PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
19733906-0	2009	Placental expression of 2,3 bisphosphoglycerate mutase in IGF-II knock out mouse: correlation of circulating maternal 2,3 bisphosphoglycerate and fetal growth.	2,3-Diphosphoglycerate	24-47	insulin-like growth factor 2	Mus musculus	58-64
19733906-1	2009	Bisphosphoglycerate mutase (BPGM) catalyses the formation of 2,3 bisphosphoglycerate (BPG) a ligand of haemoglobin.	2,3-Diphosphoglycerate	61-84	2,3-bisphosphoglycerate mutase	Mus musculus	0-26
19733906-1	2009	Bisphosphoglycerate mutase (BPGM) catalyses the formation of 2,3 bisphosphoglycerate (BPG) a ligand of haemoglobin.	2,3-Diphosphoglycerate	61-84	2,3-bisphosphoglycerate mutase	Mus musculus	28-32
17897734-2	2007	Two distinct types of PGM exist in nature, one that requires 2,3-bisphosphoglycerate as a cofactor (dPGM) and another that does not (iPGM).	2,3-Diphosphoglycerate	61-84	Phosphoglucose mutase 1	Drosophila melanogaster	22-25
18793248-1	2009	BACKGROUND: High oxygen-affinity haemoglobin variants and 2,3-diphosphoglycerate (2,3-DPG) deficiency are inherited diseases generating low tissue oxygen tension and erythropoietin-driven erythrocytosis, that characterizes the clinical phenotype of patients.	2,3-Diphosphoglycerate	58-80	erythropoietin	Homo sapiens	166-180
18793248-1	2009	BACKGROUND: High oxygen-affinity haemoglobin variants and 2,3-diphosphoglycerate (2,3-DPG) deficiency are inherited diseases generating low tissue oxygen tension and erythropoietin-driven erythrocytosis, that characterizes the clinical phenotype of patients.	2,3-Diphosphoglycerate	82-89	erythropoietin	Homo sapiens	166-180
18413611-0	2008	Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt.	2,3-Diphosphoglycerate	21-44	multiple inositol-polyphosphate phosphatase 1	Homo sapiens	48-52
17897734-2	2007	Two distinct types of PGM exist in nature, one that requires 2,3-bisphosphoglycerate as a cofactor (dPGM) and another that does not (iPGM).	2,3-Diphosphoglycerate	61-84	Phosphoglucose mutase 1	Drosophila melanogaster	100-104
17289676-8	2007	The allostery-dependent interaction of Hb with BIII appeared to contribute not only to maintenance of energy charge but also to further synthesis of 2,3-bisphosphoglycerate, which could help sustain stabilization of T-state Hb during hypoxia.	2,3-Diphosphoglycerate	149-172	calcium voltage-gated channel subunit alpha1 B	Homo sapiens	47-51
17576516-2	2007	Two structural and mechanistically unrelated types of PGMs are known, a cofactor (2,3-bisphosphoglycerate)-dependent (dPGM) and a cofactor-independent enzyme (iPGM).	2,3-Diphosphoglycerate	82-105	Phosphoglucose mutase 1	Drosophila melanogaster	118-122
15248067-5	2004	Levels of 2,3-diphosphoglycerate (2,3-DPG) increased throughout HH on return (+14.7%, P<0.05) and an inverse linear relationship was found between 2,3-DPG and EPO at the end of HH after the sojourn only ( r=-0.66, P<0.03).	2,3-Diphosphoglycerate	10-32	erythropoietin	Homo sapiens	162-165
16246416-1	2006	2,3-Bisphosphoglycerate mutase (2,3-BPGM), an erythroid-expressed enzyme, synthesises 2,3-bisphosphoglycerate (2,3-BPG), the allosteric modulator of haemoglobin.	2,3-Diphosphoglycerate	86-109	bisphosphoglycerate mutase	Homo sapiens	0-30
16246416-1	2006	2,3-Bisphosphoglycerate mutase (2,3-BPGM), an erythroid-expressed enzyme, synthesises 2,3-bisphosphoglycerate (2,3-BPG), the allosteric modulator of haemoglobin.	2,3-Diphosphoglycerate	86-109	bisphosphoglycerate mutase	Homo sapiens	36-40
16246416-1	2006	2,3-Bisphosphoglycerate mutase (2,3-BPGM), an erythroid-expressed enzyme, synthesises 2,3-bisphosphoglycerate (2,3-BPG), the allosteric modulator of haemoglobin.	2,3-Diphosphoglycerate	32-39	bisphosphoglycerate mutase	Homo sapiens	0-30
15946667-4	2005	cN-II is Mg2+-dependent, regulated and stabilised by several factors such as allosteric effectors ATP and 2,3-DPG, although these are not directly involved in the reaction stoichiometry.	2,3-Diphosphoglycerate	106-113	5'-nucleotidase, cytosolic II	Homo sapiens	0-5
15248067-7	2004	Higher 2,3-DPG levels could partly explain this decreased sensitivity of the EPO response to hypoxia.	2,3-Diphosphoglycerate	7-14	erythropoietin	Homo sapiens	77-80
17052986-4	2006	A series of high resolution crystal structures of human bisphosphoglycerate mutase co-crystallized with 2,3-bisphosphoglycerate, representing different time points in the phosphoryl transfer reaction, were solved.	2,3-Diphosphoglycerate	104-127	bisphosphoglycerate mutase	Homo sapiens	56-82
16965582-10	2006	CONCLUSION: Improvements in the maintenance of 2,3-DPG were achieved with 175 mL of a chloride-free storage solution with familiar additives at nontoxic concentrations to increase pHi.	2,3-Diphosphoglycerate	47-54	glucose-6-phosphate isomerase	Homo sapiens	180-183
15883004-1	2005	The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor.	2,3-Diphosphoglycerate	187-210	Phosphoglucose mutase 1	Drosophila melanogaster	55-59
15917509-8	2005	In phosphate-buffered saline plus ATP and 2,3-bisphosphoglycerate, the apparent Km for ribavirin is 88 microM, and k(cat) is 4.0 min-1.	2,3-Diphosphoglycerate	42-65	CD59 molecule (CD59 blood group)	Homo sapiens	129-134
15470234-11	2004	This suggests that the erythrocytic AsV reduction requires both NAD supply and operation of the lower part of the glycolytic pathway starting from glyceraldehyde-3-phosphate dehydrogenase (GAPDH) that, unlike the upper part, remains fed with substrates originating from the degradation of 2,3-bisphosphoglycerate in RBC depleted of glucose by pyruvate.	2,3-Diphosphoglycerate	289-312	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	189-194
15248067-5	2004	Levels of 2,3-diphosphoglycerate (2,3-DPG) increased throughout HH on return (+14.7%, P<0.05) and an inverse linear relationship was found between 2,3-DPG and EPO at the end of HH after the sojourn only ( r=-0.66, P<0.03).	2,3-Diphosphoglycerate	34-41	erythropoietin	Homo sapiens	162-165
15248067-5	2004	Levels of 2,3-diphosphoglycerate (2,3-DPG) increased throughout HH on return (+14.7%, P<0.05) and an inverse linear relationship was found between 2,3-DPG and EPO at the end of HH after the sojourn only ( r=-0.66, P<0.03).	2,3-Diphosphoglycerate	150-157	erythropoietin	Homo sapiens	162-165
15181008-5	2004	In association with Nm23-H1 and GAPDH, PGM could be activated by dCTP, which is a substrate of Nm23-H1, in addition to the well known PGM activator 2,3-bisphosphoglycerate.	2,3-Diphosphoglycerate	148-171	NME/NM23 nucleoside diphosphate kinase 1	Homo sapiens	20-27
15258155-1	2004	Bisphosphoglycerate mutase is a trifunctional enzyme of which the main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin.	2,3-Diphosphoglycerate	97-120	bisphosphoglycerate mutase	Homo sapiens	0-26
15181008-5	2004	In association with Nm23-H1 and GAPDH, PGM could be activated by dCTP, which is a substrate of Nm23-H1, in addition to the well known PGM activator 2,3-bisphosphoglycerate.	2,3-Diphosphoglycerate	148-171	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	32-37
12911339-0	2003	Decreased 2,3-diphosphoglycerate concentration in low cardiac output patients and its influence on the determination of in vivo p50.	2,3-Diphosphoglycerate	10-32	activating signal cointegrator 1 complex subunit 1	Homo sapiens	128-131
12147028-1	2002	BACKGROUND: Concentrations of 2,3-DPG decline rapidly in the first week of RBC storage because of the low pH of conventional storage solutions.	2,3-Diphosphoglycerate	30-37	RNA, 7SL, cytoplasmic 263, pseudogene	Homo sapiens	75-78
12792702-3	2003	Some earlier studies on diabetic patients have reported that insulin treatment may reduce the red cell concentrations of 2,3-DPG, causing a shift of the ODC to the left, but the reports are contradictory.	2,3-Diphosphoglycerate	121-128	insulin	Homo sapiens	61-68
11420051-3	2001	Studies using double-labelled PC and 2,3-diphosphoglycerate (as a phospholipase D inhibitor) showed that they were produced through different pathways: free fatty acid was released by phospholipase A2 (PLA2) while 1,2-diacylglycerol may be produced by sequential action of phospholipase D and phosphatidate phosphatase.	2,3-Diphosphoglycerate	37-59	phospholipase A2 group IB	Rattus norvegicus	184-200
11682058-3	2001	Physiologically relevant concentrations of ATP, 2,3-bisphosphoglyceric acid and inositol hexakisphosphate inhibited its enzyme activities under steady-state conditions as well as those determined under stimulation with S-nitroso-N-acetylpenicillamine, a nitric oxide donor, carbon monoxide or YC-1.	2,3-Diphosphoglycerate	48-75	RNA binding motif single stranded interacting protein 1	Homo sapiens	293-297
11420051-3	2001	Studies using double-labelled PC and 2,3-diphosphoglycerate (as a phospholipase D inhibitor) showed that they were produced through different pathways: free fatty acid was released by phospholipase A2 (PLA2) while 1,2-diacylglycerol may be produced by sequential action of phospholipase D and phosphatidate phosphatase.	2,3-Diphosphoglycerate	37-59	phospholipase A2 group IB	Rattus norvegicus	202-206
11294862-4	2001	We report here that elevation of cytosolic 2,3-bisphosphoglycerate, an increase in intracellular Ca(2+), removal of cell O(2), a decrease in intracellular pH, and activation of erythrocyte protein kinase C all promote dissociation of protein 4.1 from glycophorin C, leading to reduced retention of glycophorin C in detergent-extracted spectrin/actin skeletons.	2,3-Diphosphoglycerate	43-66	erythrocyte membrane protein band 4.1	Homo sapiens	234-245
11294862-4	2001	We report here that elevation of cytosolic 2,3-bisphosphoglycerate, an increase in intracellular Ca(2+), removal of cell O(2), a decrease in intracellular pH, and activation of erythrocyte protein kinase C all promote dissociation of protein 4.1 from glycophorin C, leading to reduced retention of glycophorin C in detergent-extracted spectrin/actin skeletons.	2,3-Diphosphoglycerate	43-66	glycophorin C (Gerbich blood group)	Homo sapiens	251-264
11294862-4	2001	We report here that elevation of cytosolic 2,3-bisphosphoglycerate, an increase in intracellular Ca(2+), removal of cell O(2), a decrease in intracellular pH, and activation of erythrocyte protein kinase C all promote dissociation of protein 4.1 from glycophorin C, leading to reduced retention of glycophorin C in detergent-extracted spectrin/actin skeletons.	2,3-Diphosphoglycerate	43-66	glycophorin C (Gerbich blood group)	Homo sapiens	298-311
11569479-4	2001	We have investigated red cell 2,3-DPG concentrations during erythropoietin treatment in healthy volunteers as a mediator of a possible physiological explanation.	2,3-Diphosphoglycerate	30-37	erythropoietin	Homo sapiens	60-74
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).	2,3-Diphosphoglycerate	81-103	glucose-6-phosphate dehydrogenase	Homo sapiens	16-49
11569479-11	2001	CONCLUSION: treatment with erythropoietin causes an increase in red cell 2,3-DPG levels.	2,3-Diphosphoglycerate	73-80	erythropoietin	Homo sapiens	27-41
10929046-6	2000	We showed that the exchange of human zeta-globin for human alpha-globin chains increased haemoglobin O2 affinity, both in the presence and in the absence of 2, 3-bisphosphoglycerate (2,3-BPG), and reduced the pH-dependent shift in its oxygen equilibrium curve (Bohr effect).	2,3-Diphosphoglycerate	157-181	hemoglobin subunit zeta	Homo sapiens	37-48
11093007-0	2000	Use of erythropoietin and its effects on blood lactate and 2, 3-diphosphoglycerate in premature neonates.	2,3-Diphosphoglycerate	59-82	erythropoietin	Homo sapiens	7-21
10931844-8	2000	PLD inhibitors 1-butanol and 2, 3-diphosphoglycerate, or the ARF6(N48R) mutant assumed to be defective in PLD activation, blocked fMLP-elicited oxidase activity in transfected cells.	2,3-Diphosphoglycerate	29-52	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	0-3
10931844-8	2000	PLD inhibitors 1-butanol and 2, 3-diphosphoglycerate, or the ARF6(N48R) mutant assumed to be defective in PLD activation, blocked fMLP-elicited oxidase activity in transfected cells.	2,3-Diphosphoglycerate	29-52	formyl peptide receptor 1	Homo sapiens	130-134
10929046-6	2000	We showed that the exchange of human zeta-globin for human alpha-globin chains increased haemoglobin O2 affinity, both in the presence and in the absence of 2, 3-bisphosphoglycerate (2,3-BPG), and reduced the pH-dependent shift in its oxygen equilibrium curve (Bohr effect).	2,3-Diphosphoglycerate	157-181	hemoglobin subunit alpha 2	Homo sapiens	59-71
10810185-0	2000	Participation of glyceraldehyde-3-phosphate dehydrogenase in the regulation of 2,3-diphosphoglycerate level in erythrocytes.	2,3-Diphosphoglycerate	79-101	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	17-57
10810185-1	2000	Data are presented concerning the possible participation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in regulation of the glycolytic pathway and the level of 2,3-diphosphoglycerate in erythrocytes.	2,3-Diphosphoglycerate	166-188	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	102-107
