PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3415679-3 1988 According to Dowex-1 column chromatography, the transported cystine was incorporated into fractions of glutathione disulfide (GSSG) and glutathione-S (GSH-S) conjugate. Glutathione 136-149 glutathione synthetase Homo sapiens 151-156 2588942-3 1989 By Dowex-1 column chromatography, the transported cystine was incorporated into fractions of glutathione disulfide (GSSG) and glutathione-S (GSH-S) conjugate. Glutathione 126-139 glutathione synthetase Homo sapiens 141-146 2874903-0 1986 Improved assay of the enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase and glutathione synthetase. Glutathione 33-44 glutathione synthetase Homo sapiens 94-116 3402554-2 1988 An increase in cellular GSH level was produced by the addition of N-acetylcysteine (NAC), a carrier of cysteine across cell membranes, into the culture medium, while a decrease in GSH level was produced by the addition of L-buthionine-(R,S)-sulfoximine (BSO), a specific inhibitor of GSH synthetase. Glutathione 24-27 glutathione synthetase Homo sapiens 284-298 2888673-2 1987 gamma-Glutamyl transpeptidase had a wide range of variability while the glutathione synthetic enzymes, gamma-glutamylcysteine synthetase and glutathione synthetase, had narrower variations and also exhibited no apparent relationship to glutathione content. Glutathione 72-83 glutathione synthetase Homo sapiens 141-163 6106548-1 1980 Glutathione is synthesized from gamma-glutamylcysteine and glycine via the action of glutathione synthetase. Glutathione 0-11 glutathione synthetase Homo sapiens 85-107 3876305-4 1985 However, a highly significant correlation has been observed between radiosensitivity under hypoxic conditions (and therefore the oxygen enhancement ratio) and the glutathione synthetase activity, suggesting that synthesis of GSH is required after irradiation. Glutathione 225-228 glutathione synthetase Homo sapiens 163-185 6140127-3 1984 It was concluded that decline of the glutathione synthetic capacity in vivo would be most likely caused by reduction of gamma-glutamylcysteine synthetase activity rather than of glutathione synthetase activity. Glutathione 37-48 glutathione synthetase Homo sapiens 178-200 3944259-1 1986 Glutathione synthetase (GSH-S) is one of the two known hereditary causes of glutathione deficiency. Glutathione 76-87 glutathione synthetase Homo sapiens 0-22 3944259-1 1986 Glutathione synthetase (GSH-S) is one of the two known hereditary causes of glutathione deficiency. Glutathione 76-87 glutathione synthetase Homo sapiens 24-29 4021803-4 1985 These findings could be explained by an increase of glutathione synthesis brought about by the stimulation of glutathione synthetase activity. Glutathione 52-63 glutathione synthetase Homo sapiens 110-132 6112263-7 1981 High activities of the two GSH-synthesizing enzymes, gamma-glutamylcysteine synthetase and GSH synthetase were found in the human fetal liver (7.1 and 3.0 mukat/kg, respectively). Glutathione 27-30 glutathione synthetase Homo sapiens 91-105 31560820-3 2020 Previously, we have developed a clickable glutathione approach that labels intracellular glutathione with azido-Ala by using a mutant of glutathione synthetase. Glutathione 42-53 glutathione synthetase Homo sapiens 137-159 5545117-6 1971 Glutathione synthetase requires gamma-glutamyl cysteine, glycine, ATP, and magnesium ions to form glutathione. Glutathione 98-109 glutathione synthetase Homo sapiens 0-22 5545117-8 1971 Glutathione synthetase also catalyzes an exchange reaction between glycine and glutathione, but this reaction is not significant under the conditions used for assay of hemolysates. Glutathione 79-90 glutathione synthetase Homo sapiens 0-22 32918744-9 2021 GSH levels were significantly reduced by 90% in VSMCs cultured in calcifying conditions, which was associated with declines in expression of gamma-glutamylcysteine synthetase and GSH synthetase. Glutathione 0-3 glutathione synthetase Homo sapiens 179-193 5545117-3 1971 The two enzymes required for de novo glutathione synthesis, glutamyl cysteine synthetase and glutathione synthetase, have been demonstrated