PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24937102-7	2014	Proteomic analysis also found an increase in the expression of glucose-6-phosphate dehydrogenase (G6PD), which supplies reducing equivalents by regenerating nicotinamide adenine dinucleotide phosphate (NADPH) levels.	NADP	157-200	glucose-6-phosphate dehydrogenase	Homo sapiens	63-96	
24937102-7	2014	Proteomic analysis also found an increase in the expression of glucose-6-phosphate dehydrogenase (G6PD), which supplies reducing equivalents by regenerating nicotinamide adenine dinucleotide phosphate (NADPH) levels.	NADP	157-200	glucose-6-phosphate dehydrogenase	Homo sapiens	98-102	
24937102-7	2014	Proteomic analysis also found an increase in the expression of glucose-6-phosphate dehydrogenase (G6PD), which supplies reducing equivalents by regenerating nicotinamide adenine dinucleotide phosphate (NADPH) levels.	NADP	202-207	glucose-6-phosphate dehydrogenase	Homo sapiens	63-96	
24937102-7	2014	Proteomic analysis also found an increase in the expression of glucose-6-phosphate dehydrogenase (G6PD), which supplies reducing equivalents by regenerating nicotinamide adenine dinucleotide phosphate (NADPH) levels.	NADP	202-207	glucose-6-phosphate dehydrogenase	Homo sapiens	98-102	
23579026-9	2013	Peptide mass mapping studies confirmed hydroimidazolone formation on multiple peptides in G6PD and IDH, including those critical for NADP(+) binding, and substrate binding, in the case of IDH.	NADP	133-140	glucose-6-phosphate dehydrogenase	Homo sapiens	90-94	
24300239-7	2014	Quantifying PPP NADPH-producing enzymes glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase by enzyme-linked immunosorbent assay, showed a reduction in the putamen of early-stage PD and interestingly in the cerebellum of early and late-stage PD.	NADP	16-21	glucose-6-phosphate dehydrogenase	Homo sapiens	40-73	
24278172-8	2013	TLQP-21 also upregulated the expression of glucose-6-phosphate dehydrogenase (G6PD), which is known as the main source of NADPH.	NADP	122-127	glucose-6-phosphate dehydrogenase	Homo sapiens	43-76	
24278172-8	2013	TLQP-21 also upregulated the expression of glucose-6-phosphate dehydrogenase (G6PD), which is known as the main source of NADPH.	NADP	122-127	glucose-6-phosphate dehydrogenase	Homo sapiens	78-82	
24278172-9	2013	Knockdown of G6PD almost completely blocked the increase of NADPH induced by TLQP-21, indicating that TLQP-21 functions mainly through G6PD to promote NADPH generation.	NADP	60-65	glucose-6-phosphate dehydrogenase	Homo sapiens	13-17	
24278172-9	2013	Knockdown of G6PD almost completely blocked the increase of NADPH induced by TLQP-21, indicating that TLQP-21 functions mainly through G6PD to promote NADPH generation.	NADP	60-65	glucose-6-phosphate dehydrogenase	Homo sapiens	135-139	
24278172-9	2013	Knockdown of G6PD almost completely blocked the increase of NADPH induced by TLQP-21, indicating that TLQP-21 functions mainly through G6PD to promote NADPH generation.	NADP	151-156	glucose-6-phosphate dehydrogenase	Homo sapiens	13-17	
24278172-9	2013	Knockdown of G6PD almost completely blocked the increase of NADPH induced by TLQP-21, indicating that TLQP-21 functions mainly through G6PD to promote NADPH generation.	NADP	151-156	glucose-6-phosphate dehydrogenase	Homo sapiens	135-139	
24278172-10	2013	In conclusion, TLQP-21 could increase G6PD expression, which in turn may increase the synthesis of NADPH and GSH, thereby partially restoring the redox status of vascular endothelial cells under high glucose injury.	NADP	99-104	glucose-6-phosphate dehydrogenase	Homo sapiens	38-42	
23665046-4	2013	Intracellularly, two compartmentalized reactions generate NADPH upon oxidation of glucose-6-phosphate: cytosolic glucose-6-phosphate dehydrogenase and microsomal hexose-6-phosphate dehydrogenase.	NADP	58-63	glucose-6-phosphate dehydrogenase	Homo sapiens	113-146	
24720642-1	2014	Glucose-6-phosphate dehydrogenase (G6PD) is critical to the maintenance of NADPH pool and redox homeostasis.	NADP	75-80	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
24720642-1	2014	Glucose-6-phosphate dehydrogenase (G6PD) is critical to the maintenance of NADPH pool and redox homeostasis.	NADP	75-80	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
25097522-6	2014	Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activity as compared to the reduction of NADP +, glutathione reductase activity was performed based on the oxidation of NADPH.	NADP	191-196	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
24929815-1	2014	Glucose 6-phosphate dehydrogenase (G6PD), the first and the rate-limiting enzyme in the pentose phosphate pathway (PPP), catalyzes the oxidation of G6P to 6-phosphogluconolactone and the reduction of NADP(+) to NADPH.	NADP	200-204	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
24929815-1	2014	Glucose 6-phosphate dehydrogenase (G6PD), the first and the rate-limiting enzyme in the pentose phosphate pathway (PPP), catalyzes the oxidation of G6P to 6-phosphogluconolactone and the reduction of NADP(+) to NADPH.	NADP	200-204	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
24929815-1	2014	Glucose 6-phosphate dehydrogenase (G6PD), the first and the rate-limiting enzyme in the pentose phosphate pathway (PPP), catalyzes the oxidation of G6P to 6-phosphogluconolactone and the reduction of NADP(+) to NADPH.	NADP	211-216	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
24929815-1	2014	Glucose 6-phosphate dehydrogenase (G6PD), the first and the rate-limiting enzyme in the pentose phosphate pathway (PPP), catalyzes the oxidation of G6P to 6-phosphogluconolactone and the reduction of NADP(+) to NADPH.	NADP	211-216	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
23967283-8	2013	[1,2- (13)C2]-glucose tracer experiments demonstrated that the oxidative branch of PPP initiated by glucose-6-phosphate dehydrogenase activity is preferentially utilized for ribose production (56-66%) that produces increased amounts of ribose necessary for growth and NADPH.	NADP	268-273	glucose-6-phosphate dehydrogenase	Homo sapiens	100-133	
23811687-6	2013	By stimulating G6PD, TAp73 increases PPP flux and directs glucose to the production of NADPH and ribose, for the synthesis of macromolecules and detoxification of reactive oxygen species (ROS).	NADP	87-92	glucose-6-phosphate dehydrogenase	Homo sapiens	15-19	
23742107-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is pivotal to reduced nicotinamide adenine dinucleotide phosphate (NADPH) production and cellular redox balance.	NADP	63-106	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
23742107-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is pivotal to reduced nicotinamide adenine dinucleotide phosphate (NADPH) production and cellular redox balance.	NADP	63-106	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
23742107-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is pivotal to reduced nicotinamide adenine dinucleotide phosphate (NADPH) production and cellular redox balance.	NADP	108-113	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
23742107-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is pivotal to reduced nicotinamide adenine dinucleotide phosphate (NADPH) production and cellular redox balance.	NADP	108-113	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
23742107-8	2013	We found a protective role of G6PD in AFB1-induced cytotoxicity, possibly via providing NADPH for NADPH oxidase to induce epoxide hydrolase 1 (EPHX1), a xenobiotic-metabolizing enzyme.	NADP	88-93	glucose-6-phosphate dehydrogenase	Homo sapiens	30-34	
23583906-2	2013	The rate of ATP appearance outside mitochondria was measured as the increase in NADPH absorbance which occurs, following external addition of ADP, when ATP is produced by oxidative phosphorylation and exported from mitochondria in the presence of glucose, hexokinase and glucose-6-phosphate dehydrogenase.	NADP	80-85	glucose-6-phosphate dehydrogenase	Homo sapiens	271-304	
23023104-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is the key enzyme of the pentose phosphate pathway, converting glucose-6-phosphate to 6-phosphoglucono-delta-lactone with parallel reduction of NADP(+).	NADP	185-189	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
23440281-6	2013	2-DG treatment increased the levels of pentose phosphate pathway (PPP) metabolites and augmented the generation of NADPH by glucose-6-phosphate dehydrogenase.	NADP	115-120	glucose-6-phosphate dehydrogenase	Homo sapiens	124-157	
23023104-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is the key enzyme of the pentose phosphate pathway, converting glucose-6-phosphate to 6-phosphoglucono-delta-lactone with parallel reduction of NADP(+).	NADP	185-189	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
23801924-1	2012	SUMMARY: G6PD catalyzes the first, pace-making reaction of pentosephosphate cycle (PPC) which produces NADPH.	NADP	103-108	glucose-6-phosphate dehydrogenase	Homo sapiens	9-13	
23390344-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway (PPP) that plays an important role in protecting cells from oxidative damage by producing NADPH and reduced glutathione.	NADP	177-182	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
23390344-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway (PPP) that plays an important role in protecting cells from oxidative damage by producing NADPH and reduced glutathione.	NADP	177-182	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
23142419-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is crucial to NADPH generation and redox homeostasis.	NADP	55-60	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
23142419-1	2013	Glucose-6-phosphate dehydrogenase (G6PD) is crucial to NADPH generation and redox homeostasis.	NADP	55-60	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
22883558-10	2012	In addition to the easy and ecofriendly method of synthesis, beta-NADPH can be regenerated by enzymatic means through glucose 6-phosphate dehydrogenase, potentially making the synthesis more cost effective.	NADP	61-71	glucose-6-phosphate dehydrogenase	Homo sapiens	118-151	
23258327-2	2012	Glucose-6-phosphate dehydrogenase (G6PD), the principal source of NADPH, serves as an antioxidant enzyme to modulate the redox milieu.	NADP	66-71	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
23258327-2	2012	Glucose-6-phosphate dehydrogenase (G6PD), the principal source of NADPH, serves as an antioxidant enzyme to modulate the redox milieu.	NADP	66-71	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
23275884-6	2012	Interactions between the enzymes were altered by environmental stress in directions and magnitudes that are consistent with differential contributions of the different enzymes to the NADPH pool: the contributions of G6PD and IDH seem to be accentuated by oxidative stress, and MEN by starvation.	NADP	183-188	glucose-6-phosphate dehydrogenase	Homo sapiens	216-220	
22494872-3	2012	The reduction of nicotinamide adenine dinucleotide phosphate to nicotinamide adenine dinucleotide phosphate-oxidase, reflecting G6PD activity, was measured spectrophotometrically.	NADP	17-60	glucose-6-phosphate dehydrogenase	Homo sapiens	128-132	
22083321-1	2012	BACKGROUND: Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway that provides the majority of NADPH required for lipid biosynthesis.	NADP	144-149	glucose-6-phosphate dehydrogenase	Homo sapiens	12-45	
22431005-4	2012	But there has been a growing understanding of the central importance of G6PD to cellular physiology as it is a major source of NADPH that is required by many essential cellular systems including the antioxidant pathways, nitric oxide synthase, NADPH oxidase, cytochrome p450 system, and others.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	72-76	
22304857-3	2012	Glucose-6-phosphate dehydrogenase (G6PD) can fuel ROS production by providing reduced nicotinamide adenine dinucleotide phosphate (NADPH) for superoxide generation by NADPH oxidase.	NADP	86-129	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
22304857-3	2012	Glucose-6-phosphate dehydrogenase (G6PD) can fuel ROS production by providing reduced nicotinamide adenine dinucleotide phosphate (NADPH) for superoxide generation by NADPH oxidase.	NADP	86-129	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
22304857-3	2012	Glucose-6-phosphate dehydrogenase (G6PD) can fuel ROS production by providing reduced nicotinamide adenine dinucleotide phosphate (NADPH) for superoxide generation by NADPH oxidase.	NADP	131-136	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
22304857-3	2012	Glucose-6-phosphate dehydrogenase (G6PD) can fuel ROS production by providing reduced nicotinamide adenine dinucleotide phosphate (NADPH) for superoxide generation by NADPH oxidase.	NADP	131-136	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
22304857-5	2012	We hypothesized that a high-sugar intake would increase flux through G6PD to increase myocardial NADPH and ROS and accelerate cardiac dysfunction and death.	NADP	97-102	glucose-6-phosphate dehydrogenase	Homo sapiens	69-73	
22083321-1	2012	BACKGROUND: Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway that provides the majority of NADPH required for lipid biosynthesis.	NADP	144-149	glucose-6-phosphate dehydrogenase	Homo sapiens	47-51	
22165289-4	2011	Compared with G6PD(WT), the Km, and Vmax of NADP+ with G6PD(G487A) were about 28-fold and 12-fold lower, respectively.	NADP	44-49	glucose-6-phosphate dehydrogenase	Homo sapiens	14-18	
22292701-1	2012	The objective of the present study was to examine changes observed in the expression of cytosolic NADP isocitrate dehydrogenase (ICDH) and glucose 6-phosphate dehydrogenase (G6PD) genes, the major implicated genes in ruminant lipogenesis in terms of produce NADPH, during the early post-weaning period in dairy ewes in respect to energy intake, and to further correlate the noted changes with their respective enzymatic activities.	NADP	258-263	glucose-6-phosphate dehydrogenase	Homo sapiens	139-172	
22292701-1	2012	The objective of the present study was to examine changes observed in the expression of cytosolic NADP isocitrate dehydrogenase (ICDH) and glucose 6-phosphate dehydrogenase (G6PD) genes, the major implicated genes in ruminant lipogenesis in terms of produce NADPH, during the early post-weaning period in dairy ewes in respect to energy intake, and to further correlate the noted changes with their respective enzymatic activities.	NADP	258-263	glucose-6-phosphate dehydrogenase	Homo sapiens	174-178	
23185302-3	2012	Previous research from our laboratory has shown that high glucose decreases the principal cellular reductant, NADPH by impairing the activity of glucose 6-phosphate dehydrogenase (G6PD).	NADP	110-115	glucose-6-phosphate dehydrogenase	Homo sapiens	145-178	
23185302-3	2012	Previous research from our laboratory has shown that high glucose decreases the principal cellular reductant, NADPH by impairing the activity of glucose 6-phosphate dehydrogenase (G6PD).	NADP	110-115	glucose-6-phosphate dehydrogenase	Homo sapiens	180-184	
22061664-3	2012	Breed-related differences in abundance and activities of malic enzyme and glucose-6-phosphate dehydrogenase NADPH-supplying enzymes suggested up-regulation of the lipogenic pathway to dispose for a greater adiposity.	NADP	108-113	glucose-6-phosphate dehydrogenase	Homo sapiens	74-107	
22219589-4	2011	But known or suspected glucose-6-phosphate dehydrogenase (G6PD) deficiency is a relative contraindication to the use of methylene blue because G6PD is the key enzyme in the formation of NADPH through pentose phosphate pathway and G6PD-deficient individuals generate insufficient NADPH to efficiently reduce methylene blue to leukomethylene blue, which is necessary for the activation of the NADPH-dependent methemoglobin reductase system.	NADP	186-191	glucose-6-phosphate dehydrogenase	Homo sapiens	58-62	
22219589-4	2011	But known or suspected glucose-6-phosphate dehydrogenase (G6PD) deficiency is a relative contraindication to the use of methylene blue because G6PD is the key enzyme in the formation of NADPH through pentose phosphate pathway and G6PD-deficient individuals generate insufficient NADPH to efficiently reduce methylene blue to leukomethylene blue, which is necessary for the activation of the NADPH-dependent methemoglobin reductase system.	NADP	279-284	glucose-6-phosphate dehydrogenase	Homo sapiens	58-62	
22219589-4	2011	But known or suspected glucose-6-phosphate dehydrogenase (G6PD) deficiency is a relative contraindication to the use of methylene blue because G6PD is the key enzyme in the formation of NADPH through pentose phosphate pathway and G6PD-deficient individuals generate insufficient NADPH to efficiently reduce methylene blue to leukomethylene blue, which is necessary for the activation of the NADPH-dependent methemoglobin reductase system.	NADP	279-284	glucose-6-phosphate dehydrogenase	Homo sapiens	58-62	
22165289-4	2011	Compared with G6PD(WT), the Km, and Vmax of NADP+ with G6PD(G487A) were about 28-fold and 12-fold lower, respectively.	NADP	44-49	glucose-6-phosphate dehydrogenase	Homo sapiens	55-59	
22165289-5	2011	The Ki values of dehydroepiandrosterone (DHEA), NADPH and ATP with G6PD(G487A) showed 29.5-fold, 2.36-fold reduction and 1.83-fold increase, respectively.	NADP	48-53	glucose-6-phosphate dehydrogenase	Homo sapiens	67-71	
21238579-4	2011	Glucose-6-phosphate dehydrogenase (G-6-PDH) inhibition partially blocked NQO1 activity in control and sulf-treated cells, but G-6-PDH overexpression via transient transfection with the human cDNA alleviated neither the restriction on intact sulf-treated cell NQO1 activity nor the impact on the NADPH/NADP(+) ratios.	NADP	295-300	glucose-6-phosphate dehydrogenase	Homo sapiens	35-42	
21467295-3	2011	Upon ATM activation, the rate-limiting PPP enzyme glucose 6-phosphate dehydrogenase (G6PDH) formed a complex with heat shock protein 27 that increased G6PDH activity, augmented NADP(+) to NADPH reduction, and stimulated nucleotide synthesis.	NADP	177-181	glucose-6-phosphate dehydrogenase	Homo sapiens	50-83	
21467295-3	2011	Upon ATM activation, the rate-limiting PPP enzyme glucose 6-phosphate dehydrogenase (G6PDH) formed a complex with heat shock protein 27 that increased G6PDH activity, augmented NADP(+) to NADPH reduction, and stimulated nucleotide synthesis.	NADP	177-181	glucose-6-phosphate dehydrogenase	Homo sapiens	85-90	
21467295-3	2011	Upon ATM activation, the rate-limiting PPP enzyme glucose 6-phosphate dehydrogenase (G6PDH) formed a complex with heat shock protein 27 that increased G6PDH activity, augmented NADP(+) to NADPH reduction, and stimulated nucleotide synthesis.	NADP	188-193	glucose-6-phosphate dehydrogenase	Homo sapiens	50-83	
21849081-5	2011	G6PD phenotype was assessed qualitatively using the NADPH fluorescence test.	NADP	52-57	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
21467295-3	2011	Upon ATM activation, the rate-limiting PPP enzyme glucose 6-phosphate dehydrogenase (G6PDH) formed a complex with heat shock protein 27 that increased G6PDH activity, augmented NADP(+) to NADPH reduction, and stimulated nucleotide synthesis.	NADP	188-193	glucose-6-phosphate dehydrogenase	Homo sapiens	85-90	
21238579-4	2011	Glucose-6-phosphate dehydrogenase (G-6-PDH) inhibition partially blocked NQO1 activity in control and sulf-treated cells, but G-6-PDH overexpression via transient transfection with the human cDNA alleviated neither the restriction on intact sulf-treated cell NQO1 activity nor the impact on the NADPH/NADP(+) ratios.	NADP	295-299	glucose-6-phosphate dehydrogenase	Homo sapiens	35-42	
21157431-6	2011	ATM activation induces glucose-6-phosphate dehydrogenase (G6PD) activity, the limiting enzyme of the PPP responsible for the production of NADPH, an essential anti-oxidant cofactor.	NADP	139-144	glucose-6-phosphate dehydrogenase	Homo sapiens	23-56	
20558052-5	2011	The combination also reduced the activity of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and transaldolase in the pentose phosphate pathway, a major mechanism for producing NADPH, resulting in a marked decrease in intracellular NADPH levels.	NADP	198-203	glucose-6-phosphate dehydrogenase	Homo sapiens	45-78	
20558052-5	2011	The combination also reduced the activity of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and transaldolase in the pentose phosphate pathway, a major mechanism for producing NADPH, resulting in a marked decrease in intracellular NADPH levels.	NADP	253-258	glucose-6-phosphate dehydrogenase	Homo sapiens	45-78	
21157431-6	2011	ATM activation induces glucose-6-phosphate dehydrogenase (G6PD) activity, the limiting enzyme of the PPP responsible for the production of NADPH, an essential anti-oxidant cofactor.	NADP	139-144	glucose-6-phosphate dehydrogenase	Homo sapiens	58-62	
19231202-2	2009	G6PDH catalyzes the first step of the pentose-phosphate pathway supplying cells with ribose 5-phosphate, a precursor of nucleic acid synthesis, and NADPH for biosynthetic processes and protection against oxidative stress.	NADP	148-153	glucose-6-phosphate dehydrogenase	Homo sapiens	0-5	
21476273-3	2011	Remaxol helps to keep intact the energetic substrates of hepatocytes by saving the activity of glucose-6-phosphatedehydrogenase (which increases restored NADPH and glutathione enzymes), thus preventing the oxidative destruction of glutathione reductase and glutathione S-transferase.	NADP	154-159	glucose-6-phosphate dehydrogenase	Homo sapiens	95-127	
20621833-3	2010	Moreover, siRNA for glucose-6-phosphate dehydrogenase, which produces NADPH, reduced the increase in HIF-1alpha protein.	NADP	70-75	glucose-6-phosphate dehydrogenase	Homo sapiens	20-53	
20570159-1	2010	Glucose 6-phosphate dehydrogenase (G6PDH) catalyzes the first step of the pentose-phosphate pathway which supplies cells with ribose 5-phosphate (R5P) and NADPH.	NADP	155-160	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
20570159-1	2010	Glucose 6-phosphate dehydrogenase (G6PDH) catalyzes the first step of the pentose-phosphate pathway which supplies cells with ribose 5-phosphate (R5P) and NADPH.	NADP	155-160	glucose-6-phosphate dehydrogenase	Homo sapiens	35-40	