10810185-2	2000	Experimental support has been obtained for the hypothesis according to which a mild oxidation of GAPDH must result in acceleration of glycolysis and in decrease in the level of 2, 3-diphosphoglycerate due to the acyl phosphatase activity of the mildly oxidized enzyme.	2,3-Diphosphoglycerate	177-200	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	97-102
10810185-5	2000	A pH-dependent complexing of GAPDH and 3-phosphoglycerate kinase or 2, 3-diphosphoglycerate mutase is found to determine the fate of 1,3-diphosphoglycerate that serves as a substrate for the synthesis of 2,3-diphosphoglycerate as well as for the 3-phosphoglycerate kinase reaction in glycolysis.	2,3-Diphosphoglycerate	204-226	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	29-34
10477268-0	1999	Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: in vivo kinetic characterization of 2,3-bisphosphoglycerate synthase/phosphatase using 13C and 31P NMR.	2,3-Diphosphoglycerate	9-32	bisphosphoglycerate mutase	Homo sapiens	149-181
9973479-5	1999	The similar effects exerted by specific PLD pharmacological inhibitors (2,3-diphosphoglycerate, ethanol) suggest that in our experimental system, sPLA2 secretion and activation are under the control of a PLD-dependent pathway.	2,3-Diphosphoglycerate	72-94	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	40-43
10437801-2	1999	Vertebrates have only the 2,3-bisphosphoglycerate-dependent enzyme (dPGM), whilst higher plants have only the cofactor-independent enzyme (iPGM).	2,3-Diphosphoglycerate	26-49	Phosphoglucose mutase 1	Drosophila melanogaster	68-72
10190972-7	1999	It is likely that the effects of DPG and other glycolytic metabolites on pancreatic beta cell signaling are physiologically significant inasmuch as we were also able to demonstrate that DPG and other glycolytic metabolites promoted the release of insulin from the pancreatic beta cell.	2,3-Diphosphoglycerate	33-36	insulin	Homo sapiens	247-254
10190972-7	1999	It is likely that the effects of DPG and other glycolytic metabolites on pancreatic beta cell signaling are physiologically significant inasmuch as we were also able to demonstrate that DPG and other glycolytic metabolites promoted the release of insulin from the pancreatic beta cell.	2,3-Diphosphoglycerate	186-189	insulin	Homo sapiens	247-254
9973503-8	1999	Phagocytosis of EIgG was reduced by two inhibitors of PLD-mediated signaling, 2,3-diphosphoglycerate or 1-butanol.	2,3-Diphosphoglycerate	78-100	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	54-57
9973479-6	1999	By using pharmacological inhibitors (2,3-diphosphoglycerate, wortmannin, ethanol) we also demonstrated that PLD activation is an important step in the CD16-triggered signaling cascade that leads to NK cytotoxic granule exocytosis.	2,3-Diphosphoglycerate	37-59	Fc gamma receptor IIIa	Homo sapiens	151-155
9973479-5	1999	The similar effects exerted by specific PLD pharmacological inhibitors (2,3-diphosphoglycerate, ethanol) suggest that in our experimental system, sPLA2 secretion and activation are under the control of a PLD-dependent pathway.	2,3-Diphosphoglycerate	72-94	phospholipase A2 group IIA	Homo sapiens	146-151
9973479-5	1999	The similar effects exerted by specific PLD pharmacological inhibitors (2,3-diphosphoglycerate, ethanol) suggest that in our experimental system, sPLA2 secretion and activation are under the control of a PLD-dependent pathway.	2,3-Diphosphoglycerate	72-94	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	204-207
9973479-6	1999	By using pharmacological inhibitors (2,3-diphosphoglycerate, wortmannin, ethanol) we also demonstrated that PLD activation is an important step in the CD16-triggered signaling cascade that leads to NK cytotoxic granule exocytosis.	2,3-Diphosphoglycerate	37-59	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	108-111
9832630-1	1998	2,3-Bisphosphoglycerate mutase (BPGM) [EC 5.4.2.4] is a multifunctional enzyme that catalyzes both the synthesis and the degradation of 2,3-diphosphoglycerate (2,3-DPG) and contains three types of activities in that it functions as a 2,3-DPG synthetase, a phosphoglycerate mutase and a 2,3-DPG phosphatase.	2,3-Diphosphoglycerate	136-158	bisphosphoglycerate mutase	Homo sapiens	0-30
9832630-1	1998	2,3-Bisphosphoglycerate mutase (BPGM) [EC 5.4.2.4] is a multifunctional enzyme that catalyzes both the synthesis and the degradation of 2,3-diphosphoglycerate (2,3-DPG) and contains three types of activities in that it functions as a 2,3-DPG synthetase, a phosphoglycerate mutase and a 2,3-DPG phosphatase.	2,3-Diphosphoglycerate	136-158	bisphosphoglycerate mutase	Homo sapiens	32-36
9832630-1	1998	2,3-Bisphosphoglycerate mutase (BPGM) [EC 5.4.2.4] is a multifunctional enzyme that catalyzes both the synthesis and the degradation of 2,3-diphosphoglycerate (2,3-DPG) and contains three types of activities in that it functions as a 2,3-DPG synthetase, a phosphoglycerate mutase and a 2,3-DPG phosphatase.	2,3-Diphosphoglycerate	160-167	bisphosphoglycerate mutase	Homo sapiens	0-30
9832630-1	1998	2,3-Bisphosphoglycerate mutase (BPGM) [EC 5.4.2.4] is a multifunctional enzyme that catalyzes both the synthesis and the degradation of 2,3-diphosphoglycerate (2,3-DPG) and contains three types of activities in that it functions as a 2,3-DPG synthetase, a phosphoglycerate mutase and a 2,3-DPG phosphatase.	2,3-Diphosphoglycerate	160-167	bisphosphoglycerate mutase	Homo sapiens	32-36
9832630-1	1998	2,3-Bisphosphoglycerate mutase (BPGM) [EC 5.4.2.4] is a multifunctional enzyme that catalyzes both the synthesis and the degradation of 2,3-diphosphoglycerate (2,3-DPG) and contains three types of activities in that it functions as a 2,3-DPG synthetase, a phosphoglycerate mutase and a 2,3-DPG phosphatase.	2,3-Diphosphoglycerate	164-167	bisphosphoglycerate mutase	Homo sapiens	0-30
9832630-1	1998	2,3-Bisphosphoglycerate mutase (BPGM) [EC 5.4.2.4] is a multifunctional enzyme that catalyzes both the synthesis and the degradation of 2,3-diphosphoglycerate (2,3-DPG) and contains three types of activities in that it functions as a 2,3-DPG synthetase, a phosphoglycerate mutase and a 2,3-DPG phosphatase.	2,3-Diphosphoglycerate	164-167	bisphosphoglycerate mutase	Homo sapiens	32-36
9832630-2	1998	In humans, BPGM occurs only in erythrocytes and plays a pivotal role in the dissociation of oxygen from hemoglobin via 2,3-DPG.	2,3-Diphosphoglycerate	119-126	bisphosphoglycerate mutase	Homo sapiens	11-15
9401778-19	1997	The phosphatase inhibitor DPG (500 microM) inhibited SAG; EC50 for fMLP 33.93 +/- 4.23 and 61.12 +/- 14.43 nM with and without DPG, respectively.	2,3-Diphosphoglycerate	26-29	formyl peptide receptor 1	Homo sapiens	67-71
9699999-6	1998	Bisphosphoglycerate mutase specific activity did not change along the fractionation profile of any cell population under study, thus providing 2,3-bisphosphoglycerate during the life-span of the red blood cells from anaemic patients.	2,3-Diphosphoglycerate	143-166	bisphosphoglycerate mutase	Homo sapiens	0-26
9401778-12	1997	The phosphatase inhibitor, 2,3-diphosphoglyceric acid (DPG) (100 microM) which inhibits phospholipase D, attenuated fMLP-induced chemotaxis; EC50 for fMLP 19.15 +/- 4.36 and 61.52 +/- 16.2 pmol/10(6) cells with and without DPG, respectively.	2,3-Diphosphoglycerate	27-53	formyl peptide receptor 1	Homo sapiens	116-120
8996245-2	1997	We report that one of these ligands, 2,3-diphosphoglyceric acid (DPG), which induces expansion of V gamma 9/V delta T cells ex vivo, antagonizes the same cell population after repetitive activation.	2,3-Diphosphoglycerate	37-63	G protein subunit gamma 8	Homo sapiens	100-107
9401778-12	1997	The phosphatase inhibitor, 2,3-diphosphoglyceric acid (DPG) (100 microM) which inhibits phospholipase D, attenuated fMLP-induced chemotaxis; EC50 for fMLP 19.15 +/- 4.36 and 61.52 +/- 16.2 pmol/10(6) cells with and without DPG, respectively.	2,3-Diphosphoglycerate	27-53	formyl peptide receptor 1	Homo sapiens	150-154
9401778-12	1997	The phosphatase inhibitor, 2,3-diphosphoglyceric acid (DPG) (100 microM) which inhibits phospholipase D, attenuated fMLP-induced chemotaxis; EC50 for fMLP 19.15 +/- 4.36 and 61.52 +/- 16.2 pmol/10(6) cells with and without DPG, respectively.	2,3-Diphosphoglycerate	55-58	formyl peptide receptor 1	Homo sapiens	116-120
9401778-12	1997	The phosphatase inhibitor, 2,3-diphosphoglyceric acid (DPG) (100 microM) which inhibits phospholipase D, attenuated fMLP-induced chemotaxis; EC50 for fMLP 19.15 +/- 4.36 and 61.52 +/- 16.2 pmol/10(6) cells with and without DPG, respectively.	2,3-Diphosphoglycerate	55-58	formyl peptide receptor 1	Homo sapiens	150-154
9401778-12	1997	The phosphatase inhibitor, 2,3-diphosphoglyceric acid (DPG) (100 microM) which inhibits phospholipase D, attenuated fMLP-induced chemotaxis; EC50 for fMLP 19.15 +/- 4.36 and 61.52 +/- 16.2 pmol/10(6) cells with and without DPG, respectively.	2,3-Diphosphoglycerate	223-226	formyl peptide receptor 1	Homo sapiens	116-120
9369240-4	1997	Such stimulation may have physiological significance as 1,3-bis-phosphoglycerate, the product of GAPDH, isomerises to 2,3-bis-phosphoglycerate, an allosteric effector that decreases the oxygen affinity of hemoglobin, thus providing a feedback loop.	2,3-Diphosphoglycerate	118-142	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	97-102
8996245-2	1997	We report that one of these ligands, 2,3-diphosphoglyceric acid (DPG), which induces expansion of V gamma 9/V delta T cells ex vivo, antagonizes the same cell population after repetitive activation.	2,3-Diphosphoglycerate	65-68	G protein subunit gamma 8	Homo sapiens	100-107
8996245-3	1997	Stimulation with DPG results in partial early protein tyrosine phosphorylation and a prolonged, but reversible, state of unresponsiveness to agonist ligands in V gamma 9/V delta 2, but not in other T cells.	2,3-Diphosphoglycerate	17-20	G protein subunit gamma 8	Homo sapiens	162-179
8624492-4	1995	The experiments yielded a total Mg2+ buffer capacity of 4.85mM with a Ka of 0.9 mM-1, indicating that 2,3 bisphosphoglycerate was the main Mg2+ buffer in haemolysates of erythrocytes which had been ATP-depleted during preparation.	2,3-Diphosphoglycerate	102-125	mucin 7, secreted	Homo sapiens	32-35
8940366-2	1996	AVP promptly increased the phosphatidylethanol formation in a concentration-dependent manner, which indicates the activation of phospholipase D. When cells were preincubated with 2,3-diphosphoglycerate or carbobenzyloxy-leucine-tyrosine-chloromethylketone (zLYCK), inhibitors of phospholipase D, the 1 x 10(-7) M AVP-produced phosphatidylethanol was significantly attenuated.	2,3-Diphosphoglycerate	179-201	arginine vasopressin	Rattus norvegicus	0-3
8940366-6	1996	Also, AVP stimulated [3H]thymidine incorporation, an effect significantly less in the presence of 2,3-diphosphoglycerate or zLYCK.	2,3-Diphosphoglycerate	98-120	arginine vasopressin	Rattus norvegicus	6-9
8851897-5	1996	These changes of serum-EPO concentration were correlated to the changes in arterial blood oxygen saturation (r = -0.60, P = 0.0009), pH (r = 0.67, P = 0.003), and in-vivo venous blood oxygen half saturation tension (r = -0.68, P = 0.004) but not to the changes in 2, 3 diphosphoglycerate.	2,3-Diphosphoglycerate	264-287	erythropoietin	Homo sapiens	23-26
8788433-6	1995	These observations suggest that a decrease in the red blood cell 2,3-diphosphoglycerate concentration is one of the factors contributing to tissue hypoxia, which results in diabetic neuropathy, and that this decrease is mediated through an aldose reductase inhibitor-sensitive pathway.	2,3-Diphosphoglycerate	65-87	aldo-keto reductase family 1 member B1	Rattus norvegicus	240-256
8624492-4	1995	The experiments yielded a total Mg2+ buffer capacity of 4.85mM with a Ka of 0.9 mM-1, indicating that 2,3 bisphosphoglycerate was the main Mg2+ buffer in haemolysates of erythrocytes which had been ATP-depleted during preparation.	2,3-Diphosphoglycerate	102-125	mucin 7, secreted	Homo sapiens	139-142
8023930-7	1994	Diabetes or insulin administration resulted in only minimal and physiologically insignificant alterations in the oxygen dissociation curve and 2,3-diphosphoglycerate of sciatic nerve.	2,3-Diphosphoglycerate	143-165	insulin	Homo sapiens	12-19
7841177-7	1994	In light of other data showing regulation of the same interactions by phosphoinositides, protein kinases, and the concentration of free cytosolic 2,3-diphosphoglycerate, it can be argued that association of protein 4.1 with integral protein anchors constitutes one of the more sensitively regulated interactions of the membrane.	2,3-Diphosphoglycerate	146-168	erythrocyte membrane protein band 4.1	Homo sapiens	207-218
7696519-5	1995	In addition, from the proximal histidine resonances, we have observed a preference for the binding of oxygen to the alpha-chain (up to about 10%) of hemoglobin over the beta-chain in both the presence and absence of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	216-238	Fc gamma receptor and transporter	Homo sapiens	116-127