in hemolysates of human erythrocytes. Glutathione 37-48 glutathione synthetase Homo sapiens 93-115 33834031-7 2021 Mechanically, acitretin dramatically increased the glutathione synthase (GSS) expression and glutathione (GSH) accumulation in MDSCs. Glutathione 51-62 glutathione synthetase Homo sapiens 73-76 32910715-9 2021 At the same time, the down-regulation of ATP production suggested the activity of glutathione biosynthesis may be attenuated even if glutamate-cysteine ligase and glutathione synthase, which are two ATP-dependent enzymes participating in glutathione biosynthesis, were enhanced. Glutathione 82-93 glutathione synthetase Homo sapiens 163-183 31560820-3 2020 Previously, we have developed a clickable glutathione approach that labels intracellular glutathione with azido-Ala by using a mutant of glutathione synthetase. Glutathione 89-100 glutathione synthetase Homo sapiens 137-159 30228819-7 2018 As this reactive metabolite is detoxified mainly by enzymatic reactions, involving microsomal epoxide hydrolase and/or GSH-S-transferases and these enzymes are polymorphically expressed in humans, arene oxide toxicity is increased when epoxide hydrolase or GSH-S-transferases is either defective or inhibited or a depletion of intracellular glutathione levels is taking place. Glutathione 341-352 glutathione synthetase Homo sapiens 119-124 30581542-1 2019 The second step in the biosynthesis of the cellular antioxidant glutathione (GSH) is catalyzed by human glutathione synthetase (hGS), a negatively cooperative homodimer. Glutathione 64-75 glutathione synthetase Homo sapiens 104-126 30581542-1 2019 The second step in the biosynthesis of the cellular antioxidant glutathione (GSH) is catalyzed by human glutathione synthetase (hGS), a negatively cooperative homodimer. Glutathione 77-80 glutathione synthetase Homo sapiens 104-126 26059756-3 2015 GSH is synthesized from glutamic acid, cysteine, and glycine via two sequential ATP-consuming steps, which are catalyzed by glutamate cysteine ligase (GCL) and GSH synthetase (GSS). Glutathione 0-3 glutathione synthetase Homo sapiens 160-174 27216279-3 2016 In this report, we use our clickable glutathione approach, which forms clickable glutathione (azido-glutathione) by using a mutant of glutathione synthetase (GS M4), for detection and identification of protein glutathionylation in response to glucose starvation. Glutathione 37-48 glutathione synthetase Homo sapiens 134-156 27216279-3 2016 In this report, we use our clickable glutathione approach, which forms clickable glutathione (azido-glutathione) by using a mutant of glutathione synthetase (GS M4), for detection and identification of protein glutathionylation in response to glucose starvation. Glutathione 81-92 glutathione synthetase Homo sapiens 134-156 28838761-7 2017 Glutathione depletion with the glutathione synthetase inhibitor buthionine sulfoximine increased the cytotoxic effect of the photochemical treatment (PDT) most strongly in the SK-LMS-1 cells, and reduced PCIBLM-induced H2AX activation in the MES-SA cells, but not in the SK-LMS-1 cells. Glutathione 0-11 glutathione synthetase Homo sapiens 31-53 28571779-2 2017 Glutathione is synthesized by the consecutive action of the enzymes glutamate-cysteine ligase (GCL) and glutathione synthetase. Glutathione 0-11 glutathione synthetase Homo sapiens 104-126 25817250-5 2015 In conditions involving down regulated GSH homeostasis, GGC serves asa crucialrate-limiting substrate for GSH synthetase, the main enzyme responsible for condensing glycine with GGC to form the final thiol tripeptide, GSH. Glutathione 39-42 glutathione synthetase Homo sapiens 106-120 25731620-8 2015 In conditions involving down regulated GSH homeostasis, GGC serves as a crucialrate-limiting substrate for GSH synthetase, the main enzyme responsible for condensing glycine with GGC to form the final thiol tripeptide, GSH. Glutathione 39-42 glutathione synthetase Homo sapiens 107-121 23765060-8 2013 To confirm this, the expression of precursor genes of GSH [glutamate cysteine ligase (GCLC) and glutathione synthetase (GSS)] and the GPX gene was analyzed using quantitative PCR in cultured