20228249-3	2010	Here, we have identified glucose-6-phosphate dehydrogenase (G6PDH) as an important source of NADPH in mitochondria.	NADP	93-98	glucose-6-phosphate dehydrogenase	Homo sapiens	25-58	
20228249-3	2010	Here, we have identified glucose-6-phosphate dehydrogenase (G6PDH) as an important source of NADPH in mitochondria.	NADP	93-98	glucose-6-phosphate dehydrogenase	Homo sapiens	60-65	
20228249-5	2010	6-ANAM, a specific G6PDH inhibitor, depleted mitochondrial NADPH pools and increased oxidative stress revealing the importance of G6PDH in NADPH maintenance.	NADP	59-64	glucose-6-phosphate dehydrogenase	Homo sapiens	19-24	
20228249-5	2010	6-ANAM, a specific G6PDH inhibitor, depleted mitochondrial NADPH pools and increased oxidative stress revealing the importance of G6PDH in NADPH maintenance.	NADP	139-144	glucose-6-phosphate dehydrogenase	Homo sapiens	130-135	
20228249-7	2010	Indeed, cells cultured in high glucose (HG) not only adopted a glycolytic phenotype but also relied heavily on matrix-associated G6PDH as a source of NADPH.	NADP	150-155	glucose-6-phosphate dehydrogenase	Homo sapiens	129-134	
20228249-13	2010	Hence, we not only identified a matrix-associated G6PDH but also provide evidence that metabolic state/glucose availability modulate enzymatic sources of NADPH.	NADP	154-159	glucose-6-phosphate dehydrogenase	Homo sapiens	50-55	
20484601-1	2010	PURPOSE: Glucose-6-phosphate dehydrogenase (G6PD) is an important site of metabolic control in the pentose phosphate pathway (PPP), providing reducing power (NADPH) and pentose phosphates.	NADP	158-163	glucose-6-phosphate dehydrogenase	Homo sapiens	9-42	
20484601-1	2010	PURPOSE: Glucose-6-phosphate dehydrogenase (G6PD) is an important site of metabolic control in the pentose phosphate pathway (PPP), providing reducing power (NADPH) and pentose phosphates.	NADP	158-163	glucose-6-phosphate dehydrogenase	Homo sapiens	44-48	
19465117-0	2009	Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP(+) binding affects both folding and stability.	NADP	75-82	glucose-6-phosphate dehydrogenase	Homo sapiens	26-59	
19465117-1	2009	Human glucose 6-phosphate dehydrogenase (G6PD) has both the "catalytic" NADP(+) site and a "structural" NADP(+) site where a number of severe G6PD deficiency mutations are located.	NADP	72-76	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
19465117-1	2009	Human glucose 6-phosphate dehydrogenase (G6PD) has both the "catalytic" NADP(+) site and a "structural" NADP(+) site where a number of severe G6PD deficiency mutations are located.	NADP	72-76	glucose-6-phosphate dehydrogenase	Homo sapiens	41-45	
19283805-1	2009	Triple duty: A synthetic molecular clip traps nicotinamide adenine dinucleotide phosphate (NADP(+); see picture) as well as occupying both the cofactor- and the substrate-binding site in glucose-6-phosphate (G6P) dehydrogenase.	NADP	46-89	glucose-6-phosphate dehydrogenase	Homo sapiens	187-226	
19283805-1	2009	Triple duty: A synthetic molecular clip traps nicotinamide adenine dinucleotide phosphate (NADP(+); see picture) as well as occupying both the cofactor- and the substrate-binding site in glucose-6-phosphate (G6P) dehydrogenase.	NADP	91-96	glucose-6-phosphate dehydrogenase	Homo sapiens	187-226	
18992234-0	2009	Could G6PD-Buenos-Aires confirm the existence of the "structural NADP+ binding site" and its strategic role for the stability and/or activity enzyme?	NADP	65-70	glucose-6-phosphate dehydrogenase	Homo sapiens	6-10	
20851888-4	2010	Conditional expression of the glucose-6-phosphate dehydrogenase-encoding gene zwf, shown here to be under DksA control, increases both the NADPH pool and antioxidant defenses of dksA mutant Salmonella.	NADP	139-144	glucose-6-phosphate dehydrogenase	Homo sapiens	30-63	
20420899-1	2010	Glucose-6-phosphate dehydrogenase (G6PD) plays a key role in the regeneration of NADPH and maintenance of cellular redox balance.	NADP	81-86	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
20420899-1	2010	Glucose-6-phosphate dehydrogenase (G6PD) plays a key role in the regeneration of NADPH and maintenance of cellular redox balance.	NADP	81-86	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
20216965-2	2009	The enzymatic glucose assay involves the two-step oxidation of glucose, which was catalyzed by hexokinase and glucose-6-phosphate dehydrogenase, with the concomitant reduction of NADP(+) to NADPH.	NADP	179-186	glucose-6-phosphate dehydrogenase	Homo sapiens	110-143	
20216965-2	2009	The enzymatic glucose assay involves the two-step oxidation of glucose, which was catalyzed by hexokinase and glucose-6-phosphate dehydrogenase, with the concomitant reduction of NADP(+) to NADPH.	NADP	190-195	glucose-6-phosphate dehydrogenase	Homo sapiens	110-143	
19465117-1	2009	Human glucose 6-phosphate dehydrogenase (G6PD) has both the "catalytic" NADP(+) site and a "structural" NADP(+) site where a number of severe G6PD deficiency mutations are located.	NADP	104-108	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
19465117-1	2009	Human glucose 6-phosphate dehydrogenase (G6PD) has both the "catalytic" NADP(+) site and a "structural" NADP(+) site where a number of severe G6PD deficiency mutations are located.	NADP	104-108	glucose-6-phosphate dehydrogenase	Homo sapiens	41-45	
19284595-1	2009	BACKGROUND: Human glucose 6-phosphate dehydrogenase (G6PD), active in both dimer and tetramer forms, is the key entry enzyme in the pentose phosphate pathway (PPP), providing NADPH for biosynthesis and various other purposes, including protection against oxidative stress in erythrocytes.	NADP	175-180	glucose-6-phosphate dehydrogenase	Homo sapiens	18-51	
19284595-1	2009	BACKGROUND: Human glucose 6-phosphate dehydrogenase (G6PD), active in both dimer and tetramer forms, is the key entry enzyme in the pentose phosphate pathway (PPP), providing NADPH for biosynthesis and various other purposes, including protection against oxidative stress in erythrocytes.	NADP	175-180	glucose-6-phosphate dehydrogenase	Homo sapiens	53-57	
19284595-9	2009	CONCLUSION: L-Arg is the key player in the refolding of human G6PD, preventing the aggregation of folding intermediate, and NADP+ is essential for the folding intermediate to adopt native structure.	NADP	124-129	glucose-6-phosphate dehydrogenase	Homo sapiens	62-66	
18335175-2	2008	We have determined glucose and 1,5-AG, based on glucokinase (GK) converting glucose to G6P, a compound that can be catalyzed ultimately into 6-PGA by G-6PD and its coenzyme NADP(+), and then calculated glucose concentration according to absorbance variety.	NADP	173-177	glucose-6-phosphate dehydrogenase	Homo sapiens	150-155	
18549810-1	2008	BACKGROUND: Glucose-6-phosphate dehydrogenase (G6PD) is a cytosolic enzyme encoded by a housekeeping X-linked gene whose main function is to produce NADPH, a key electron donor in the defence against oxidizing agents and in reductive biosynthetic reactions.	NADP	149-154	glucose-6-phosphate dehydrogenase	Homo sapiens	12-45	
18549810-1	2008	BACKGROUND: Glucose-6-phosphate dehydrogenase (G6PD) is a cytosolic enzyme encoded by a housekeeping X-linked gene whose main function is to produce NADPH, a key electron donor in the defence against oxidizing agents and in reductive biosynthetic reactions.	NADP	149-154	glucose-6-phosphate dehydrogenase	Homo sapiens	47-51	
18392752-4	2008	The G6PD phenotype was determined by measuring the enzyme activity in erythrocytes, as the absorbance rate change due to NADPH reduction.	NADP	121-126	glucose-6-phosphate dehydrogenase	Homo sapiens	4-8	
18493020-0	2008	What is the role of the second "structural" NADP+-binding site in human glucose 6-phosphate dehydrogenase?	NADP	44-49	glucose-6-phosphate dehydrogenase	Homo sapiens	72-105	
18493020-1	2008	Human glucose 6-phosphate dehydrogenase, purified after overexpression in E. coli, was shown to contain one molecule/subunit of acid-extractable "structural" NADP+ and no NADPH.	NADP	158-163	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
18493020-10	2008	Human G6PD thus forms active dimer without structural NADP+.	NADP	54-59	glucose-6-phosphate dehydrogenase	Homo sapiens	6-10	
18493020-14	2008	Preparation of native apoenzyme and measurement of Kd constant for structural NADP+ will now allow quantitative assessment of this defect in clinical G6PD mutations.	NADP	78-83	glucose-6-phosphate dehydrogenase	Homo sapiens	150-154	
19918114-1	2008	BACKGROUND/AIMS: The enzyme glucose-6-phosphate dehydrogenase (G6PD) is the principal source of reducing equivalents, necessary for regenerating reduced glutathione through NADPH in order to protect cells from oxidative damage, and whichin erythrocytes produces hemolysis.	NADP	173-178	glucose-6-phosphate dehydrogenase	Homo sapiens	28-61	
18313308-0	2008	Catechin gallates are NADP+-competitive inhibitors of glucose-6-phosphate dehydrogenase and other enzymes that employ NADP+ as a coenzyme.	NADP	22-27	glucose-6-phosphate dehydrogenase	Homo sapiens	54-87	
18313308-0	2008	Catechin gallates are NADP+-competitive inhibitors of glucose-6-phosphate dehydrogenase and other enzymes that employ NADP+ as a coenzyme.	NADP	118-123	glucose-6-phosphate dehydrogenase	Homo sapiens	54-87	
18313308-2	2008	In this study, we used in silico and conventional screening approaches to identify putative inhibitors of G6PD and found that gallated catechins (EGCG, GCG, ECG, CG), but not ungallated catechins (ECG, GC, EC, C), were NADP(+)-competitive inhibitors of G6PD and other enzymes that employ NADP(+) as a coenzyme, such as IDH and 6PGD.	NADP	219-226	glucose-6-phosphate dehydrogenase	Homo sapiens	106-110	
18313308-2	2008	In this study, we used in silico and conventional screening approaches to identify putative inhibitors of G6PD and found that gallated catechins (EGCG, GCG, ECG, CG), but not ungallated catechins (ECG, GC, EC, C), were NADP(+)-competitive inhibitors of G6PD and other enzymes that employ NADP(+) as a coenzyme, such as IDH and 6PGD.	NADP	288-295	glucose-6-phosphate dehydrogenase	Homo sapiens	106-110	
19918114-1	2008	BACKGROUND/AIMS: The enzyme glucose-6-phosphate dehydrogenase (G6PD) is the principal source of reducing equivalents, necessary for regenerating reduced glutathione through NADPH in order to protect cells from oxidative damage, and whichin erythrocytes produces hemolysis.	NADP	173-178	glucose-6-phosphate dehydrogenase	Homo sapiens	63-67	
17137780-2	2007	The principle of the determination scheme is as follows: G6PDH catalyzes the specific dehydrogenation of glucose-6-phosphate by consuming NADP(+).	NADP	138-145	glucose-6-phosphate dehydrogenase	Homo sapiens	57-62	
17852823-9	2008	CONCLUSION: Red blood cell G(6)PD activity in athletes may be reduced post-race as a consequence of the modulation of NADP/NADPH levels and elevation of the erythrocyte GSSG, and especially GSSG/GSH ratio, resulting in an impairment of the hexose monophosphate shunt.	NADP	118-122	glucose-6-phosphate dehydrogenase	Homo sapiens	27-33	
17852823-9	2008	CONCLUSION: Red blood cell G(6)PD activity in athletes may be reduced post-race as a consequence of the modulation of NADP/NADPH levels and elevation of the erythrocyte GSSG, and especially GSSG/GSH ratio, resulting in an impairment of the hexose monophosphate shunt.	NADP	123-128	glucose-6-phosphate dehydrogenase	Homo sapiens	27-33	
17637841-5	2007	Two of the three mutated amino acids of G6PD Vancouver are closer to the binding site of NADP(+).	NADP	89-96	glucose-6-phosphate dehydrogenase	Homo sapiens	40-44	
17637841-6	2007	The G6PD Aachen mutation is also closer to the second NADP(+) unit.	NADP	54-61	glucose-6-phosphate dehydrogenase	Homo sapiens	4-8	
17452057-5	2007	In this review, we will discuss the possible roles of cellular NADP(+)/NADPH, which function as redox potential regulators, in the induction of obesity-associated oxidative stress, chronic inflammation, and insulin resistance and suggest G6PD, a NADPH-generating enzyme, as a novel target for treating metabolic disorders.	NADP	63-70	glucose-6-phosphate dehydrogenase	Homo sapiens	238-242	
16934959-1	2006	Two severe Class I human glucose-6-phosphate dehydrogenase (G6PD, EC1.1.1.49) mutations, G6PD(Wisconsin) (nt1177 C-->G, R393G) and G6PD(Nashville) (nt1178 G-->A, R393H), affect the same codon, altering a residue in the dimer interface close to the "structural" NADP+ site.	NADP	267-272	glucose-6-phosphate dehydrogenase	Homo sapiens	60-64	
17157446-1	2007	Glucose 6-phosphate dehydrogenase (G6PD) plays an important role in ruminant"s lipogenesis, as it provides necessary compounds of NADPH for the synthesis of fatty acids catalyzing the first committed reaction in the pentose phosphate pathway.	NADP	130-135	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
17157446-1	2007	Glucose 6-phosphate dehydrogenase (G6PD) plays an important role in ruminant"s lipogenesis, as it provides necessary compounds of NADPH for the synthesis of fatty acids catalyzing the first committed reaction in the pentose phosphate pathway.	NADP	130-135	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
17623517-1	2007	Glucose-6-phosphate dehydrogenase (G6PD), the first and rate-limiting enzyme of the pentose phosphate pathway, is indispensable to maintenance of the cytosolic pool of NADPH and thus the cellular redox balance.	NADP	168-173	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
17623517-1	2007	Glucose-6-phosphate dehydrogenase (G6PD), the first and rate-limiting enzyme of the pentose phosphate pathway, is indispensable to maintenance of the cytosolic pool of NADPH and thus the cellular redox balance.	NADP	168-173	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	NADP	22-65	glucose-6-phosphate dehydrogenase	Homo sapiens	186-219	
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	NADP	67-74	glucose-6-phosphate dehydrogenase	Homo sapiens	186-219	
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	NADP	67-71	glucose-6-phosphate dehydrogenase	Homo sapiens	186-219	
17047791-1	2006	The coimmobilization of nitrobenzene nitroreductase and glucose-6-phosphate dehydrogenase in silica particles enables the continuous conversion of nitrobenzene to hydroxylaminobenzene with NADPH recycling.	NADP	189-194	glucose-6-phosphate dehydrogenase	Homo sapiens	56-89	
16934959-5	2006	However, investigations of thermostability, urea denaturation, protease digestion, and hydrophobic exposure demonstrated that G6PD R393H is less stable than normal G6PD or R393G, and stability was more NADP+-dependent.	NADP	202-207	glucose-6-phosphate dehydrogenase	Homo sapiens	126-130	
16934959-7	2006	Again the G6PD(Nashville) protein was markedly less stable, and its dissociation constant for "structural" NADP+ is approximately 500 nM, about 10 times higher than values for R393G (53 nM) and normal G6PD (37 nM).	NADP	107-112	glucose-6-phosphate dehydrogenase	Homo sapiens	10-14	
16934959-8	2006	These results, together with structural information, suggest that the instability of the R393H protein, enhanced by the weakened binding of "structural" NADP+, is the likely cause of the severe clinical manifestation observed for G6PD(Nashville).	NADP	153-158	glucose-6-phosphate dehydrogenase	Homo sapiens	230-234	
16607506-6	2006	Moreover, functional analysis of the human G6PD variants showed the following: (1) The charge property, polarity, pK-radical and side-chain radical of the substituting amino acid have an effect on G6PD activity, (2) The G6PDArg459 and Arg463 play important roles in anchoring NADP+ to the catalytic domain to maintain the enzymatic activity, and (3) The sequence from codon 459 to the carboxyl terminal is essential for the enzymatic function.	NADP	276-281	glucose-6-phosphate dehydrogenase	Homo sapiens	43-47	
16607506-6	2006	Moreover, functional analysis of the human G6PD variants showed the following: (1) The charge property, polarity, pK-radical and side-chain radical of the substituting amino acid have an effect on G6PD activity, (2) The G6PDArg459 and Arg463 play important roles in anchoring NADP+ to the catalytic domain to maintain the enzymatic activity, and (3) The sequence from codon 459 to the carboxyl terminal is essential for the enzymatic function.	NADP	276-281	glucose-6-phosphate dehydrogenase	Homo sapiens	197-201	
16789437-4	2006	In this study G-6-PD from lamb kidney cortex was competitively inhibited by zinc both with respect to glucose-6-phosphate (G-6-P) and NADP+ with Ki values of 1.066 +/- 0.106 and 0.111 +/- 0.007 mM respectively whereas cadmium was a non-competitive inhibitor with respect to both G-6-P and NADP+ Ki values of 2.028 +/- 0.175 and 2.044 +/- 0.289 mM respectively.	NADP	134-139	glucose-6-phosphate dehydrogenase	Homo sapiens	14-20	
16789437-4	2006	In this study G-6-PD from lamb kidney cortex was competitively inhibited by zinc both with respect to glucose-6-phosphate (G-6-P) and NADP+ with Ki values of 1.066 +/- 0.106 and 0.111 +/- 0.007 mM respectively whereas cadmium was a non-competitive inhibitor with respect to both G-6-P and NADP+ Ki values of 2.028 +/- 0.175 and 2.044 +/- 0.289 mM respectively.	NADP	134-138	glucose-6-phosphate dehydrogenase	Homo sapiens	14-20	
15752725-3	2005	C-3 epimerization activity was detected using a NADPH-generating system containing glucose-6-phosphate, NADP, glucose-6-phosphate dehydrogenase, and Mg(2+).	NADP	48-52	glucose-6-phosphate dehydrogenase	Homo sapiens	110-143	
16461898-3	2006	We previously found that avoidance of NADPH depletion during the pulses of oxidative load to which erythrocytes are normally exposed is the main functional requirement mediating selection for high glucose-6-phosphate dehydrogenase activity.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	197-230	
16323551-1	2005	The major role of glucose-6-phosphate dehydrogenase (G6PD) is to generate reduced nicotinamide adenine dinucleotide phosphate (NADPH), which is indispensable to reductive metabolism and maintenance of cellular redox homeostasis.	NADP	82-125	glucose-6-phosphate dehydrogenase	Homo sapiens	18-51	
16323551-1	2005	The major role of glucose-6-phosphate dehydrogenase (G6PD) is to generate reduced nicotinamide adenine dinucleotide phosphate (NADPH), which is indispensable to reductive metabolism and maintenance of cellular redox homeostasis.	NADP	82-125	glucose-6-phosphate dehydrogenase	Homo sapiens	53-57	
16323551-1	2005	The major role of glucose-6-phosphate dehydrogenase (G6PD) is to generate reduced nicotinamide adenine dinucleotide phosphate (NADPH), which is indispensable to reductive metabolism and maintenance of cellular redox homeostasis.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	18-51	
16323551-1	2005	The major role of glucose-6-phosphate dehydrogenase (G6PD) is to generate reduced nicotinamide adenine dinucleotide phosphate (NADPH), which is indispensable to reductive metabolism and maintenance of cellular redox homeostasis.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	53-57	
15752725-3	2005	C-3 epimerization activity was detected using a NADPH-generating system containing glucose-6-phosphate, NADP, glucose-6-phosphate dehydrogenase, and Mg(2+).	NADP	48-53	glucose-6-phosphate dehydrogenase	Homo sapiens	110-143	
15774558-2	2005	It is distinct from the cytosolic enzyme, glucose-6-phosphate dehydrogenase (G6PDH), using a separate pool of NAD(P)+ and capable of oxidizing several phosphorylated hexoses.	NADP	110-117	glucose-6-phosphate dehydrogenase	Homo sapiens	42-75	
15774558-2	2005	It is distinct from the cytosolic enzyme, glucose-6-phosphate dehydrogenase (G6PDH), using a separate pool of NAD(P)+ and capable of oxidizing several phosphorylated hexoses.	NADP	110-117	glucose-6-phosphate dehydrogenase	Homo sapiens	77-82	
15858258-0	2005	Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.	NADP	46-51	glucose-6-phosphate dehydrogenase	Homo sapiens	69-102	
15858258-1	2005	Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt.	NADP	50-57	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
15858258-1	2005	Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt.	NADP	50-57	glucose-6-phosphate dehydrogenase	Homo sapiens	41-45	
15858258-3	2005	The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site.	NADP	129-133	glucose-6-phosphate dehydrogenase	Homo sapiens	100-104	
15858258-3	2005	The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site.	NADP	129-133	glucose-6-phosphate dehydrogenase	Homo sapiens	106-118	
15858258-5	2005	NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes.	NADP	65-72	glucose-6-phosphate dehydrogenase	Homo sapiens	101-105	
15858258-8	2005	Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered.	NADP	11-15	glucose-6-phosphate dehydrogenase	Homo sapiens	59-63	
15858258-8	2005	Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered.	NADP	64-68	glucose-6-phosphate dehydrogenase	Homo sapiens	59-63	
15858258-8	2005	Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered.	NADP	64-68	glucose-6-phosphate dehydrogenase	Homo sapiens	59-63	
15858258-8	2005	Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered.	NADP	64-68	glucose-6-phosphate dehydrogenase	Homo sapiens	59-63	
15128828-3	2004	NADPH is produced by glucose-6-phosphate dehydrogenase (G-6-PDase) and 6-phosphogluconate dehydrogenase (6-PGDase), which are the first two steps of the hexose monophosphate shunt (HMS).	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	21-54	
15542105-3	2004	Considering the importance of G6PD reaction and its products NADPH and glutathione (GSH) against oxidative stress, we hypothesized the failure of detoxification of H(2)O(2) in G6PD-deficient white blood cells that could probably induce primary DNA damage.	NADP	61-66	glucose-6-phosphate dehydrogenase	Homo sapiens	30-34	
15358777-9	2004	We suggest that the DPI-elicited inhibition of the pentose phosphate pathway and tricarboxylic acid cycle may be mediated by the blockade of several NAD(P)-dependent enzymes, such as glucose 6-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase, and lactate dehydrogenase.	NADP	149-155	glucose-6-phosphate dehydrogenase	Homo sapiens	183-216	