7735316-3	1994	Casein kinase II activity is inhibited by 2,3-bisphosphoglycerate and stimulated by polyamines at levels which are physiological in red cells.	2,3-Diphosphoglycerate	42-65	casein kinase IIalpha	Drosophila melanogaster	0-16
8170953-0	1994	A recombinant bisphosphoglycerate mutase variant with acid phosphatase homology degrades 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	89-111	bisphosphoglycerate mutase	Homo sapiens	14-40
8170953-2	1994	Since the erythrocyte glycerate 2,3-bisphosphate (2,3-DPG) has been shown to facilitate this polymerization, one therapeutic approach would be to decrease the intraerythrocytic level of 2,3-DPG by increasing the phosphatase activity of the bisphosphoglycerate mutase (BPGM; 3-phospho-D-glycerate 1,2-phosphomutase, EC 5.4.2.4).	2,3-Diphosphoglycerate	22-48	bisphosphoglycerate mutase	Homo sapiens	240-266
8170953-2	1994	Since the erythrocyte glycerate 2,3-bisphosphate (2,3-DPG) has been shown to facilitate this polymerization, one therapeutic approach would be to decrease the intraerythrocytic level of 2,3-DPG by increasing the phosphatase activity of the bisphosphoglycerate mutase (BPGM; 3-phospho-D-glycerate 1,2-phosphomutase, EC 5.4.2.4).	2,3-Diphosphoglycerate	22-48	bisphosphoglycerate mutase	Homo sapiens	268-272
8170953-2	1994	Since the erythrocyte glycerate 2,3-bisphosphate (2,3-DPG) has been shown to facilitate this polymerization, one therapeutic approach would be to decrease the intraerythrocytic level of 2,3-DPG by increasing the phosphatase activity of the bisphosphoglycerate mutase (BPGM; 3-phospho-D-glycerate 1,2-phosphomutase, EC 5.4.2.4).	2,3-Diphosphoglycerate	50-57	bisphosphoglycerate mutase	Homo sapiens	240-266
8170953-2	1994	Since the erythrocyte glycerate 2,3-bisphosphate (2,3-DPG) has been shown to facilitate this polymerization, one therapeutic approach would be to decrease the intraerythrocytic level of 2,3-DPG by increasing the phosphatase activity of the bisphosphoglycerate mutase (BPGM; 3-phospho-D-glycerate 1,2-phosphomutase, EC 5.4.2.4).	2,3-Diphosphoglycerate	186-193	bisphosphoglycerate mutase	Homo sapiens	240-266
8170953-2	1994	Since the erythrocyte glycerate 2,3-bisphosphate (2,3-DPG) has been shown to facilitate this polymerization, one therapeutic approach would be to decrease the intraerythrocytic level of 2,3-DPG by increasing the phosphatase activity of the bisphosphoglycerate mutase (BPGM; 3-phospho-D-glycerate 1,2-phosphomutase, EC 5.4.2.4).	2,3-Diphosphoglycerate	186-193	bisphosphoglycerate mutase	Homo sapiens	268-272
8015732-0	1994	2,3-diphosphoglyceric acid blocks long-term potentiation of excitatory postsynaptic currents in hippocampal CA1 neurons of the rat.	2,3-Diphosphoglycerate	0-26	carbonic anhydrase 1	Rattus norvegicus	108-111
8170953-2	1994	Since the erythrocyte glycerate 2,3-bisphosphate (2,3-DPG) has been shown to facilitate this polymerization, one therapeutic approach would be to decrease the intraerythrocytic level of 2,3-DPG by increasing the phosphatase activity of the bisphosphoglycerate mutase (BPGM; 3-phospho-D-glycerate 1,2-phosphomutase, EC 5.4.2.4).	2,3-Diphosphoglycerate	50-57	bisphosphoglycerate mutase	Homo sapiens	268-272
8496163-6	1993	In contrast, inhibition of protein 4.1 binding to the membrane reached 65% at physiological DPG concentrations (approximately approximately 5.9 mM); at more elevated concentrations, blockade was nearly quantitative, affecting glycophorin and band 3 sites alike.	2,3-Diphosphoglycerate	92-95	erythrocyte membrane protein band 4.1	Homo sapiens	27-38
8125885-5	1993	Whereas the recombinant and native Hbs displayed similar sensitivities to pH, chloride, and 2,3-diphosphoglycerate, the oxygenation heat of the alpha-chain mutant decreased in the presence of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	192-214	Fc gamma receptor and transporter	Homo sapiens	144-155
8289479-8	1994	Standardized in vivo p50 was positively correlated to red cell 2,3 diphosphoglycerate concentration, although this was not the only factor influencing the oxygen dissociation curve.	2,3-Diphosphoglycerate	63-85	nuclear factor kappa B subunit 1	Homo sapiens	21-24
8387514-8	1993	PRSII was less sensitive to feedback inhibition by purine nucleotides and more sensitive to inhibition by 2,3-diphosphoglycerate than PRSI.	2,3-Diphosphoglycerate	106-128	phosphoribosyl pyrophosphate synthetase 2	Homo sapiens	0-5
8387514-8	1993	PRSII was less sensitive to feedback inhibition by purine nucleotides and more sensitive to inhibition by 2,3-diphosphoglycerate than PRSI.	2,3-Diphosphoglycerate	106-128	phosphoribosyl pyrophosphate synthetase 1	Homo sapiens	0-4
8302459-0	1993	Increased red cell 2,3-diphosphoglycerate levels in haemodialysis patients treated with erythropoietin.	2,3-Diphosphoglycerate	19-41	erythropoietin	Homo sapiens	88-102
8477721-10	1993	It is noteworthy that the H187N variant is protected against thermal instability by glycerate 2,3-bisphosphate (GriP2).	2,3-Diphosphoglycerate	84-110	glutamate receptor interacting protein 2	Homo sapiens	112-117
1284690-2	1992	We observed a good correlation between 2,3-BPG and p50 (i.e. the oxygen tension, at which hemoglobin is half-saturated with oxygen).	2,3-Diphosphoglycerate	39-46	nuclear factor kappa B subunit 1	Homo sapiens	51-54
1421379-1	1992	Erythrocyte bisphosphoglycerate mutase (BPGM) deficiency is a rare disease associated with a decrease in 2,3-diphosphoglycerate concentration.	2,3-Diphosphoglycerate	105-127	bisphosphoglycerate mutase	Homo sapiens	12-38
1421379-1	1992	Erythrocyte bisphosphoglycerate mutase (BPGM) deficiency is a rare disease associated with a decrease in 2,3-diphosphoglycerate concentration.	2,3-Diphosphoglycerate	105-127	bisphosphoglycerate mutase	Homo sapiens	40-44
1654767-0	1991	Effect of 2,3-diphosphoglycerate on the phosphorylation of protein 4.1 by protein kinase C. We have previously shown that 2,3-diphosphoglycerate (2,3-DPG) inhibits the phosphorylation of erythrocyte membrane cytoskeletal proteins by endogenous casein kinases.	2,3-Diphosphoglycerate	10-32	erythrocyte membrane protein band 4.1	Homo sapiens	59-70
1430586-1	1992	In a previous paper, published in this journal, we showed that the data obtained in patients with severe ketoacidosis suggest that inorganic phosphates (K2HPO4) can increase their P50 and therefore enhance tissue oxygenation without concomitant alteration of the 2,3 diphosphoglycerate (DPG).	2,3-Diphosphoglycerate	263-285	activating signal cointegrator 1 complex subunit 1	Homo sapiens	180-183
1826331-1	1991	Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells.	2,3-Diphosphoglycerate	81-103	bisphosphoglycerate mutase	Homo sapiens	0-26
1654767-0	1991	Effect of 2,3-diphosphoglycerate on the phosphorylation of protein 4.1 by protein kinase C. We have previously shown that 2,3-diphosphoglycerate (2,3-DPG) inhibits the phosphorylation of erythrocyte membrane cytoskeletal proteins by endogenous casein kinases.	2,3-Diphosphoglycerate	122-144	erythrocyte membrane protein band 4.1	Homo sapiens	59-70
1654767-0	1991	Effect of 2,3-diphosphoglycerate on the phosphorylation of protein 4.1 by protein kinase C. We have previously shown that 2,3-diphosphoglycerate (2,3-DPG) inhibits the phosphorylation of erythrocyte membrane cytoskeletal proteins by endogenous casein kinases.	2,3-Diphosphoglycerate	146-153	erythrocyte membrane protein band 4.1	Homo sapiens	59-70
1654767-1	1991	Here, we report that 2,3-DPG stimulates the phosphorylation of protein 4.1 by protein kinase C. Studies with red cell membrane preparations showed that while the phosphorylation of most of the membrane proteins by endogenous membrane-bound kinases and purified kinase C was inhibited by 2,3-DPG, the phosphorylation of protein 4.1 was slightly enhanced by the metabolite.	2,3-Diphosphoglycerate	21-28	erythrocyte membrane protein band 4.1	Homo sapiens	63-74
1654767-1	1991	Here, we report that 2,3-DPG stimulates the phosphorylation of protein 4.1 by protein kinase C. Studies with red cell membrane preparations showed that while the phosphorylation of most of the membrane proteins by endogenous membrane-bound kinases and purified kinase C was inhibited by 2,3-DPG, the phosphorylation of protein 4.1 was slightly enhanced by the metabolite.	2,3-Diphosphoglycerate	21-28	erythrocyte membrane protein band 4.1	Homo sapiens	319-330
1654767-1	1991	Here, we report that 2,3-DPG stimulates the phosphorylation of protein 4.1 by protein kinase C. Studies with red cell membrane preparations showed that while the phosphorylation of most of the membrane proteins by endogenous membrane-bound kinases and purified kinase C was inhibited by 2,3-DPG, the phosphorylation of protein 4.1 was slightly enhanced by the metabolite.	2,3-Diphosphoglycerate	287-294	erythrocyte membrane protein band 4.1	Homo sapiens	63-74
1654767-3	1991	Our results indicate that 2,3-DPG stimulates both the rate and the extent of phosphorylation of purified protein 4.1 by kinase C. The amount of phosphate incorporated was found to double to 2 mol of phosphate per mole of protein 4.1 in the presence of 10 mM 2,3-DPG.	2,3-Diphosphoglycerate	26-33	erythrocyte membrane protein band 4.1	Homo sapiens	105-116
1654767-3	1991	Our results indicate that 2,3-DPG stimulates both the rate and the extent of phosphorylation of purified protein 4.1 by kinase C. The amount of phosphate incorporated was found to double to 2 mol of phosphate per mole of protein 4.1 in the presence of 10 mM 2,3-DPG.	2,3-Diphosphoglycerate	26-33	erythrocyte membrane protein band 4.1	Homo sapiens	221-232
1654767-3	1991	Our results indicate that 2,3-DPG stimulates both the rate and the extent of phosphorylation of purified protein 4.1 by kinase C. The amount of phosphate incorporated was found to double to 2 mol of phosphate per mole of protein 4.1 in the presence of 10 mM 2,3-DPG.	2,3-Diphosphoglycerate	258-265	erythrocyte membrane protein band 4.1	Homo sapiens	105-116
1654767-3	1991	Our results indicate that 2,3-DPG stimulates both the rate and the extent of phosphorylation of purified protein 4.1 by kinase C. The amount of phosphate incorporated was found to double to 2 mol of phosphate per mole of protein 4.1 in the presence of 10 mM 2,3-DPG.	2,3-Diphosphoglycerate	258-265	erythrocyte membrane protein band 4.1	Homo sapiens	221-232
1654767-5	1991	The stimulatory effect of 2,3-DPG on the phosphorylation of protein 4.1 was observed only with kinase C. Phosphorylation by the cytosolic erythrocyte casein kinase and the cyclic AMP-dependent protein kinase was inhibited by 2,3-DPG.	2,3-Diphosphoglycerate	26-33	erythrocyte membrane protein band 4.1	Homo sapiens	60-71
1654767-5	1991	The stimulatory effect of 2,3-DPG on the phosphorylation of protein 4.1 was observed only with kinase C. Phosphorylation by the cytosolic erythrocyte casein kinase and the cyclic AMP-dependent protein kinase was inhibited by 2,3-DPG.	2,3-Diphosphoglycerate	225-232	erythrocyte membrane protein band 4.1	Homo sapiens	60-71
1654767-6	1991	Moreover, the stimulatory effect of 2,3-DPG seemed to be unique to the phosphorylation of protein 4.1 since a similar effect had not been observed with other protein kinase C substrates.	2,3-Diphosphoglycerate	36-43	erythrocyte membrane protein band 4.1	Homo sapiens	90-101
2340273-3	1990	The results indicate that 2,3-diphosphoglycerate binds to deoxyhemoglobin at the central cavity between the two beta chains and the binding involves the beta 2-histidyl residues.	2,3-Diphosphoglycerate	26-48	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	153-159
2166231-1	1990	An inverse relationship between 2,3-bisphosphoglycerate levels and the ratio calculated from pyruvate kinase and bisphosphoglycerate mutase activities has been observed in red populations of rats during animal development.	2,3-Diphosphoglycerate	32-55	bisphosphoglycerate mutase	Rattus norvegicus	113-139
1668552-4	1991	These results suggest that the impurity interacts with the soluble 5"-nucleotidase at the same site as ATP and 2,3-diphosphoglycerate, however with a much higher affinity than these two compounds.	2,3-Diphosphoglycerate	111-133	5' nucleotidase, ecto	Rattus norvegicus	67-82
2288424-6	1990	In patients with cardio-respiratory disturbances 2,3-DPG concentration increased by 0.55 mcM/ml on average, with plasma pH increased by 0.1.	2,3-Diphosphoglycerate	49-56	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha	Homo sapiens	89-92
2340273-5	1990	As a result of the specific interactions with 2,3-diphosphoglycerate, the beta 2-histidyl residues make a significant contribution to the alkaline Bohr effect under these experimental conditions (up to 0.5 proton/Hb tetramer).	2,3-Diphosphoglycerate	46-68	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	74-80
2386500-7	1990	In contrast, RBC with reduced hexokinase activity have a reduced 2, 3-diphosphoglycerate concentration and are not able to maintain their ATP concentration.	2,3-Diphosphoglycerate	65-88	hexokinase 1	Homo sapiens	30-40
2344351-7	1990	The GPI-1sb-m2Neu homodimer, in contrast, is characterized by an even stronger instability, slightly altered pH dependence, an increased Ki for 2,3-DPG, normal other kinetics, and normal isoelectric point.	2,3-Diphosphoglycerate	144-151	glucose-6-phosphate isomerase 1	Mus musculus	4-7