neoplastic mammary cells treated with doxorubicin. Glutathione 54-57 glutathione synthetase Homo sapiens 96-118 25006124-6 2014 The expression of GSH synthetase correlated with PRIMA-1(Met) LD50 values, and we showed that a GSH decrease mediated by GSH synthetase silencing or by and L-buthionine sulphoximine, an irreversible inhibitor of gamma-glutamylcysteine synthetase, increased PRIMA-1(Met)-induced cell death and overcame PRIMA-1(Met) resistance. Glutathione 18-21 glutathione synthetase Homo sapiens 121-135 25028796-2 2014 This study investigated the role of fucoxanthin in the induction of antioxidant enzymes involved in the synthesis of reduced glutathione (GSH), synthesized by glutamate-cysteine ligase catalytic subunit (GCLC) and glutathione synthetase (GSS), via Akt/nuclear factor-erythroid 2-related (Nrf2) pathway in human keratinocytes (HaCaT) and elucidated the underlying mechanism. Glutathione 125-136 glutathione synthetase Homo sapiens 214-236 25028796-2 2014 This study investigated the role of fucoxanthin in the induction of antioxidant enzymes involved in the synthesis of reduced glutathione (GSH), synthesized by glutamate-cysteine ligase catalytic subunit (GCLC) and glutathione synthetase (GSS), via Akt/nuclear factor-erythroid 2-related (Nrf2) pathway in human keratinocytes (HaCaT) and elucidated the underlying mechanism. Glutathione 138-141 glutathione synthetase Homo sapiens 214-236 22969728-9 2012 By using a model of the glutathione pathway we predict a significant increase in the flux through glutathione synthesis as both gamma-glutamylcysteine synthetase and glutathione synthetase have an increased flux. Glutathione 24-35 glutathione synthetase Homo sapiens 166-188 22995213-5 2013 The second enzyme of GSH synthesis is GSH synthetase (GS). Glutathione 21-24 glutathione synthetase Homo sapiens 38-52 23430506-1 2013 The inherited 5-oxoprolinuria is primarily suggestive of genetic defects in two enzymes belonging to the gamma-glutamyl cycle in the glutathione (GSH) metabolism: the glutathione synthetase (GSS) and the 5-oxoprolinase (OPLAH). Glutathione 133-144 glutathione synthetase Homo sapiens 167-189 23430506-1 2013 The inherited 5-oxoprolinuria is primarily suggestive of genetic defects in two enzymes belonging to the gamma-glutamyl cycle in the glutathione (GSH) metabolism: the glutathione synthetase (GSS) and the 5-oxoprolinase (OPLAH). Glutathione 133-144 glutathione synthetase Homo sapiens 191-194 23430506-1 2013 The inherited 5-oxoprolinuria is primarily suggestive of genetic defects in two enzymes belonging to the gamma-glutamyl cycle in the glutathione (GSH) metabolism: the glutathione synthetase (GSS) and the 5-oxoprolinase (OPLAH). Glutathione 146-149 glutathione synthetase Homo sapiens 167-189 23430506-1 2013 The inherited 5-oxoprolinuria is primarily suggestive of genetic defects in two enzymes belonging to the gamma-glutamyl cycle in the glutathione (GSH) metabolism: the glutathione synthetase (GSS) and the 5-oxoprolinase (OPLAH). Glutathione 146-149 glutathione synthetase Homo sapiens 191-194 22969728-9 2012 By using a model of the glutathione pathway we predict a significant increase in the flux through glutathione synthesis as both gamma-glutamylcysteine synthetase and glutathione synthetase have an increased flux. Glutathione 98-109 glutathione synthetase Homo sapiens 166-188 22442424-2 2012 In legumes, homoglutathione (hGSH) can replace GSH and is synthesized by gammaECS and a specific homoglutathione synthetase (hGSHS). Glutathione 30-33 glutathione synthetase Homo sapiens 125-130 22426003-0 2012 Glutathione synthetase promotes the reduction of arsenate via arsenolysis of glutathione. Glutathione 77-88 glutathione synthetase Homo sapiens 0-22 22426003-3 2012 Glutathione synthetase (GS) can catalyze the arsenolysis of GSH (gamma-Glu-Cys-Gly) yielding two arsenylated products, i.e. gamma-Glu-Cys-arsenate and ADP-arsenate. Glutathione 60-63 glutathione synthetase Homo sapiens 0-22 22426003-4 2012 Thus, GS may also promote the reduction of As(V) by GSH. Glutathione 52-55 glutathione synthetase Homo sapiens 6-8 21105962-3 2011 Three enzymes are responsible for GSH synthesis: glutamate cysteine ligase modifier (GCLM), glutamate cysteine ligase catalytic subunit (GCLC), and glutathione synthetase (GSS). Glutathione 34-37 glutathione synthetase Homo sapiens 148-170 21771585-1 2011 Human glutathione synthetase (hGS) catalyzes the second ATP-dependent step in the biosynthesis of glutathione (GSH) and is negatively cooperative to the gamma-glutamyl substrate. Glutathione 111-114 glutathione synthetase Homo sapiens 6-28 21668606-1 2011 Recent studies of transgenic poplars over-expressing the genes gsh1 and gsh2 encoding gamma-glutamylcysteine synthetase (gamma-ECS) and glutathione synthetase, respectively, provided detailed information on regulation of GSH synthesis, enzymes activities and mRNA expression. Glutathione 221-224 glutathione synthetase Homo sapiens 136-158 22387200-4 2012 15d-PGJ(2) upregulates the Nrf2-related glutathione synthase gene and thereby increases the GSH levels. Glutathione 92-95 glutathione synthetase Homo sapiens 40-60 22075492-8 2012 Subsequent GSH synthesis might be affected by the suppression of GSS expression in tested conditions. Glutathione 11-14 glutathione synthetase Homo sapiens 65-68 22645536-5 2011 Two enzymes catalyze glutathione synthesis: glutamate-cysteine ligase, and glutathione synthetase. Glutathione 21-32 glutathione synthetase Homo sapiens 75-97 16477124-9 2006 Reduced glutathione (GSH) is an important antioxidant and the precursor of PCs, glutamylcysteine synthetase (GCS) and glutathione synthetase (GS) catalyze GSH synthesis from Cys, overexpression of the two enzymes can improve Cd(2+) tolerance in plant. Glutathione 8-19 glutathione synthetase Homo sapiens 118-140 21815068-4 2011 GSH is synthesized into two enzymatic steps, the first, and the rate-limiting one, is catalyzed by glutamate-cysteine ligase (GCL) to form a dipeptide which is then converted to GSH by GSH synthetase. Glutathione 0-3 glutathione synthetase Homo sapiens 185-199 21815068-4 2011 GSH is synthesized into two enzymatic steps, the first, and the rate-limiting one, is catalyzed by glutamate-cysteine ligase (GCL) to form a dipeptide which is then converted to GSH by GSH synthetase. Glutathione 178-181 glutathione synthetase Homo sapiens 185-199 19672693-2 2010 Glutathione is the most abundant mammalian antioxidant, and is synthesized by glutathione synthetase (GSS). Glutathione 0-11 glutathione synthetase Homo sapiens 78-100 19672693-2 2010 Glutathione is the most abundant mammalian antioxidant, and is synthesized by glutathione synthetase (GSS). Glutathione 0-11 glutathione synthetase Homo sapiens 102-105 19672693-11 2010 Understanding the regulation of GSS expression is very important for the development of new strategies for controlling the development of GSH-based redox homeostasis. Glutathione 138-141 glutathione synthetase Homo sapiens 32-35 20123783-8 2010 However expression of the genes encoding GLYT1 and the glutathione synthesising enzymes glutamate-cysteine ligase, both catalytic and modifier subunits, and glutathione synthetase was not altered by glycine or tert-butylhydroperoxide, suggesting transcriptional regulation is not involved. Glutathione 55-66 glutathione synthetase Homo sapiens 157-179 18624917-3 2008 The anti-oxidant response element (ARE) promotes the expression of protective proteins including those required for glutathione synthesis (xCT cystine antiporter, gamma-glutamylcysteine synthetase and glutathione synthase). Glutathione 116-127 glutathione synthetase Homo sapiens 201-221 18045546-7 2008 Treatment of primary cortical neurons or 3T3 fibroblasts with the glutathione synthetase inhibitor buthionine sulfoximine resulted in substantial loss of intracellular GSH and increased cytotoxicity. Glutathione 168-171 glutathione synthetase Homo sapiens 66-88 17400258-7 2007 In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death. Glutathione 17-28 glutathione synthetase Homo sapiens 187-209 16125728-3 2006 GSH is synthesized in two steps catalysed by gamma-glutamylcysteine synthetase (gamma-ECS) and glutathione synthetase. Glutathione 0-3 glutathione synthetase Homo sapiens 95-117 17400258-7 2007 