15506519-1	2004	Glucose 6-phosphate dehydrogenase (G6PD) catalyses the first step of the pentose phosphate pathway, which in the RBC leads to the formation of NADPH, essential to prevent the cell from an oxidative stress.	NADP	143-148	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
15506519-1	2004	Glucose 6-phosphate dehydrogenase (G6PD) catalyses the first step of the pentose phosphate pathway, which in the RBC leads to the formation of NADPH, essential to prevent the cell from an oxidative stress.	NADP	143-148	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
15128828-3	2004	NADPH is produced by glucose-6-phosphate dehydrogenase (G-6-PDase) and 6-phosphogluconate dehydrogenase (6-PGDase), which are the first two steps of the hexose monophosphate shunt (HMS).	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	56-65	
15242018-7	2004	Examination of substrate level effect found that BCFA slightly inhibited fatty acid synthetase and acetyl-CoA carboxylase, and significantly the glucose-6-phosphate dehydrogenase which was the main NADPH generating system in breast cancer cells.	NADP	198-203	glucose-6-phosphate dehydrogenase	Homo sapiens	145-178	
15177053-2	2004	DHEA is a potent uncompetitive inhibitor of mammalian glucose-6-phosphate dehydrogenase (G6PDH) and as a consequence lowers NADPH levels and reduces NADPH-dependent oxygen-free radical production.	NADP	124-129	glucose-6-phosphate dehydrogenase	Homo sapiens	54-87	
15177053-2	2004	DHEA is a potent uncompetitive inhibitor of mammalian glucose-6-phosphate dehydrogenase (G6PDH) and as a consequence lowers NADPH levels and reduces NADPH-dependent oxygen-free radical production.	NADP	124-129	glucose-6-phosphate dehydrogenase	Homo sapiens	89-94	
15177053-2	2004	DHEA is a potent uncompetitive inhibitor of mammalian glucose-6-phosphate dehydrogenase (G6PDH) and as a consequence lowers NADPH levels and reduces NADPH-dependent oxygen-free radical production.	NADP	149-154	glucose-6-phosphate dehydrogenase	Homo sapiens	89-94	
15322329-3	2004	G6PD activity was assessed based on the spectrophotometric determination of generated NADPH.	NADP	86-91	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
14980702-1	2004	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of cellular redox balance.	NADP	82-125	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
14980702-1	2004	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of cellular redox balance.	NADP	82-125	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
14980702-1	2004	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of cellular redox balance.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
14980702-1	2004	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of cellular redox balance.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
14614139-4	2003	G6PD catalyses the first step of the pathway that supplies NADPH for antioxidant defense mechanisms.	NADP	59-64	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
14614139-8	2003	Our analysis indicates that normal G6PD activity is sufficient but not superfluous to avoid NADPH depletion and ensure timely adaptation of the NADPH supply during pulses of oxidative load such as those that occur during adherence of erythrocytes to phagocytes.	NADP	92-97	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
14614139-8	2003	Our analysis indicates that normal G6PD activity is sufficient but not superfluous to avoid NADPH depletion and ensure timely adaptation of the NADPH supply during pulses of oxidative load such as those that occur during adherence of erythrocytes to phagocytes.	NADP	144-149	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
14637108-6	2003	The activity of glucose-6-phosphate dehydrogenase involved in the maintenance of the NADPH that can be used for the regeneration of the GSH pool, was increased by infection with amplicon vectors.	NADP	85-90	glucose-6-phosphate dehydrogenase	Homo sapiens	16-49	
12466018-3	2003	Under normal growth conditions, ES G6pd delta cells show a high ratio of NADPH to NADP(+) and a normal intracellular level of GSH.	NADP	73-78	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
12552364-2	2003	High glucose concentrations may, however, impair the production of O(2)(-) through inhibition of glucose-6-phosphate dehydrogenase (G6PD), which catalyzes the formation of NADPH.	NADP	172-177	glucose-6-phosphate dehydrogenase	Homo sapiens	97-130	
12552364-2	2003	High glucose concentrations may, however, impair the production of O(2)(-) through inhibition of glucose-6-phosphate dehydrogenase (G6PD), which catalyzes the formation of NADPH.	NADP	172-177	glucose-6-phosphate dehydrogenase	Homo sapiens	132-136	
12791063-6	2003	As the new method is both qualitative and quantitative, it is possible to express G6PD activity as increase of NADPH concentration by reading absorbance at 460 nm after incubation for 30 or 60 min.	NADP	111-116	glucose-6-phosphate dehydrogenase	Homo sapiens	82-86	
12956017-1	2003	BACKGROUND: Glucose-6-phosphate dehydrogenase (G-6-PD) is an enzyme in the first step of the hexose-monophosphate shunt required for the generation of nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	151-194	glucose-6-phosphate dehydrogenase	Homo sapiens	12-45	
12956017-1	2003	BACKGROUND: Glucose-6-phosphate dehydrogenase (G-6-PD) is an enzyme in the first step of the hexose-monophosphate shunt required for the generation of nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	151-194	glucose-6-phosphate dehydrogenase	Homo sapiens	47-53	
12956017-1	2003	BACKGROUND: Glucose-6-phosphate dehydrogenase (G-6-PD) is an enzyme in the first step of the hexose-monophosphate shunt required for the generation of nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	196-201	glucose-6-phosphate dehydrogenase	Homo sapiens	12-45	
12956017-1	2003	BACKGROUND: Glucose-6-phosphate dehydrogenase (G-6-PD) is an enzyme in the first step of the hexose-monophosphate shunt required for the generation of nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	196-201	glucose-6-phosphate dehydrogenase	Homo sapiens	47-53	
12466018-3	2003	Under normal growth conditions, ES G6pd delta cells show a high ratio of NADPH to NADP(+) and a normal intracellular level of GSH.	NADP	73-77	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
11788599-1	2002	Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the oxidative pentose phosphate cycle, regulates the NADPH/NADP(+) ratio in eukaryotic cells.	NADP	123-127	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
11997374-7	2002	The recycling of NADPH from NADP(+) can be carried out in peroxisomes by three dehydrogenases: glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and isocitrate dehydrogenase.	NADP	17-22	glucose-6-phosphate dehydrogenase	Homo sapiens	95-128	
11997374-7	2002	The recycling of NADPH from NADP(+) can be carried out in peroxisomes by three dehydrogenases: glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and isocitrate dehydrogenase.	NADP	28-35	glucose-6-phosphate dehydrogenase	Homo sapiens	95-128	
14509567-0	2003	Glucose-6-phosphate dehydrogenase expression associated with NADPH-dependent reactions in cerebellar neurons.	NADP	61-66	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
14509567-4	2003	The results show that cerebellar G6PD activity changes with different neuron types as a function of its role in sustaining NADPH dependent pathways in these cells.	NADP	123-128	glucose-6-phosphate dehydrogenase	Homo sapiens	33-37	
12102606-3	2002	We hypothesized that the clinical problems associated with sarcoidosis might be related to a decreased anti-oxidant defence and we therefore measured the activity of the NADPH-generating enzyme glucose-6-phosphate dehydrogenase (G6PD), the GSH-regenerating enzyme glutathione reductase (GR) and indirectly the level of NADPH in red blood cells from patients with sarcoidosis.	NADP	170-175	glucose-6-phosphate dehydrogenase	Homo sapiens	194-227	
12102606-3	2002	We hypothesized that the clinical problems associated with sarcoidosis might be related to a decreased anti-oxidant defence and we therefore measured the activity of the NADPH-generating enzyme glucose-6-phosphate dehydrogenase (G6PD), the GSH-regenerating enzyme glutathione reductase (GR) and indirectly the level of NADPH in red blood cells from patients with sarcoidosis.	NADP	170-175	glucose-6-phosphate dehydrogenase	Homo sapiens	229-233	
12102606-3	2002	We hypothesized that the clinical problems associated with sarcoidosis might be related to a decreased anti-oxidant defence and we therefore measured the activity of the NADPH-generating enzyme glucose-6-phosphate dehydrogenase (G6PD), the GSH-regenerating enzyme glutathione reductase (GR) and indirectly the level of NADPH in red blood cells from patients with sarcoidosis.	NADP	319-324	glucose-6-phosphate dehydrogenase	Homo sapiens	194-227	
11788599-1	2002	Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the oxidative pentose phosphate cycle, regulates the NADPH/NADP(+) ratio in eukaryotic cells.	NADP	123-128	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
11788599-1	2002	Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the oxidative pentose phosphate cycle, regulates the NADPH/NADP(+) ratio in eukaryotic cells.	NADP	123-128	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
12108790-5	2002	G6PD and HK enzyme activities were measured spectrophotometrically via absorbance change (at 340 nm) in NADPH formed as a result of the reactions catalysed by these enzymes.	NADP	104-109	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
11788599-1	2002	Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the oxidative pentose phosphate cycle, regulates the NADPH/NADP(+) ratio in eukaryotic cells.	NADP	123-127	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
11852566-1	2002	Inactivation of glucose 6-phosphate dehydrogenase (G6PDH) complexed with its substrate, glucose 6-phosphate (GP), and/or cofactor, NADP+, has been studied within the range 20-40 degrees C in three media: (a) 0.04 M NaOH-glycine buffer (pH 9.1); (b) Aerosol OT (AOT) reversed micelles in octane; and (c) Triton X-100 micelles in octane supplemented with 10% hexanol.	NADP	131-135	glucose-6-phosphate dehydrogenase	Homo sapiens	16-49	
11787865-4	2002	DNA studies indicate that the mutation was G6PD Guadalajara 1159 C --> T (387 Arg --> Cys) that is situated at the NADP binding site.	NADP	121-125	glucose-6-phosphate dehydrogenase	Homo sapiens	43-47	
11852566-1	2002	Inactivation of glucose 6-phosphate dehydrogenase (G6PDH) complexed with its substrate, glucose 6-phosphate (GP), and/or cofactor, NADP+, has been studied within the range 20-40 degrees C in three media: (a) 0.04 M NaOH-glycine buffer (pH 9.1); (b) Aerosol OT (AOT) reversed micelles in octane; and (c) Triton X-100 micelles in octane supplemented with 10% hexanol.	NADP	131-135	glucose-6-phosphate dehydrogenase	Homo sapiens	51-56	
11852566-3	2002	In the case of G6PDH-NADP+ complexes, the values of kin were independent of the initial concentrations of G6PDH, either in aqueous medium or AOT micelles.	NADP	21-26	glucose-6-phosphate dehydrogenase	Homo sapiens	15-20	
11852566-3	2002	In the case of G6PDH-NADP+ complexes, the values of kin were independent of the initial concentrations of G6PDH, either in aqueous medium or AOT micelles.	NADP	21-26	glucose-6-phosphate dehydrogenase	Homo sapiens	106-111	
11463792-7	2001	The generation of reduced glutathione requires NADPH, and we therefore examined the activity and expression of the rate-limiting enzyme in NADPH production, glucose-6-phosphate dehydrogenase (G6PD).	NADP	139-144	glucose-6-phosphate dehydrogenase	Homo sapiens	157-190	
11718577-6	2001	Hofbauer cell G6PD may play a role in placental defense, by supplying NADPH-dependent enzymes (i.e. nitric oxide synthase or NADPH oxidase) with NADPH.	NADP	70-75	glucose-6-phosphate dehydrogenase	Homo sapiens	14-18	
11718577-6	2001	Hofbauer cell G6PD may play a role in placental defense, by supplying NADPH-dependent enzymes (i.e. nitric oxide synthase or NADPH oxidase) with NADPH.	NADP	125-130	glucose-6-phosphate dehydrogenase	Homo sapiens	14-18	
11763298-6	2001	G6PD generates nicotinamide adenine dinucleotide phosphate (NADPH), a co-factor in the synthesis of nitric oxide.	NADP	15-58	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
11763298-6	2001	G6PD generates nicotinamide adenine dinucleotide phosphate (NADPH), a co-factor in the synthesis of nitric oxide.	NADP	60-65	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
11444838-4	2001	NADP, a coenzyme of glucose-6-phosphate dehydrogenase, also releases its folding intermediates from GroEL and increases reactivation.	NADP	0-4	glucose-6-phosphate dehydrogenase	Homo sapiens	20-53	
11440553-1	2001	We examined the ultrastructural localization of glucose-6-phosphate dehydrogenase (G6PD), a NADPH-generating enzyme, in human fetal membranes at various gestational ages, using newly developed enzyme histochemistry (copper-ferrocyanide method).	NADP	92-97	glucose-6-phosphate dehydrogenase	Homo sapiens	48-81	
11440553-1	2001	We examined the ultrastructural localization of glucose-6-phosphate dehydrogenase (G6PD), a NADPH-generating enzyme, in human fetal membranes at various gestational ages, using newly developed enzyme histochemistry (copper-ferrocyanide method).	NADP	92-97	glucose-6-phosphate dehydrogenase	Homo sapiens	83-87	
11440553-5	2001	Chorion laeve trophoblast G6PD may play a significant role in fetal membrane physiology, by delivering NADPH to NADPH-dependent oxidoreductases which these cells possess.	NADP	103-108	glucose-6-phosphate dehydrogenase	Homo sapiens	26-30	
11245448-11	2001	Treatment with 1,25(OH)2D3 resulted in a approximately 40% increase in glucose-6-phosphate dehydrogenase, the rate-limiting enzyme in the generation of NADPH.	NADP	152-157	glucose-6-phosphate dehydrogenase	Homo sapiens	71-104	
11376568-3	2001	The major role of G6PD is to generate NADPH to protect cells from oxidative damage, which is a major contributing factor to certain degenerative diseases, such as aging and cancer.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	18-22	
11311853-11	2001	Human placental glucose-6-phosphate dehydrogenase was inhibited competitively by 2,3-diphosphoglycerate (K(i)=15+/-3 mM) and NADPH (K(i)=17.1+/-3.2 microM).	NADP	125-130	glucose-6-phosphate dehydrogenase	Homo sapiens	16-49	
11311853-12	2001	The small dissociation constant for the G6PD:NADPH complex pointed to tight enzyme:NADPH binding and the important role of NADPH in the regulation of the pentose phosphate pathway.	NADP	45-50	glucose-6-phosphate dehydrogenase	Homo sapiens	40-44	
11311853-12	2001	The small dissociation constant for the G6PD:NADPH complex pointed to tight enzyme:NADPH binding and the important role of NADPH in the regulation of the pentose phosphate pathway.	NADP	83-88	glucose-6-phosphate dehydrogenase	Homo sapiens	40-44	
11311853-12	2001	The small dissociation constant for the G6PD:NADPH complex pointed to tight enzyme:NADPH binding and the important role of NADPH in the regulation of the pentose phosphate pathway.	NADP	83-88	glucose-6-phosphate dehydrogenase	Homo sapiens	40-44	
10745013-0	2000	Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency.	NADP	84-91	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
11261854-2	2001	The sucrose electrode is based on the tri-enzymatic system of sucrose phosphorylase, phosphoglucomutase and glucose-6-phosphate 1-dehydrogenase, where NAD(P)H is produced from the last enzymatic reaction and recycled into NAD(P)+ through its electrocatalytic oxidation by Os(4,4"-dimethyl-2,2-bypyridine)2(1,10-phenanthroline-5,6-dione).	NADP	222-229	glucose-6-phosphate dehydrogenase	Homo sapiens	108-143	
10698963-1	2000	Glucose 6-phosphate dehydrogenase (G6PD) is a cytosolic enzyme encoded by a housekeeping X-linked gene whose main function is to produce NADPH, a key electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions.	NADP	137-142	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
11007790-3	2000	Glucose-6-phosphate dehydrogenase (G6PD) plays an essential role in the regulation of oxidative stress by primarily regulating NADPH, the main intracellular reductant.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
11007790-3	2000	Glucose-6-phosphate dehydrogenase (G6PD) plays an essential role in the regulation of oxidative stress by primarily regulating NADPH, the main intracellular reductant.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
11120643-8	2000	Given that G6PDH and GR are the most significant NADPH producers and consumers in the liver, respectively, and that GR is responsible for recycling the free radical scavenger glutathione, these data are consistent with the notion that hepatic metabolic changes are in part due to the induction of liver antioxidant defenses.	NADP	49-54	glucose-6-phosphate dehydrogenase	Homo sapiens	11-16	
10980404-1	2000	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of the cellular redox balance.	NADP	82-125	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
10980404-1	2000	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of the cellular redox balance.	NADP	82-125	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
10980404-1	2000	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of the cellular redox balance.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
10980404-1	2000	Glucose-6-phosphate dehydrogenase (G6PD) is involved in the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and the maintenance of the cellular redox balance.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
10698963-1	2000	Glucose 6-phosphate dehydrogenase (G6PD) is a cytosolic enzyme encoded by a housekeeping X-linked gene whose main function is to produce NADPH, a key electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions.	NADP	137-142	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
10745013-7	2000	Despite very similar dimer topology, there are two major differences from G6PD of Leuconostoc mesenteroides: a structural NADP(+) molecule, close to the dimer interface but integral to the subunit, is visible in all subunits of the human enzyme; and an intrasubunit disulphide bond tethers the otherwise disordered N-terminal segment.	NADP	122-126	glucose-6-phosphate dehydrogenase	Homo sapiens	74-78	
9915806-1	1999	Glucose-6-phosphate dehydrogenase (G6PD) is the key enzyme of the pentose phosphate pathway that is responsible for the generation of NADPH, which is required in many detoxifying reactions.	NADP	134-139	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
10329961-2	1999	The principal intracellular reductant NADPH is mainly produced by the pentose phosphate pathway by glucose-6-phosphate dehydrogenase (G6PDH), the rate-limiting enzyme, and by 6-phosphogluconate dehydrogenase.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	99-132	
10329961-2	1999	The principal intracellular reductant NADPH is mainly produced by the pentose phosphate pathway by glucose-6-phosphate dehydrogenase (G6PDH), the rate-limiting enzyme, and by 6-phosphogluconate dehydrogenase.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	134-139	
10329961-3	1999	Considering the importance of NADPH, we hypothesized that G6PDH plays a critical role in cell death.	NADP	30-35	glucose-6-phosphate dehydrogenase	Homo sapiens	58-63	
10556177-3	1999	In cultured skin fibroblasts, G6PD activity was approximately 15% of normal, with 4- to 5-fold increased Michaelis constant (Km) for NADP and for glucose 6-phosphate.	NADP	133-137	glucose-6-phosphate dehydrogenase	Homo sapiens	30-34	
9915806-1	1999	Glucose-6-phosphate dehydrogenase (G6PD) is the key enzyme of the pentose phosphate pathway that is responsible for the generation of NADPH, which is required in many detoxifying reactions.	NADP	134-139	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
9553122-2	1998	The principal intracellular reductant is NADPH, which is mainly produced by the pentose phosphate pathway through the actions of glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the pentose phosphate pathway, and by 6-phosphogluconate dehydrogenase.	NADP	41-46	glucose-6-phosphate dehydrogenase	Homo sapiens	129-162	
9553122-4	1998	In this article, we suggest that G6PD activity plays a critical role in cell growth by providing NADPH for redox regulation.	NADP	97-102	glucose-6-phosphate dehydrogenase	Homo sapiens	33-37	
9565698-8	1998	It was suggested from the simulation study that GSSG reductase is more important than G6PD in determining the rate of the NADPH-dependent H2O2 elimination.	NADP	122-127	glucose-6-phosphate dehydrogenase	Homo sapiens	86-90	
9553122-2	1998	The principal intracellular reductant is NADPH, which is mainly produced by the pentose phosphate pathway through the actions of glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the pentose phosphate pathway, and by 6-phosphogluconate dehydrogenase.	NADP	41-46	glucose-6-phosphate dehydrogenase	Homo sapiens	164-168	
9508091-3	1998	The reducing equivalents needed for regeneration of GSH through the action of glutathione reductase (GRD) are provided by NADPH, produced by the action of glucose-6-phosphate dehydrogenase (G6P-DH) on substrates glucose-6-phosphate and NADP+.	NADP	236-241	glucose-6-phosphate dehydrogenase	Homo sapiens	155-188	
9508091-3	1998	The reducing equivalents needed for regeneration of GSH through the action of glutathione reductase (GRD) are provided by NADPH, produced by the action of glucose-6-phosphate dehydrogenase (G6P-DH) on substrates glucose-6-phosphate and NADP+.	NADP	236-241	glucose-6-phosphate dehydrogenase	Homo sapiens	190-196	
9237246-13	1997	The capacity of the GPX/GRD system appears to be limited by the glucose-6-phosphate dehydrogenase-catalysed rate of production of NADPH, the required reductive substrate for GRD.	NADP	130-135	glucose-6-phosphate dehydrogenase	Homo sapiens	64-97	
9492308-0	1998	Amino acid substitutions at the dimer interface of human glucose-6-phosphate dehydrogenase that increase thermostability and reduce the stabilising effect of NADP.	NADP	158-162	glucose-6-phosphate dehydrogenase	Homo sapiens	57-90	
9492308-8	1998	NADP is known to exert a concentration dependent stabilising effect on the glucose-6-phosphate dehydrogenase dimer.	NADP	0-4	glucose-6-phosphate dehydrogenase	Homo sapiens	75-108	
