS and by sequencing analysis of messenger RNA (mRNA) and genomic DNA of ALDH7A1.	alpha-aasa	92-102	aldehyde dehydrogenase 7 family member A1	Homo sapiens	384-391
17620346-1	2007	In rats, it has been reported that rofecoxib, a cyclooxygenase-2 (COX-2) inhibitor, reacts with the aldehyde group of allysine in elastin to give a condensation covalent adduct, thereby preventing the formation of cross-linkages in the elastin and causing degradation of the elastic fibers in aortas in vivo.	alpha-aasa	118-126	prostaglandin-endoperoxide synthase 2	Rattus norvegicus	48-64
23147983-1	2012	alpha-Amino adipic semialdehyde (alpha-AASA) accumulates in body fluids from patients with pyridoxine-dependent epilepsy because of mutations in antiquitin (ALDH7A1) and serves as the biomarker for this condition.	alpha-aasa	0-31	aldehyde dehydrogenase 7 family member A1	Homo sapiens	157-164
22241472-7	2012	The phosphorylation product made by this enzyme was metabolized by AGXT2L2, which converted it to ammonia, inorganic phosphate, and 2-aminoadipate semialdehyde.	alpha-aasa	132-159	5-phosphohydroxy-L-lysine phospho-lyase	Homo sapiens	67-74
20814824-1	2010	Pyridoxine-dependent epilepsy is a disorder associated with severe seizures that may be caused by deficient activity of alpha-aminoadipic semialdehyde dehydrogenase, encoded by the ALDH7A1 gene, with accumulation of alpha-aminoadipic semialdehyde and piperideine-6-carboxylic acid.	alpha-aasa	251-280	aldehyde dehydrogenase 7 family member A1	Homo sapiens	120-164
20814824-1	2010	Pyridoxine-dependent epilepsy is a disorder associated with severe seizures that may be caused by deficient activity of alpha-aminoadipic semialdehyde dehydrogenase, encoded by the ALDH7A1 gene, with accumulation of alpha-aminoadipic semialdehyde and piperideine-6-carboxylic acid.	alpha-aasa	251-280	aldehyde dehydrogenase 7 family member A1	Homo sapiens	181-188
19142996-8	2009	RESULTS: Both patients reported here had increased CSF alpha-AASA, CSF pipecolic acid, and known or likely pathogenic mutations in the ALDH7A1 gene, consistent with alpha-AASA dehydrogenase deficiency.	alpha-aasa	55-65	aldehyde dehydrogenase 7 family member A1	Homo sapiens	135-142
17620346-1	2007	In rats, it has been reported that rofecoxib, a cyclooxygenase-2 (COX-2) inhibitor, reacts with the aldehyde group of allysine in elastin to give a condensation covalent adduct, thereby preventing the formation of cross-linkages in the elastin and causing degradation of the elastic fibers in aortas in vivo.	alpha-aasa	118-126	prostaglandin-endoperoxide synthase 2	Rattus norvegicus	66-71
17620346-1	2007	In rats, it has been reported that rofecoxib, a cyclooxygenase-2 (COX-2) inhibitor, reacts with the aldehyde group of allysine in elastin to give a condensation covalent adduct, thereby preventing the formation of cross-linkages in the elastin and causing degradation of the elastic fibers in aortas in vivo.	alpha-aasa	118-126	elastin	Rattus norvegicus	130-137
17620346-1	2007	In rats, it has been reported that rofecoxib, a cyclooxygenase-2 (COX-2) inhibitor, reacts with the aldehyde group of allysine in elastin to give a condensation covalent adduct, thereby preventing the formation of cross-linkages in the elastin and causing degradation of the elastic fibers in aortas in vivo.	alpha-aasa	118-126	elastin	Rattus norvegicus	236-243
17620346-3	2007	The in vitro covalent binding was inhibited in the presence of beta-aminopropionitrile, D-penicillamine, and hydralazine, which suggested that the aldehyde group of allysine in human elastin was relevant to the covalent binding.	alpha-aasa	165-173	elastin	Homo sapiens	183-190
11278561-6	2001	The elastin incubated with ammonium chloride showed that DESP and IDP levels increased as the allysine content decreased.	alpha-aasa	94-102	elastin	Rattus norvegicus	4-11
11960488-2	2002	The synthesis relies on the reaction of the mercapto group of a cysteine residue in position 3 with the formyl group of allysine incorporated in position 5 of angiotensin II.	alpha-aasa	120-128	angiotensinogen	Homo sapiens	159-173