In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death. Glutathione 30-33 glutathione synthetase Homo sapiens 187-209 16477124-9 2006 Reduced glutathione (GSH) is an important antioxidant and the precursor of PCs, glutamylcysteine synthetase (GCS) and glutathione synthetase (GS) catalyze GSH synthesis from Cys, overexpression of the two enzymes can improve Cd(2+) tolerance in plant. Glutathione 21-24 glutathione synthetase Homo sapiens 118-140 16477124-9 2006 Reduced glutathione (GSH) is an important antioxidant and the precursor of PCs, glutamylcysteine synthetase (GCS) and glutathione synthetase (GS) catalyze GSH synthesis from Cys, overexpression of the two enzymes can improve Cd(2+) tolerance in plant. Glutathione 155-158 glutathione synthetase Homo sapiens 118-140 15990954-1 2005 Glutathione (GSH), one of the most important antioxidants in the eukaryotic organism, is synthesized in a two-step procedure where the last step is catalysed by the enzyme glutathione synthetase (GSS). Glutathione 0-11 glutathione synthetase Homo sapiens 172-194 15890065-1 2005 GSH synthesis occurs through a two-step enzymatic reaction driven by GCL (glutamate-cysteine ligase; made up of catalytic and modifying subunits) and GSS (glutathione synthetase). Glutathione 0-3 glutathione synthetase Homo sapiens 150-153 15890065-1 2005 GSH synthesis occurs through a two-step enzymatic reaction driven by GCL (glutamate-cysteine ligase; made up of catalytic and modifying subunits) and GSS (glutathione synthetase). Glutathione 0-3 glutathione synthetase Homo sapiens 155-177 15890065-3 2005 In the rat, GSS and GCL are regulated co-ordinately by oxidative stress, and induction of GSS further increases GSH synthetic capacity. Glutathione 112-115 glutathione synthetase Homo sapiens 90-93 15990954-1 2005 Glutathione (GSH), one of the most important antioxidants in the eukaryotic organism, is synthesized in a two-step procedure where the last step is catalysed by the enzyme glutathione synthetase (GSS). Glutathione 0-11 glutathione synthetase Homo sapiens 196-199 15990954-1 2005 Glutathione (GSH), one of the most important antioxidants in the eukaryotic organism, is synthesized in a two-step procedure where the last step is catalysed by the enzyme glutathione synthetase (GSS). Glutathione 13-16 glutathione synthetase Homo sapiens 172-194 15990954-1 2005 Glutathione (GSH), one of the most important antioxidants in the eukaryotic organism, is synthesized in a two-step procedure where the last step is catalysed by the enzyme glutathione synthetase (GSS). Glutathione 13-16 glutathione synthetase Homo sapiens 196-199 15981742-3 2005 The synthesis of glutathione is a two-step process in which the first step is catalysed by gamma-glutamylcysteine synthetase and the second step by glutathione synthetase. Glutathione 17-28 glutathione synthetase Homo sapiens 148-170 15693022-5 2005 The decrease in GSH content in red blood cells from male AD patients was associated with reduced activities of glutamate cysteine ligase and glutathione synthase, the two enzymes involved in de novo GSH synthesis, with no change in the amount of oxidized glutathione or the activity of glutathione reductase, suggesting that a decreased de novo GSH synthetic capacity is responsible for the decline in GSH content in AD. Glutathione 16-19 glutathione synthetase Homo sapiens 141-161 12442906-4 2002 Total glutathione content is also about 1.4-fold higher in HepG2, which is supported by significant increases in gamma-glutamylcysteine synthetase and glutathione synthetase activities. Glutathione 6-17 glutathione synthetase Homo sapiens 151-173 15632350-3 2005 The main goal of the present study was to measure the activities of the enzymes that are responsible for de novo GSH generation, namely gamma-glutamylcysteine synthetase (gamma-GCS) and glutathione synthetase (GSH-S), in erythrocytes from uraemic and dialysis patients. Glutathione 113-116 glutathione synthetase Homo sapiens 186-208 15632350-3 2005 The main goal of the present study was to measure the activities of the enzymes that are responsible for de novo GSH generation, namely gamma-glutamylcysteine synthetase (gamma-GCS) and glutathione synthetase (GSH-S), in erythrocytes from uraemic and dialysis patients. Glutathione 113-116 glutathione synthetase Homo sapiens 210-215 12631446-7 2003 These studies provide the first evidence for the reciprocal sensitivity of the trans-sulfuration pathway to pro- and antioxidants, and demonstrate that the upstream half of the glutathione biosynthetic pathway (i.e. leading to cysteine biosynthesis) is redox sensitive as is the regulation of the well-studied enzymes in the downstream half (leading from cysteine to glutathione), namely, gamma-glutamyl-cysteine ligase and glutathione synthetase. Glutathione 177-188 glutathione synthetase Homo sapiens 424-446 14988435-2 2004 The synthesis of GSH from glutamate, cysteine, and glycine is catalyzed sequentially by two cytosolic enzymes, gamma-glutamylcysteine synthetase and GSH synthetase. Glutathione 17-20 glutathione synthetase Homo sapiens 149-163 9034235-9 1997 Cell exposure to the glutathione synthetase inhibitor buthionine-sulfoximine depleted intracellular glutathione and inhibited nitroxide reduction; exposure to dehydroascorbate or glutathione-monoethylester increased intracellular ascorbate or glutathione concentration and stimulated nitroxide reduction. Glutathione 100-111 glutathione synthetase Homo sapiens 21-43 12018983-7 2002 Arsenite cytotoxicity increased markedly when cellular GSH was depleted with the glutathione synthase inhibitor, L-buthionine-[S,R]-sulfoximine (BSO). Glutathione 55-58 glutathione synthetase Homo sapiens 81-101 11500568-5 2001 These substitutions resulted in a strongly stimulated GSH accumulation in the transformed E. coli strain showing that these residues play a crucial role in the differential recognition of beta-alanine and glycine by hGSHS. Glutathione 54-57 glutathione synthetase Homo sapiens 216-221 10924859-2 2000 Glutathione is synthesized from its constituent amino acids by the sequential action of gamma-glutamylcysteine synthetase (gamma-GCS) and GSH synthetase. Glutathione 0-11 glutathione synthetase Homo sapiens 138-152 12361807-2 2002 The glutathione content is controlled at several levels, the most important being the rate of de novo synthesis, which is mediated by two enzymes, glutamate cysteine ligase (GCL), and glutathione synthetase (GS), with GCL being rate-limiting generally. Glutathione 4-15 glutathione synthetase Homo sapiens 184-206 11167850-1 2001 In four unrelated patients with chronic haemolysis and markedly reduced red blood cell (RBC) glutathione (49.5%, 12.6%, 11.5% and 15% of the normal concentration respectively), a severe glutathione synthetase (GSH-S, EC 6.3.2.3) deficiency was found. Glutathione 93-104 glutathione synthetase Homo sapiens 186-208 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 22-33 glutathione synthetase Homo sapiens 202-216 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 22-33 glutathione synthetase Homo sapiens 218-222 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 22-33 glutathione synthetase Homo sapiens 229-244 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 22-33 glutathione synthetase Homo sapiens 246-251 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 35-38 glutathione synthetase Homo sapiens 202-216 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 35-38 glutathione synthetase Homo sapiens 218-222 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 35-38 glutathione synthetase Homo sapiens 229-244 11080313-2 2000 The thiol tripeptides glutathione (GSH) and homoglutathione (hGSH) are very abundant in legume root nodules and their synthesis is catalyzed by the enzymes gamma-glutamylcysteine synthetase (gammaECS), GSH synthetase (GSHS), and hGSH synthetase (hGSHS). Glutathione 35-38 glutathione synthetase Homo sapiens 246-251 10369661-1 1999 Glutathione synthetase (GS) catalyses the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner. Glutathione 56-67 glutathione synthetase Homo sapiens 0-22 10068944-8 1999 Since GSH-S-Ts are actively engaged in cell detoxificative functions through conjugation of xenobiotics with glutathione, the present findings suggest that this enzyme may have a relevant protective role during the critical period