PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12574942-8 2003 Also, the availability of a common non-synonymous SNP can allow for testing of association of the CTH gene with biochemical traits affected by trans-sulfuration, such as plasma concentrations of homocysteine or even cystathionine itself, in addition to more downstream clinical phenotypes, such as vascular disease. Cystathionine 216-229 cystathionine gamma-lyase Homo sapiens 98-101 12631446-2 2003 The latter condenses homocysteine and serine to cystathionine in a reaction catalyzed by cystathionine beta-synthase followed by cleavage of cystathionine to cysteine and alpha-ketoglutarate by gamma-cystathionase. Cystathionine 48-61 cystathionine gamma-lyase Homo sapiens 194-213 12631446-2 2003 The latter condenses homocysteine and serine to cystathionine in a reaction catalyzed by cystathionine beta-synthase followed by cleavage of cystathionine to cysteine and alpha-ketoglutarate by gamma-cystathionase. Cystathionine 89-102 cystathionine gamma-lyase Homo sapiens 194-213 10994627-0 2000 Is the increase in serum cystathionine levels in patients with liver cirrhosis a consequence of impaired homocysteine transsulfuration at the level of gamma-cystathionase? Cystathionine 25-38 cystathionine gamma-lyase Homo sapiens 151-170 31160338-6 2019 We observed that CPC inhibited the gamma-elimination reaction of cystathionine and H2S synthesis from cysteine by human CSE with Ki values of 50 +- 3 and 180 +- 15 mum, respectively. Cystathionine 65-78 cystathionine gamma-lyase Homo sapiens 120-123 8507876-3 1993 Cystathionine is subsequently cleaved to cysteine and alpha-ketobutyrate by the pyridoxal phosphate-dependent enzyme gamma-cystathionase. Cystathionine 0-13 cystathionine gamma-lyase Homo sapiens 117-136 30726924-7 2019 Selective accumulation of cystathionine was observed in codeleted gliomas in vivo, in brain tissue samples, as well as in cells harboring heterozygous deletions for serine- and cystathionine-pathway genes located on 1p: phosphoglycerate dehydrogenase (PHGDH) and cystathionine gamma-lyase (CTH). Cystathionine 26-39 cystathionine gamma-lyase Homo sapiens 263-288 30726924-7 2019 Selective accumulation of cystathionine was observed in codeleted gliomas in vivo, in brain tissue samples, as well as in cells harboring heterozygous deletions for serine- and cystathionine-pathway genes located on 1p: phosphoglycerate dehydrogenase (PHGDH) and cystathionine gamma-lyase (CTH). Cystathionine 26-39 cystathionine gamma-lyase Homo sapiens 290-293 30646578-4 2019 A common mutation (1364T/T) of the cystathionine-gamma-lyase (CTH) gene affects the enzyme that converts cystathionine to cysteine in the transsulfuration pathway causing plasma elevation of total homocysteine (tHcy) or hyperhomocysteinemia-a strong and independent risk factor for cognitive loss and AD. Cystathionine 35-48 cystathionine gamma-lyase Homo sapiens 62-65 26791043-1 2016 Two enzymes in the transsulfuration pathway of homocysteine -cystathionine beta-synthase (CBS) and gamma-cystathionase (CTH)-use cysteine and/or homocysteine to produce the important signaling molecule hydrogen sulfide (H2S) and simultaneously the thioethers lanthionine, cystathionine or homolanthionine. Cystathionine 61-74 cystathionine gamma-lyase Homo sapiens 120-123 27311614-2 2016 The accumulation of CTH, specifically in HBC, was attributed to the overexpression of cystathionine beta synthase (CBS), its synthesizing enzyme, and the undetectable levels of its downstream metabolizing enzyme, cystathionine gamma lyase (CGL). Cystathionine 20-23 cystathionine gamma-lyase Homo sapiens 213-238 27311614-2 2016 The accumulation of CTH, specifically in HBC, was attributed to the overexpression of cystathionine beta synthase (CBS), its synthesizing enzyme, and the undetectable levels of its downstream metabolizing enzyme, cystathionine gamma lyase (CGL). Cystathionine 20-23 cystathionine gamma-lyase Homo sapiens 240-243 27365395-3 2016 We demonstrate that a kinetically controlled heme-dependent metabolite switch in CBS regulates these competing reactions