16491085-1	2006	We show here that children with pyridoxine-dependent seizures (PDS) have mutations in the ALDH7A1 gene, which encodes antiquitin; these mutations abolish the activity of antiquitin as a delta1-piperideine-6-carboxylate (P6C)-alpha-aminoadipic semialdehyde (alpha-AASA) dehydrogenase.	alpha-aasa	225-255	aldehyde dehydrogenase 7 family member A1	Homo sapiens	90-97
16491085-1	2006	We show here that children with pyridoxine-dependent seizures (PDS) have mutations in the ALDH7A1 gene, which encodes antiquitin; these mutations abolish the activity of antiquitin as a delta1-piperideine-6-carboxylate (P6C)-alpha-aminoadipic semialdehyde (alpha-AASA) dehydrogenase.	alpha-aasa	257-267	aldehyde dehydrogenase 7 family member A1	Homo sapiens	90-97
10992159-1	2000	We examined the formation of quaternary pyridinium crosslinks of elastin formed by condensation of lysine and allysine residues using the model compounds propanal (allysine) and n-butylamine (lysine) under quasi-physiological conditions.	alpha-aasa	110-118	elastin	Homo sapiens	65-72
11332453-0	2001	High-performance liquid chromatographic quantification of allysine as bis-p-cresol derivative in elastin.	alpha-aasa	58-66	elastin	Rattus norvegicus	97-104
11332453-1	2001	The first step in normal cross-linking in elastin is the formation of alpha-aminoadipic-delta-semialdehyde, allysine, through oxidative deamination of specific peptidyl lysine by the enzyme lysyl oxidase (EC 1.4.3.13).	alpha-aasa	108-116	elastin	Rattus norvegicus	42-49
11332453-4	2001	A bis-p-cresol derivative of allysine was isolated from bovine ligamentum nuchae elastin hydrolysates, and was characterized by UV, FAB-MS and NMR.	alpha-aasa	29-37	elastin	Bos taurus	81-88
11332453-8	2001	This method was applied to the determination of allysine in bovine ligamentum nuchae, aorta, lung, and rat aorta elastin.	alpha-aasa	48-56	elastin	Rattus norvegicus	113-120
11332453-9	2001	The allysine content in rat aorta elastin dramatically increased from 1 week to 2 weeks of age.	alpha-aasa	4-12	elastin	Rattus norvegicus	34-41
10755371-1	2000	Allysine is the most important precursor of physiologically essential cross-links formation in collagen and elastin and is formed by enzymatic oxidative deamination of lysine residues.	alpha-aasa	0-8	elastin	Bos taurus	108-115
10992159-1	2000	We examined the formation of quaternary pyridinium crosslinks of elastin formed by condensation of lysine and allysine residues using the model compounds propanal (allysine) and n-butylamine (lysine) under quasi-physiological conditions.	alpha-aasa	164-172	elastin	Homo sapiens	65-72
33802856-0	2021	Allysine and alpha-Aminoadipic Acid as Markers of the Glyco-Oxidative Damage to Human Serum Albumin under Pathological Glucose Concentrations.	alpha-aasa	0-8	albumin	Homo sapiens	92-99
34226627-4	2021	Using LOXL2 as a representative member of the LOX family, we developed an in situ activity assay by utilizing the strong reaction between hydrazide and aldehyde to label the LOX-catalyzed allysine (-CHO) residues with biotin-hydrazide.	alpha-aasa	188-196	lysyl oxidase like 2	Homo sapiens	6-11
34756024-5	2021	Pyridoxine-dependent epilepsy (PDE-ALDH7A1) is an inborn error of lysine metabolism, resulting from a mutation in the ALDH7A1 gene that leads to an accumulation of toxic levels of alpha-aminoadipic semialdehyde (alpha-AASA), piperideine-6-carboxylate (P6C), and pipecolic acid in body fluids.	alpha-aasa	180-210	aldehyde dehydrogenase 7 family member A1	Homo sapiens	31-34
34756024-5	2021	Pyridoxine-dependent epilepsy (PDE-ALDH7A1) is an inborn error of lysine metabolism, resulting from a mutation in the ALDH7A1 gene that leads to an accumulation of toxic levels of alpha-aminoadipic semialdehyde (alpha-AASA), piperideine-6-carboxylate (P6C), and pipecolic acid in body fluids.	alpha-aasa	180-210	aldehyde dehydrogenase 7 family member A1	Homo sapiens	35-42