2386518-0	1990	Influence of erythropoietin treatment on 2,3-bisphosphoglycerate and O2-affinity of red blood cells in children with renal anemia.	2,3-Diphosphoglycerate	41-64	erythropoietin	Homo sapiens	13-27
2291322-7	1990	A positive relationship was revealed between the 2,3-DPG level and standard P50 value.	2,3-Diphosphoglycerate	49-56	nuclear factor kappa B subunit 1	Homo sapiens	76-79
2291322-9	1990	It is most probable, that 2,3-DPG mediates the buffer effect eliminating the drastic P50 deviations and is not completely responsible for additional ODC shifts in cardiopulmonary disorders.	2,3-Diphosphoglycerate	26-33	nuclear factor kappa B subunit 1	Homo sapiens	85-88
2553728-2	1989	Bisphosphoglycerate mutase is an erythrocyte-specific enzyme whose main function is to synthesize 2,3-diphosphoglycerate, the allosteric effector of hemoglobin.	2,3-Diphosphoglycerate	98-120	bisphosphoglycerate mutase	Homo sapiens	0-26
34138843-8	2021	Mechanistically, erythrocyte ADORA2B-mediated activation of AMP-activated protein kinase (AMPK) and bisphosphoglycerate mutase (BPGM) promotes hypoxic and metabolic reprogramming to enhance production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite triggering O2 delivery.	2,3-Diphosphoglycerate	204-227	adenosine A2b receptor	Mus musculus	29-36
34138843-8	2021	Mechanistically, erythrocyte ADORA2B-mediated activation of AMP-activated protein kinase (AMPK) and bisphosphoglycerate mutase (BPGM) promotes hypoxic and metabolic reprogramming to enhance production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite triggering O2 delivery.	2,3-Diphosphoglycerate	204-227	2,3-bisphosphoglycerate mutase	Mus musculus	100-126
34138843-8	2021	Mechanistically, erythrocyte ADORA2B-mediated activation of AMP-activated protein kinase (AMPK) and bisphosphoglycerate mutase (BPGM) promotes hypoxic and metabolic reprogramming to enhance production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite triggering O2 delivery.	2,3-Diphosphoglycerate	204-227	2,3-bisphosphoglycerate mutase	Mus musculus	128-132
34138843-8	2021	Mechanistically, erythrocyte ADORA2B-mediated activation of AMP-activated protein kinase (AMPK) and bisphosphoglycerate mutase (BPGM) promotes hypoxic and metabolic reprogramming to enhance production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite triggering O2 delivery.	2,3-Diphosphoglycerate	229-236	adenosine A2b receptor	Mus musculus	29-36
34138843-8	2021	Mechanistically, erythrocyte ADORA2B-mediated activation of AMP-activated protein kinase (AMPK) and bisphosphoglycerate mutase (BPGM) promotes hypoxic and metabolic reprogramming to enhance production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite triggering O2 delivery.	2,3-Diphosphoglycerate	229-236	2,3-bisphosphoglycerate mutase	Mus musculus	100-126
34138843-8	2021	Mechanistically, erythrocyte ADORA2B-mediated activation of AMP-activated protein kinase (AMPK) and bisphosphoglycerate mutase (BPGM) promotes hypoxic and metabolic reprogramming to enhance production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite triggering O2 delivery.	2,3-Diphosphoglycerate	229-236	2,3-bisphosphoglycerate mutase	Mus musculus	128-132
35362470-1	2022	Bisphosphoglycerate mutase (BPGM) is an erythrocyte-specific multifunctional enzyme that is responsible for the regulation of 2,3-bisphosphoglycerate (2,3-BPG) in red blood cells through its synthase and phosphatase activities; the latter enzymatic function is stimulated by the endogenous activator 2-phosphoglycolate (2-PG).	2,3-Diphosphoglycerate	126-149	bisphosphoglycerate mutase	Homo sapiens	0-26
35362470-1	2022	Bisphosphoglycerate mutase (BPGM) is an erythrocyte-specific multifunctional enzyme that is responsible for the regulation of 2,3-bisphosphoglycerate (2,3-BPG) in red blood cells through its synthase and phosphatase activities; the latter enzymatic function is stimulated by the endogenous activator 2-phosphoglycolate (2-PG).	2,3-Diphosphoglycerate	126-149	bisphosphoglycerate mutase	Homo sapiens	28-32
35362470-1	2022	Bisphosphoglycerate mutase (BPGM) is an erythrocyte-specific multifunctional enzyme that is responsible for the regulation of 2,3-bisphosphoglycerate (2,3-BPG) in red blood cells through its synthase and phosphatase activities; the latter enzymatic function is stimulated by the endogenous activator 2-phosphoglycolate (2-PG).	2,3-Diphosphoglycerate	151-158	bisphosphoglycerate mutase	Homo sapiens	0-26
35362470-1	2022	Bisphosphoglycerate mutase (BPGM) is an erythrocyte-specific multifunctional enzyme that is responsible for the regulation of 2,3-bisphosphoglycerate (2,3-BPG) in red blood cells through its synthase and phosphatase activities; the latter enzymatic function is stimulated by the endogenous activator 2-phosphoglycolate (2-PG).	2,3-Diphosphoglycerate	151-158	bisphosphoglycerate mutase	Homo sapiens	28-32
35019238-6	2022	Etavopivat exhibited a linear and time-independent pharmacokinetic profile (at doses <=400 mg) and elicited the expected pharmacodynamic effects of PKR activation (decreased 2,3-diphosphoglycerate and increased adenosine triphosphate) and evidence of improved hemoglobin-oxygen affinity.	2,3-Diphosphoglycerate	174-196	pyruvate kinase L/R	Homo sapiens	148-151
2803567-0	1989	Improved stability of 2,3-bisphosphoglycerate during storage of hexokinase-overloaded erythrocytes.	2,3-Diphosphoglycerate	22-45	hexokinase 1	Homo sapiens	64-74
2546605-0	1989	Stimulation by glycerate 2,3-bisphosphate: a common property of cytosolic IMP-GMP 5"-nucleotidase in rat and human tissues.	2,3-Diphosphoglycerate	15-41	5'-nucleotidase ecto	Homo sapiens	82-97
2546605-1	1989	Glycerate 2,3-bisphosphate, a potent stimulator of the cytosolic 5"-nucleotidase which preferentially hydrolyzes IMP and GMP in human erythrocytes (Bontemps et al., 1988, Biochem.	2,3-Diphosphoglycerate	0-26	5'-nucleotidase ecto	Homo sapiens	65-80
3196327-0	1988	2,3-Bisphosphoglycerate inhibits hemoglobin synthesis and phosphorylation of initiation factor 2 by casein kinase II in reticulocyte lysates.	2,3-Diphosphoglycerate	0-23	transcription termination factor 2	Homo sapiens	88-96
2738066-7	1989	These results indicate that NADPH binds at the beta-chain anion-binding site and can be considered as a fluorescent analog of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	126-148	2,4-dienoyl-CoA reductase 1	Homo sapiens	28-33
2920177-9	1989	In hexokinase-deficient cells, two major abnormalities are found: when the cells were deoxygenated, the concentration of ATP and 2,3-DPG fell.	2,3-Diphosphoglycerate	129-136	hexokinase 1	Homo sapiens	3-13
2662543-2	1989	The revealed differences in the autooxidation rate of the studied myoglobins are explained by differences in the conformational state of a protein globule, which more actively protects a heme (in semi-aquatic animals) from spontaneous oxidation under conditions of muscular saturation of cells with oxygen, which is confirmed by the results obtained from the analysis of the universal links of pair amino acid residues which stabilize the protein molecule, 2,3-DPG and carnosine decrease the resistance of myoglobin to autooxidation.	2,3-Diphosphoglycerate	457-464	myoglobin	Homo sapiens	66-75
2558534-0	1989	Stimulation by glycerate 2,3-bisphosphate: a common property of cytosolic purine 5"-nucleotidase in various tissues.	2,3-Diphosphoglycerate	15-41	5'-nucleotidase, cytosolic II	Homo sapiens	64-96
2492818-0	1989	In vivo regeneration of red cell 2,3-diphosphoglycerate following transfusion of DPG-depleted AS-1, AS-3 and CPDA-1 red cells.	2,3-Diphosphoglycerate	33-55	prostaglandin D2 receptor	Homo sapiens	94-104
2506561-4	1989	The glycosylated aldose reductase exhibits lower Km for glucose and NADPH as compared to unglycosylated enzyme and is not inhibited by phosphorylated intermediates such as ADP, 1,3-DPG, 2,3-DPG and 3-PGA, whereas physiological concentrations of these intermediates almost completely inhibit the unglycosylated enzyme.	2,3-Diphosphoglycerate	186-193	aldo-keto reductase family 1 member B	Homo sapiens	17-33
3394615-4	1988	Patients with high erythropoietin titers had lower Pao2 (36 +/- 7 vs 49 +/- 7 mm Hg, p less than 0.01), lower aortic saturation (68 +/- 12 vs 81 +/- 9%, p less than 0.01), and higher red cell 2,3-DPG (2.47 +/- 0.34 vs 3.23 +/- 0.73 mumol/ml, p less than 0.01).	2,3-Diphosphoglycerate	192-199	erythropoietin	Homo sapiens	19-33
2839144-1	1988	Identification of a purine 5"-nucleotidase stimulated by ATP and glycerate 2,3-bisphosphate.	2,3-Diphosphoglycerate	65-91	5'-nucleotidase ecto	Homo sapiens	27-42
2839144-6	1988	The purine 5"-nucleotidase is inhibited by Pi, and is strongly stimulated by ATP, dATP and GTP, and by glycerate 2,3-bisphosphate.	2,3-Diphosphoglycerate	103-129	5'-nucleotidase ecto	Homo sapiens	11-26
2839144-10	1988	It is concluded that the glycerate 2,3-bisphosphate-stimulated purine 5"-nucleotidase is responsible for the dephosphorylation of IMP and GMP, but not of AMP, in human erythrocytes.	2,3-Diphosphoglycerate	25-51	5'-nucleotidase ecto	Homo sapiens	70-85
3444005-0	1987	[Computerized estimation of P50 with automatic blood gas analyzer and CO-oximeter parameters, and its modification for 2,3-DPG].	2,3-Diphosphoglycerate	119-126	nuclear factor kappa B subunit 1	Homo sapiens	28-31
3129913-6	1988	In vivo study, after administration of pentoxifylline 300 mg per day orally for 4 weeks to seven patients with COPD, P50 increased significantly from 29.0 +/- 0.6 to 30.4 +/- 0.6 Torr (p less than 0.05) and 2,3-DPG increased slightly from 11.67 +/- 0.56 to 14.33 +/- 1.12 mumol/gHb (p less than 0.1).	2,3-Diphosphoglycerate	207-214	nuclear factor kappa B subunit 1	Homo sapiens	117-120
2854949-6	1988	The erythrocytic purine 5"-nucleotidase is also stimulated by glycerate 2,3-bisphosphate.	2,3-Diphosphoglycerate	62-88	5' nucleotidase, ecto	Rattus norvegicus	24-39
3590297-0	1987	Correlation of red cell 2,3-diphosphoglycerate to P50 values in stored blood.	2,3-Diphosphoglycerate	24-46	nuclear factor kappa B subunit 1	Homo sapiens	50-53
2832777-5	1987	The concentration of 2,3-diphosphoglycerate in the erythrocytes was determined by Bartlett"s method twice: before and after ACTH treatment.	2,3-Diphosphoglycerate	21-43	proopiomelanocortin	Homo sapiens	124-128
3111176-7	1987	The rise in 2,3-DPG is caused by decrease of pyruvate kinase, probably due to proteolytic inactivation of the enzyme.	2,3-Diphosphoglycerate	12-19	pyruvate kinase PKLR	Oryctolagus cuniculus	45-60
3599659-6	1987	Within a few hours after each transfusion of 2,3-diphosphoglycerate-poor red cells, both EP (P = 0.009) and CRC (P = 0.007) increased temporarily between one to 18 and three to 38 hours, respectively.	2,3-Diphosphoglycerate	45-67	erythropoietin	Homo sapiens	89-91
2832777-7	1987	It was demonstrated, furthermore, that 2,3-DPG concentration in the erythrocytes could change before ACTH treatment depending on the age of the patients and the clinical course of the disease.	2,3-Diphosphoglycerate	39-46	proopiomelanocortin	Homo sapiens	101-105
3036106-1	1987	The human erythrocyte 2,3-bisphosphoglycerate mutase (BPGM) is a multifunctional enzyme which controls the metabolism of 2,3-diphosphoglycerate (DPG), the main allosteric effector of haemoglobin.	2,3-Diphosphoglycerate	121-143	bisphosphoglycerate mutase	Homo sapiens	10-52
3548716-2	1987	2,3-bisphosphoglycerate protects also many other mitochondrial and cytosolic proteins, such as glutamate dehydrogenase (GDH) an glyceraldehyde-3-phosphate dehydrogenase (GAPDH), from proteolysis by broken lysosomes and other proteases.	2,3-Diphosphoglycerate	0-23	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	128-168
3548716-2	1987	2,3-bisphosphoglycerate protects also many other mitochondrial and cytosolic proteins, such as glutamate dehydrogenase (GDH) an glyceraldehyde-3-phosphate dehydrogenase (GAPDH), from proteolysis by broken lysosomes and other proteases.	2,3-Diphosphoglycerate	0-23	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	170-175
3038084-0	1987	The bisphosphonomethyl analogue of 2,3-bisphosphoglycerate inhibits yeast but not wheat-germ phosphoglycerate mutase.	2,3-Diphosphoglycerate	35-58	2,3-bisphosphoglycerate-independent phosphoglycerate mutase	Triticum aestivum	93-116
3038084-1	1987	The bisphosphonomethyl analogue of 2,3-bisphosphoglycerate [4-phosphono-2-(phosphonomethyl) butanoate] was a potent competitive inhibitor of cofactor-dependent phosphoglycerate mutase from yeast, with a Ki of 0.8 mM.	2,3-Diphosphoglycerate	35-58	2,3-bisphosphoglycerate-independent phosphoglycerate mutase	Triticum aestivum	160-183
3036106-1	1987	The human erythrocyte 2,3-bisphosphoglycerate mutase (BPGM) is a multifunctional enzyme which controls the metabolism of 2,3-diphosphoglycerate (DPG), the main allosteric effector of haemoglobin.	2,3-Diphosphoglycerate	121-143	bisphosphoglycerate mutase	Homo sapiens	54-58