9492308-10	1998	These results suggest that changes at the dimer interface can also affect the distant (> 20 A) NADP-binding site, and vice versa; an attempt has been made to explain these interactions based on the molecular model of human glucose-6-phosphate dehydrogenase.	NADP	98-102	glucose-6-phosphate dehydrogenase	Homo sapiens	226-259	
9392523-7	1997	In carcinomas, G6PDH levels are upregulated but the low Km values are kept to increase the NADPH production capacity required in cancer cells showing that posttranslational regulation processes are important to control cellular metabolism under various environmental conditions.	NADP	91-96	glucose-6-phosphate dehydrogenase	Homo sapiens	15-20	
8890580-4	1996	Glucose-6-phosphate dehydrogenase (G6PD) plays a key role in the generation of NADPH.	NADP	79-84	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
8890580-4	1996	Glucose-6-phosphate dehydrogenase (G6PD) plays a key role in the generation of NADPH.	NADP	79-84	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
8831947-8	1996	Thus the additional mutation in G6PD A(-) must be responsible for its increased affinity for NADP(+) when compared to G6PD A(+) from which it has been derived.	NADP	93-97	glucose-6-phosphate dehydrogenase	Homo sapiens	32-36	
8579052-11	1996	Molecular studies have disclosed that most of the class 1 G6PD variants associated with chronic hemolysis have the mutations surrounding either the substrate or the NADP binding site.	NADP	165-169	glucose-6-phosphate dehydrogenase	Homo sapiens	58-62	
7612656-5	1995	Km for glucose-6-phosphate (G6P) does not vary significantly with temperature, whereas Km for NADP increases at increasing temperature, kcat increases with temperature, with a break point at 35 degrees C (in human G6PD, the break point is at 15 degrees C).	NADP	94-98	glucose-6-phosphate dehydrogenase	Homo sapiens	214-218	
7654215-2	1995	Adrenaline has recently been shown to stimulate both glucose metabolism and H2O2 release by macrophages but the activity of the key pentose phosphate pathway enzyme, glucose-6-phosphate dehydrogenase (which generates the NADPH crucial for the reduction of molecular oxygen), was reduced under these conditions [Costa Rosa, Safi, Cury and Curi (1992) Biochem.	NADP	221-226	glucose-6-phosphate dehydrogenase	Homo sapiens	166-199	
7654215-5	1995	We report here that adrenaline activates another NADPH-producing enzyme, NADP(+)-dependent "malic" enzyme, while also inhibiting glucose-6-phosphate dehydrogenase, via cyclic AMP-dependent protein kinase (PKA) activation.	NADP	49-54	glucose-6-phosphate dehydrogenase	Homo sapiens	129-162	
7654215-5	1995	We report here that adrenaline activates another NADPH-producing enzyme, NADP(+)-dependent "malic" enzyme, while also inhibiting glucose-6-phosphate dehydrogenase, via cyclic AMP-dependent protein kinase (PKA) activation.	NADP	73-80	glucose-6-phosphate dehydrogenase	Homo sapiens	129-162	
7602782-1	1995	Glucose 6-phosphate dehydrogenase (G6PD) plays a key role in the generation of NADPH which is essential for maintaining glutathione in the reduce state, and in the production of ribose 5-phosphate for the synthesis of nucleotides.	NADP	79-84	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
7726568-3	1995	In order to elucidate the detailed mechanism of this rare type of inhibition, we examined the effects of steroids on human glucose 6-phosphate dehydrogenase catalyzing the reverse reaction, i.e., the reduction of the gluconolactone by NADPH.	NADP	235-240	glucose-6-phosphate dehydrogenase	Homo sapiens	123-156	
7602782-1	1995	Glucose 6-phosphate dehydrogenase (G6PD) plays a key role in the generation of NADPH which is essential for maintaining glutathione in the reduce state, and in the production of ribose 5-phosphate for the synthesis of nucleotides.	NADP	79-84	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
7785782-2	1995	The product NADPH of the reaction between glucose-6-phosphate and NADP+ catalyzed by glucose-6-phosphate dehydrogenase (G6PDH) is monitored.	NADP	12-17	glucose-6-phosphate dehydrogenase	Homo sapiens	85-118	
7785782-2	1995	The product NADPH of the reaction between glucose-6-phosphate and NADP+ catalyzed by glucose-6-phosphate dehydrogenase (G6PDH) is monitored.	NADP	12-17	glucose-6-phosphate dehydrogenase	Homo sapiens	120-125	
7785782-2	1995	The product NADPH of the reaction between glucose-6-phosphate and NADP+ catalyzed by glucose-6-phosphate dehydrogenase (G6PDH) is monitored.	NADP	66-71	glucose-6-phosphate dehydrogenase	Homo sapiens	85-118	
7785782-2	1995	The product NADPH of the reaction between glucose-6-phosphate and NADP+ catalyzed by glucose-6-phosphate dehydrogenase (G6PDH) is monitored.	NADP	66-71	glucose-6-phosphate dehydrogenase	Homo sapiens	120-125	
1651223-3	1991	Dehydroepiandrosterone (DHEA) is a normally occurring adrenal androgen that inhibits glucose-6-phosphate dehydrogenase, the initial enzyme in the pentose phosphate shunt necessary for NADPH generation and superoxide anion formation.	NADP	184-189	glucose-6-phosphate dehydrogenase	Homo sapiens	85-118	
8086463-5	1994	The unusually large N-terminus and the distance between the NADP-binding site and G6PD-binding site is novel for the parasite G6PD.	NADP	60-64	glucose-6-phosphate dehydrogenase	Homo sapiens	126-130	
8241497-6	1993	While this is one of the most drastic structural alterations found in G6PD variants, the region with the amino acid deletion was distant from both the G6P and NADP+ binding sites and was located in a domain with low sequence homology among species.	NADP	159-164	glucose-6-phosphate dehydrogenase	Homo sapiens	70-74	
7733451-6	1995	NADPH was regenerated by coupling the NR reaction with that catalyzed by glucose-6-phosphate dehydrogenase (GD).	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	73-106	
7803801-1	1995	Human erythrocytes contain a nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein, FX, whose levels are significantly increased in erythrocytes from glucose-6-phosphate dehydrogenase (G6PD)-deficient individuals bearing the mediterranean variant of G6PD.	NADP	29-72	glucose-6-phosphate dehydrogenase	Homo sapiens	201-205	
7803801-1	1995	Human erythrocytes contain a nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein, FX, whose levels are significantly increased in erythrocytes from glucose-6-phosphate dehydrogenase (G6PD)-deficient individuals bearing the mediterranean variant of G6PD.	NADP	74-81	glucose-6-phosphate dehydrogenase	Homo sapiens	201-205	
8118045-3	1994	When we compared the recombinant normal enzyme with authentic human G6PD, indistinguishable Km values for glucose-6-phosphate (G6P) and NADP were obtained, and the utilization rates for two substrate analogues (2-deoxy G6P and deamino NADP) also showed no difference between the enzymes.	NADP	136-140	glucose-6-phosphate dehydrogenase	Homo sapiens	68-72	
8141125-3	1994	The markedly abnormal kinetics of glucose-6-phosphate (G6P) of G6PD Kobe suggest the interaction between both NADP and G6P binding sites.	NADP	110-114	glucose-6-phosphate dehydrogenase	Homo sapiens	63-67	
8354277-5	1993	Reduction of internal GSSG by NADPH-dependent enzymes was excluded by experiments with glucose-supplied or glucose-6-phosphate dehydrogenase deficient cells.	NADP	30-35	glucose-6-phosphate dehydrogenase	Homo sapiens	107-140	
8466510-7	1993	Since G6PDH is essential in providing NADPH for the reduction of glutathione required for subsequent DHAA reduction, its decreased activity is consistent with altered levels of AA and DHAA observed in diabetic tissues.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	6-11	
18601259-4	1993	As a NADPH-regenerating enzyme, glucose-6-phosphate dehydrogenase or isocitrate dehydrogenase is conceived.	NADP	5-10	glucose-6-phosphate dehydrogenase	Homo sapiens	32-65	
1810251-1	1991	ATP is known to be easily determined fluorometrically after it is utilized to produce the corresponding amount of NADPH by combined reactions of hexokinase and glucose-6-phosphate dehydrogenase.	NADP	114-119	glucose-6-phosphate dehydrogenase	Homo sapiens	160-193	
1718124-4	1991	In diseased muscle fibres, there is generally a positive relationship between the activity of the NADPH producing enzymes glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase and the level of reduced glutathione.	NADP	98-103	glucose-6-phosphate dehydrogenase	Homo sapiens	122-155	
1901343-4	1991	Some agents like methylene blue (MB), phenazine methosulfate, and pyrroline carboxylate do not require GSSG-R to increase CO2 production; they activate G6PD and 6-phosphogluconic dehydrogenase by directly oxidizing reduced nicotinamide adenine dinucleotide phosphate (NADPH) to oxidized nicotinamide adenine dinucleotide phosphate (NADP).	NADP	223-266	glucose-6-phosphate dehydrogenase	Homo sapiens	152-156	
1901343-4	1991	Some agents like methylene blue (MB), phenazine methosulfate, and pyrroline carboxylate do not require GSSG-R to increase CO2 production; they activate G6PD and 6-phosphogluconic dehydrogenase by directly oxidizing reduced nicotinamide adenine dinucleotide phosphate (NADPH) to oxidized nicotinamide adenine dinucleotide phosphate (NADP).	NADP	268-273	glucose-6-phosphate dehydrogenase	Homo sapiens	152-156	
1901343-4	1991	Some agents like methylene blue (MB), phenazine methosulfate, and pyrroline carboxylate do not require GSSG-R to increase CO2 production; they activate G6PD and 6-phosphogluconic dehydrogenase by directly oxidizing reduced nicotinamide adenine dinucleotide phosphate (NADPH) to oxidized nicotinamide adenine dinucleotide phosphate (NADP).	NADP	287-330	glucose-6-phosphate dehydrogenase	Homo sapiens	152-156	
1901343-4	1991	Some agents like methylene blue (MB), phenazine methosulfate, and pyrroline carboxylate do not require GSSG-R to increase CO2 production; they activate G6PD and 6-phosphogluconic dehydrogenase by directly oxidizing reduced nicotinamide adenine dinucleotide phosphate (NADPH) to oxidized nicotinamide adenine dinucleotide phosphate (NADP).	NADP	268-272	glucose-6-phosphate dehydrogenase	Homo sapiens	152-156	
2082184-6	1990	Removal (with glucose-6-phosphate dehydrogenase) of NADP+ produced by the reductase reaction significantly increased reductase activity.	NADP	52-57	glucose-6-phosphate dehydrogenase	Homo sapiens	14-47	
1703936-9	1990	The control values were 3.6 +/- 0.8 nmol formed NADPH/mg protein/min (M +/- SD) in G6PDH and 0.69 +/- 0.17 micrograms/mg non-collagen protein in RNA.	NADP	48-53	glucose-6-phosphate dehydrogenase	Homo sapiens	83-88	
2154300-4	1990	The calcium increase is responsible for the NADP change (via NAD kinase) and possibly the change in G6PD.	NADP	44-48	glucose-6-phosphate dehydrogenase	Homo sapiens	100-104	
2297768-1	1990	Hormonal modulation of glucose-6-phosphate dehydrogenase (G6PD) and of utilization pathways of NADPH generated by G6PD was studied in the MCF-7 human breast cancer cell line, using a quantitative cytochemical method.	NADP	95-100	glucose-6-phosphate dehydrogenase	Homo sapiens	114-118	
2297768-7	1990	When we studied the effect of the steroid on the two utilization pathways of NADPH generated by G6PD activity, we observed that, in the cells treated with estradiol, there is an increase in reducing equivalents generated by G6PD activity which only affects the NADPH2 pathway, and that there is cell growth stimulation.	NADP	77-82	glucose-6-phosphate dehydrogenase	Homo sapiens	96-100	
2297768-7	1990	When we studied the effect of the steroid on the two utilization pathways of NADPH generated by G6PD activity, we observed that, in the cells treated with estradiol, there is an increase in reducing equivalents generated by G6PD activity which only affects the NADPH2 pathway, and that there is cell growth stimulation.	NADP	77-82	glucose-6-phosphate dehydrogenase	Homo sapiens	224-228	
2235911-4	1990	The chromatographic conditions for the purification of glucose-6-phosphate dehydrogenase were optimized by varying the pH of the buffer; the concentrations of eluting agents, i.e. NADP (specific elution) and sodium chloride (nonspecific elution); flow rate; residence time of the protein on the column bed; and protein load.	NADP	180-184	glucose-6-phosphate dehydrogenase	Homo sapiens	55-88	
2287610-8	1990	By our method, the DEAE-Sephadex step is omitted, the G6PD is eluted from P11 with citrate and NADP, and from 2"5" ADP-Sepharose with KC1, NADP and EDTA.	NADP	95-99	glucose-6-phosphate dehydrogenase	Homo sapiens	54-58	
2287610-8	1990	By our method, the DEAE-Sephadex step is omitted, the G6PD is eluted from P11 with citrate and NADP, and from 2"5" ADP-Sepharose with KC1, NADP and EDTA.	NADP	139-143	glucose-6-phosphate dehydrogenase	Homo sapiens	54-58	
2078922-6	1990	In this way, G6PDH supplies reduced amounts of NADPH to the glutathione reductase enzyme affecting the integrity of the glutathione system; on the other hand, the activation by glucose of the polyol pathway also reduces the levels of NADPH for the glutathione reductase enzyme.	NADP	47-52	glucose-6-phosphate dehydrogenase	Homo sapiens	13-18	
2078922-6	1990	In this way, G6PDH supplies reduced amounts of NADPH to the glutathione reductase enzyme affecting the integrity of the glutathione system; on the other hand, the activation by glucose of the polyol pathway also reduces the levels of NADPH for the glutathione reductase enzyme.	NADP	234-239	glucose-6-phosphate dehydrogenase	Homo sapiens	13-18	
2270145-10	1990	Kmapp values of the G6PD isozymes were similar for NADP+ (6-8 microM), but different for G6P (56-180 microM).	NADP	51-56	glucose-6-phosphate dehydrogenase	Homo sapiens	20-24	
11978492-7	2002	Some antioxidant enzymes were also analyzed in RBCs, including glucose-6-phosphate dehydrogenase (G6PD), which provides the RBC"s main reducing power, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and catalase detoxifies H2O2 by catalyzing its reduction to O2 and H2O.	NADP	159-202	glucose-6-phosphate dehydrogenase	Homo sapiens	63-96	
11978492-7	2002	Some antioxidant enzymes were also analyzed in RBCs, including glucose-6-phosphate dehydrogenase (G6PD), which provides the RBC"s main reducing power, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and catalase detoxifies H2O2 by catalyzing its reduction to O2 and H2O.	NADP	159-202	glucose-6-phosphate dehydrogenase	Homo sapiens	98-102	
34387395-6	2021	The present work confirms the experimental results obtained by Eggleston and Krebs and proves that GSSG in the absence of NADPH is a direct inhibitor of G6PD.	NADP	122-127	glucose-6-phosphate dehydrogenase	Homo sapiens	153-157	
34790195-7	2021	Blocking glycolysis and pentose phosphate pathway (PPP) via 2-DG and NADPH production through glucose-6-phosphate dehydrogenase inhibitor resulted in significantly diminished conidial processing in wild-type BEAS-2B cells to the levels of Nlrx1-deficient BEAS-2B cells.	NADP	69-74	glucose-6-phosphate dehydrogenase	Homo sapiens	94-127	
34175765-10	2021	In addition, we also include some mutations in G6PD, the gene on the X chromosome that encodes glucose-6-phosphate dehydrogenase, because inactivity of this enzyme may lead to shortage of NADPH and thus to insufficient activity of NADPH oxidase.	NADP	188-193	glucose-6-phosphate dehydrogenase	Homo sapiens	95-128	
34387395-2	2021	The paradox is that, in basal-like conditions, the activity of G6PD evaluated "in vitro" is very low or nearly null because of the potent inhibiting effect exerted by NADPH, a coenzyme whose concentration in the cell is much higher than that of the substrate NADP+ .	NADP	167-172	glucose-6-phosphate dehydrogenase	Homo sapiens	63-67	
34387395-2	2021	The paradox is that, in basal-like conditions, the activity of G6PD evaluated "in vitro" is very low or nearly null because of the potent inhibiting effect exerted by NADPH, a coenzyme whose concentration in the cell is much higher than that of the substrate NADP+ .	NADP	259-264	glucose-6-phosphate dehydrogenase	Homo sapiens	63-67	
34387395-8	2021	An unknown element with a molecular weight ranging between 12 and 50 kDa has been found to reverse part of G6PD inhibition by NADPH.	NADP	126-131	glucose-6-phosphate dehydrogenase	Homo sapiens	107-111	
35368337-2	2022	Because the enzymatic activities of many mutants are different from that of the wildtype, the genetic polymorphism of G6PD plays an important role in the synthesis of nucleic acids via ribulose-5-phosphate and formation of reduced NADP in response to oxidative stress.	NADP	231-235	glucose-6-phosphate dehydrogenase	Homo sapiens	118-122	
35110412-5	2022	G6PD mutant melanomas exhibited increased levels of reactive oxygen species, decreased NADPH levels, and depleted glutathione as compared to control melanomas.	NADP	87-92	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
35207558-3	2022	Glucose-6-phosphate dehydrogenase (G6PD) is a housekeeping protein with 514 amino acids that is also the rate-limiting enzyme of PPP, catalyzing G6P into 6-phosphogluconolactone (6PGL) and producing the first NADPH of this pathway.	NADP	209-214	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
35207558-3	2022	Glucose-6-phosphate dehydrogenase (G6PD) is a housekeeping protein with 514 amino acids that is also the rate-limiting enzyme of PPP, catalyzing G6P into 6-phosphogluconolactone (6PGL) and producing the first NADPH of this pathway.	NADP	209-214	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
35065072-2	2022	To date, over 150 non-synonymous mutations have been identified in G6PD, with pathogenic mutations clustering near the dimer and/or tetramer interface and the allosteric NADP+-binding site.	NADP	170-175	glucose-6-phosphate dehydrogenase	Homo sapiens	67-71	
35065072-3	2022	Recently, our lab identified a small molecule which activates G6PD variants by stabilizing the allosteric NADP+ and dimer complex, suggesting therapeutics that target these regions may improve structural defects.	NADP	106-111	glucose-6-phosphate dehydrogenase	Homo sapiens	62-66	
35065072-5	2022	We first solved the crystal structure for G6PDK403Q, a mutant which mimics the physiological acetylation of wildtype G6PD in erythrocytes, and demonstrated that loss of allosteric NADP+ binding induces conformational changes in the dimer.	NADP	180-185	glucose-6-phosphate dehydrogenase	Homo sapiens	117-121	
2912886-5	1989	A molecular study using standard methods showed G6PD in the patient to have normal electrophoretic mobility (at pH 7.0, 8.0 and 8.8), normal apparent affinity for substrates (Km, G6P and NADP) and a slightly abnormal utilization of substrate analogues (decreased deamino-NADP and increased 2-deoxyglucose-6-phosphate utilization).	NADP	187-191	glucose-6-phosphate dehydrogenase	Homo sapiens	48-52	
2591977-2	1989	G6PD Thessaloniki had a low Michaelis constant (Km) for G6P (20 microM), high Km for NADP (10.1 microM), normal pH optimum, reduced heat stability, decreased electrophoretic mobility (96-98% of the normal), increased 2-deoxy-G6P and decreased galactose 6-phosphate utilization.	NADP	85-89	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
2602358-0	1989	Identification of the binding domain for NADP+ of human glucose-6-phosphate dehydrogenase by sequence analysis of mutants.	NADP	41-45	glucose-6-phosphate dehydrogenase	Homo sapiens	56-89	
2602358-1	1989	Human erythrocyte glucose-6-phosphate dehydrogenase is normally quite stable in the presence of 10 microM NADP+.	NADP	106-111	glucose-6-phosphate dehydrogenase	Homo sapiens	18-51	
2602358-2	1989	Certain glucose-6-phosphate dehydrogenase variants lose virtually all their activity at this concentration of NADP+ but are reactivated by 200 microM NADP+.	NADP	110-115	glucose-6-phosphate dehydrogenase	Homo sapiens	8-41	
2602358-2	1989	Certain glucose-6-phosphate dehydrogenase variants lose virtually all their activity at this concentration of NADP+ but are reactivated by 200 microM NADP+.	NADP	150-155	glucose-6-phosphate dehydrogenase	Homo sapiens	8-41	
2746239-8	1989	Preincubation of aluminum with citrate, NADP+, EDTA, NaF, ATP, and apotransferrin protected the G6PD isozymes against aluminum inactivation.	NADP	40-45	glucose-6-phosphate dehydrogenase	Homo sapiens	96-100	
2495021-8	1989	DE-II and DE-III protect glucose-6-phosphate dehydrogenase, which furnishes NADPH for fatty acid synthesis, from the feed-back inhibition exerted by added palmitoyl-CoA and oleate.	NADP	76-81	glucose-6-phosphate dehydrogenase	Homo sapiens	25-58	
3706292-3	1986	The enzymatic characteristics of G6PD Amman-1 were markedly reduced activity, fast eletrophoretic mobility, slightly increased km for NADP, normal km for G-6-P, normal heat stability, normal utilization of substrate analogues 2-deoxy G-6-P and deamino-NADP, and a monophasic pH curve with a peak at 8.5 to 9.3.	NADP	134-138	glucose-6-phosphate dehydrogenase	Homo sapiens	33-37	
3366466-5	1988	Additionally, the enzyme variant is characterized by normal electrophoretic mobility, biphasic and slightly alkaline pH optimum, and abnormal kinetics for the natural substrates G6PD and NADP as well as the artificial substrates deamino NADP.	NADP	237-241	glucose-6-phosphate dehydrogenase	Homo sapiens	178-182	
3338798-2	1988	G6PD Viangchan was found in a Laotian immigrant to Calgary, Canada, and was characterized by severe enzyme deficiency, normal electrophoretic mobility, increased pH optimum, and abnormal kinetics for the natural substrates G6PD and NADP, as well as the artificial substrates 2-deoxy G6PD and deamino NADP.	NADP	232-236	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
3338798-2	1988	G6PD Viangchan was found in a Laotian immigrant to Calgary, Canada, and was characterized by severe enzyme deficiency, normal electrophoretic mobility, increased pH optimum, and abnormal kinetics for the natural substrates G6PD and NADP, as well as the artificial substrates 2-deoxy G6PD and deamino NADP.	NADP	300-304	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