34756024-5	2021	Pyridoxine-dependent epilepsy (PDE-ALDH7A1) is an inborn error of lysine metabolism, resulting from a mutation in the ALDH7A1 gene that leads to an accumulation of toxic levels of alpha-aminoadipic semialdehyde (alpha-AASA), piperideine-6-carboxylate (P6C), and pipecolic acid in body fluids.	alpha-aasa	180-210	aldehyde dehydrogenase 7 family member A1	Homo sapiens	118-125
34756024-5	2021	Pyridoxine-dependent epilepsy (PDE-ALDH7A1) is an inborn error of lysine metabolism, resulting from a mutation in the ALDH7A1 gene that leads to an accumulation of toxic levels of alpha-aminoadipic semialdehyde (alpha-AASA), piperideine-6-carboxylate (P6C), and pipecolic acid in body fluids.	alpha-aasa	212-222	aldehyde dehydrogenase 7 family member A1	Homo sapiens	31-34
34756024-5	2021	Pyridoxine-dependent epilepsy (PDE-ALDH7A1) is an inborn error of lysine metabolism, resulting from a mutation in the ALDH7A1 gene that leads to an accumulation of toxic levels of alpha-aminoadipic semialdehyde (alpha-AASA), piperideine-6-carboxylate (P6C), and pipecolic acid in body fluids.	alpha-aasa	212-222	aldehyde dehydrogenase 7 family member A1	Homo sapiens	35-42
34756024-5	2021	Pyridoxine-dependent epilepsy (PDE-ALDH7A1) is an inborn error of lysine metabolism, resulting from a mutation in the ALDH7A1 gene that leads to an accumulation of toxic levels of alpha-aminoadipic semialdehyde (alpha-AASA), piperideine-6-carboxylate (P6C), and pipecolic acid in body fluids.	alpha-aasa	212-222	aldehyde dehydrogenase 7 family member A1	Homo sapiens	118-125
34572752-5	2021	LOX-sensitive peptides (LS-peptides) contain lysine residues that are converted to allysine in the presence of LOX, which is highly reactive and binds to adjacent allysine, resulting in the aggregation of the AuNPs.	alpha-aasa	83-91	lysyl oxidase	Homo sapiens	0-3
34572752-5	2021	LOX-sensitive peptides (LS-peptides) contain lysine residues that are converted to allysine in the presence of LOX, which is highly reactive and binds to adjacent allysine, resulting in the aggregation of the AuNPs.	alpha-aasa	83-91	lysyl oxidase	Homo sapiens	111-114
34572752-5	2021	LOX-sensitive peptides (LS-peptides) contain lysine residues that are converted to allysine in the presence of LOX, which is highly reactive and binds to adjacent allysine, resulting in the aggregation of the AuNPs.	alpha-aasa	163-171	lysyl oxidase	Homo sapiens	0-3
34572752-5	2021	LOX-sensitive peptides (LS-peptides) contain lysine residues that are converted to allysine in the presence of LOX, which is highly reactive and binds to adjacent allysine, resulting in the aggregation of the AuNPs.	alpha-aasa	163-171	lysyl oxidase	Homo sapiens	111-114
34226627-4	2021	Using LOXL2 as a representative member of the LOX family, we developed an in situ activity assay by utilizing the strong reaction between hydrazide and aldehyde to label the LOX-catalyzed allysine (-CHO) residues with biotin-hydrazide.	alpha-aasa	188-196	lysyl oxidase	Homo sapiens	46-49
34226627-4	2021	Using LOXL2 as a representative member of the LOX family, we developed an in situ activity assay by utilizing the strong reaction between hydrazide and aldehyde to label the LOX-catalyzed allysine (-CHO) residues with biotin-hydrazide.	alpha-aasa	188-196	lysyl oxidase	Homo sapiens	174-177
3123231-2	1988	Several enzymes of the lysine pathway of Saccharomyces cerevisiae were found to respond to an induction mechanism mediated by the product of gene LYS14 in the presence of 2-aminoadipate semialdehyde, an intermediate of this pathway.	alpha-aasa	171-198	Lys14p	Saccharomyces cerevisiae S288C	146-151
2864042-6	1985	B-6 deficiency decreased the number of lysine residues in elastin that were converted into the cross-linking amino acid precursor allysine.	alpha-aasa	130-138	elastin	Rattus norvegicus	58-65