3036106-1	1987	The human erythrocyte 2,3-bisphosphoglycerate mutase (BPGM) is a multifunctional enzyme which controls the metabolism of 2,3-diphosphoglycerate (DPG), the main allosteric effector of haemoglobin.	2,3-Diphosphoglycerate	145-148	bisphosphoglycerate mutase	Homo sapiens	10-52
3036106-1	1987	The human erythrocyte 2,3-bisphosphoglycerate mutase (BPGM) is a multifunctional enzyme which controls the metabolism of 2,3-diphosphoglycerate (DPG), the main allosteric effector of haemoglobin.	2,3-Diphosphoglycerate	145-148	bisphosphoglycerate mutase	Homo sapiens	54-58
3023066-1	1986	The human erythrocyte 2,3-bisphosphoglycerate mutase (BPGM) is a multifunctional enzyme which controls the metabolism of 2,3-diphosphoglycerate, the main allosteric effector of haemoglobin.	2,3-Diphosphoglycerate	121-143	bisphosphoglycerate mutase	Homo sapiens	10-52
3772222-4	1986	ATP, as well as adenosine diphosphate and 2,3-diphosphoglyceric acid, interacts synergistically with the ammonium sulfate hemolysate fraction to promote iron release from transferrin.	2,3-Diphosphoglycerate	42-68	transferrin	Homo sapiens	171-182
3023066-1	1986	The human erythrocyte 2,3-bisphosphoglycerate mutase (BPGM) is a multifunctional enzyme which controls the metabolism of 2,3-diphosphoglycerate, the main allosteric effector of haemoglobin.	2,3-Diphosphoglycerate	121-143	bisphosphoglycerate mutase	Homo sapiens	54-58
4095774-3	1985	It was found that 2,3 DPG levels were significantly lower (p less than 0.005) in both sexes at Dead Sea level than that of Amman.	2,3-Diphosphoglycerate	18-25	S13 erythroblastosis (avian) oncogene homolog	Homo sapiens	100-103
3082363-3	1986	Native enzyme showed biphasic kinetics with substrates (glucose and glyceraldehyde), was strongly inhibited by 15 microM ADP, 1,3-diphosphoglycerate, 2,3-diphosphoglycerate and 3-phosphoglycerate, and aldose reductase inhibitors such as sorbinil and alrestatin.	2,3-Diphosphoglycerate	150-172	aldo-keto reductase family 1 member B	Homo sapiens	201-217
3931871-0	1985	[Relation between 2,3-diphosphoglyceric acids and HbA1 in insulin-dependent diabetic children].	2,3-Diphosphoglycerate	18-45	hemoglobin subunit alpha 1	Homo sapiens	50-54
4063353-6	1985	When the enzymes of the futile cycle are combined with the enzymes of the lower glycolytic pathway in a reconstitution experiment designed to represent conditions within the stored erythrocyte, the futile cycle does provide an ATPase activity which results in the metabolic loss of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	282-304	dynein axonemal heavy chain 8	Homo sapiens	227-233
4018089-6	1985	The dependence of the rate of GSH production on the concentration of the hexokinase inhibitors glucose 1,6-bisphosphate and glycerate 2,3-bisphosphate showed that, under conditions of oxidative stress, hexokinase was the principal determinant of flux through the shunt.	2,3-Diphosphoglycerate	124-150	hexokinase 1	Homo sapiens	73-83
4018089-6	1985	The dependence of the rate of GSH production on the concentration of the hexokinase inhibitors glucose 1,6-bisphosphate and glycerate 2,3-bisphosphate showed that, under conditions of oxidative stress, hexokinase was the principal determinant of flux through the shunt.	2,3-Diphosphoglycerate	124-150	hexokinase 1	Homo sapiens	202-212
6465889-8	1984	His-2 and His-143 are among the residues reported to be implicated in the binding of 2,3-bisphosphoglycerate by deoxyhemoglobin [A. Arnone (1972) Nature (London) 237, 146-148].	2,3-Diphosphoglycerate	85-108	histatin 3	Homo sapiens	0-5
4013446-8	1985	The intraerythrocytic 2,3-DPG concentration changes simultaneously with the P50.	2,3-Diphosphoglycerate	22-29	nuclear factor kappa B subunit 1	Homo sapiens	76-79
3916400-8	1985	Patients with congenital cyanotic heart disease have an increased P50 mediated through an increase in 2,3-DPG.	2,3-Diphosphoglycerate	102-109	nuclear factor kappa B subunit 1	Homo sapiens	66-69
3856279-4	1985	Without inhibitors or in the presence of glucose 1,6-bisphosphate,2,3-diphosphoglycerate, and ADP, maximum hexokinase activity was observed at 5 mM glucose concentration.	2,3-Diphosphoglycerate	66-88	hexokinase 1	Homo sapiens	107-117
3917634-3	1985	Nine patients received oxygen for 24 h, and 5 received oxygen for 72 h. In these 5 patients, oxygen supplementation resulted in a shift in P50 to a normal value of 26.7 +/- 1.8 (this value was different from the patients" level while breathing room air and not different from that of the normoxemic control subjects) and a decrease in 2,3-DPG toward but not to a normal value (16.34 +/- 1.92; p less than 0.01).	2,3-Diphosphoglycerate	335-342	nuclear factor kappa B subunit 1	Homo sapiens	139-142
3917634-4	1985	This shift in P50 to the left could be related to the decrease in 2,3-DPG.	2,3-Diphosphoglycerate	66-73	nuclear factor kappa B subunit 1	Homo sapiens	14-17
6418564-2	1983	Empirical equations are reported to predict the oxygen partial pressure at half-saturation of hemoglobin (p50) from known values for pH, pCO2 and 2,3-diphosphoglycerate, with an accuracy of +/- 0.82 torr.	2,3-Diphosphoglycerate	146-168	HGB	Sus scrofa	94-104
6428779-2	1984	The d(log p50)/d[COHb] coefficient is 0.00848, independent of pH and 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	69-91	nuclear factor kappa B subunit 1	Homo sapiens	10-13
6731081-7	1984	However, in these diabetic subjects, the P50 had been increased by the somewhat elevated levels of 2,3-DPG.	2,3-Diphosphoglycerate	99-106	nuclear factor kappa B subunit 1	Homo sapiens	41-44
6711924-6	1984	There was a positive correlation between P50 std and 2,3-DPG, arterial blood pH, haemoglobin and cardiac index, as well as between 2,3-DPG and arterial blood pH.	2,3-Diphosphoglycerate	53-60	nuclear factor kappa B subunit 1	Homo sapiens	41-44
6693310-5	1984	As expected, increased 2,3-DPG was associated with slightly increased P50, when expressed at pH 7.4.	2,3-Diphosphoglycerate	23-30	nuclear factor kappa B subunit 1	Homo sapiens	70-73
6612103-9	1983	The analysis shows that any rise in P50 caused by increased 2,3-diphosphoglycerate is a liability.	2,3-Diphosphoglycerate	60-82	nuclear factor kappa B subunit 1	Homo sapiens	36-39
6141763-2	1983	The first kinase, present in greatest activity in microsomal extracts, appears to be identical to casein kinase I by characteristic molecular size on gel filtration (Mr 40,000) and sodium dodecyl sulfate-gel electrophoresis (Mr 34,000), autophosphorylation of this single subunit, inability to efficiently utilize GTP, and resistance to inhibition by heparin and 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	363-385	casein kinase 1, epsilon	Rattus norvegicus	98-113
6860590-3	1983	The activity of glucose-6-phosphate dehydrogenase (G6PD) as well as that of 6-phosphogluconate dehydrogenase (6PGD) was inhibited to 20% of baseline in normal red cell haemolysate by 4 mM 2,3-diphosphoglycerate at pH 7.1.	2,3-Diphosphoglycerate	188-210	glucose-6-phosphate dehydrogenase	Homo sapiens	16-49
6860590-3	1983	The activity of glucose-6-phosphate dehydrogenase (G6PD) as well as that of 6-phosphogluconate dehydrogenase (6PGD) was inhibited to 20% of baseline in normal red cell haemolysate by 4 mM 2,3-diphosphoglycerate at pH 7.1.	2,3-Diphosphoglycerate	188-210	glucose-6-phosphate dehydrogenase	Homo sapiens	51-55
6860590-3	1983	The activity of glucose-6-phosphate dehydrogenase (G6PD) as well as that of 6-phosphogluconate dehydrogenase (6PGD) was inhibited to 20% of baseline in normal red cell haemolysate by 4 mM 2,3-diphosphoglycerate at pH 7.1.	2,3-Diphosphoglycerate	188-210	phosphogluconate dehydrogenase	Homo sapiens	76-108
6860590-3	1983	The activity of glucose-6-phosphate dehydrogenase (G6PD) as well as that of 6-phosphogluconate dehydrogenase (6PGD) was inhibited to 20% of baseline in normal red cell haemolysate by 4 mM 2,3-diphosphoglycerate at pH 7.1.	2,3-Diphosphoglycerate	188-210	phosphogluconate dehydrogenase	Homo sapiens	110-114
6860590-4	1983	2,3-Diphosphoglycerate was a competitive inhibitor with 6-phosphogluconate (Ki=1.05 mM) and a noncompetitive inhibitor with NADP (Ki=3.3 mM) for 6PGD.	2,3-Diphosphoglycerate	0-22	phosphogluconate dehydrogenase	Homo sapiens	145-149
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.	2,3-Diphosphoglycerate	188-210	glucose-6-phosphate dehydrogenase	Homo sapiens	115-119
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.	2,3-Diphosphoglycerate	188-210	phosphogluconate dehydrogenase	Homo sapiens	124-128
6312283-4	1983	The accumulation of 2,3-bisphosphoglycerate was primarily attributable to an increase in 2,3-bisphosphoglycerate synthase.	2,3-Diphosphoglycerate	20-43	bisphosphoglycerate mutase	Homo sapiens	89-121
6581148-5	1983	On the contrary, the minor cytosolic casein kinase CTS, is inhibited by both 2,3-DPG and heparin under all conditions tested in the assay.	2,3-Diphosphoglycerate	77-84	transthyretin	Homo sapiens	51-54
6840425-3	1983	The content of 2,3-diphosphoglycerate correlated significantly with haemoglobin-oxygen affinity expressed as P50 at pH 7.4 (r = 0.34, p less than 0.05).	2,3-Diphosphoglycerate	15-37	nuclear factor kappa B subunit 1	Homo sapiens	109-112
6848245-2	1983	The d(log p50)/d(pH) coefficient varied from 0.39 at 19 degrees C to 0.35 at 43 degrees C. The relationship between log p50 and 1/T (T = degrees Kelvin) was linear under the experimental conditions used, and the d(log p50)/d(1/T) coefficient varied between -2138 at pH 7.0 and -2162 at pH 7.6, independent of the concentration of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	330-352	nuclear factor kappa B subunit 1	Homo sapiens	10-13
6848245-2	1983	The d(log p50)/d(pH) coefficient varied from 0.39 at 19 degrees C to 0.35 at 43 degrees C. The relationship between log p50 and 1/T (T = degrees Kelvin) was linear under the experimental conditions used, and the d(log p50)/d(1/T) coefficient varied between -2138 at pH 7.0 and -2162 at pH 7.6, independent of the concentration of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	330-352	nuclear factor kappa B subunit 1	Homo sapiens	120-123
6848245-2	1983	The d(log p50)/d(pH) coefficient varied from 0.39 at 19 degrees C to 0.35 at 43 degrees C. The relationship between log p50 and 1/T (T = degrees Kelvin) was linear under the experimental conditions used, and the d(log p50)/d(1/T) coefficient varied between -2138 at pH 7.0 and -2162 at pH 7.6, independent of the concentration of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	330-352	nuclear factor kappa B subunit 1	Homo sapiens	120-123
6848245-3	1983	Assuming that the effect of pco2 on the p50 value is the same at 19, 30, and 43 degrees C as at 37 degrees C, one can use the reported coefficients to calculate the p50 value for normal human blood under conditions of temperature, pH, pco2, and 2,3-diphosphoglycerate concentrations prevailing under physiological and pathological conditions.	2,3-Diphosphoglycerate	245-267	nuclear factor kappa B subunit 1	Homo sapiens	165-168
6842358-3	1983	Twenty-two sets of analyses were performed to measure oxygen affinity (P50) 2,3-diphosphoglycerate concentration and full blood gas analysis on umbilical arterial and venous samples.	2,3-Diphosphoglycerate	76-98	nuclear factor kappa B subunit 1	Homo sapiens	71-74
6816650-2	1982	Diabetic blood p50 was higher (29.79 +/- 1.68 versus 28.26 +/- 1.16 mmHg, p less than 0.001) and with a higher 2,3-diphosphoglyceric acid/haemoglobin molar ratio (1.04 +/- 0.15 versus 0.86 +/- 0.10, p less than 0.001).	2,3-Diphosphoglycerate	111-137	nuclear factor kappa B subunit 1	Homo sapiens	15-18
6219662-1	1982	A major locus (Dpg) with two alleles (d and D) controls erythrocyte 2,3-diphosphoglycerate (DPG) levels in Long-Evans rats and is closely linked to a locus (Hbb) determining a hemoglobin electrophoretic polymorphism.	2,3-Diphosphoglycerate	68-90	hemoglobin subunit beta	Rattus norvegicus	157-160
6813948-2	1982	The influence of pH on P50 expressed as the H+ factor (delta log P50/delta pH)PCO2 was measured under conditions of varying PCO2, temperature and concentration of 2,3-diphosphoglycerate (2,3-DPG), resulting in a set of data expressing second-order inter-ligand interactions.	2,3-Diphosphoglycerate	163-185	granzyme A	Homo sapiens	44-53
7122212-0	1982	Characterization of the pyruvate kinase which induces the low 2,3-DPG level of fetal rabbit red cells.	2,3-Diphosphoglycerate	62-69	pyruvate kinase PKLR	Oryctolagus cuniculus	24-39
7122212-1	1982	The low 2,3-disphosphoglycerate (2,3-DPG) level of fetal rabbit red cells has been attributed previously to a very high pyruvate kinase (PK) activity.	2,3-Diphosphoglycerate	33-40	pyruvate kinase PKLR	Oryctolagus cuniculus	120-135
7122212-1	1982	The low 2,3-disphosphoglycerate (2,3-DPG) level of fetal rabbit red cells has been attributed previously to a very high pyruvate kinase (PK) activity.	2,3-Diphosphoglycerate	33-40	pyruvate kinase PKLR	Oryctolagus cuniculus	137-139
7122212-8	1982	But in view of the role of PK in the control of the 2,3-DPG level and thereby of the oxygen affinity of red blood cells, we assume that the physiological significance of the PK isozyme change is akin to that of the switch from fetal to adult hemoglobin in other species.	2,3-Diphosphoglycerate	52-59	pyruvate kinase PKLR	Oryctolagus cuniculus	27-29