2889685-3	1987	The activities of pentose phosphate enzymes, such as glucose-6-phosphate dehydrogenase and transketolase in developing human fetus reach the highest level between 25 and 28 weeks and 21 and 24 weeks of gestation, respectively, indicating the most actively synthesizing period of the fetus for providing NADPH and ribose-5-phosphate for steroidogenesis and nucleotide and nucleic acid synthesis.	NADP	303-308	glucose-6-phosphate dehydrogenase	Homo sapiens	53-86	
3505333-9	1987	NADPH is a powerful regulator of G6PDH activity in the normal astrocytes and in gliomas.	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	33-38	
3505333-10	1987	At a NADPH/NADP+ ratio of 7:1 the normal astrocyte G6PDH is entirely inhibited, while the glioma enzyme is only 70% inhibited even at a ratio of 20:1.	NADP	5-10	glucose-6-phosphate dehydrogenase	Homo sapiens	51-56	
3505333-10	1987	At a NADPH/NADP+ ratio of 7:1 the normal astrocyte G6PDH is entirely inhibited, while the glioma enzyme is only 70% inhibited even at a ratio of 20:1.	NADP	11-16	glucose-6-phosphate dehydrogenase	Homo sapiens	51-56	
3576073-1	1987	It has been observed that human lymphocytes (HL) and fibroblasts, isolated in vitro from donors carrying the Mediterranean variant of glucose-6-phosphate dehydrogenase (G6PD), show a great decrease in this enzymatic activity, the hexose monophosphate shunt, and the NADPH/NADP+ ratio.	NADP	272-277	glucose-6-phosphate dehydrogenase	Homo sapiens	134-167	
3576073-1	1987	It has been observed that human lymphocytes (HL) and fibroblasts, isolated in vitro from donors carrying the Mediterranean variant of glucose-6-phosphate dehydrogenase (G6PD), show a great decrease in this enzymatic activity, the hexose monophosphate shunt, and the NADPH/NADP+ ratio.	NADP	272-277	glucose-6-phosphate dehydrogenase	Homo sapiens	169-173	
3740052-0	1986	G-6-PD Walter Reed: possible insight into "structural" NADP in G-6-PD.	NADP	55-59	glucose-6-phosphate dehydrogenase	Homo sapiens	0-6	
3706292-5	1986	G6PD Amman-2 characteristics were severely reduced activity, slow electrophoretic mobility, normal km for NADP, decreased km for G-6-P, decreased heat stability, increased utilization of substrate analogues, and a monophasic pH curve with a narrow peak at pH 9.5.	NADP	106-110	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
3949801-6	1986	These features of intracellular binding of NADP: 1) account for the previously unexplained inhibition and sigmoid kinetics of glucose-6-phosphate dehydrogenase within human erythrocytes and 2) represent a system in which activity of a rate-limiting enzyme is largely determined by the binding and release of substrate and product by intracellular proteins other than the enzyme itself.	NADP	43-47	glucose-6-phosphate dehydrogenase	Homo sapiens	126-159	
16744176-0	1986	Effect of oxidized glutathione on the inhibition of glucose-6-phosphate dehydrogenase by NADPH.	NADP	89-94	glucose-6-phosphate dehydrogenase	Homo sapiens	52-85	
4074340-0	1985	Reversal effect of oxidized glutathione on the inhibition of glucose-6-phosphate dehydrogenase by NADPH.	NADP	98-103	glucose-6-phosphate dehydrogenase	Homo sapiens	61-94	
3888984-2	1985	Inorganic vanadate (Vi) activates catalysis by glucose-6-phosphate dehydrogenase of the oxidation of glucose by NADP+.	NADP	112-117	glucose-6-phosphate dehydrogenase	Homo sapiens	47-80	
3355174-1	1988	Several disagreements and inconsistencies have appeared regarding whether human erythrocyte glucose-6-phosphate dehydrogenase exhibits sigmoid or classical kinetics with respect to NADP+ binding.	NADP	181-186	glucose-6-phosphate dehydrogenase	Homo sapiens	92-125	
3664503-4	1987	We found the Vmax values for glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were 50- and 4-fold lower, respectively, in ADRR than WT cells and the Kms of NADP+ were 10-fold lower in ADRR than WT.	NADP	178-183	glucose-6-phosphate dehydrogenase	Homo sapiens	29-62	
3552078-6	1987	Parasite G6PD exhibited much higher affinity (low Km) to G6P and nicotinamide-adenine dinucleotide phosphate (NADP) than did human G6PD.	NADP	65-108	glucose-6-phosphate dehydrogenase	Homo sapiens	9-13	
3552078-6	1987	Parasite G6PD exhibited much higher affinity (low Km) to G6P and nicotinamide-adenine dinucleotide phosphate (NADP) than did human G6PD.	NADP	110-114	glucose-6-phosphate dehydrogenase	Homo sapiens	9-13	
3740052-0	1986	G-6-PD Walter Reed: possible insight into "structural" NADP in G-6-PD.	NADP	55-59	glucose-6-phosphate dehydrogenase	Homo sapiens	63-69	
3740052-4	1986	The mutation in G-6-PD Walter Reed, like that of the previously described variant, G-6-PD Torrance, may be due to a mutation of the "structural" site for NADP.	NADP	154-158	glucose-6-phosphate dehydrogenase	Homo sapiens	16-22	
3740052-4	1986	The mutation in G-6-PD Walter Reed, like that of the previously described variant, G-6-PD Torrance, may be due to a mutation of the "structural" site for NADP.	NADP	154-158	glucose-6-phosphate dehydrogenase	Homo sapiens	83-89	
3711719-3	1986	We have now investigated the reverse G-6-PD reaction, namely, the oxidation of reduced nicotinamide-adenine dinucleotide phosphate (NADPH) by 6-phosphoglucono-delta-lactone to form glucose-6-phosphate and nicotinamide-adenine dinucleotide phosphate (NADP).	NADP	87-130	glucose-6-phosphate dehydrogenase	Homo sapiens	37-43	
3711719-3	1986	We have now investigated the reverse G-6-PD reaction, namely, the oxidation of reduced nicotinamide-adenine dinucleotide phosphate (NADPH) by 6-phosphoglucono-delta-lactone to form glucose-6-phosphate and nicotinamide-adenine dinucleotide phosphate (NADP).	NADP	132-137	glucose-6-phosphate dehydrogenase	Homo sapiens	37-43	
3711719-3	1986	We have now investigated the reverse G-6-PD reaction, namely, the oxidation of reduced nicotinamide-adenine dinucleotide phosphate (NADPH) by 6-phosphoglucono-delta-lactone to form glucose-6-phosphate and nicotinamide-adenine dinucleotide phosphate (NADP).	NADP	205-248	glucose-6-phosphate dehydrogenase	Homo sapiens	37-43	
3711719-3	1986	We have now investigated the reverse G-6-PD reaction, namely, the oxidation of reduced nicotinamide-adenine dinucleotide phosphate (NADPH) by 6-phosphoglucono-delta-lactone to form glucose-6-phosphate and nicotinamide-adenine dinucleotide phosphate (NADP).	NADP	132-136	glucose-6-phosphate dehydrogenase	Homo sapiens	37-43	
3511989-1	1986	Plasmodium falciparum-infected human red cells possess at least two pathways for the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH): (1) the glucose-6-phosphate dehydrogenase (G6PD) pathway and (2) the glutamate dehydrogenase (GD) pathway using glutamate as a substrate.	NADP	107-150	glucose-6-phosphate dehydrogenase	Homo sapiens	168-201	
3511989-1	1986	Plasmodium falciparum-infected human red cells possess at least two pathways for the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH): (1) the glucose-6-phosphate dehydrogenase (G6PD) pathway and (2) the glutamate dehydrogenase (GD) pathway using glutamate as a substrate.	NADP	107-150	glucose-6-phosphate dehydrogenase	Homo sapiens	203-207	
3511989-1	1986	Plasmodium falciparum-infected human red cells possess at least two pathways for the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH): (1) the glucose-6-phosphate dehydrogenase (G6PD) pathway and (2) the glutamate dehydrogenase (GD) pathway using glutamate as a substrate.	NADP	152-157	glucose-6-phosphate dehydrogenase	Homo sapiens	168-201	
3511989-1	1986	Plasmodium falciparum-infected human red cells possess at least two pathways for the generation of reduced nicotinamide adenine dinucleotide phosphate (NADPH): (1) the glucose-6-phosphate dehydrogenase (G6PD) pathway and (2) the glutamate dehydrogenase (GD) pathway using glutamate as a substrate.	NADP	152-157	glucose-6-phosphate dehydrogenase	Homo sapiens	203-207	
3711795-11	1986	NADPH consumed in this reaction (and in the dihydroxyacetone phosphate pathway of glycerolipid synthesis) might be provided by glucose-6-phosphate dehydrogenase which was recently also found in peroxisomes.	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	127-160	
3986998-3	1985	The reaction rate is determined from the change in absorbance at 340 nm as NADPH is produced by the action of glucose-6-phosphate dehydrogenase.	NADP	75-80	glucose-6-phosphate dehydrogenase	Homo sapiens	110-143	
2984461-9	1985	In addition, the specific activity of glucose-6-phosphate dehydrogenase, a key enzyme for cellular production of NADPH, was not related to the degree of O2 tolerance.	NADP	113-118	glucose-6-phosphate dehydrogenase	Homo sapiens	38-71	
2985042-4	1985	Nucleotide-binding proteins enhanced NADPH oxidation induced by DL-glyceraldehyde, up to 10.6-fold with glucose-6-phosphate dehydrogenase.	NADP	37-42	glucose-6-phosphate dehydrogenase	Homo sapiens	104-137	
4029955-5	1985	G-6-PD Morelia is the first variant from its class with a high Km for NADP and a low Ki for NADPH.	NADP	70-74	glucose-6-phosphate dehydrogenase	Homo sapiens	0-6	
4029955-5	1985	G-6-PD Morelia is the first variant from its class with a high Km for NADP and a low Ki for NADPH.	NADP	92-97	glucose-6-phosphate dehydrogenase	Homo sapiens	0-6	
3856275-1	1985	Glucose-6-phosphate dehydrogenase (G6PD) is a ubiquitous enzyme that supplies the cell with NADPH required for a variety of reductive reactions and biosynthetic processes.	NADP	92-97	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
3856275-1	1985	Glucose-6-phosphate dehydrogenase (G6PD) is a ubiquitous enzyme that supplies the cell with NADPH required for a variety of reductive reactions and biosynthetic processes.	NADP	92-97	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
6201483-2	1984	We proposed that: 1) pyrroline-5-carboxylate is converted to proline by pyrroline-5-carboxylate reductase with concomitant oxidation of NADPH, 2) NADP+ augments glucose-6-phosphate dehydrogenase activity, and 3) production of ribose-5-phosphate via the pentose shunt is increased.	NADP	136-141	glucose-6-phosphate dehydrogenase	Homo sapiens	161-194	
6201483-2	1984	We proposed that: 1) pyrroline-5-carboxylate is converted to proline by pyrroline-5-carboxylate reductase with concomitant oxidation of NADPH, 2) NADP+ augments glucose-6-phosphate dehydrogenase activity, and 3) production of ribose-5-phosphate via the pentose shunt is increased.	NADP	146-151	glucose-6-phosphate dehydrogenase	Homo sapiens	161-194	
6440265-9	1984	The NADPH-cytochrome c (P450) reductase of G6PD-deficient HL and HSF homogenates becomes lower than that of controls when endogenous G6PD and exogenous glucose 6-phosphate (G6P) and NADP+ are used as a hydrogen donor system in place of NADPH.	NADP	182-187	glucose-6-phosphate dehydrogenase	Homo sapiens	43-47	
6200703-4	1984	We have also demonstrated that the decreased synthesis of NADPH was produced by a competitive inhibition of both G6P and NADP binding to the G6PD enzyme.	NADP	58-63	glucose-6-phosphate dehydrogenase	Homo sapiens	141-145	
6200703-4	1984	We have also demonstrated that the decreased synthesis of NADPH was produced by a competitive inhibition of both G6P and NADP binding to the G6PD enzyme.	NADP	58-62	glucose-6-phosphate dehydrogenase	Homo sapiens	141-145	
6671112-3	1983	An addition of NADP to cell extracts which had partly lost their glucose-6-phosphate dehydrogenase activity, resulted in reactivation and stabilization of the enzyme.	NADP	15-19	glucose-6-phosphate dehydrogenase	Homo sapiens	65-98	
6671112-7	1983	A mechanism of destabilization and inactivation of glucose-6-phosphate dehydrogenase is proposed, which consists in NADP hydrolysis and enzyme decomposition to inactive monomers which are less stable to proteolysis.	NADP	116-120	glucose-6-phosphate dehydrogenase	Homo sapiens	51-84	
6727447-5	1984	In young cells, the induced alteration of glucose 6-phosphate dehydrogenase disappeared if the pH of the medium was lowered to 6.5 or if NADP+ was added.	NADP	137-142	glucose-6-phosphate dehydrogenase	Homo sapiens	42-75	
6727447-6	1984	In old cells, the disappearance of the natural heat-labile glucose 6-phosphate dehydrogenase was possible only if both pH 6.5 and NADP+ were present.	NADP	130-135	glucose-6-phosphate dehydrogenase	Homo sapiens	59-92	
6320929-6	1984	The mean Kis of lead for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP) for G6PD were 1.5 microM and 2.1 microM, respectively, which is within the range of intraerythrocytic lead concentrations found in clinical lead poisoning.	NADP	49-92	glucose-6-phosphate dehydrogenase	Homo sapiens	104-108	
6320929-6	1984	The mean Kis of lead for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP) for G6PD were 1.5 microM and 2.1 microM, respectively, which is within the range of intraerythrocytic lead concentrations found in clinical lead poisoning.	NADP	94-98	glucose-6-phosphate dehydrogenase	Homo sapiens	104-108	
6661453-2	1983	The thermostability of glucose-6-phosphate dehydrogenase was shown to be dependent on the coenzyme (NADP) concentration and to be coupled with the activity of alkaline phosphatase.	NADP	100-104	glucose-6-phosphate dehydrogenase	Homo sapiens	23-56	
6860590-5	1983	Since the intracellular concentrations of glucose-6-phosphate, 6-phosphogluconate and NADP are below their Kms for G6PD and 6PGD, the kinetic data suggest that increased concentrations of 2,3-diphosphoglycerate in pyruvate kinase deficient red cells are sufficiently high to suppress pentose phosphate shunt activity.	NADP	86-90	glucose-6-phosphate dehydrogenase	Homo sapiens	115-119	
6886661-5	1983	In all species except the goby, two groups of isozymes were distinguished, corresponding to the mammalian G6PD (specific for glucose-6-phosphate (G6P) and NADP+) and H6PD (capable of utilizing galactose-6-phosphate and in certain cases other monosaccharide phosphates in addition to G6P).	NADP	155-160	glucose-6-phosphate dehydrogenase	Homo sapiens	106-110	
6871163-1	1983	Transferred nuclear Overhauser enhancement was used to examine the conformation of NAD+ and NADP+ bound to glucose-6-phosphate dehydrogenase and glutamate dehydrogenase and of NAD+ bound to lactate dehydrogenase.	NADP	92-97	glucose-6-phosphate dehydrogenase	Homo sapiens	107-140	
6440265-9	1984	The NADPH-cytochrome c (P450) reductase of G6PD-deficient HL and HSF homogenates becomes lower than that of controls when endogenous G6PD and exogenous glucose 6-phosphate (G6P) and NADP+ are used as a hydrogen donor system in place of NADPH.	NADP	4-9	glucose-6-phosphate dehydrogenase	Homo sapiens	43-47	
6856959-2	1983	In heart muscle, NADP-linked isocitrate dehydrogenase activity is particularly high when compared with that of the other representative NADPH-generating enzyme, glucose-6-phosphate dehydrogenase.	NADP	136-141	glucose-6-phosphate dehydrogenase	Homo sapiens	161-194	
6317373-2	1983	T4 competitively inhibits NADP in human erythrocyte G6PD variants G6PDA, G6PDB and G6PDA- with inhibition constants of 2.40 +/- 0.90 X 10(-6), 3.44 +/- 0.63 X 10(-6) and 6.53 +/- 0.60 X 10(-6) mol/l, respectively.	NADP	26-30	glucose-6-phosphate dehydrogenase	Homo sapiens	52-56	
6859536-2	1983	In the assay, production of ATP from carbamoyl phosphate and ADP by carbamate kinase is coupled to the formation of NADPH, using glucose, hexokinase, NADP+, and glucose-6-phosphate dehydrogenase.	NADP	116-121	glucose-6-phosphate dehydrogenase	Homo sapiens	161-194	
6289944-8	1982	Since the intracellular concentrations of G6P and NADP+ are below their KmS for G6PD, these data suggest that high concentrations of pyrimidine 5"-nucleotides depress pentose phosphate shunt activity in pyrimidin 5"-nucleotidase deficiency.	NADP	50-55	glucose-6-phosphate dehydrogenase	Homo sapiens	80-84	
6298917-1	1982	Human skin fibroblasts, isolated in vitro, from donors carrying the Mediterranean variant of glucose-6-phosphate dehydrogenase, exhibit a sharp decrease of hexose monophosphate shunt and NADPH/NADP+ ratio when compared to the fibroblasts from normal donors.	NADP	187-192	glucose-6-phosphate dehydrogenase	Homo sapiens	93-126	
6298917-1	1982	Human skin fibroblasts, isolated in vitro, from donors carrying the Mediterranean variant of glucose-6-phosphate dehydrogenase, exhibit a sharp decrease of hexose monophosphate shunt and NADPH/NADP+ ratio when compared to the fibroblasts from normal donors.	NADP	193-198	glucose-6-phosphate dehydrogenase	Homo sapiens	93-126	
7082864-3	1982	The fluorescence of NADPH formed by G-6-PD was not interfered with by 6-PGD activity.	NADP	20-25	glucose-6-phosphate dehydrogenase	Homo sapiens	36-42	
7440254-5	1980	As for the activity of the NADPH regenerating enzymes, the activity of 6-phosphogluconate dehydrogenase and malate dehydrogenase (oxaloacetate-decarboxylating) is somewhat higher, and the activity of glucose-6-phosphate dehydrogenase similar, in the Purkinje fibres compared to that in the myocardial fibres.	NADP	27-32	glucose-6-phosphate dehydrogenase	Homo sapiens	200-233	
7166314-5	1982	The enzymatic characteristics were examined when he was 5 years old, and his G6PD showed faster-than-normal electrophoretic mobility, low Km G6P, high Km NADP, low Ki NADPH, normal utilization of substrate analogues, heat instability, and a normal pH optimum curve.	NADP	154-158	glucose-6-phosphate dehydrogenase	Homo sapiens	77-81	
7166314-5	1982	The enzymatic characteristics were examined when he was 5 years old, and his G6PD showed faster-than-normal electrophoretic mobility, low Km G6P, high Km NADP, low Ki NADPH, normal utilization of substrate analogues, heat instability, and a normal pH optimum curve.	NADP	167-172	glucose-6-phosphate dehydrogenase	Homo sapiens	77-81	
7315103-5	1981	The other two are new variants: G6PD Tashkent (low Ki by NADPH, class 3) and G6PD Nukus (Km for G6P 127 microM, class 2).	NADP	57-62	glucose-6-phosphate dehydrogenase	Homo sapiens	32-36	
6252945-9	1980	Mechanisms are discussed by which G-6-PD deficient cells retain adequate levels of NADPH during resting conditions, and it is suggested that the chronic haemolysis associated with G-6-PD Helsinki could be due to a defect in the lipid region of the cell membrane.	NADP	83-88	glucose-6-phosphate dehydrogenase	Homo sapiens	34-40	
6161446-1	1980	Substitution of nicotinamide adenine dinucleotide dependent glucose-6-phosphate dehydrogenase for the nicotinamide adenine dinucleotide phosphate dependent enzyme has produced identical results in a number of enzyme-linked electrophoretic staining procedures.	NADP	102-145	glucose-6-phosphate dehydrogenase	Homo sapiens	60-93	
6896174-5	1982	As could be predicted by its trophic action, TSH stimulated the generation of NADPH by glucose 6-phosphate dehydrogenase.	NADP	78-83	glucose-6-phosphate dehydrogenase	Homo sapiens	87-120	
6896174-9	1982	In all specimens tested, there was good correlation between the amount of DNA-synthesis, measured by Feulgen cytophotometry, and the activity of glucose 6-phosphate dehydrogenase activity that generated NADPH.	NADP	203-208	glucose-6-phosphate dehydrogenase	Homo sapiens	145-178	
7442656-1	1980	Bioluminescence photokinetic assay of NADP+ is described, using the glucose-6-phosphate dehydrogenase reaction for conversion to its reduced form and subsequent measurement of this with luciferase extracts of Vibria fisherii.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	68-101	
7353069-2	1980	Characterization of G6PD purified from leukocytes using standard WHO techniques revealed diminished electrophoretic mobility, marked lability on heating at 46 degrees C, normal pH optimum and utilization of alternate substrates (2-deoxy G6P, D-amino NADP), elevated Km NADP, and striking susceptibility to NADPH inhibition.	NADP	250-254	glucose-6-phosphate dehydrogenase	Homo sapiens	20-24	
7353069-2	1980	Characterization of G6PD purified from leukocytes using standard WHO techniques revealed diminished electrophoretic mobility, marked lability on heating at 46 degrees C, normal pH optimum and utilization of alternate substrates (2-deoxy G6P, D-amino NADP), elevated Km NADP, and striking susceptibility to NADPH inhibition.	NADP	306-311	glucose-6-phosphate dehydrogenase	Homo sapiens	20-24	
6452104-4	1980	Purified erythrocyte glucose-6-phosphate dehydrogenase was also affected by Bilipolinum and its affinity for NADP was decreased.	NADP	109-113	glucose-6-phosphate dehydrogenase	Homo sapiens	21-54	
7440222-1	1980	The presumed "physiologic activity" of normal glucose 6-phosphate dehydrogenase (G6PD), i.e. activity assayed in the presence of physiologic concentrations of ATP, 2,3-diphosphoglycerate, glucose 6-phosphate, NADP and NADPH in the normal red cells, is comparable to shunt pathway activity of intact normal red cells.	NADP	209-213	glucose-6-phosphate dehydrogenase	Homo sapiens	81-85	
7440222-1	1980	The presumed "physiologic activity" of normal glucose 6-phosphate dehydrogenase (G6PD), i.e. activity assayed in the presence of physiologic concentrations of ATP, 2,3-diphosphoglycerate, glucose 6-phosphate, NADP and NADPH in the normal red cells, is comparable to shunt pathway activity of intact normal red cells.	NADP	218-223	glucose-6-phosphate dehydrogenase	Homo sapiens	81-85	
7440222-4	1980	The apparent discrepancy could be attributed either to (a) over-estimation of NADP and under-estimation of NADPH concentrations in the G6PD deficient red cells due to rapid oxidation of NADPH to NADP in preparation of hemolysate, or to (b) a large portion of NADP which accumulated in the G6PD deficient red cells binds with cellular components of intact red cells and is not available as substrate for G6PD.	NADP	107-112	glucose-6-phosphate dehydrogenase	Homo sapiens	135-139	
7440222-4	1980	The apparent discrepancy could be attributed either to (a) over-estimation of NADP and under-estimation of NADPH concentrations in the G6PD deficient red cells due to rapid oxidation of NADPH to NADP in preparation of hemolysate, or to (b) a large portion of NADP which accumulated in the G6PD deficient red cells binds with cellular components of intact red cells and is not available as substrate for G6PD.	NADP	186-191	glucose-6-phosphate dehydrogenase	Homo sapiens	135-139	
7440222-4	1980	The apparent discrepancy could be attributed either to (a) over-estimation of NADP and under-estimation of NADPH concentrations in the G6PD deficient red cells due to rapid oxidation of NADPH to NADP in preparation of hemolysate, or to (b) a large portion of NADP which accumulated in the G6PD deficient red cells binds with cellular components of intact red cells and is not available as substrate for G6PD.	NADP	107-111	glucose-6-phosphate dehydrogenase	Homo sapiens	135-139	