when spermatogenesis is being established. Glutathione 109-120 glutathione synthetase Homo sapiens 6-11 9688640-8 1998 The decrease of GSH was correlated to the reduced GSH synthetase activity seen at 24 h postoperatively. Glutathione 16-19 glutathione synthetase Homo sapiens 50-64 9688640-10 1998 The depletion of the GSH pool is associated with a decreased activity of GSH synthetase, indicating a decreased GSH synthetic capacity in skeletal muscle tissue. Glutathione 21-24 glutathione synthetase Homo sapiens 73-87 9067456-5 1997 Depletion of GSH to 21.4 +/- 3.3% of controls by the glutathione synthetase inhibitor buthionine sulfoximine resulted in more rapid injury by glucose deprivation, yet depletion of glutathione alone did not kill astrocytes. Glutathione 13-16 glutathione synthetase Homo sapiens 53-75 9003420-1 1997 Glutathione is essential for a variety of cellular functions, and is synthesized from gamma-glutamylcysteine and glycine by the action of glutathione synthase (EC 6.3.2.3). Glutathione 0-11 glutathione synthetase Homo sapiens 138-158 7659181-7 1995 It may indicate that GSH synthetase, catalysing the final step in GSH synthesis, may participate in the elevation of GSH concentration in RCCs. Glutathione 66-69 glutathione synthetase Homo sapiens 21-35 8698748-3 1996 On the other hand, in this tumour lower activities of catalase and the glutathione-associated enzymes glutathione synthetase, gamma-glutamyl transpeptidase, glutathione reductase and total glutathione S-transferases (GST) were found. Glutathione 71-82 glutathione synthetase Homo sapiens 102-124 7909755-0 1994 Enhancement of glutathione content in glutathione synthetase-deficient fibroblasts from a patient with 5-oxoprolinuria via metabolic cooperation with normal fibroblasts. Glutathione 15-26 glutathione synthetase Homo sapiens 38-60 8098321-1 1993 PURPOSE: To assess the activities of the two enzymes required for glutathione synthesis, gamma-glutamylcysteine synthetase and glutathione synthetase, in various forms of human cataracts. Glutathione 66-77 glutathione synthetase Homo sapiens 127-149 2015281-4 1991 In the present study we use inhibition experiments, kinetic studies, trans-stimulation of GSH uptake and HPLC determination to demonstrate (for the first time) that GSH and two GSH-S-conjugates (chosen as model compounds) share a common transport system. Glutathione 90-93 glutathione synthetase Homo sapiens 177-182 34575035-1 2021 The present study investigated whether type 2 diabetes (T2D) is associated with polymorphisms of genes encoding glutathione-metabolizing enzymes such as glutathione synthetase (GSS) and gamma-glutamyl transferase 7 (GGT7). Glutathione 112-123 glutathione synthetase Homo sapiens 153-175 34575035-1 2021 The present study investigated whether type 2 diabetes (T2D) is associated with polymorphisms of genes encoding glutathione-metabolizing enzymes such as glutathione synthetase (GSS) and gamma-glutamyl transferase 7 (GGT7). Glutathione 112-123 glutathione synthetase Homo sapiens 177-180 34575035-4 2021 We found that the GSS and GGT7 gene polymorphisms alone and in combinations are associated with T2D risk regardless of sex, age, and body mass index, as well as correlated with plasma glutathione, hydrogen peroxide, and fasting blood glucose levels. Glutathione 184-195 glutathione synthetase Homo sapiens 18-21 34179023-2 2021 Here we found that CREB1 and ATF1 unexpectedly regulate glutathione (GSH) biosynthesis by suppressing the expression of glutamate-cysteine ligase modifier subunit (GCLM) and glutathione synthase (GSS), two key enzymes of GSH biosynthesis pathway. Glutathione 56-67 glutathione synthetase Homo sapiens 174-194 34179023-2 2021 Here we found that CREB1 and ATF1 unexpectedly regulate glutathione (GSH) biosynthesis by suppressing the expression of glutamate-cysteine ligase modifier subunit (GCLM) and glutathione synthase (GSS), two key enzymes of GSH biosynthesis pathway. Glutathione 56-67 glutathione synthetase Homo sapiens 196-199 34179023-2 2021 Here we found that CREB1 and ATF1 unexpectedly regulate glutathione (GSH) biosynthesis by suppressing the expression of glutamate-cysteine