7090336-1	1982	A sucrose medium containing relatively great amounts of adenine and inosine (AIS-CPD) was more effective for maintaining adenosine triphosphate (ATP) and 2,3-diphosphoglyceric acid (DPG) levels of human erythrocytes for more than 35 days at 4 degrees C than control ACD-packed cells, sucrose medium (S-CPD), and sucrose medium containing a small amount of adenine.	2,3-Diphosphoglycerate	154-180	carboxypeptidase D	Homo sapiens	81-84
6271255-1	1981	We have studied iron transfer from transferrin to ferritin in the presence of ATP, GTP, ADP, AMP and 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	101-123	transferrin	Homo sapiens	35-46
7090336-1	1982	A sucrose medium containing relatively great amounts of adenine and inosine (AIS-CPD) was more effective for maintaining adenosine triphosphate (ATP) and 2,3-diphosphoglyceric acid (DPG) levels of human erythrocytes for more than 35 days at 4 degrees C than control ACD-packed cells, sucrose medium (S-CPD), and sucrose medium containing a small amount of adenine.	2,3-Diphosphoglycerate	182-185	carboxypeptidase D	Homo sapiens	81-84
7291198-3	1981	The transport of PEP through the erythrocyte membrane was essential to the increase of 2,3-DPG and ATP.	2,3-Diphosphoglycerate	87-94	progestagen associated endometrial protein	Homo sapiens	17-20
6974156-2	1981	Orthophosphate (Pi) at low concentrations, is able to activate the glucose 6-phosphate, glucose-1,6-diphosphate or 2,3-diphosphoglycerate-inhibited hexokinase (E.C.	2,3-Diphosphoglycerate	115-137	hexokinase-2	Oryctolagus cuniculus	148-158
6794946-0	1981	Equations and nomogram for the relationship of human blood p50 to 2,3-diphosphoglycerate, CO2, and H+.	2,3-Diphosphoglycerate	66-88	nuclear factor kappa B subunit 1	Homo sapiens	59-62
6794946-5	1981	Empirical equations and a nomogram were derived, which allow the calculation of p50 from known values of pCO2, pH, and [2,3-DPG]/[Hb4] molar ratio with a SD of 97 and 114 Pa (0.73 and 0.86 mmHg), respectively.	2,3-Diphosphoglycerate	120-127	nuclear factor kappa B subunit 1	Homo sapiens	80-83
7031980-0	1981	The in vitro inhibitory effect on thrombin by 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	46-68	coagulation factor II, thrombin	Homo sapiens	34-42
7031980-1	1981	Thrombin incubated with 2,3-diphosphoglycerate (150 nmol 2,3-DPG/1 NIH thrombin unit) lost up to 70% of its clotting activity, whereas the esterase activity remained unchanged.	2,3-Diphosphoglycerate	24-46	coagulation factor II, thrombin	Homo sapiens	0-8
7031980-1	1981	Thrombin incubated with 2,3-diphosphoglycerate (150 nmol 2,3-DPG/1 NIH thrombin unit) lost up to 70% of its clotting activity, whereas the esterase activity remained unchanged.	2,3-Diphosphoglycerate	24-46	coagulation factor II, thrombin	Homo sapiens	71-79
7031980-1	1981	Thrombin incubated with 2,3-diphosphoglycerate (150 nmol 2,3-DPG/1 NIH thrombin unit) lost up to 70% of its clotting activity, whereas the esterase activity remained unchanged.	2,3-Diphosphoglycerate	57-64	coagulation factor II, thrombin	Homo sapiens	0-8
7031980-1	1981	Thrombin incubated with 2,3-diphosphoglycerate (150 nmol 2,3-DPG/1 NIH thrombin unit) lost up to 70% of its clotting activity, whereas the esterase activity remained unchanged.	2,3-Diphosphoglycerate	57-64	coagulation factor II, thrombin	Homo sapiens	71-79
7031980-5	1981	In presence of 2,3-DPG, alpha-thrombin was not eluted.	2,3-Diphosphoglycerate	15-22	coagulation factor II, thrombin	Homo sapiens	30-38
7031980-6	1981	Likely, 2,3-DPG can interfere with thrombin.	2,3-Diphosphoglycerate	8-15	coagulation factor II, thrombin	Homo sapiens	35-43
7291198-6	1981	Addition of ascorbic acid, purine or purine nucleosides to the ACD-sucrose-PEP solution improved the PEP effect of maintaining ATP and/or 2,3-DPG in erythrocytes during storage at 4 degrees C.	2,3-Diphosphoglycerate	138-145	progestagen associated endometrial protein	Homo sapiens	75-78
7291198-6	1981	Addition of ascorbic acid, purine or purine nucleosides to the ACD-sucrose-PEP solution improved the PEP effect of maintaining ATP and/or 2,3-DPG in erythrocytes during storage at 4 degrees C.	2,3-Diphosphoglycerate	138-145	progestagen associated endometrial protein	Homo sapiens	101-104
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.	2,3-Diphosphoglycerate	164-186	glucose-6-phosphate dehydrogenase	Homo sapiens	81-85
7364608-4	1980	2,3-Diphosphoglycerate (2,3-DPG) was significantly elevated after exercise, but not during or 30 min postexercise, and it correlated significantly with P50 in 2 studies (r, 0.43--0.68).	2,3-Diphosphoglycerate	0-22	nuclear factor kappa B subunit 1	Homo sapiens	152-155
7364608-4	1980	2,3-Diphosphoglycerate (2,3-DPG) was significantly elevated after exercise, but not during or 30 min postexercise, and it correlated significantly with P50 in 2 studies (r, 0.43--0.68).	2,3-Diphosphoglycerate	24-31	nuclear factor kappa B subunit 1	Homo sapiens	152-155
7364608-8	1980	Multiple correlation regression analysis between P50 and 2,3-DPG, ATP, and [Na+] yields a coefficient of 0.86.	2,3-Diphosphoglycerate	57-64	nuclear factor kappa B subunit 1	Homo sapiens	49-52
6254918-1	1980	Erythrocyte 2,3-diphosphoglycerate levels are determined principally by a single molecule which has both diphosphoglycerate mutase (DPGM) and diphosphoglycerate phosphatase activities.	2,3-Diphosphoglycerate	12-34	bisphosphoglycerate mutase	Homo sapiens	105-130
6254918-1	1980	Erythrocyte 2,3-diphosphoglycerate levels are determined principally by a single molecule which has both diphosphoglycerate mutase (DPGM) and diphosphoglycerate phosphatase activities.	2,3-Diphosphoglycerate	12-34	bisphosphoglycerate mutase	Homo sapiens	132-136
6948372-2	1981	Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1.	2,3-Diphosphoglycerate	31-53	erythrocyte membrane protein band 4.1	Homo sapiens	104-112
6948372-2	1981	Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1.	2,3-Diphosphoglycerate	55-62	erythrocyte membrane protein band 4.1	Homo sapiens	104-112
7269456-0	1980	Effect of age and 2,3-DPG content of transfused blood on serum erythropoietin.	2,3-Diphosphoglycerate	18-25	erythropoietin	Homo sapiens	63-77
7269456-2	1980	A greater fall in erythropoietin was found following the transfusion of fresh blood than after an equal amount of stored blood in which 2,3-diphosphoglycerate concentrations were depleted.	2,3-Diphosphoglycerate	136-158	erythropoietin	Homo sapiens	18-32
6780749-3	1980	A multivariate analysis demonstrated that an increase in the concentration of 2,3-diphosphoglycerate and adenosine monophosphatic acid with prolonged work in CS2 exposure mainly results from changes dependent on subjects" age.	2,3-Diphosphoglycerate	78-100	chorionic somatomammotropin hormone 2	Homo sapiens	158-161
497234-1	1979	The organic phosphate allosteric effectors of hemoglobin, inositol hexaphosphate, 2,3-diphosphoglycerate, and ATP, interact with NADH-methemoglobin reductase (NADH-diaphorase).	2,3-Diphosphoglycerate	82-104	hemoglobin subunit gamma 2	Homo sapiens	134-147
34418-4	1979	The effect of 2,3-DPG on the position of the OEC (p50, the pO2 at one-half maximal O2 saturation) is via its allosteric effect on haemoglobin at 2,3-DPG/haemoglobin less than 1.	2,3-Diphosphoglycerate	14-21	nuclear factor kappa B subunit 1	Homo sapiens	50-53
29278-0	1978	High pyruvate kinase activity causes low concentration of 2,3-diphosphoglycerate in fetal rabbit red cells.	2,3-Diphosphoglycerate	58-80	pyruvate kinase PKLR	Oryctolagus cuniculus	5-20
29888-4	1978	The bound fumarase was released from the membrane by the substrates, isocitrate, citrate or 2,3-diphosphoglycerate at low concentrations.	2,3-Diphosphoglycerate	92-114	fumarate hydratase	Rattus norvegicus	10-18
44990-4	1979	The increase of the hemoglobin oxygen affinity, associated with a decrease of the 2,3-DPG level appears to be very fast in the samples of ACD stored blood since two hours after sampling, the P50 decrease was of 4 torr.	2,3-Diphosphoglycerate	82-89	nuclear factor kappa B subunit 1	Homo sapiens	191-194
44990-7	1979	When freezed red blood cells, were defreezed the P50 was found to be 4 torr lower than that of fresh blood and the 2,3-DPG level was also decreased (-4.1 muM.gHb-1).	2,3-Diphosphoglycerate	115-122	latexin	Homo sapiens	154-157
545945-4	1979	Analysis of statistically verified results reveals that zinc ions increase the oxygen affinity of hemoglobin bringing about a leftward shift of the HbO2 dissociation curve (by 3.85 mm Hg for P50) the level of 2,3-DPG remaining constant in the red cells incubated with ZnSO4.	2,3-Diphosphoglycerate	209-216	activating signal cointegrator 1 complex subunit 1	Homo sapiens	191-194
27696-2	1978	In 10 newly discovered diabetics the average P50 at in vivo pH was normal prior to insulin (26.2 mm Hg), decreased to 24.5 mm Hg (p less than 0.005) on the day following the initial insulin administration, and was within normal limits (26.9 mm Hg) when the diabetes was finally well controlled and red cell 2,3-diphosphoglycerate (2,3-DPG) had risen to elevated levels.	2,3-Diphosphoglycerate	307-329	nuclear factor kappa B subunit 1	Homo sapiens	45-48
27696-2	1978	In 10 newly discovered diabetics the average P50 at in vivo pH was normal prior to insulin (26.2 mm Hg), decreased to 24.5 mm Hg (p less than 0.005) on the day following the initial insulin administration, and was within normal limits (26.9 mm Hg) when the diabetes was finally well controlled and red cell 2,3-diphosphoglycerate (2,3-DPG) had risen to elevated levels.	2,3-Diphosphoglycerate	331-338	nuclear factor kappa B subunit 1	Homo sapiens	45-48
27696-5	1978	The study indicates that insulin administration to diabetics with high blood glucose levels may lead to transient decreases in red cell 2,3-DPG and in oxygen-releasing capacity of the red blood cells.	2,3-Diphosphoglycerate	136-143	insulin	Homo sapiens	25-32
29278-9	1978	This higher activity of PK will lead to a decreased concentration of 3-PGA with a consecutive fall in 2,3-DPG concentration.	2,3-Diphosphoglycerate	102-109	pyruvate kinase PKLR	Oryctolagus cuniculus	24-26
19087-4	1977	GTP, 2,3-diphosphoglycerate, ATP, ADP and citrate produced the most rapid exchange of iron between the two types of transferrin, but many other compounds showed some degree of activity.	2,3-Diphosphoglycerate	5-27	transferrin	Homo sapiens	116-127
101433-5	1978	Closely negative correlations were observed between CA-B levels and T3 resin sponge uptake T4, protein bound iodine levels, or 2,3-DPG concentrations.	2,3-Diphosphoglycerate	127-134	carbonic anhydrase 2	Homo sapiens	52-56
669574-5	1978	The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, 3-bisphosphoglycerate contact position beta2 His in human hemoglobin to beta2 Asn in llama hemoglobin, whereby one of the four 2, 3-bisphosphoglycerate contact points is interrupted.	2,3-Diphosphoglycerate	96-120	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	204-209
669574-5	1978	The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, 3-bisphosphoglycerate contact position beta2 His in human hemoglobin to beta2 Asn in llama hemoglobin, whereby one of the four 2, 3-bisphosphoglycerate contact points is interrupted.	2,3-Diphosphoglycerate	96-120	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	237-242
669574-5	1978	The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, 3-bisphosphoglycerate contact position beta2 His in human hemoglobin to beta2 Asn in llama hemoglobin, whereby one of the four 2, 3-bisphosphoglycerate contact points is interrupted.	2,3-Diphosphoglycerate	162-186	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	204-209
669574-5	1978	The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, 3-bisphosphoglycerate contact position beta2 His in human hemoglobin to beta2 Asn in llama hemoglobin, whereby one of the four 2, 3-bisphosphoglycerate contact points is interrupted.	2,3-Diphosphoglycerate	162-186	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	237-242
669574-5	1978	The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, 3-bisphosphoglycerate contact position beta2 His in human hemoglobin to beta2 Asn in llama hemoglobin, whereby one of the four 2, 3-bisphosphoglycerate contact points is interrupted.	2,3-Diphosphoglycerate	162-186	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	204-209
669574-5	1978	The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, 3-bisphosphoglycerate contact position beta2 His in human hemoglobin to beta2 Asn in llama hemoglobin, whereby one of the four 2, 3-bisphosphoglycerate contact points is interrupted.	2,3-Diphosphoglycerate	162-186	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	237-242
25408-0	1978	Oxygen affinity of hemoglobins F and A partially oxidized to methemoglobin: influence of 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	89-111	hemoglobin subunit gamma 2	Homo sapiens	61-74
706929-0	1978	[Importance of binding of 2,3-diphosphoglycerate and ATP to hemoglobin for erythrocyte glycolysis: activation by 2,3-diphosphoglycerate of hexokinase at intracellular conditions].	2,3-Diphosphoglycerate	26-48	hexokinase 1	Homo sapiens	139-149