7440222-4	1980	The apparent discrepancy could be attributed either to (a) over-estimation of NADP and under-estimation of NADPH concentrations in the G6PD deficient red cells due to rapid oxidation of NADPH to NADP in preparation of hemolysate, or to (b) a large portion of NADP which accumulated in the G6PD deficient red cells binds with cellular components of intact red cells and is not available as substrate for G6PD.	NADP	107-111	glucose-6-phosphate dehydrogenase	Homo sapiens	135-139	
230449-5	1979	3) The dissociation constants of red blood cell G6PD for NADP and NADPH, which were obtained from the investigations on the reactivation of cold-inactivated G6PD at 37 degrees C, were about 3 times higher in the patient as compared to the values of the normal controls.	NADP	57-61	glucose-6-phosphate dehydrogenase	Homo sapiens	48-52	
230449-5	1979	3) The dissociation constants of red blood cell G6PD for NADP and NADPH, which were obtained from the investigations on the reactivation of cold-inactivated G6PD at 37 degrees C, were about 3 times higher in the patient as compared to the values of the normal controls.	NADP	57-61	glucose-6-phosphate dehydrogenase	Homo sapiens	157-161	
230449-5	1979	3) The dissociation constants of red blood cell G6PD for NADP and NADPH, which were obtained from the investigations on the reactivation of cold-inactivated G6PD at 37 degrees C, were about 3 times higher in the patient as compared to the values of the normal controls.	NADP	66-71	glucose-6-phosphate dehydrogenase	Homo sapiens	48-52	
230449-5	1979	3) The dissociation constants of red blood cell G6PD for NADP and NADPH, which were obtained from the investigations on the reactivation of cold-inactivated G6PD at 37 degrees C, were about 3 times higher in the patient as compared to the values of the normal controls.	NADP	66-71	glucose-6-phosphate dehydrogenase	Homo sapiens	157-161	
38114-8	1979	It is further shown that the observed differences in the heat stability of glucose-6-phosphate dehydrogenase in the fractions obtained by graded hemolysis are due to the presence of different concentrations of endogeneous NADP.	NADP	222-226	glucose-6-phosphate dehydrogenase	Homo sapiens	75-108	
43719-6	1979	Concurrently, the macro-NADP+ is reduced by G-6-P and G-6-PD in the cofactor regeneration portion of the device.	NADP	24-28	glucose-6-phosphate dehydrogenase	Homo sapiens	54-60	
730178-2	1978	G6PD Ogikubo, found in a 17-year-old male whose red cells contained 3% of normal enzyme activity, had normal Km G6P, normal Km NADP, normal utilization of deamino-NADP, decreased heat stability, and a normal pH curve.	NADP	127-131	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
31177-1	1978	Pure glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ 1-oxidoreductase, EC 1.1.1.49) is transformed into "hyperanodic forms" when incubated at acidic pH and in the presence of NADP+ with excess of glucose-6-phosphate or with some "NADP+ modifying proteins" purified from the same cells.	NADP	62-66	glucose-6-phosphate dehydrogenase	Homo sapiens	5-38	
31177-1	1978	Pure glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ 1-oxidoreductase, EC 1.1.1.49) is transformed into "hyperanodic forms" when incubated at acidic pH and in the presence of NADP+ with excess of glucose-6-phosphate or with some "NADP+ modifying proteins" purified from the same cells.	NADP	190-194	glucose-6-phosphate dehydrogenase	Homo sapiens	5-38	
23188-3	1977	The abnormal enzyme differs from the normal by decreased Michaelis constant for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP), by increased utilization of analogues of substrates--2-deoxy-glucose-6-phosphate and particularly deamino-NADP, by low thermal stability, by the character of pH-dependence, by the appearance of a single band of G6PD activity in polyacrylamide gel electrophoresis.	NADP	104-147	glucose-6-phosphate dehydrogenase	Homo sapiens	367-371	
21101-0	1977	Decay of a specific NADP(H)-binding protein during aging of normal and glucose 6-phosphate dehydrogenase-deficient erythrocytes.	NADP	20-27	glucose-6-phosphate dehydrogenase	Homo sapiens	71-104	
16911-0	1977	Effects of estradiol and nicotinamide adenine dinucleotide phosphate on rate of degradation of uterine glucose-6-phosphate dehydrogenase.	NADP	25-68	glucose-6-phosphate dehydrogenase	Homo sapiens	103-136	
23634-3	1977	The abnormal variant differs from the normal enzyme by a decreased Michaelis constant for G-6-P and NADP, by increased utilization of substrate-analogues (2-deoxy-G-6-P and deamino NADP in particular), by low heat stability, the character of pH dependence, and by the appearance of one band of G-6-PD activity during electrophoresis in polyacrylamide gel.	NADP	100-104	glucose-6-phosphate dehydrogenase	Homo sapiens	294-300	
1276080-4	1976	One variant (G6PD Hamm) had a low Km-value for glucose-6-phosphate, the other (G6PD Tarsus) exhibited an increased affinity for glucose-6-phosphate and a reduced affinity for NADP+.	NADP	175-180	glucose-6-phosphate dehydrogenase	Homo sapiens	13-17	
131232-5	1976	The normal activity of glucose-6-phosphate dehydrogenase and malate dehydrogenase (decarboxylating) (NADP), which supply NADPH for the reduction of acetyl-CoA to fatty acids, would suggest that the change in lipogenesis is of moderate degree, thereb) affecting only the most rate-limiting enzyme, ATP citrate-lyase.	NADP	101-105	glucose-6-phosphate dehydrogenase	Homo sapiens	23-56	
131232-5	1976	The normal activity of glucose-6-phosphate dehydrogenase and malate dehydrogenase (decarboxylating) (NADP), which supply NADPH for the reduction of acetyl-CoA to fatty acids, would suggest that the change in lipogenesis is of moderate degree, thereb) affecting only the most rate-limiting enzyme, ATP citrate-lyase.	NADP	121-126	glucose-6-phosphate dehydrogenase	Homo sapiens	23-56	
416-1	1975	Human glucose 6-phosphate dehydrogenase associated with NADPH was efficiently bound with agarose-bound NADP, whereas the enzyme associated with NADP was poorly bound with agarose-bound NADP.	NADP	56-61	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
416-1	1975	Human glucose 6-phosphate dehydrogenase associated with NADPH was efficiently bound with agarose-bound NADP, whereas the enzyme associated with NADP was poorly bound with agarose-bound NADP.	NADP	56-60	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
416-1	1975	Human glucose 6-phosphate dehydrogenase associated with NADPH was efficiently bound with agarose-bound NADP, whereas the enzyme associated with NADP was poorly bound with agarose-bound NADP.	NADP	103-107	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
416-1	1975	Human glucose 6-phosphate dehydrogenase associated with NADPH was efficiently bound with agarose-bound NADP, whereas the enzyme associated with NADP was poorly bound with agarose-bound NADP.	NADP	103-107	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
239915-2	1975	A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP).	NADP	27-31	glucose-6-phosphate dehydrogenase	Homo sapiens	114-147	
239915-2	1975	A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP).	NADP	27-31	glucose-6-phosphate dehydrogenase	Homo sapiens	149-153	
239915-2	1975	A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP).	NADP	217-221	glucose-6-phosphate dehydrogenase	Homo sapiens	114-147	
239915-2	1975	A number of derivatives of NADP(H) were tested with respect to their effectiveness in interacting with tetrameric glucose 6-phosphate dehydrogenase (G6PD) retaining only the fraction of "structural" coenzyme (4 moles NADP).	NADP	217-221	glucose-6-phosphate dehydrogenase	Homo sapiens	149-153	
239915-3	1975	Interaction was probed by two parameters: a) increased thermostability of G6PD activity, measured as the difference in the corresponding transition temperature (Tm) of samples containing and lacking the NADP derivatives, respectively; b) competitive inhibition toward NADP, expressed a Ki values.	NADP	203-207	glucose-6-phosphate dehydrogenase	Homo sapiens	74-78	
239915-3	1975	Interaction was probed by two parameters: a) increased thermostability of G6PD activity, measured as the difference in the corresponding transition temperature (Tm) of samples containing and lacking the NADP derivatives, respectively; b) competitive inhibition toward NADP, expressed a Ki values.	NADP	268-272	glucose-6-phosphate dehydrogenase	Homo sapiens	74-78	
239915-8	1975	These data show that the adenosine moiety of NADP is more critically involved than the nicotinamide portion in the interaction with human G6PD.	NADP	45-49	glucose-6-phosphate dehydrogenase	Homo sapiens	138-142	
5339-2	1975	The results of physico-chemical study of these enzymes (determination of electrophoretic mobility, kappaM for G6P and NADP, pH optimum and thermostability) permit tu consider 5 of them to be new mutations of G6PD previously not described in literature.	NADP	118-122	glucose-6-phosphate dehydrogenase	Homo sapiens	208-212	
4152244-0	1974	Effects of 8-azaguanine on the induction of uterine glucose-6-phosphate dehydrogenase activity by estradiol or NADP plus.	NADP	111-115	glucose-6-phosphate dehydrogenase	Homo sapiens	52-85	
4396123-0	1970	Active molecular unit and NADP content of human glucose 6-phosphate dehydrogenase.	NADP	26-30	glucose-6-phosphate dehydrogenase	Homo sapiens	48-81	
4392409-0	1970	Distinctive patterns of NADP binding to dimeric and tetrameric glucose 6-phosphate dehydrogenase from human red cells.	NADP	24-28	glucose-6-phosphate dehydrogenase	Homo sapiens	63-96	
4383500-0	1967	Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH.	NADP	67-72	glucose-6-phosphate dehydrogenase	Homo sapiens	30-63	
4383500-0	1967	Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH.	NADP	77-82	glucose-6-phosphate dehydrogenase	Homo sapiens	30-63	
14120013-0	1963	[NADP-DEPENDENT ACTIVITIES (GLUCOSE-6-PHOSPHATE DEHYDROGENASE AND ISOCITRATE DEHYDROGENASE) OF THE SUBCELLULAR FRACTIONS OF NORMAL AND PATHOLOGICAL HUMAN LIVER].	NADP	1-5	glucose-6-phosphate dehydrogenase	Homo sapiens	28-61	
37930-6	1979	It was also demonstrated that glucose-6-phosphate dehydrogenase stability in HeLa and T-9 extracts is the same at low concentrations of the coenzyme and after addition of crystalline NADP.	NADP	183-187	glucose-6-phosphate dehydrogenase	Homo sapiens	30-63	
657477-1	1978	Erythrocyte glucose-6-phosphate dehydrogenase activity is measured with a centrifugal analyzer by use of a commercial reagent kit and of the reaction glucose-6-phosphate + NADP+ leads to 6-phosphogluconolactone + NADPH.	NADP	172-176	glucose-6-phosphate dehydrogenase	Homo sapiens	12-45	
657477-1	1978	Erythrocyte glucose-6-phosphate dehydrogenase activity is measured with a centrifugal analyzer by use of a commercial reagent kit and of the reaction glucose-6-phosphate + NADP+ leads to 6-phosphogluconolactone + NADPH.	NADP	213-218	glucose-6-phosphate dehydrogenase	Homo sapiens	12-45	
25652-4	1978	The effects of GSSG (oxidized glutathione) on the inhibition of glucose 6-phosphate dehydrogenase by NADPH [Eggleston & Krebs (1974) Biochem.	NADP	101-106	glucose-6-phosphate dehydrogenase	Homo sapiens	64-97	
25561-0	1978	A study of co-operation of commercial NADP+ and the coenzyme extracted from liver and spleen in the recycling system: glucose-6-phosphate dehydrogenase--glutathione reductase.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	118-151	
23988-0	1977	Parallel occurrence of oxidant-sensitivity and decreased inhibition by NADPH in G-6-PD Lublin and G-6-PD Poxnan.	NADP	71-76	glucose-6-phosphate dehydrogenase	Homo sapiens	80-86	
23988-1	1977	In two studied variants of G-6-PD without chronic hemolysis in probands, sensitivity of enzymes to inhibition by NADPH was decreased.	NADP	113-118	glucose-6-phosphate dehydrogenase	Homo sapiens	27-33	
23988-3	1977	Susceptibility to the oxidant-induced hemolysis was described in probands, as well as in patients hemizygous for two other variants of G-6-PD with increased Ki for NADPH.	NADP	164-169	glucose-6-phosphate dehydrogenase	Homo sapiens	135-141	
884873-2	1977	The procedure is a fluorometric rate method measuring the formation of NADPH catalyzed by immobilized glucose-6-phosphate dehydrogenase and hexokinase held within a tiny stirrer.	NADP	71-76	glucose-6-phosphate dehydrogenase	Homo sapiens	102-135	
15940-2	1977	G6PD "Mediterranean-like" had markedly decreased activity, normal electrophoretic mobility, low Km G6P, low Km NADP, increased utilization of all three substrate analogues (2-deoxy-G6P, Gal-6P, and deamino-NADP) and slightly decreased heat stability and slightly biphasic pH curve.	NADP	111-115	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
15940-4	1977	G6PD "Hofu" had moderately decreased activity, normal electrophoretic mobility, slightly reduced Km G6P, normal Km NADP, normal utilization of 2-deoxy-G6P and Gal-6P, but increased utilization of deamino-NADP and normal heat stability as well as normal pH curve.	NADP	115-119	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
18829-3	1977	The addition of crystalline glucose-6-phosphate dehydrogenase to the  extracts is not accompanied by formation of lactate, but reduced NADP accumulates which oxidizes due to introduction of pyruvate or oxalacetate into the medium.	NADP	135-139	glucose-6-phosphate dehydrogenase	Homo sapiens	28-61	
18829-4	1977	This process is reconstructed in the system with pure enzymes (glucose-6-phosphate dehydrogenase, lactate dehydrogenase), that evidences for hydrogen transfer from reduced NADP to pyruvate, or to the oxalacetate without participation of transhydrogenase.	NADP	172-176	glucose-6-phosphate dehydrogenase	Homo sapiens	63-96	
14326-3	1977	Storage at 4 degrees or heating at 37 degrees over a 120-min period revealed a marked lability of G-6-PD activity in the patient"s cells which could not be stabilized by the addition of NADP and 2-mercaptoethanol; this lability was not seen in other family members tested.	NADP	186-190	glucose-6-phosphate dehydrogenase	Homo sapiens	98-104	
835572-3	1977	Two of them and an additional two cases have the same variant, G6PD Ube, characterized by moderate enzyme deficiency, fast moving enzyme activity on electrophoresis, high Ki Nadph, utilization of substrate analogues, kinetics, pH optima, and stability.	NADP	174-179	glucose-6-phosphate dehydrogenase	Homo sapiens	63-67	
16398-4	1976	Glucose-6-phosphate dehydrogenase, dialyzed in presence of 1-10(-5) M NADP, had critical temperature about 52 degrees within 10 min of incubation; without NADP it was at 45 degrees.	NADP	70-74	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
16398-4	1976	Glucose-6-phosphate dehydrogenase, dialyzed in presence of 1-10(-5) M NADP, had critical temperature about 52 degrees within 10 min of incubation; without NADP it was at 45 degrees.	NADP	155-159	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
1278159-3	1976	NADPH-specific mitochondrial enoyl-CoA reductase can be assayed by a sensitive radioactive test, employing tritium-labelled NADPH, synthesized in a prefixed reaction from D-[1-3H]-glucose via the hexokinase and glucose-6-phosphate dehydrogenase reactions.	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	211-244	
1278159-3	1976	NADPH-specific mitochondrial enoyl-CoA reductase can be assayed by a sensitive radioactive test, employing tritium-labelled NADPH, synthesized in a prefixed reaction from D-[1-3H]-glucose via the hexokinase and glucose-6-phosphate dehydrogenase reactions.	NADP	124-129	glucose-6-phosphate dehydrogenase	Homo sapiens	211-244	
4299-5	1976	The incubation at 37 degrees C in the presence of NADP+ and dithiothreitol normalize Km-G-6-P of platelet G-6-PD; the incubation with boiled and ultrafiltered leukemic granulocyte extracts led to an anodisation of G-6-PD active forms, a decrease of the molecular specific activity and a further increase of Km-G-6-P; these last modifications are the same as those undergone by G-6-PD incubated in crude extracts of normal or leukemic granulocytes.	NADP	50-55	glucose-6-phosphate dehydrogenase	Homo sapiens	106-112	
4299-5	1976	The incubation at 37 degrees C in the presence of NADP+ and dithiothreitol normalize Km-G-6-P of platelet G-6-PD; the incubation with boiled and ultrafiltered leukemic granulocyte extracts led to an anodisation of G-6-PD active forms, a decrease of the molecular specific activity and a further increase of Km-G-6-P; these last modifications are the same as those undergone by G-6-PD incubated in crude extracts of normal or leukemic granulocytes.	NADP	50-55	glucose-6-phosphate dehydrogenase	Homo sapiens	214-220	
4299-5	1976	The incubation at 37 degrees C in the presence of NADP+ and dithiothreitol normalize Km-G-6-P of platelet G-6-PD; the incubation with boiled and ultrafiltered leukemic granulocyte extracts led to an anodisation of G-6-PD active forms, a decrease of the molecular specific activity and a further increase of Km-G-6-P; these last modifications are the same as those undergone by G-6-PD incubated in crude extracts of normal or leukemic granulocytes.	NADP	50-55	glucose-6-phosphate dehydrogenase	Homo sapiens	214-220	
3047-3	1975	Kinetic experiments with glucose-6-phosphate dehydrogenase reveal that, in the dark, the enzyme activity is strongly inhibited by the accumulation of NADPH.	NADP	150-155	glucose-6-phosphate dehydrogenase	Homo sapiens	25-58	
745-2	1975	This stimulation was observed only when the supply of DADPH generating system (isocitric dehydrogenase or glucose 6 phosphate dehydrogenase) was insufficient, leading to a NADPH oxidation rate which was greater than the rate of reduction of NADP+ during the oxidation of a drug.	NADP	172-177	glucose-6-phosphate dehydrogenase	Homo sapiens	106-139	
236846-1	1975	With respect to the enzymes of NADPH-forming metabolic pathways in human leukocytes: (a) Glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating) were less active in leukocytes (mostly myeloblasts) from eight patients with acute myeloblastic leukemia (I) than in leukocytes (mostly granulocytes) from 16 normal subjects (II).	NADP	31-36	glucose-6-phosphate dehydrogenase	Homo sapiens	89-122	
4153668-0	1974	Effects of estradiol and nicotinamide adenine dinucleotide phosphate on the rate of synthesis of uterine glucose 6-phosphate dehydrogenase.	NADP	25-68	glucose-6-phosphate dehydrogenase	Homo sapiens	105-138	
4154443-6	1974	A low NADPH/NADP ratio in unstressed cells deficient in glucose-6-phosphate dehydrogenase is confirmed by direct measurement.	NADP	6-10	glucose-6-phosphate dehydrogenase	Homo sapiens	56-89	
4151903-0	1974	G6PD San Jose: a new variant characterized by NADPH inhibition studies.	NADP	46-51	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
4405605-4	1973	However, examination of the normal and variant enzymes under simulated physiologic conditions, with the effects of various intermediate metabolites and co-enzymes in red cells being taken into consideration, reveal that the G6PD"s from hemolytic variant subjects are strongly inhibited by a physiologic concentration of NADPH because of their high Michaelis constant for NADP or low inhibition constant for NADPH, and they are more sensitive to inhibition by ATP.	NADP	320-325	glucose-6-phosphate dehydrogenase	Homo sapiens	224-228	
4405605-4	1973	However, examination of the normal and variant enzymes under simulated physiologic conditions, with the effects of various intermediate metabolites and co-enzymes in red cells being taken into consideration, reveal that the G6PD"s from hemolytic variant subjects are strongly inhibited by a physiologic concentration of NADPH because of their high Michaelis constant for NADP or low inhibition constant for NADPH, and they are more sensitive to inhibition by ATP.	NADP	320-324	glucose-6-phosphate dehydrogenase	Homo sapiens	224-228	
4405605-4	1973	However, examination of the normal and variant enzymes under simulated physiologic conditions, with the effects of various intermediate metabolites and co-enzymes in red cells being taken into consideration, reveal that the G6PD"s from hemolytic variant subjects are strongly inhibited by a physiologic concentration of NADPH because of their high Michaelis constant for NADP or low inhibition constant for NADPH, and they are more sensitive to inhibition by ATP.	NADP	407-412	glucose-6-phosphate dehydrogenase	Homo sapiens	224-228	
4404963-12	1972	Since even in cells from starved animals, in which the pentose phosphate-cycle activity is extremely low, no accumulation of 6-phosphogluconate was observed, it is concluded that the control of this pathway is achieved by the rate of regeneration of NADP at the site of glucose 6-phosphate dehydrogenase.	NADP	250-254	glucose-6-phosphate dehydrogenase	Homo sapiens	270-303	
4401271-12	1972	These data indicate that a complete absence of leukocyte glucose-6-phosphate dehydrogenase with defective hexose monophosphate shunt activity is associated with low H(2)O(2) production and inadequate bactericidal activity, and further suggest an important role for NADPH in the production of H(2)O(2) in human granulocytes.	NADP	265-270	glucose-6-phosphate dehydrogenase	Homo sapiens	57-90	
5432368-5	1970	Further studies disclosed that both salicylate and gentisate competitively inhibited the G-6-PD from the ASA-sensitive patient resulting in a marked change in the K(m) for NADP.	NADP	172-176	glucose-6-phosphate dehydrogenase	Homo sapiens	89-95	
23195185-2	1970	Based on the activity of the glucose-6-phosphate-dehydrogenase-NADPH(2) cytochrome c reductase system and the ultrastructural findings of free polyribosomes well developed granular endoplasmic reticulum extended Golgi-complex and secretory granules the three main functions of the pentose shunt was discussed: 1. the shunting of ribose-S-phosphate into nucleic acid synthesis 2. the generation of NADPH(2) for lipid synthesis in developing cytoplasmic membranes further supported by the findings of an activity of beta-hydroxybutyrate dehydrogenase and of small scattered lipid droplets in some of the larger cells 3. the ATP production.	NADP	63-68	glucose-6-phosphate dehydrogenase	Homo sapiens	29-62	