where by cystathionine, the product of CBS, inhibits H2S synthesis by the second enzyme, CSE. Cystathionine 130-143 cystathionine gamma-lyase Homo sapiens 210-213 27365395-4 2016 Under endoplasmic reticulum stress conditions, induction of CSE and up-regulation of the CBS inhibitor, CO, a product of heme oxygenase-1, flip the operating preference of CSE from cystathionine to cysteine, transiently stimulating H2S production. Cystathionine 181-194 cystathionine gamma-lyase Homo sapiens 172-175 27365395-6 2016 This metabolite switch from cystathionine to cysteine and/or homocysteine renders H2S synthesis by CSE responsive to the known modulators of CBS: S-adenosylmethionine, NO, and CO. Used acutely, it regulates H2S synthesis; used chronically, it might contribute to disease pathology. Cystathionine 28-41 cystathionine gamma-lyase Homo sapiens 99-102 27664576-9 2016 The metabolites of CTH and CBS, l-cystathionine and l-cysteine, attenuated the formaldehyde-induced upregulation of pro-inflammatory DEGs, MMP1, PTGS2, and CXCL8, suggesting that CTH and CBS play a role in the negative feedback regulation of formaldehyde-induced pro-inflammatory responses in NHKs. Cystathionine 32-47 cystathionine gamma-lyase Homo sapiens 19-22 27664576-9 2016 The metabolites of CTH and CBS, l-cystathionine and l-cysteine, attenuated the formaldehyde-induced upregulation of pro-inflammatory DEGs, MMP1, PTGS2, and CXCL8, suggesting that CTH and CBS play a role in the negative feedback regulation of formaldehyde-induced pro-inflammatory responses in NHKs. Cystathionine 32-47 cystathionine gamma-lyase Homo sapiens 179-182 26765812-4 2016 Thus, cellular and plasma cystathionine concentrations increase in vitamin B6 deficiency mainly due to the bottleneck caused by reduced CSE activity. Cystathionine 26-39 cystathionine gamma-lyase Homo sapiens 136-139 26791043-7 2016 In the remethylation defects the accumulation of homocysteine and the increased flux of metabolites through the transsulfuration pathway resulted in elevation of cystathionine and homolanthionine (857% and 400% of median control values, respectively) indicating a possibility of an increased biosynthesis of H2S by both CBS and CTH. Cystathionine 162-175 cystathionine gamma-lyase Homo sapiens 328-331 19486201-1 2009 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulphuration pathway for the biosynthesis of cysteine from methionine and catalyses the hydrolysis of cystathionine into cysteine. Cystathionine 163-176 cystathionine gamma-lyase Homo sapiens 0-25 24278674-1 2012 Hydrogen sulfide (H2S) is a well-known toxic gas that is synthesized in the human body from the amino acids cystathionine, homocysteine, and cysteine by the action of at least two distinct enzymes: cystathionine-gamma-lyase and cystathionine-beta-synthase. Cystathionine 108-121 cystathionine gamma-lyase Homo sapiens 198-223 21275900-2 2011 CBS catalyzes the pyridoxal 5"-phosphate (PLP)-dependent conversion of homocysteine in Cystathionine whilst CSE the pyridoxal 5"-phosphate (PLP)-dependent synthesis of L-cysteine from Cystathionine. Cystathionine 184-197 cystathionine gamma-lyase Homo sapiens 108-111 26435880-1 2015 BACKGROUND: Recently a profound depletion of cystathionine gamma-lyase (CSE), the principal enzyme involved in the generation of cysteine from cystathionine, was shown in Huntington disease (HD) patients and several transgenic HD mouse models. Cystathionine 45-58 cystathionine gamma-lyase Homo sapiens 72-75 19486201-1 2009 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulphuration pathway for the biosynthesis of cysteine from methionine and catalyses the hydrolysis of cystathionine into cysteine. Cystathionine 163-176 cystathionine gamma-lyase Homo sapiens 27-30 19374684-1 2009 Hydrogen sulfide (H(2)S) is a well known and pungent toxic gas that has recently been shown to be synthesised in man from the amino acids cystathionine, homocysteine and cysteine by at least two distinct enzymes; cystathionine-gamma-lyase and cystathionine-beta-synthase. Cystathionine 138-151 cystathionine gamma-lyase Homo sapiens 213-238