706929-0	1978	[Importance of binding of 2,3-diphosphoglycerate and ATP to hemoglobin for erythrocyte glycolysis: activation by 2,3-diphosphoglycerate of hexokinase at intracellular conditions].	2,3-Diphosphoglycerate	113-135	hexokinase 1	Homo sapiens	139-149
844210-0	1977	The effect of 2,3-diphosphoglycerate on oxygen consumption burst in thrombin-stimulated platelets.	2,3-Diphosphoglycerate	14-36	coagulation factor II, thrombin	Homo sapiens	68-76
892715-4	1977	This interpretation is based on the exchange of the 2,3-diphosphoglycerate contact beta2His leads to Asn from man to llama: the interaction between the heterotropic allosteric effector 2,3-diphosphoglycerate and protein is diminished, which results in higher oxygen affinity of the hemoglobin of llama.	2,3-Diphosphoglycerate	52-74	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	83-88
892715-4	1977	This interpretation is based on the exchange of the 2,3-diphosphoglycerate contact beta2His leads to Asn from man to llama: the interaction between the heterotropic allosteric effector 2,3-diphosphoglycerate and protein is diminished, which results in higher oxygen affinity of the hemoglobin of llama.	2,3-Diphosphoglycerate	185-207	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	83-88
14829-3	1977	The results indicatethat 2,3-gisphosphoglycerate phosphatase breaks down 2,3-bisphosphoglycerate nearly independent of pH at a rate of 480 mumol 2,3-bisphosphoglycerate x1 cells-1xh-1.2,3-Bisphosphoglycerate mutase is practically completely inhibited below pH value increases in long-term experiments with lower 2,3-bisphosphoglycerate levels.	2,3-Diphosphoglycerate	73-96	bisphosphoglycerate mutase	Homo sapiens	188-214
14829-3	1977	The results indicatethat 2,3-gisphosphoglycerate phosphatase breaks down 2,3-bisphosphoglycerate nearly independent of pH at a rate of 480 mumol 2,3-bisphosphoglycerate x1 cells-1xh-1.2,3-Bisphosphoglycerate mutase is practically completely inhibited below pH value increases in long-term experiments with lower 2,3-bisphosphoglycerate levels.	2,3-Diphosphoglycerate	145-168	bisphosphoglycerate mutase	Homo sapiens	188-214
844210-3	1977	Since the release reaction occurs simultaneously with a burst in the consumption of oxygen, the authors have studied the effect of 2,3-DPG on oxygen consumption after the addition of thrombin with or without the addition of substances which modify platelet metabolism (aspirin, theophylline, glucagon, etc.).	2,3-Diphosphoglycerate	131-138	coagulation factor II, thrombin	Homo sapiens	183-191
844210-4	1977	It was observed that 2,3-DPG diminishes oxygen consumption induced by thrombin.	2,3-Diphosphoglycerate	21-28	coagulation factor II, thrombin	Homo sapiens	70-78
954989-0	1976	Stimulative effect of 2,3-diphosphoglycerate on methemoglobin reduction by ascorbic acid.	2,3-Diphosphoglycerate	22-44	hemoglobin subunit gamma 2	Homo sapiens	48-61
618355-6	1977	The changes in the ODC"s are thought to be secondary to the hyperchylomicronemia for the following reasons: (1) the change was minimized by incubating red cells from the patients in normal donor plasma; (2) normal red cells increased their oxygen affinity when incubated in lactescent plasma; (3) the change was not explainable by a decrease in red cell 2,3-diphosphoglycerate content or in arterial blood hydrogen ion concentration.	2,3-Diphosphoglycerate	354-376	ornithine decarboxylase 1	Homo sapiens	19-22
977598-2	1976	31P relaxation studies reveal a 3-fold enhancement of the longitudinal relaxation rate of both phosphoryl groups of hemoglobin-bound 2,3-bisphosphoglycerate upon conversion of methemoglobin to fluoromethemoglobin presumably due to an order of magnitude increase in the electron spin relaxation time.	2,3-Diphosphoglycerate	133-156	hemoglobin subunit gamma 2	Homo sapiens	176-189
596059-1	1977	Pyruvate and K-ferricyanide stimulation of net ATP and 2,3-bisphosphoglycerate synthesis is very probably due to enhancement of glyceraldehyde 3-phosphate dehydrogenase activity.	2,3-Diphosphoglycerate	55-78	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	128-168
12167-1	1976	The rate of methemoglobin reduction by ascorbic acid was accelerated in the presence of ATP,2,3-diphosphoglycerate (2,3-DPG), and inositol hexaphosphate (IHP).	2,3-Diphosphoglycerate	92-114	hemoglobin subunit gamma 2	Homo sapiens	12-25
12167-1	1976	The rate of methemoglobin reduction by ascorbic acid was accelerated in the presence of ATP,2,3-diphosphoglycerate (2,3-DPG), and inositol hexaphosphate (IHP).	2,3-Diphosphoglycerate	116-123	hemoglobin subunit gamma 2	Homo sapiens	12-25
12167-4	1976	The reduction rate of methemoglobin by ascorbic acid was compared at different concentrations of organic phosphates (ATP,2,3-DPG, and IHP) at various pH values (6.3, 7.0, 7.7).	2,3-Diphosphoglycerate	121-128	hemoglobin subunit gamma 2	Homo sapiens	22-35
12167-5	1976	From the changes in the reduction rate under different concentrations of organic phosphates, the dissociation constants of ATP, 2,3-DPG, and IHP to methemoglobin could be determined and were estimated to be 3.3 X 10(-4) M, 2 X 10(-3) M, and 8 X 10(-6) M at pH 7.0, respectively.	2,3-Diphosphoglycerate	128-135	hemoglobin subunit gamma 2	Homo sapiens	148-161
12167-7	1976	The physiological role of 2,3-DPG in human red cells was discussed in relation to the reduction of methemoglobin by ascorbic acid.	2,3-Diphosphoglycerate	26-33	hemoglobin subunit gamma 2	Homo sapiens	99-112
10958-2	1976	The disappearance of PLP from the cells was accelerated by the generation of 2,3-DPG in a medium of inosine, pyruvate and phosphate.	2,3-Diphosphoglycerate	77-84	pyridoxal phosphatase	Homo sapiens	21-24
10958-4	1976	However, the dependency of the oxygen affinity on the intracellular PLP concentration showed a different pattern from the observed for 2,3-DPG.	2,3-Diphosphoglycerate	135-142	pyridoxal phosphatase	Homo sapiens	68-71
1201209-3	1975	When the cells from two of these people with homozygous Hb E were depleted of 2,3-DPG.	2,3-Diphosphoglycerate	78-85	hemoglobin subunit epsilon 1	Homo sapiens	56-60
1630-2	1976	The red cell 2,3-diphosphoglycerate (DPG) concentration before and throughout immersion period was positively correlated both with aldosterone excretion in 2 hr pooled urine (r = +0.69; 2 p less than 0.001) and with renin activity (r = + 0.54; 2p less than 0.001) despite a concomitant increase of cubital venous pH and inorganic phosphate concentration.	2,3-Diphosphoglycerate	13-35	renin	Homo sapiens	216-221
1630-2	1976	The red cell 2,3-diphosphoglycerate (DPG) concentration before and throughout immersion period was positively correlated both with aldosterone excretion in 2 hr pooled urine (r = +0.69; 2 p less than 0.001) and with renin activity (r = + 0.54; 2p less than 0.001) despite a concomitant increase of cubital venous pH and inorganic phosphate concentration.	2,3-Diphosphoglycerate	37-40	renin	Homo sapiens	216-221
5407-6	1975	ATP and 2,3-diphosphoglycerate (DPG) were well-maintained in heparinized blood when it was acidified and pHe and pHi at 4degrees were both about 7.4, which suggests that improvement of blood preservation may be attained by suitable adjustment of the pHi and pHe of the blood.	2,3-Diphosphoglycerate	32-35	glucose-6-phosphate isomerase	Homo sapiens	250-253
393-3	1975	X-ray crystallography of normal human hemoglobin has shown that the beta 2 residue is normally part of the binding site for 2,3-diphosphoglycerate.	2,3-Diphosphoglycerate	124-146	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	68-74
1222331-7	1975	There is a good correlation between 2,3-DPG and P50 (r = 0.707), none between P50 and Pao2.	2,3-Diphosphoglycerate	36-43	nuclear factor kappa B subunit 1	Homo sapiens	48-51
1222331-10	1975	The DPG-pHi correlation is very good (r = 0.691 ; pless 0.001) and the changes of the acid-base balance seem to be the main factors for controlling the DPG synthesis : it increases it in chronic alkalosis and reduces it in chronic acidosis.	2,3-Diphosphoglycerate	4-7	glucose-6-phosphate isomerase	Homo sapiens	8-11
4686431-0	1973	Influence of 2,3-diphosphoglycerate on the rate of oxidation of hemoglobin to methemoglobin.	2,3-Diphosphoglycerate	13-35	hemoglobin subunit gamma 2	Homo sapiens	78-91
1142109-4	1975	3) Purified human carbonic anhydrase B had no phosphatase activity on 2,3-DPG and it appears unlikely that the enzyme hydrolyzes other phosphate esters of the erythrocyte which could indirectly alter 2,3-DPG content.	2,3-Diphosphoglycerate	200-207	carbonic anhydrase 2	Homo sapiens	18-38
1130194-6	1975	In the diabetics 2,3-DPG was positively correlated to the P50 (7.40) and to the P50 (in vivo ph) of the ODC.	2,3-Diphosphoglycerate	17-24	activating signal cointegrator 1 complex subunit 1	Homo sapiens	58-61
1130194-6	1975	In the diabetics 2,3-DPG was positively correlated to the P50 (7.40) and to the P50 (in vivo ph) of the ODC.	2,3-Diphosphoglycerate	17-24	activating signal cointegrator 1 complex subunit 1	Homo sapiens	80-83
33054048-4	2020	The biochemical consequences of PKD result in hemolytic anemia due to red cell pyruvate and ATP deficiency while simultaneously causing increased red cell 2,3-diphosphoglycerate, which facilitates oxygen unloading.	2,3-Diphosphoglycerate	155-177	protein kinase D1	Homo sapiens	32-35
34052998-5	2021	Towards understanding the role of 2,3-BPG in the oocyte, we characterized gene expression and protein abundance of bisphosphoglycerate mutase (Bpgm), which synthesizes 2,3-BPG, and whether this is altered under low oxygen or hemoglobin addition during IVM.	2,3-Diphosphoglycerate	34-41	2,3-bisphosphoglycerate mutase	Mus musculus	115-141
34052998-5	2021	Towards understanding the role of 2,3-BPG in the oocyte, we characterized gene expression and protein abundance of bisphosphoglycerate mutase (Bpgm), which synthesizes 2,3-BPG, and whether this is altered under low oxygen or hemoglobin addition during IVM.	2,3-Diphosphoglycerate	34-41	2,3-bisphosphoglycerate mutase	Mus musculus	143-147
34052998-5	2021	Towards understanding the role of 2,3-BPG in the oocyte, we characterized gene expression and protein abundance of bisphosphoglycerate mutase (Bpgm), which synthesizes 2,3-BPG, and whether this is altered under low oxygen or hemoglobin addition during IVM.	2,3-Diphosphoglycerate	168-175	2,3-bisphosphoglycerate mutase	Mus musculus	115-141
34052998-5	2021	Towards understanding the role of 2,3-BPG in the oocyte, we characterized gene expression and protein abundance of bisphosphoglycerate mutase (Bpgm), which synthesizes 2,3-BPG, and whether this is altered under low oxygen or hemoglobin addition during IVM.	2,3-Diphosphoglycerate	168-175	2,3-bisphosphoglycerate mutase	Mus musculus	143-147
33978488-6	2021	The most plausible cause for this finding is formation of methemoglobin, which increases the oxygen affinity and thus apparently compensates for the 2,3-BPG effect.	2,3-Diphosphoglycerate	149-156	hemoglobin subunit gamma 2	Homo sapiens	58-71
33390177-11	2021	Metabolic experiments showed that the miRNA-30b-5p/MINPP1 axis is able to accelerate the conversion of glucose to lactate and 2,3-bisphosphoglycerate (2,3-BPG).	2,3-Diphosphoglycerate	126-149	multiple inositol-polyphosphate phosphatase 1	Homo sapiens	51-57
33390177-11	2021	Metabolic experiments showed that the miRNA-30b-5p/MINPP1 axis is able to accelerate the conversion of glucose to lactate and 2,3-bisphosphoglycerate (2,3-BPG).	2,3-Diphosphoglycerate	151-158	multiple inositol-polyphosphate phosphatase 1	Homo sapiens	51-57
5370013-0	1969	Erythrocyte metabolism and function: hexokinase inhibition by 2,3-diphosphogly- cerate and interaction with ATP and Mg2+.	2,3-Diphosphoglycerate	62-86	hexokinase 1	Homo sapiens	37-47
33628390-3	2021	Using mice with a genetic deficiency in a H2S natural synthesis enzyme cystathionine-gamma-lyase (CSE) and high-throughput metabolomic profiling, we found that levels of erythrocyte 2,3-bisphosphoglycerate (2,3-BPG), an erythroid-specific metabolite negatively regulating hemoglobin- (Hb-) oxygen (O2) binding affinity, were increased in CSE knockout (Cse -/-) mice under normoxia.	2,3-Diphosphoglycerate	182-205	cystathionase (cystathionine gamma-lyase)	Mus musculus	71-96
33628390-3	2021	Using mice with a genetic deficiency in a H2S natural synthesis enzyme cystathionine-gamma-lyase (CSE) and high-throughput metabolomic profiling, we found that levels of erythrocyte 2,3-bisphosphoglycerate (2,3-BPG), an erythroid-specific metabolite negatively regulating hemoglobin- (Hb-) oxygen (O2) binding affinity, were increased in CSE knockout (Cse -/-) mice under normoxia.	2,3-Diphosphoglycerate	182-205	cystathionase (cystathionine gamma-lyase)	Mus musculus	98-101
33628390-3	2021	Using mice with a genetic deficiency in a H2S natural synthesis enzyme cystathionine-gamma-lyase (CSE) and high-throughput metabolomic profiling, we found that levels of erythrocyte 2,3-bisphosphoglycerate (2,3-BPG), an erythroid-specific metabolite negatively regulating hemoglobin- (Hb-) oxygen (O2) binding affinity, were increased in CSE knockout (Cse -/-) mice under normoxia.	2,3-Diphosphoglycerate	182-205	cystathionase (cystathionine gamma-lyase)	Mus musculus	338-341