4382147-2	1967	Optimum conditions were established for determining the activities of the NADP(+)-linked enzymes, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and isocitrate dehydrogenase, in mosquito tissues.	NADP	74-81	glucose-6-phosphate dehydrogenase	Homo sapiens	98-131	
13922935-0	1962	A study of the mechanism by which triphosphopyridine nucleotide affects human erythrocyte glucose-6-phosphate dehydrogenase.	NADP	34-63	glucose-6-phosphate dehydrogenase	Homo sapiens	90-123	
33326820-4	2021	G6PD is involved in the rate-limiting step of the pentose phosphate pathway, which generates reduced nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	101-144	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
33326820-4	2021	G6PD is involved in the rate-limiting step of the pentose phosphate pathway, which generates reduced nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	146-151	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
33326820-5	2021	In RBCs, the NADPH/G6PD pathway is the only source for recycling reduced glutathione and provides protection from oxidative stress.	NADP	13-18	glucose-6-phosphate dehydrogenase	Homo sapiens	19-23	
33689874-3	2021	Here we developed a reducing equivalent nicotinamide adenine dinucleotide phosphate (NADPH) absorption photometry assay based on enzyme kinetics to characterize G6PD activity.	NADP	40-83	glucose-6-phosphate dehydrogenase	Homo sapiens	161-165	
33689874-3	2021	Here we developed a reducing equivalent nicotinamide adenine dinucleotide phosphate (NADPH) absorption photometry assay based on enzyme kinetics to characterize G6PD activity.	NADP	85-90	glucose-6-phosphate dehydrogenase	Homo sapiens	161-165	
33894275-4	2021	NADP formed, is rapidly converted to NADPH by glucose 6-phosphate dehydrogenase and malic enzymes, overexpressed in tumor cells with mutant p53.	NADP	0-4	glucose-6-phosphate dehydrogenase	Homo sapiens	46-79	
33686238-4	2021	Activated G6PD therefore augments the PPP flux for NADPH and ribose-5-phosphate production which is required for detoxification of intracellular reactive oxygen species (ROS) and biosynthesis of cancer cells, and eventually contributes to tumorigenesis.	NADP	51-56	glucose-6-phosphate dehydrogenase	Homo sapiens	10-14	
33398181-5	2021	NIK prevents autophagic degradation of HK2 through controlling cellular reactive oxygen species levels, which in turn involves modulation of glucose-6-phosphate dehydrogenase (G6PD), an enzyme that mediates production of the antioxidant NADPH.	NADP	237-242	glucose-6-phosphate dehydrogenase	Homo sapiens	141-174	
33562490-8	2021	NADP+/NADPH and GSH/GSSG were measured to determine redox status, and NADPH production by both G6PDH and 6PGDH was assayed spectrophotometrically to characterize pentose phosphate pathway activity.	NADP	70-75	glucose-6-phosphate dehydrogenase	Homo sapiens	95-100	
33468660-4	2021	The crystal structure of G6PD reveals these mutations are located away from the active site, concentrating around the noncatalytic NADP+-binding site and the dimer interface.	NADP	131-136	glucose-6-phosphate dehydrogenase	Homo sapiens	25-29	
33468660-6	2021	To resolve this, we performed integral structural characterization of five G6PD mutants, including four class I mutants, associated with the noncatalytic NADP+ and dimerization, using crystallography, small-angle X-ray scattering (SAXS), cryogenic electron microscopy (cryo-EM), and biophysical analyses.	NADP	154-159	glucose-6-phosphate dehydrogenase	Homo sapiens	75-79	
33398181-5	2021	NIK prevents autophagic degradation of HK2 through controlling cellular reactive oxygen species levels, which in turn involves modulation of glucose-6-phosphate dehydrogenase (G6PD), an enzyme that mediates production of the antioxidant NADPH.	NADP	237-242	glucose-6-phosphate dehydrogenase	Homo sapiens	176-180	
33398181-6	2021	We show that the G6PD-NADPH redox system is important for HK2 stability and metabolism in activated T cells.	NADP	22-27	glucose-6-phosphate dehydrogenase	Homo sapiens	17-21	
31892224-0	2019	Identification of the NADP+ Structural Binding Site and Coenzyme Effect on the Fused G6PD::6PGL Protein from Giardia lamblia.	NADP	22-27	glucose-6-phosphate dehydrogenase	Homo sapiens	85-89	
32033390-6	2020	The flux of glucose into a PPP-particularly under extreme oxidative and toxic challenges-is critical for survival, whereas the glycolytic pathway is primarily activated when glucose is abundant, and there is lack of NADP+ that is required for the activation of glucose-6 phosphate dehydrogenase.	NADP	216-220	glucose-6-phosphate dehydrogenase	Homo sapiens	261-294	
31600627-5	2019	Furthermore, inhibiting glucose-6-phosphate dehydrogenase (G6PD) in the pentose phosphate pathway with dehydroandrosterone (DHEA) and knockdown of G6PD transcripts gradually decreased NADPH when diamide was added to living cells.	NADP	184-189	glucose-6-phosphate dehydrogenase	Homo sapiens	24-57	
31600627-5	2019	Furthermore, inhibiting glucose-6-phosphate dehydrogenase (G6PD) in the pentose phosphate pathway with dehydroandrosterone (DHEA) and knockdown of G6PD transcripts gradually decreased NADPH when diamide was added to living cells.	NADP	184-189	glucose-6-phosphate dehydrogenase	Homo sapiens	59-63	
31600627-5	2019	Furthermore, inhibiting glucose-6-phosphate dehydrogenase (G6PD) in the pentose phosphate pathway with dehydroandrosterone (DHEA) and knockdown of G6PD transcripts gradually decreased NADPH when diamide was added to living cells.	NADP	184-189	glucose-6-phosphate dehydrogenase	Homo sapiens	147-151	
33159852-4	2021	Mechanistically, G6PD augments the NADPH pool by stimulating NAD+ kinase-mediated NADP+ biosynthesis in addition to converting NADP+ to NADPH, bolstering antioxidant defense.	NADP	35-40	glucose-6-phosphate dehydrogenase	Homo sapiens	17-21	
33159852-4	2021	Mechanistically, G6PD augments the NADPH pool by stimulating NAD+ kinase-mediated NADP+ biosynthesis in addition to converting NADP+ to NADPH, bolstering antioxidant defense.	NADP	82-87	glucose-6-phosphate dehydrogenase	Homo sapiens	17-21	
33159852-4	2021	Mechanistically, G6PD augments the NADPH pool by stimulating NAD+ kinase-mediated NADP+ biosynthesis in addition to converting NADP+ to NADPH, bolstering antioxidant defense.	NADP	127-132	glucose-6-phosphate dehydrogenase	Homo sapiens	17-21	
33159852-4	2021	Mechanistically, G6PD augments the NADPH pool by stimulating NAD+ kinase-mediated NADP+ biosynthesis in addition to converting NADP+ to NADPH, bolstering antioxidant defense.	NADP	136-141	glucose-6-phosphate dehydrogenase	Homo sapiens	17-21	
33159852-5	2021	G6PD also increases nucleotide precursor levels through the production of ribose and NADPH, promoting cell proliferation.	NADP	85-90	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
33123534-1	2020	Glucose-6-phosphate dehydrogenase (G6PDH) is the rate-limiting enzyme in the pentose phosphate pathway (PPP) and plays a crucial role in the maintenance of redox homeostasis by producing nicotinamide adenine dinucleotide phosphate (NADPH), the major intracellular reductant.	NADP	187-230	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
33123534-1	2020	Glucose-6-phosphate dehydrogenase (G6PDH) is the rate-limiting enzyme in the pentose phosphate pathway (PPP) and plays a crucial role in the maintenance of redox homeostasis by producing nicotinamide adenine dinucleotide phosphate (NADPH), the major intracellular reductant.	NADP	187-230	glucose-6-phosphate dehydrogenase	Homo sapiens	35-40	
33123534-1	2020	Glucose-6-phosphate dehydrogenase (G6PDH) is the rate-limiting enzyme in the pentose phosphate pathway (PPP) and plays a crucial role in the maintenance of redox homeostasis by producing nicotinamide adenine dinucleotide phosphate (NADPH), the major intracellular reductant.	NADP	232-237	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
33123534-1	2020	Glucose-6-phosphate dehydrogenase (G6PDH) is the rate-limiting enzyme in the pentose phosphate pathway (PPP) and plays a crucial role in the maintenance of redox homeostasis by producing nicotinamide adenine dinucleotide phosphate (NADPH), the major intracellular reductant.	NADP	232-237	glucose-6-phosphate dehydrogenase	Homo sapiens	35-40	
33123534-5	2020	Mechanistically, caffeine directly binds to G6PDH with high affinity (K D = 0.1923 muM) and competes with the coenzyme NADP+ for G6PDH binding, as demonstrated by the decreased binding affinities of G6PDH for its coenzyme and substrate.	NADP	119-124	glucose-6-phosphate dehydrogenase	Homo sapiens	129-134	
33123534-5	2020	Mechanistically, caffeine directly binds to G6PDH with high affinity (K D = 0.1923 muM) and competes with the coenzyme NADP+ for G6PDH binding, as demonstrated by the decreased binding affinities of G6PDH for its coenzyme and substrate.	NADP	119-124	glucose-6-phosphate dehydrogenase	Homo sapiens	129-134	
33123534-6	2020	Molecular docking studies revealed that caffeine binds to G6PDH at the structural NADP+ binding site, and chemical cross-linking analysis demonstrated that caffeine inhibits the formation of dimeric G6PDH.	NADP	82-87	glucose-6-phosphate dehydrogenase	Homo sapiens	58-63	
33123534-8	2020	Moreover, inhibition of G6PDH activity by caffeine led to a reduction in the intracellular levels of NADPH and reactive oxygen species (ROS), and altered the expression of redox-related proteins in RCC cells.	NADP	101-106	glucose-6-phosphate dehydrogenase	Homo sapiens	24-29	
32650494-5	2020	The kinetic parameters for the G6PD domain were determined using glucose-6-phosphate (G6P) and nicotinamide adenine dinucleotide phosphate (NADP+) as substrates.	NADP	95-138	glucose-6-phosphate dehydrogenase	Homo sapiens	31-35	
32650494-5	2020	The kinetic parameters for the G6PD domain were determined using glucose-6-phosphate (G6P) and nicotinamide adenine dinucleotide phosphate (NADP+) as substrates.	NADP	140-145	glucose-6-phosphate dehydrogenase	Homo sapiens	31-35	
31707353-1	2020	Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway that modulates cellular redox homeostasis via the regeneration of NADPH.	NADP	168-173	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
31707353-1	2020	Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway that modulates cellular redox homeostasis via the regeneration of NADPH.	NADP	168-173	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
31892224-4	2019	The objective of the present work was to show the presence of the structural NADP+ binding site on the fused G6PD::6PGL protein and evaluate the effect of the NADP+ molecule on protein stability using biochemical and computational analysis.	NADP	77-82	glucose-6-phosphate dehydrogenase	Homo sapiens	109-113	
31892224-6	2019	By molecular docking, we determined the possible structural-NADP+ binding site, which is located between the Rossmann fold of G6PD and 6PGL.	NADP	60-65	glucose-6-phosphate dehydrogenase	Homo sapiens	126-130	
32117550-2	2019	Glucose-6-phosphate dehydrogenase (G6PD) produces nicotinamide adenine dinucleotide phosphate (NADPH) via the pentose phosphate pathway.	NADP	50-93	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
30403147-2	2019	Recent Advances and Critical Issues: Aspects of vascular remodeling induction mechanisms described are associated with shifts in glucose metabolism through the pentose phosphate pathway and increased cytosolic NADPH generation by glucose-6-phosphate dehydrogenase, increased glycolysis generation of cytosolic NADH and lactate, mitochondrial dysfunction associated with superoxide dismutase-2 depletion, changes in reactive oxygen species and iron metabolism, and redox signaling.	NADP	210-215	glucose-6-phosphate dehydrogenase	Homo sapiens	230-263	
32117550-2	2019	Glucose-6-phosphate dehydrogenase (G6PD) produces nicotinamide adenine dinucleotide phosphate (NADPH) via the pentose phosphate pathway.	NADP	50-93	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
32117550-2	2019	Glucose-6-phosphate dehydrogenase (G6PD) produces nicotinamide adenine dinucleotide phosphate (NADPH) via the pentose phosphate pathway.	NADP	95-100	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
32117550-2	2019	Glucose-6-phosphate dehydrogenase (G6PD) produces nicotinamide adenine dinucleotide phosphate (NADPH) via the pentose phosphate pathway.	NADP	95-100	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
31500396-1	2019	The generation of reducing equivalent NADPH via glucose-6-phosphate dehydrogenase (G6PD) is critical for the maintenance of redox homeostasis and reductive biosynthesis in cells.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	48-81	
31500396-1	2019	The generation of reducing equivalent NADPH via glucose-6-phosphate dehydrogenase (G6PD) is critical for the maintenance of redox homeostasis and reductive biosynthesis in cells.	NADP	38-43	glucose-6-phosphate dehydrogenase	Homo sapiens	83-87	
31183991-4	2019	Our study supports a mechanism of action whereby AG1 bridges the dimer interface at the structural nicotinamide adenine dinucleotide phosphate (NADP+ ) binding sites of two interacting G6PD monomers.	NADP	99-142	glucose-6-phosphate dehydrogenase	Homo sapiens	185-189	
31183991-4	2019	Our study supports a mechanism of action whereby AG1 bridges the dimer interface at the structural nicotinamide adenine dinucleotide phosphate (NADP+ ) binding sites of two interacting G6PD monomers.	NADP	144-149	glucose-6-phosphate dehydrogenase	Homo sapiens	185-189	
31058257-5	2019	Loss of G6PD results in high NADP, which induces compensatory increases in ME1 and IDH1 flux.	NADP	29-33	glucose-6-phosphate dehydrogenase	Homo sapiens	8-12	
30661088-3	2019	It was hypothesized that double deficiency of the NADPH-generating enzymes, GSPD-1 (Glucose-6-phosphate 1-dehydrogenase), a functional homolog of human glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the pentose phosphate pathway, and IDH-1 (isocitrate dehydrogenase-1) affect growth and development in the nematode, Caenorhabditis elegans (C. elegans).	NADP	50-55	glucose-6-phosphate dehydrogenase	Homo sapiens	152-185	
30661088-3	2019	It was hypothesized that double deficiency of the NADPH-generating enzymes, GSPD-1 (Glucose-6-phosphate 1-dehydrogenase), a functional homolog of human glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the pentose phosphate pathway, and IDH-1 (isocitrate dehydrogenase-1) affect growth and development in the nematode, Caenorhabditis elegans (C. elegans).	NADP	50-55	glucose-6-phosphate dehydrogenase	Homo sapiens	187-191	
30930048-1	2019	Glucose-6-phosphate dehydrogenase (G6PDH) is the key enzyme supplying reducing power (NADPH) to the cells, by oxidation of glucose-6-phosphate (G6P), and in the process providing a precursor of ribose-5-phosphate.	NADP	86-91	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
30930048-1	2019	Glucose-6-phosphate dehydrogenase (G6PDH) is the key enzyme supplying reducing power (NADPH) to the cells, by oxidation of glucose-6-phosphate (G6P), and in the process providing a precursor of ribose-5-phosphate.	NADP	86-91	glucose-6-phosphate dehydrogenase	Homo sapiens	35-40	
30582899-1	2019	Glucose-6-phosphate dehydrogenase is a major enzyme that supplies the reducing agent nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), which is required to recycle oxidized/glutathione disulfide (GSSH) to reduced glutathione (GSH).	NADP	139-144	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
28692052-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme that generates NADPH to maintain reduced glutathione (GSH), which scavenges reactive oxygen species (ROS) to protect cancer cell from oxidative damage.	NADP	72-77	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
30593978-8	2019	Blocking NADPH generation with the G6PD inhibitor dehydroepiandrosterone was found to protect against AGE-induced oxidant species generation, loss of viability, and neurite degeneration.	NADP	9-14	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
30123865-1	2018	Background: Glucose-6-phosphate dehydrogenase (G6PD) is the first enzyme of the pentose phosphate metabolic pathway that supplies reducing agents by maintaining the level of reduced nicotinamide adenine dinucleotide phosphate.	NADP	182-225	glucose-6-phosphate dehydrogenase	Homo sapiens	12-45	
30123865-1	2018	Background: Glucose-6-phosphate dehydrogenase (G6PD) is the first enzyme of the pentose phosphate metabolic pathway that supplies reducing agents by maintaining the level of reduced nicotinamide adenine dinucleotide phosphate.	NADP	182-225	glucose-6-phosphate dehydrogenase	Homo sapiens	47-51	
29471502-3	2018	Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the PPP, is elevated in many cancers and contributes to tumor growth by producing ribose-5-phosphate and NADPH through PPP.	NADP	175-180	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
29471502-3	2018	Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme of the PPP, is elevated in many cancers and contributes to tumor growth by producing ribose-5-phosphate and NADPH through PPP.	NADP	175-180	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
28986240-1	2018	Glucose-6-phosphate dehydrogenase (G6PDH) (EC 1.1.1.363) plays an important role in the human pathogen Pseudomonas aeruginosa because it generates NADPH, an essential cofactor for several biosynthetic pathways and antioxidant enzymes.	NADP	147-152	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
28986240-1	2018	Glucose-6-phosphate dehydrogenase (G6PDH) (EC 1.1.1.363) plays an important role in the human pathogen Pseudomonas aeruginosa because it generates NADPH, an essential cofactor for several biosynthetic pathways and antioxidant enzymes.	NADP	147-152	glucose-6-phosphate dehydrogenase	Homo sapiens	35-40	
29228460-3	2018	The latter can be engaged in NADP-specific coupled enzymatic transformations involving conversion to Ntz ADPH by glucose-6-phosphate dehydrogenase and reoxidation to Ntz ADP+ by glutathione reductase.	NADP	29-33	glucose-6-phosphate dehydrogenase	Homo sapiens	113-146	
29312589-6	2017	G6PD up-regulated ROS generation by facilitating NADPH-dependent NOX4 activation, which led to increased expression of p-STAT3 and CyclinD1.	NADP	49-54	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
30272333-10	2018	Consequently, oxidative PPP flux analysis revealed that suppression of G6PD by miR-1 decreased the production of nicotinamide adenine dinucleotide phosphate and the glycolysis of pituitary cancer cells.	NADP	113-156	glucose-6-phosphate dehydrogenase	Homo sapiens	71-75	
30123865-12	2018	Conclusion: Higher spermatozoa G6PD activity in October, where the level of polyunsaturated fatty acids is suggested to be increased, may reflect the increased need of nicotinamide adenine dinucleotide phosphate and thus higher G6PD activity for the oxidative balance.	NADP	168-211	glucose-6-phosphate dehydrogenase	Homo sapiens	31-35	
29531803-6	2018	Within these gene networks, glucose-6-phosphate dehydrogenase (G6PD), the first and rate-limiting enzyme (producing NADPH) in pentose phosphate pathway, emerged as the critical node regulating cellular effects of H2S.	NADP	116-121	glucose-6-phosphate dehydrogenase	Homo sapiens	28-61	
29531803-6	2018	Within these gene networks, glucose-6-phosphate dehydrogenase (G6PD), the first and rate-limiting enzyme (producing NADPH) in pentose phosphate pathway, emerged as the critical node regulating cellular effects of H2S.	NADP	116-121	glucose-6-phosphate dehydrogenase	Homo sapiens	63-67	
28402154-2	2017	Glucose-6-phosphate dehydrogenase is an enzyme that leads to the production of NADPH, required to destroy microorganisms in the respiratory burst reaction of white blood cells.	NADP	79-84	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
28609580-4	2017	Meanwhile, a pool of NADPH-the reductive engine of many ROS-combating enzymes-is maintained by metabolic enzymes including, but not exclusively, glucose-6 phosphate dehydrogenase (G6PDH) and NADP-dependent isocitrate dehydrogenase (ICDH-NADP).	NADP	21-26	glucose-6-phosphate dehydrogenase	Homo sapiens	145-178	
28609580-4	2017	Meanwhile, a pool of NADPH-the reductive engine of many ROS-combating enzymes-is maintained by metabolic enzymes including, but not exclusively, glucose-6 phosphate dehydrogenase (G6PDH) and NADP-dependent isocitrate dehydrogenase (ICDH-NADP).	NADP	21-26	glucose-6-phosphate dehydrogenase	Homo sapiens	180-185	
28692052-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme that generates NADPH to maintain reduced glutathione (GSH), which scavenges reactive oxygen species (ROS) to protect cancer cell from oxidative damage.	NADP	72-77	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
28692052-5	2017	Suppressing G6PD decreases NADPH production, lowers GSH levels, impairs the ability to scavenge ROS levels, and enhances oxaliplatin-induced apoptosis in CRC via ROS-mediated damage in vitro.	NADP	27-32	glucose-6-phosphate dehydrogenase	Homo sapiens	12-16	
28692052-7	2017	In summary, our finding indicated that disrupting G6PD-mediated NADPH homeostasis enhances oxaliplatin-induced apoptosis in CRC through redox modulation.	NADP	64-69	glucose-6-phosphate dehydrogenase	Homo sapiens	50-54	
28581494-4	2017	We found that mammalian cells have a strong tendency to maintain physiological NADPH homeostasis, which is regulated by glucose-6-phosphate dehydrogenase and AMP kinase.	NADP	79-84	glucose-6-phosphate dehydrogenase	Homo sapiens	120-153	
28370139-1	2017	Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the oxidation of glucose-6-phoshate to 6-phospho-gluconolactone with the concomitant reduction of NADP+ to NADPH.	NADP	150-155	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
28370139-1	2017	Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the oxidation of glucose-6-phoshate to 6-phospho-gluconolactone with the concomitant reduction of NADP+ to NADPH.	NADP	150-155	glucose-6-phosphate dehydrogenase	Homo sapiens	35-40	
