PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
11286508-1	2001	In mammals, L-lysine is first catabolized to alpha-aminoadipate semialdehyde by the bifunctional enzyme alpha-aminoadipate semialdehyde synthase (AASS), followed by a conversion to alpha-aminoadipate by alpha-aminoadipate semialdehyde dehydrogenase.	Lysine	12-20	aminoadipate-semialdehyde synthase	Homo sapiens	104-144
11286508-1	2001	In mammals, L-lysine is first catabolized to alpha-aminoadipate semialdehyde by the bifunctional enzyme alpha-aminoadipate semialdehyde synthase (AASS), followed by a conversion to alpha-aminoadipate by alpha-aminoadipate semialdehyde dehydrogenase.	2-Aminoadipic Acid	45-63	aminoadipate-semialdehyde synthase	Homo sapiens	104-144
32567100-3	2020	We show that loss of AASS function in GCDH-deficient HEK-293 cells leads to a ~ 5-fold reduction in the established GA1 clinical biomarker glutarylcarnitine.	glutarylcarnitine	139-156	aminoadipate-semialdehyde synthase	Homo sapiens	21-25
10775527-11	2000	On the basis of these and other results, we propose that AASS catalyzes the first two steps of the major lysine-degradation pathway in human cells and that inactivating mutations in the AASS gene are a cause of hyperlysinemia.	Lysine	105-111	aminoadipate-semialdehyde synthase	Homo sapiens	57-61
10775527-11	2000	On the basis of these and other results, we propose that AASS catalyzes the first two steps of the major lysine-degradation pathway in human cells and that inactivating mutations in the AASS gene are a cause of hyperlysinemia.	Lysine	105-111	aminoadipate-semialdehyde synthase	Homo sapiens	186-190
3110158-0	1987	The bifunctional aminoadipic semialdehyde synthase in lysine degradation.	Lysine	54-60	aminoadipate-semialdehyde synthase	Homo sapiens	17-50
3110158-2	1987	The mammalian aminoadipic semialdehyde synthase is a bifunctional enzyme that catalyzes the first two sequential steps in lysine degradation in the major saccharopine pathway (Markovitz, P. J., Chuang, D. T., and Cox, R. P. (1984) J. Biol.	Lysine	122-128	aminoadipate-semialdehyde synthase	Homo sapiens	14-47
3110158-2	1987	The mammalian aminoadipic semialdehyde synthase is a bifunctional enzyme that catalyzes the first two sequential steps in lysine degradation in the major saccharopine pathway (Markovitz, P. J., Chuang, D. T., and Cox, R. P. (1984) J. Biol.	saccharopine	154-166	aminoadipate-semialdehyde synthase	Homo sapiens	14-47
4774398-1	1973	The enzymes involved in the initial degradative steps of lysine metabolism, lysine-2-oxoglutarate reductase and saccharopine dehydrogenase, were studied and their activities in different mammals compared.	Lysine	57-63	aminoadipate-semialdehyde synthase	Homo sapiens	76-107
23890588-12	2013	Mutational screening of the AASS gene revealed that case 1 was a compound heterozygote for c.2662 + 1_2662 + 5delGTAAGinsTT and c.874A>G and that case 2 was a compound heterozygote for c.976_977delCA and c.1925C>G. In conclusion, we present two children with hyperlysinemia type I and neurological impairment in which implementation of lysine-restricted diet achieved a mild improvement of symptoms but did not reverse cognitive impairment.	Lysine	270-276	aminoadipate-semialdehyde synthase	Homo sapiens	28-32
33100873-2	2020	Homozygous frameshift mutation in Pseudouridine Synthase 7, Putative; (PUS7) OMIM# 616,261 NM_019042.3 and splice acceptor variants in Alpha-Aminoadipic Semialdehyde Synthase; (AASS) OMIM# 605,113 NM_005763.3 was funded.	semialdehyde	153-165	aminoadipate-semialdehyde synthase	Homo sapiens	177-181
33100873-4	2020	Different bioinformatics analysis done for WES data and we identified two novel mutations one as frameshift mutation c.606_607delGA, p.Ser282CysfsTer9 in the PUS7 gene and splice acceptor variants c.1767-1 G > A in the AASS gene has been reported.	ser282cysfster9	135-150	aminoadipate-semialdehyde synthase	Homo sapiens	219-223
19774086-1	2009	BACKGROUND: Lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) is a bifunctional enzyme catalyzing the first two steps of lysine catabolism in plants and mammals.	Lysine	139-145	aminoadipate-semialdehyde synthase	Homo sapiens	12-69
19774086-1	2009	BACKGROUND: Lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) is a bifunctional enzyme catalyzing the first two steps of lysine catabolism in plants and mammals.	Lysine	139-145	aminoadipate-semialdehyde synthase	Homo sapiens	71-78
19774086-2	2009	However, to date, the properties of the lysine degradation pathway and biological functions of LKR/SDH have been very little described in arthropods such as ticks.	Lysine	40-46	aminoadipate-semialdehyde synthase	Homo sapiens	95-102
19774086-7	2009	CONCLUSIONS/SIGNIFICANCE: Transcription analysis and gene silencing of LKR/SDH indicated that tick LKR/SDH enzyme plays not only important roles in egg production, reproduction and development of the tick, but also in carbon, nitrogen and water balance, crucial physiological processes for the survival of ticks.	Carbon	218-224	aminoadipate-semialdehyde synthase	Homo sapiens	71-78
19774086-7	2009	CONCLUSIONS/SIGNIFICANCE: Transcription analysis and gene silencing of LKR/SDH indicated that tick LKR/SDH enzyme plays not only important roles in egg production, reproduction and development of the tick, but also in carbon, nitrogen and water balance, crucial physiological processes for the survival of ticks.	Carbon	218-224	aminoadipate-semialdehyde synthase	Homo sapiens	99-106
19774086-7	2009	CONCLUSIONS/SIGNIFICANCE: Transcription analysis and gene silencing of LKR/SDH indicated that tick LKR/SDH enzyme plays not only important roles in egg production, reproduction and development of the tick, but also in carbon, nitrogen and water balance, crucial physiological processes for the survival of ticks.	Nitrogen	226-234	aminoadipate-semialdehyde synthase	Homo sapiens	71-78
19774086-7	2009	CONCLUSIONS/SIGNIFICANCE: Transcription analysis and gene silencing of LKR/SDH indicated that tick LKR/SDH enzyme plays not only important roles in egg production, reproduction and development of the tick, but also in carbon, nitrogen and water balance, crucial physiological processes for the survival of ticks.	Nitrogen	226-234	aminoadipate-semialdehyde synthase	Homo sapiens	99-106
16525756-3	2006	The first two enzymes of lysine catabolism are synthesized from a single LKR/SDH gene.	Lysine	25-31	aminoadipate-semialdehyde synthase	Homo sapiens	73-80