ligase modifier subunit (GCLM) and glutathione synthase (GSS), two key enzymes of GSH biosynthesis pathway. Glutathione 69-72 glutathione synthetase Homo sapiens 174-194 34179023-2 2021 Here we found that CREB1 and ATF1 unexpectedly regulate glutathione (GSH) biosynthesis by suppressing the expression of glutamate-cysteine ligase modifier subunit (GCLM) and glutathione synthase (GSS), two key enzymes of GSH biosynthesis pathway. Glutathione 69-72 glutathione synthetase Homo sapiens 196-199 34179023-2 2021 Here we found that CREB1 and ATF1 unexpectedly regulate glutathione (GSH) biosynthesis by suppressing the expression of glutamate-cysteine ligase modifier subunit (GCLM) and glutathione synthase (GSS), two key enzymes of GSH biosynthesis pathway. Glutathione 221-224 glutathione synthetase Homo sapiens 174-194 34179023-2 2021 Here we found that CREB1 and ATF1 unexpectedly regulate glutathione (GSH) biosynthesis by suppressing the expression of glutamate-cysteine ligase modifier subunit (GCLM) and glutathione synthase (GSS), two key enzymes of GSH biosynthesis pathway. Glutathione 221-224 glutathione synthetase Homo sapiens 196-199 35398749-0 2022 Regulatory mechanism of alpha-hederin upon cisplatin sensibility in NSCLC at safe dose by destroying GSS/GSH/GPX2 axis-mediated glutathione oxidation-reduction system. Glutathione 105-108 glutathione synthetase Homo sapiens 101-104 35398749-0 2022 Regulatory mechanism of alpha-hederin upon cisplatin sensibility in NSCLC at safe dose by destroying GSS/GSH/GPX2 axis-mediated glutathione oxidation-reduction system. Glutathione 128-139 glutathione synthetase Homo sapiens 101-104 34679719-6 2021 Pretreatment with inhibitors of glutathione synthase or the cysteine-glutamine antiporter (xC transporter) abrogate the requirement for aquaporin/H2O2-mediated glutathione depletion, thus demonstrating that intracellular glutathione is the target of intruding H2O2. Glutathione 221-232 glutathione synthetase Homo sapiens 32-52 35398749-6 2022 Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system. Glutathione 223-234 glutathione synthetase Homo sapiens 157-177 35398749-6 2022 Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system. Glutathione 223-234 glutathione synthetase Homo sapiens 179-182 35398749-6 2022 Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system. Glutathione 236-239 glutathione synthetase Homo sapiens 157-177 35398749-6 2022 Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system. Glutathione 236-239 glutathione synthetase Homo sapiens 179-182 35398749-6 2022 Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system. Glutathione 262-265 glutathione synthetase Homo sapiens 157-177 35398749-6 2022 Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system. Glutathione 262-265 glutathione synthetase Homo sapiens 179-182 35398749-8 2022 Taken together, the study provided molecular data to confirm that alpha-hederin induced ferroptosis, apoptosis, and membrane permeabilization in NSCLC by destroying the GSS/GSH/GPX2 axis-mediated GSH oxidation-reduction system at a safe and low-toxicity dose. Glutathione 173-176 glutathione synthetase Homo sapiens 169-172 35398749-8 2022 Taken together, the study provided molecular data to confirm that alpha-hederin induced ferroptosis, apoptosis, and membrane permeabilization in NSCLC by destroying the GSS/GSH/GPX2 axis-mediated GSH oxidation-reduction system at a safe and low-toxicity dose. Glutathione 196-199 glutathione synthetase Homo sapiens 169-172 35420434-4 2022 In the present study, we engineered a cell system in which the glutathione synthetase (GS) mutant was expressed that catalyzed the formation of a glutathione analogue from azido-alanine to profile changes of glutathionylome in CD38-overexpressing cells. Glutathione 146-157 glutathione synthetase Homo sapiens 63-85 35420434-4 2022 In the present study, we engineered a cell system in which the glutathione synthetase (GS) mutant was expressed that catalyzed the formation of a glutathione analogue from azido-alanine to profile changes of glutathionylome in CD38-overexpressing cells. Glutathione 146-157 glutathione synthetase Homo sapiens 87-89