33628390-3	2021	Using mice with a genetic deficiency in a H2S natural synthesis enzyme cystathionine-gamma-lyase (CSE) and high-throughput metabolomic profiling, we found that levels of erythrocyte 2,3-bisphosphoglycerate (2,3-BPG), an erythroid-specific metabolite negatively regulating hemoglobin- (Hb-) oxygen (O2) binding affinity, were increased in CSE knockout (Cse -/-) mice under normoxia.	2,3-Diphosphoglycerate	182-205	cystathionase (cystathionine gamma-lyase)	Mus musculus	352-355
33037242-7	2020	P50 at rest differs significantly between women and men, with women showing lower Hb-O2 affinity that is determined by higher 2,3-BPG and BPGM levels.	2,3-Diphosphoglycerate	126-133	nuclear factor kappa B subunit 1	Homo sapiens	0-3
32434995-4	2020	Unbiased high-throughput metabolic profiling coupled with in vitro and in vivo flux analyses with isotopically labeled tracers led us to discover that maternal eENT1-dependent adenosine uptake is critical in activating AMPK by controlling the AMP/ATP ratio and its downstream target, bisphosphoglycerate mutase (BPGM); in turn, BPGM mediates 2,3-BPG production, which enhances O2 delivery to maintain placental oxygenation.	2,3-Diphosphoglycerate	342-349	protein kinase AMP-activated catalytic subunit alpha 1	Homo sapiens	219-223
32434995-4	2020	Unbiased high-throughput metabolic profiling coupled with in vitro and in vivo flux analyses with isotopically labeled tracers led us to discover that maternal eENT1-dependent adenosine uptake is critical in activating AMPK by controlling the AMP/ATP ratio and its downstream target, bisphosphoglycerate mutase (BPGM); in turn, BPGM mediates 2,3-BPG production, which enhances O2 delivery to maintain placental oxygenation.	2,3-Diphosphoglycerate	342-349	bisphosphoglycerate mutase	Homo sapiens	284-310
32434995-4	2020	Unbiased high-throughput metabolic profiling coupled with in vitro and in vivo flux analyses with isotopically labeled tracers led us to discover that maternal eENT1-dependent adenosine uptake is critical in activating AMPK by controlling the AMP/ATP ratio and its downstream target, bisphosphoglycerate mutase (BPGM); in turn, BPGM mediates 2,3-BPG production, which enhances O2 delivery to maintain placental oxygenation.	2,3-Diphosphoglycerate	342-349	bisphosphoglycerate mutase	Homo sapiens	312-316
32434995-4	2020	Unbiased high-throughput metabolic profiling coupled with in vitro and in vivo flux analyses with isotopically labeled tracers led us to discover that maternal eENT1-dependent adenosine uptake is critical in activating AMPK by controlling the AMP/ATP ratio and its downstream target, bisphosphoglycerate mutase (BPGM); in turn, BPGM mediates 2,3-BPG production, which enhances O2 delivery to maintain placental oxygenation.	2,3-Diphosphoglycerate	342-349	bisphosphoglycerate mutase	Homo sapiens	328-332
32141895-11	2020	More recent studies demonstrated the beneficial role of erythrocyte ADORA2B-mediated 2,3-BPG production in CKD.	2,3-Diphosphoglycerate	85-92	adenosine A2b receptor	Homo sapiens	68-75
31278195-5	2019	RESULTS: Untargeted metabolomics showed increased production of 2,3-biphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite promoting O2 delivery, in mice given Ang II to induce CKD.	2,3-Diphosphoglycerate	88-95	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	170-176
30713045-0	2019	The expression of CD47 and its association with 2,3-DPG levels in stored leuco-reduced blood units.	2,3-Diphosphoglycerate	48-55	CD47 molecule	Homo sapiens	18-22
30713045-5	2019	The aim of this study was to validate the impact of storage time and leuco-depletion on CD47 expression on the RBCs, which could be a prospective marker for detection of RBCs viability and to clarify if the changes in CD47 expression and 2,3-DPG levels are correlated during storage of Packed RBCs.	2,3-Diphosphoglycerate	238-245	CD47 molecule	Homo sapiens	88-92
31278195-6	2019	Genetic studies in mice revealed that erythrocyte ADORA2B signaling leads to AMPK-stimulated activation of BPG mutase, promoting 2,3-BPG production and O2 delivery to counteract kidney hypoxia, tissue damage, and disease progression in Ang II-induced CKD.	2,3-Diphosphoglycerate	129-136	adenosine A2b receptor	Mus musculus	50-57
31278195-10	2019	CONCLUSIONS: Mouse and human evidence reveals that ADORA2B-AMPK signaling cascade-induced 2,3-BPG production promotes O2 delivery by erythrocytes to counteract kidney hypoxia and progression of CKD.	2,3-Diphosphoglycerate	90-97	adenosine A2b receptor	Homo sapiens	51-58
30097462-5	2018	AMPK functions downstream of adenosine receptor ADORA2B signaling and contributes to sickling by regulating the production of erythrocyte 2,3-bisphosphoglycerate (2,3-BPG), a negative allosteric regulator of hemoglobin-O2 binding affinity.	2,3-Diphosphoglycerate	138-161	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	0-4
28805803-5	2017	We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM).	2,3-Diphosphoglycerate	60-83	phosphoglycerate mutase 1	Homo sapiens	25-30
29447940-0	2018	The relationship between plasma vascular endothelial growth factor and erythrocyte 2,3-bisphosphoglycerate: The putative role of chronic hypoxia.	2,3-Diphosphoglycerate	83-106	vascular endothelial growth factor A	Homo sapiens	32-66
28805803-5	2017	We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM).	2,3-Diphosphoglycerate	60-83	bisphosphoglycerate mutase	Homo sapiens	179-205
28805803-5	2017	We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM).	2,3-Diphosphoglycerate	60-83	bisphosphoglycerate mutase	Homo sapiens	207-211
28805803-5	2017	We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM).	2,3-Diphosphoglycerate	85-92	phosphoglycerate mutase 1	Homo sapiens	25-30
28805803-5	2017	We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM).	2,3-Diphosphoglycerate	85-92	bisphosphoglycerate mutase	Homo sapiens	179-205
28805803-5	2017	We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM).	2,3-Diphosphoglycerate	85-92	bisphosphoglycerate mutase	Homo sapiens	207-211
26249166-4	2015	Erythrocytes from Ampd3(-/-) mice exhibited higher half-saturation pressure of oxygen (p50) and about 3-fold higher levels of ATP and ADP, while they maintained normal 2,3-bisphosphoglycerate (2,3-BPG), methemoglobin levels and intracellular pH.	2,3-Diphosphoglycerate	193-200	adenosine monophosphate deaminase 3	Mus musculus	18-23
27417539-4	2016	Mechanistically, we show that intracellular S1P promotes deoxygenated Hb anchoring to the membrane, enhances the release of membrane-bound glycolytic enzymes to the cytosol, induces glycolysis and thus the production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific glycolytic intermediate, which facilitates O2 release.	2,3-Diphosphoglycerate	220-243	sphingosine-1-phosphate receptor 1	Mus musculus	44-47
27417539-4	2016	Mechanistically, we show that intracellular S1P promotes deoxygenated Hb anchoring to the membrane, enhances the release of membrane-bound glycolytic enzymes to the cytosol, induces glycolysis and thus the production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific glycolytic intermediate, which facilitates O2 release.	2,3-Diphosphoglycerate	245-252	sphingosine-1-phosphate receptor 1	Mus musculus	44-47
24115288-5	2014	These include hemoglobin variants with increased affinity for oxygen (HBB, HBA mutations), decreased production of 2,3-bisphosphoglycerate due to BPGM mutations, or mutations in the genes involved in the hypoxia sensing pathway (VHL, EPAS1, and EGLN1).	2,3-Diphosphoglycerate	115-138	bisphosphoglycerate mutase	Homo sapiens	146-150
23926230-7	2013	BPG, Pi and HCO3(-) also reversibly bind to HbA with similar energies as glucose isomers (~3-5 kcal/mol) and share common binding sites with glucose isomers.	2,3-Diphosphoglycerate	0-3	sodium voltage-gated channel alpha subunit 2	Homo sapiens	44-47
23926230-9	2013	The clinical difference between average blood glucose and predicted HbA1c, and the presence of unstable HbA-glucose complexes may be more fully explained by initial noncovalent binding interactions and different concentrations of BPG, Pi and HCO3(-) in serum vs. erythrocytes.	2,3-Diphosphoglycerate	230-233	sodium voltage-gated channel alpha subunit 2	Homo sapiens	68-71
22683445-5	2012	I hypothesize that NO may suppress BPG production by (1) inhibiting glyceraldehyde-3-phosphate dehydrogenase (G3PDH), the most critical glycolytic enzyme for the bioavailability of 1,3-bisphosphoglycerate; and to a lesser extent by (2) associated pH changes in the deoxy-Hb-catalyzed depletion of nitrite, a metabolic reservoir of NO.	2,3-Diphosphoglycerate	35-38	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	68-108
23653202-3	2013	Here we report a novel mechanism in which Y26 phosphorylation enhances PGAM1 activation through release of inhibitory E19 that blocks the active site, stabilising cofactor 2,3-bisphosphoglycerate binding and H11 phosphorylation.	2,3-Diphosphoglycerate	172-195	phosphoglycerate mutase 1	Homo sapiens	71-76
22683445-5	2012	I hypothesize that NO may suppress BPG production by (1) inhibiting glyceraldehyde-3-phosphate dehydrogenase (G3PDH), the most critical glycolytic enzyme for the bioavailability of 1,3-bisphosphoglycerate; and to a lesser extent by (2) associated pH changes in the deoxy-Hb-catalyzed depletion of nitrite, a metabolic reservoir of NO.	2,3-Diphosphoglycerate	35-38	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	110-115
21324604-6	2011	The mammalian enzyme requires 2,3-bisphosphoglycerate as a cofactor (dependent PGM or dPGM), while the other type of PGM does not (independent PGM or iPGM).	2,3-Diphosphoglycerate	30-53	Phosphoglucose mutase 1	Drosophila melanogaster	79-82
21324604-6	2011	The mammalian enzyme requires 2,3-bisphosphoglycerate as a cofactor (dependent PGM or dPGM), while the other type of PGM does not (independent PGM or iPGM).	2,3-Diphosphoglycerate	30-53	Phosphoglucose mutase 1	Drosophila melanogaster	86-90
21324604-6	2011	The mammalian enzyme requires 2,3-bisphosphoglycerate as a cofactor (dependent PGM or dPGM), while the other type of PGM does not (independent PGM or iPGM).	2,3-Diphosphoglycerate	30-53	Phosphoglucose mutase 1	Drosophila melanogaster	87-90
21324604-6	2011	The mammalian enzyme requires 2,3-bisphosphoglycerate as a cofactor (dependent PGM or dPGM), while the other type of PGM does not (independent PGM or iPGM).	2,3-Diphosphoglycerate	30-53	Phosphoglucose mutase 1	Drosophila melanogaster	87-90
21187861-2	2010	Cofactor-dependent PGM (dPGM) requires 2,3-bisphosphoglycerate for activity; cofactor-independent PGM (iPGM) does not.	2,3-Diphosphoglycerate	39-62	Phosphoglucose mutase 1	Drosophila melanogaster	19-22
21045285-1	2010	Erythrocyte-specific bisphosphoglycerate mutase is a trifunctional enzyme which modulates the levels of 2,3-bisphosphoglycerate (2,3-BPG) in red blood cells by virtue of its synthase and phosphatase activities.	2,3-Diphosphoglycerate	104-127	bisphosphoglycerate mutase	Homo sapiens	21-47
21045285-3	2010	2,3-BPG levels in stored blood decline rapidly owing to the phosphatase activity of bisphosphoglycerate mutase, which is enhanced by a fall in pH.	2,3-Diphosphoglycerate	0-7	bisphosphoglycerate mutase	Homo sapiens	84-110
21045285-8	2010	The characterization of bisphosphoglycerate mutase-citrate interactions will provide a framework for the design of specific inhibitors of the phosphatase activity of this enzyme, which may limit the decline of 2,3-BPG in stored blood.	2,3-Diphosphoglycerate	210-217	bisphosphoglycerate mutase	Homo sapiens	24-50
21187861-2	2010	Cofactor-dependent PGM (dPGM) requires 2,3-bisphosphoglycerate for activity; cofactor-independent PGM (iPGM) does not.	2,3-Diphosphoglycerate	39-62	Phosphoglucose mutase 1	Drosophila melanogaster	24-28
21187861-2	2010	Cofactor-dependent PGM (dPGM) requires 2,3-bisphosphoglycerate for activity; cofactor-independent PGM (iPGM) does not.	2,3-Diphosphoglycerate	39-62	Phosphoglucose mutase 1	Drosophila melanogaster	25-28
20530968-8	2010	The L. lactis PGM was dependent on 2,3-bisphosphoglyceric acid for activity, which showed that the enzyme is of the dPGM type in accordance with its predicted homology to dPGM enzymes from other organisms.	2,3-Diphosphoglycerate	35-62	Phosphoglucose mutase 1	Drosophila melanogaster	14-17
20530968-8	2010	The L. lactis PGM was dependent on 2,3-bisphosphoglyceric acid for activity, which showed that the enzyme is of the dPGM type in accordance with its predicted homology to dPGM enzymes from other organisms.	2,3-Diphosphoglycerate	35-62	Phosphoglucose mutase 1	Drosophila melanogaster	116-120
20530968-8	2010	The L. lactis PGM was dependent on 2,3-bisphosphoglyceric acid for activity, which showed that the enzyme is of the dPGM type in accordance with its predicted homology to dPGM enzymes from other organisms.	2,3-Diphosphoglycerate	35-62	Phosphoglucose mutase 1	Drosophila melanogaster	171-175