1244854-5	1976	Further evidence for the synthesis of elastin and collagen was the finding of radiolabelled epsilon-hydroxynorleucine and the reduced aldol condensate of two residues of allysine after reduction of [14C] lysine pulsed cells with NaBH4.	alpha-aasa	170-178	elastin	Oryctolagus cuniculus	38-45
5659685-3	1968	We show that penicillamine acts after the initial step, causing the accumulation of an elastin rich in alpha-amino adipic-delta-semialdehyde.	alpha-aasa	103-140	elastin	Homo sapiens	87-94
33543005-0	2019	Allysine modifications perturb tropoelastin structure and mobility on a local and global scale.	alpha-aasa	0-8	elastin	Homo sapiens	31-43
33543005-2	2019	Here, we leverage the recently published full atomistic model of tropoelastin to assess how allysine modifications, which are essential to cross-linking, contribute to the dynamics and structural changes that occur in tropoelastin in the context of elastin assembly.	alpha-aasa	92-100	elastin	Homo sapiens	65-77
33543005-2	2019	Here, we leverage the recently published full atomistic model of tropoelastin to assess how allysine modifications, which are essential to cross-linking, contribute to the dynamics and structural changes that occur in tropoelastin in the context of elastin assembly.	alpha-aasa	92-100	elastin	Homo sapiens	218-230
30930802-4	2019	Mutations in ALDH7A1, MOCS2, and ALDH4A1 entail build-up of reactive aldehydes (alpha-aminoadipic semialdehyde, gamma-glutamic semialdehyde) that may react non-enzymatically with macromolecules of brain cells.	alpha-aasa	80-110	aldehyde dehydrogenase 7 family member A1	Homo sapiens	13-20
30930802-4	2019	Mutations in ALDH7A1, MOCS2, and ALDH4A1 entail build-up of reactive aldehydes (alpha-aminoadipic semialdehyde, gamma-glutamic semialdehyde) that may react non-enzymatically with macromolecules of brain cells.	alpha-aasa	80-110	molybdenum cofactor synthesis 2	Homo sapiens	22-27
30930802-4	2019	Mutations in ALDH7A1, MOCS2, and ALDH4A1 entail build-up of reactive aldehydes (alpha-aminoadipic semialdehyde, gamma-glutamic semialdehyde) that may react non-enzymatically with macromolecules of brain cells.	alpha-aasa	80-110	aldehyde dehydrogenase 4 family member A1	Homo sapiens	33-40
427211-7	1979	Its sequence (Gly-Ala-Glu-allysine-(Glu)...) and amino acid composition suggest: (1) clustering of glutamic acid residues in the elastin molecule, and (2) that allysine residues are not restricted to the alanine-enriched sites described for other elastin cross-links.	alpha-aasa	26-34	LOC100620140	Sus scrofa	129-136
427211-7	1979	Its sequence (Gly-Ala-Glu-allysine-(Glu)...) and amino acid composition suggest: (1) clustering of glutamic acid residues in the elastin molecule, and (2) that allysine residues are not restricted to the alanine-enriched sites described for other elastin cross-links.	alpha-aasa	160-168	LOC100620140	Sus scrofa	247-254
31834666-3	2020	The oxidative deamination of peptidyl lysine to peptidyl allysine in elastin"s precursor tropoelastin is a crucial posttranslational step in their formation.	alpha-aasa	57-65	elastin	Homo sapiens	69-76
31834666-3	2020	The oxidative deamination of peptidyl lysine to peptidyl allysine in elastin"s precursor tropoelastin is a crucial posttranslational step in their formation.	alpha-aasa	57-65	elastin	Homo sapiens	89-101
31811253-3	2019	Pigs differed for a polymorphism at the aminoadipate-semialdehyde synthase (AASS) gene, involved in lysine (Lys) metabolism.	alpha-aasa	40-65	aminoadipate-semialdehyde synthase	Sus scrofa	76-80
33543005-2	2019	Here, we leverage the recently published full atomistic model of tropoelastin to assess how allysine modifications, which are essential to cross-linking, contribute to the dynamics and structural changes that occur in tropoelastin in the context of elastin assembly.	alpha-aasa	92-100	elastin	Homo sapiens	70-77
33543005-3	2019	We used replica exchange molecular dynamics to generate structural ensembles of allysine containing tropoelastin.	alpha-aasa	80-88	elastin	Homo sapiens	100-112