28370139-1	2017	Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the oxidation of glucose-6-phoshate to 6-phospho-gluconolactone with the concomitant reduction of NADP+ to NADPH.	NADP	159-164	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
28370139-1	2017	Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the oxidation of glucose-6-phoshate to 6-phospho-gluconolactone with the concomitant reduction of NADP+ to NADPH.	NADP	159-164	glucose-6-phosphate dehydrogenase	Homo sapiens	35-40	
27789056-5	2017	Both global and tubular-specific Nrf2 activation enhanced gene expression of antioxidant and NADPH synthesis enzymes, including glucose-6-phosphate dehydrogenase, and ameliorated both the initiation of injury in the outer medulla and the progression of tubular damage in the cortex.	NADP	93-98	glucose-6-phosphate dehydrogenase	Homo sapiens	128-161	
28425844-8	2017	Here, we provide an overview of cell type- specific roles of G6PD in the regulation of ROS balance as well as additional details on the significance of G6PD that contributes to pro-oxidant NADPH generation in obesity-related chronic inflammation and insulin resistance.	NADP	189-194	glucose-6-phosphate dehydrogenase	Homo sapiens	152-156	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	137-180	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
28041936-4	2017	Recently, it has been suggested that a quick acceleration mechanism of G6PD activity could be produced by the reduction of NADPH-inhibition of G6PD.	NADP	123-128	glucose-6-phosphate dehydrogenase	Homo sapiens	71-75	
28041936-4	2017	Recently, it has been suggested that a quick acceleration mechanism of G6PD activity could be produced by the reduction of NADPH-inhibition of G6PD.	NADP	123-128	glucose-6-phosphate dehydrogenase	Homo sapiens	143-147	
27755120-2	2017	G6PD is the main source of the essential cellular reductant, NADPH.	NADP	61-66	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
27755120-3	2017	The purpose of this review is to describe the biochemistry of G6PD and NADPH, cellular factors that regulate G6PD, normal physiologic roles of G6PD, and the pathogenic role altered G6PD/NADPH plays in kidney disease.	NADP	186-191	glucose-6-phosphate dehydrogenase	Homo sapiens	62-66	
27941691-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme in the pentose phosphate pathway which produces nicotinamide adenine dinucleotide phosphate (NADPH) to maintain an adequate reducing environment in the cells and is especially important in red blood cells (RBC).	NADP	116-159	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27941691-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme in the pentose phosphate pathway which produces nicotinamide adenine dinucleotide phosphate (NADPH) to maintain an adequate reducing environment in the cells and is especially important in red blood cells (RBC).	NADP	116-159	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
27941691-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme in the pentose phosphate pathway which produces nicotinamide adenine dinucleotide phosphate (NADPH) to maintain an adequate reducing environment in the cells and is especially important in red blood cells (RBC).	NADP	161-166	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27941691-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme in the pentose phosphate pathway which produces nicotinamide adenine dinucleotide phosphate (NADPH) to maintain an adequate reducing environment in the cells and is especially important in red blood cells (RBC).	NADP	161-166	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
28090457-2	2016	G6PD plays a key role in the pentose phosphate pathway, which is a major source of nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	83-126	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
28090457-2	2016	G6PD plays a key role in the pentose phosphate pathway, which is a major source of nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	128-133	glucose-6-phosphate dehydrogenase	Homo sapiens	0-4	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	137-180	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	182-187	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	182-187	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	220-225	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	220-225	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	229-234	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27914961-1	2017	Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme in the pentose phosphate pathway that ensures sufficient production of coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) by catalyzing the reduction of NADP+ to NADPH.	NADP	229-234	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
27711253-6	2016	Besides, HSPB1 activates G6PD to sustain cellular NADPH and pentose production in glioma cells.	NADP	50-55	glucose-6-phosphate dehydrogenase	Homo sapiens	25-29	
27582489-2	2016	NADP+ is then reduced to NADPH by dehydrogenases, in particular glucose-6-phosphate dehydrogenase and the malic enzymes.	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	64-97	
27582489-2	2016	NADP+ is then reduced to NADPH by dehydrogenases, in particular glucose-6-phosphate dehydrogenase and the malic enzymes.	NADP	25-30	glucose-6-phosphate dehydrogenase	Homo sapiens	64-97	
27353740-1	2016	In mature erythrocytes, glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) yield NADPH, a crucial cofactor of the enzyme glutathione reductase (GR) converting glutathione disulfide (GSSG) into its reduced state (GSH).	NADP	117-122	glucose-6-phosphate dehydrogenase	Homo sapiens	24-57	
27335172-4	2016	JO2 was measured via a polarigraphic oxygen sensor and JATP via fluorescence using an enzyme-linked assay system (hexokinase II, glucose-6-phosphate dehydrogenase) linked to NADPH production.	NADP	174-179	glucose-6-phosphate dehydrogenase	Homo sapiens	129-162	
27356773-9	2016	Acetylation of G6PD at several sites, including K235 (K205 in isoform b), may mediate inhibition of G6PD activity, which may contribute to the ability of aspirin to exert anticancer effects through decreased synthesis of ribose sugars and NADPH.	NADP	239-244	glucose-6-phosphate dehydrogenase	Homo sapiens	15-19	
27356773-9	2016	Acetylation of G6PD at several sites, including K235 (K205 in isoform b), may mediate inhibition of G6PD activity, which may contribute to the ability of aspirin to exert anticancer effects through decreased synthesis of ribose sugars and NADPH.	NADP	239-244	glucose-6-phosphate dehydrogenase	Homo sapiens	100-104	
27113762-3	2016	Here, we report that SIRT5 desuccinylates and deglutarylates isocitrate dehydrogenase 2 (IDH2) and glucose-6-phosphate dehydrogenase (G6PD), respectively, and thus activates both NADPH-producing enzymes.	NADP	179-184	glucose-6-phosphate dehydrogenase	Homo sapiens	99-132	
27113762-3	2016	Here, we report that SIRT5 desuccinylates and deglutarylates isocitrate dehydrogenase 2 (IDH2) and glucose-6-phosphate dehydrogenase (G6PD), respectively, and thus activates both NADPH-producing enzymes.	NADP	179-184	glucose-6-phosphate dehydrogenase	Homo sapiens	134-138	
27113762-4	2016	Moreover, we show that knockdown or knockout of SIRT5 leads to high levels of cellular ROS SIRT5 inactivation leads to the inhibition of IDH2 and G6PD, thereby decreasing NADPH production, lowering GSH, impairing the ability to scavenge ROS, and increasing cellular susceptibility to oxidative stress.	NADP	171-176	glucose-6-phosphate dehydrogenase	Homo sapiens	146-150	
27113762-5	2016	Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH homeostasis and redox potential by promoting IDH2 desuccinylation and G6PD deglutarylation.	NADP	71-76	glucose-6-phosphate dehydrogenase	Homo sapiens	147-151	
27586085-0	2016	SIRT2 activates G6PD to enhance NADPH production and promote leukaemia cell proliferation.	NADP	32-37	glucose-6-phosphate dehydrogenase	Homo sapiens	16-20	
27586085-5	2016	Knockdown of G6PD reduces NADPH level in acute myeloid leukaemia (AML) cell lines.	NADP	26-31	glucose-6-phosphate dehydrogenase	Homo sapiens	13-17	
27586085-7	2016	Deacetylase SIRT2 promotes NADPH production through deacetylating G6PD at lysine 403 (K403).	NADP	27-32	glucose-6-phosphate dehydrogenase	Homo sapiens	66-70	
26827633-1	2016	OBJECTIVE: The enzyme glucose-6-phosphate dehydrogenase (G6PD) catalyses the first step in the pentose phosphate pathway, producing nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	132-175	glucose-6-phosphate dehydrogenase	Homo sapiens	22-55	
26827633-1	2016	OBJECTIVE: The enzyme glucose-6-phosphate dehydrogenase (G6PD) catalyses the first step in the pentose phosphate pathway, producing nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	132-175	glucose-6-phosphate dehydrogenase	Homo sapiens	57-61	
26827633-1	2016	OBJECTIVE: The enzyme glucose-6-phosphate dehydrogenase (G6PD) catalyses the first step in the pentose phosphate pathway, producing nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	177-182	glucose-6-phosphate dehydrogenase	Homo sapiens	22-55	
26827633-1	2016	OBJECTIVE: The enzyme glucose-6-phosphate dehydrogenase (G6PD) catalyses the first step in the pentose phosphate pathway, producing nicotinamide adenine dinucleotide phosphate (NADPH).	NADP	177-182	glucose-6-phosphate dehydrogenase	Homo sapiens	57-61	
27053284-7	2016	The presence of NADP(+) is shown to improve the stability of G6PD enzymes.	NADP	16-23	glucose-6-phosphate dehydrogenase	Homo sapiens	61-65	
26802575-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) regulates nicotinamide adenine dinucleotide phosphate (NADPH) levels and is related to the pathogenesis of various diseases, including G6PD deficiency, type 2 diabetes, aldosterone-induced endothelial dysfunction, and cancer.	NADP	51-94	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
26802575-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) regulates nicotinamide adenine dinucleotide phosphate (NADPH) levels and is related to the pathogenesis of various diseases, including G6PD deficiency, type 2 diabetes, aldosterone-induced endothelial dysfunction, and cancer.	NADP	51-94	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
26802575-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) regulates nicotinamide adenine dinucleotide phosphate (NADPH) levels and is related to the pathogenesis of various diseases, including G6PD deficiency, type 2 diabetes, aldosterone-induced endothelial dysfunction, and cancer.	NADP	96-101	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
26802575-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) regulates nicotinamide adenine dinucleotide phosphate (NADPH) levels and is related to the pathogenesis of various diseases, including G6PD deficiency, type 2 diabetes, aldosterone-induced endothelial dysfunction, and cancer.	NADP	96-101	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
26921441-2	2016	In this study, we tested the hypothesis that inhibition of glucose-6-phosphate dehydrogenase (G6PD), a major source of NADPH in the cell, prevents 20-HETE synthesis and 20-HETE-induced proinflammatory signaling that promotes secretory phenotype of vascular smooth muscle cells.	NADP	119-124	glucose-6-phosphate dehydrogenase	Homo sapiens	59-92	
26921441-2	2016	In this study, we tested the hypothesis that inhibition of glucose-6-phosphate dehydrogenase (G6PD), a major source of NADPH in the cell, prevents 20-HETE synthesis and 20-HETE-induced proinflammatory signaling that promotes secretory phenotype of vascular smooth muscle cells.	NADP	119-124	glucose-6-phosphate dehydrogenase	Homo sapiens	94-98	
27353740-1	2016	In mature erythrocytes, glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) yield NADPH, a crucial cofactor of the enzyme glutathione reductase (GR) converting glutathione disulfide (GSSG) into its reduced state (GSH).	NADP	117-122	glucose-6-phosphate dehydrogenase	Homo sapiens	59-64	
27353740-8	2016	The specific G6PDH inhibitory effect of these compounds may be exploited for the treatment of human diseases with high NADPH and GSH consumption rates, including malaria, trypanosomiasis, cancer or obesity.	NADP	119-124	glucose-6-phosphate dehydrogenase	Homo sapiens	13-18	
27097228-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) provides the reducing agent NADPH to meet the cellular needs for reductive biosynthesis and the maintenance of redox homeostasis.	NADP	69-74	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27097228-1	2016	Glucose-6-phosphate dehydrogenase (G6PD) provides the reducing agent NADPH to meet the cellular needs for reductive biosynthesis and the maintenance of redox homeostasis.	NADP	69-74	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
27009267-4	2016	Excess G6PD shunted glucose into the pentose phosphate pathway, resulting in NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) accumulation and reactive oxygen species (ROS) consumption.	NADP	77-82	glucose-6-phosphate dehydrogenase	Homo sapiens	7-11	
27232511-3	2016	The results in this study confirm and extend previous observations that RRx-001 exerts its anti-proliferative effect, at least partially, through interference with glucose 6 phosphate dehydrogenase (G6PD), a key enzyme in the pentose phosphate pathway, responsible for maintaining adequate levels of the major cellular reductant, NADPH.	NADP	330-335	glucose-6-phosphate dehydrogenase	Homo sapiens	164-197	
27232511-3	2016	The results in this study confirm and extend previous observations that RRx-001 exerts its anti-proliferative effect, at least partially, through interference with glucose 6 phosphate dehydrogenase (G6PD), a key enzyme in the pentose phosphate pathway, responsible for maintaining adequate levels of the major cellular reductant, NADPH.	NADP	330-335	glucose-6-phosphate dehydrogenase	Homo sapiens	199-203	
26774511-10	2016	In support of this concept, the expression of GCLC (which codes for the rate-limiting enzyme in GSH synthesis) and genes which generate reducing equivalents in the form of NADPH (ie, G6PD, PGD, IDH2) are elevated in 1,25D-treated cells.	NADP	172-177	glucose-6-phosphate dehydrogenase	Homo sapiens	183-187	
26763177-0	2016	NADP+ binding effects tryptophan accessibility, folding and stability of recombinant B. malayi G6PD.	NADP	0-5	glucose-6-phosphate dehydrogenase	Homo sapiens	95-99	
27009267-4	2016	Excess G6PD shunted glucose into the pentose phosphate pathway, resulting in NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) accumulation and reactive oxygen species (ROS) consumption.	NADP	100-143	glucose-6-phosphate dehydrogenase	Homo sapiens	7-11	
26694452-4	2015	The HSCARG protein, a nicotinamide adenine dinucleotide phosphate (NADPH) sensor and negative regulator of NF-kappaB, was upregulated in G6PD-knockdown cells with decreased NADPH/NADP+ ratio.	NADP	22-65	glucose-6-phosphate dehydrogenase	Homo sapiens	137-141	
26456480-2	2016	Glucose-6-phosphate dehydrogenase (G6PD) is essential for protection against oxidative stress by producing NADPH.	NADP	107-112	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
26456480-2	2016	Glucose-6-phosphate dehydrogenase (G6PD) is essential for protection against oxidative stress by producing NADPH.	NADP	107-112	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
26711700-1	2016	CONTEXT: Glucose-6-phosphate dehydrogenase (G6PD) is an important enzyme of hexose monophosphate shunt, involved in the biosynthesis of reduced nicotinamide adenine dinucleotide phosphate hydrogen (NADPH).	NADP	198-203	glucose-6-phosphate dehydrogenase	Homo sapiens	9-42	
26711700-1	2016	CONTEXT: Glucose-6-phosphate dehydrogenase (G6PD) is an important enzyme of hexose monophosphate shunt, involved in the biosynthesis of reduced nicotinamide adenine dinucleotide phosphate hydrogen (NADPH).	NADP	198-203	glucose-6-phosphate dehydrogenase	Homo sapiens	44-48	
26694452-0	2015	Glucose-6-Phosphate Dehydrogenase Enhances Antiviral Response through Downregulation of NADPH Sensor HSCARG and Upregulation of NF-kappaB Signaling.	NADP	88-93	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27974910-3	2016	Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway, which leads to the production of NADPH.	NADP	121-126	glucose-6-phosphate dehydrogenase	Homo sapiens	0-33	
27974910-3	2016	Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway, which leads to the production of NADPH.	NADP	121-126	glucose-6-phosphate dehydrogenase	Homo sapiens	35-39	
27656260-8	2016	The NADPH/NADP and GSH/GSSG ratio were significantly lower in the cells with inhibited G6PD than in the control cells at the same BQ concentration.	NADP	4-9	glucose-6-phosphate dehydrogenase	Homo sapiens	87-91	
27656260-8	2016	The NADPH/NADP and GSH/GSSG ratio were significantly lower in the cells with inhibited G6PD than in the control cells at the same BQ concentration.	NADP	4-8	glucose-6-phosphate dehydrogenase	Homo sapiens	87-91	
26694452-4	2015	The HSCARG protein, a nicotinamide adenine dinucleotide phosphate (NADPH) sensor and negative regulator of NF-kappaB, was upregulated in G6PD-knockdown cells with decreased NADPH/NADP+ ratio.	NADP	67-72	glucose-6-phosphate dehydrogenase	Homo sapiens	137-141	
26694452-4	2015	The HSCARG protein, a nicotinamide adenine dinucleotide phosphate (NADPH) sensor and negative regulator of NF-kappaB, was upregulated in G6PD-knockdown cells with decreased NADPH/NADP+ ratio.	NADP	173-178	glucose-6-phosphate dehydrogenase	Homo sapiens	137-141	
26694452-4	2015	The HSCARG protein, a nicotinamide adenine dinucleotide phosphate (NADPH) sensor and negative regulator of NF-kappaB, was upregulated in G6PD-knockdown cells with decreased NADPH/NADP+ ratio.	NADP	179-184	glucose-6-phosphate dehydrogenase	Homo sapiens	137-141	
26160839-4	2015	As expected, reduced level of NADPH was also observed, at least in part due to inactivation of glucose-6-phosphate dehydrogenase in pentose phosphate pathway upon HF treatment.	NADP	30-35	glucose-6-phosphate dehydrogenase	Homo sapiens	95-128	
26198639-6	2015	Herein we demonstrate that a metabolic shift toward the pentose phosphate pathway (PPP) is necessary for NET release because glucose-6-phosphate dehydrogenase (G6PD), an important enzyme from PPP, fuels NADPH oxidase with NADPH to produce superoxide and thus induce NETs.	NADP	203-208	glucose-6-phosphate dehydrogenase	Homo sapiens	125-158	
26198639-6	2015	Herein we demonstrate that a metabolic shift toward the pentose phosphate pathway (PPP) is necessary for NET release because glucose-6-phosphate dehydrogenase (G6PD), an important enzyme from PPP, fuels NADPH oxidase with NADPH to produce superoxide and thus induce NETs.	NADP	203-208	glucose-6-phosphate dehydrogenase	Homo sapiens	160-164	
26468025-1	2015	Bioluminescent method for measurements of the neutrophilic NAD(P)-dependent dehydrogenases (lactate dehydrogenase, NAD-dependent malate dehydrogenase, NADP-dependent decarboxylating malate dehydrogenase, NAD-dependent isocitrate dehydrogenase, and glucose- 6-phosphate dehydrogenase) is developed.	NADP	59-65	glucose-6-phosphate dehydrogenase	Homo sapiens	248-282	
26291555-9	2015	Elevated levels of activated G6PD consequent to PDGF-BB induction led to increased dihydronicotinamide adenine dinucleotide phosphate generation through stimulation of the pentose phosphate pathway, which enhanced VSMC viability and reduced apoptosis in vivo and in vitro via glutathione homeostasis.	NADP	83-133	glucose-6-phosphate dehydrogenase	Homo sapiens	29-33	
25556665-1	2015	AIMS: Glucose 6-phosphate dehydrogenase (G6PD) is essential for maintenance of nicotinamide dinucleotide hydrogen phosphate (NADPH) levels and redox homeostasis.	NADP	125-130	glucose-6-phosphate dehydrogenase	Homo sapiens	6-39	
25556665-1	2015	AIMS: Glucose 6-phosphate dehydrogenase (G6PD) is essential for maintenance of nicotinamide dinucleotide hydrogen phosphate (NADPH) levels and redox homeostasis.	NADP	125-130	glucose-6-phosphate dehydrogenase	Homo sapiens	41-45	
25661916-6	2015	The level of tryptophan in membranes was determined by spectrofluorimetry, whilst the activity of glucose-6-phosphate dehydrogenase was determined by measuring the reduction of oxidated NADP.	NADP	186-190	glucose-6-phosphate dehydrogenase	Homo sapiens	98-131	
25121555-1	2014	The enzyme glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the first step of the oxidative branch of the pentose phosphate pathway, which provides cells with NADPH, an essential cofactor for many biosynthetic pathways and antioxidizing enzymes.	NADP	162-167	glucose-6-phosphate dehydrogenase	Homo sapiens	11-44	
25121555-1	2014	The enzyme glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the first step of the oxidative branch of the pentose phosphate pathway, which provides cells with NADPH, an essential cofactor for many biosynthetic pathways and antioxidizing enzymes.	NADP	162-167	glucose-6-phosphate dehydrogenase	Homo sapiens	46-51	
25408203-3	2014	The paradox consists of the strong inhibition that the NADPH exerts on the both dehydrogenases of the pathway, especially on the regulating enzyme glucose-6-phosphate dehydrogenase (G6PD).	NADP	55-60	glucose-6-phosphate dehydrogenase	Homo sapiens	147-180	
25408203-3	2014	The paradox consists of the strong inhibition that the NADPH exerts on the both dehydrogenases of the pathway, especially on the regulating enzyme glucose-6-phosphate dehydrogenase (G6PD).	NADP	55-60	glucose-6-phosphate dehydrogenase	Homo sapiens	182-186	
25408203-4	2014	Theoretically, in anabolic situations, the increase of gene expression of G6PD and 6-phosphogluconate dehydrogenase can induce a rise in the production of NADPH, which would cause the immediate inhibition of the enzyme and a drastic flow reduction.	NADP	155-160	glucose-6-phosphate dehydrogenase	Homo sapiens	74-78	
25408203-7	2014	In 1974, the presence of a protein capable of reversing the inhibition of G6PD by NADPH was detected; however, to date, this paradox remains undisclosed.	NADP	82-87	glucose-6-phosphate dehydrogenase	Homo sapiens	74-78	
25408203-9	2014	The model has many similarities with the hypothesis proposed some 40 years back on the reversion of G6PD inhibition by NADPH.	NADP	119-124	glucose-6-phosphate dehydrogenase	Homo sapiens	100-104