PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
17176070-0	2006	Functional role of the conserved active site proline of triosephosphate isomerase.	Proline	45-52	triosephosphate isomerase 1	Homo sapiens	56-81
16919384-1	2007	2-Phosphoglycolate (PGA), a strong competitive inhibitor of the dimeric enzyme triosephosphate isomerase (TIM), brings about a large decrease in the unfolding rate constant of the protein.	phosphoglycolate	0-18	triosephosphate isomerase 1	Homo sapiens	79-104
16919384-1	2007	2-Phosphoglycolate (PGA), a strong competitive inhibitor of the dimeric enzyme triosephosphate isomerase (TIM), brings about a large decrease in the unfolding rate constant of the protein.	phosphoglycolate	0-18	triosephosphate isomerase 1	Homo sapiens	106-109
16919384-1	2007	2-Phosphoglycolate (PGA), a strong competitive inhibitor of the dimeric enzyme triosephosphate isomerase (TIM), brings about a large decrease in the unfolding rate constant of the protein.	Folic Acid	20-23	triosephosphate isomerase 1	Homo sapiens	79-104
16919384-1	2007	2-Phosphoglycolate (PGA), a strong competitive inhibitor of the dimeric enzyme triosephosphate isomerase (TIM), brings about a large decrease in the unfolding rate constant of the protein.	Folic Acid	20-23	triosephosphate isomerase 1	Homo sapiens	106-109
16919384-3	2007	However, if the thermodynamics for binding of PGA to native TIM is taken into account, it becomes clear that a dimeric TS is the right assumption.	Folic Acid	46-49	triosephosphate isomerase 1	Homo sapiens	60-63
17098463-1	2007	Thymidine phosphorylase (TP) and uridine phosphorylase (UP) are often upregulated in solid tumors and catalyze the phosphorolysis of natural (deoxy)nucleosides and a wide variety of fluorinated pyrimidine nucleosides.	(deoxy)nucleosides	141-159	triosephosphate isomerase 1	Homo sapiens	25-27
17098463-1	2007	Thymidine phosphorylase (TP) and uridine phosphorylase (UP) are often upregulated in solid tumors and catalyze the phosphorolysis of natural (deoxy)nucleosides and a wide variety of fluorinated pyrimidine nucleosides.	fluorinated pyrimidine nucleosides	182-216	triosephosphate isomerase 1	Homo sapiens	25-27
17098463-2	2007	Because the relative contribution of each of the two enzymes to these reactions is still largely unknown, we investigated the substrate specificity of TP and UP in colon cancer cells for the (fluoro)pyrimidine nucleosides thymidine (TdR), uridine (Urd), 5"-deoxy-5-fluorouridine (5"DFUR), and 5FU.	(fluoro)pyrimidine nucleosides thymidine	191-231	triosephosphate isomerase 1	Homo sapiens	151-153
17098463-2	2007	Because the relative contribution of each of the two enzymes to these reactions is still largely unknown, we investigated the substrate specificity of TP and UP in colon cancer cells for the (fluoro)pyrimidine nucleosides thymidine (TdR), uridine (Urd), 5"-deoxy-5-fluorouridine (5"DFUR), and 5FU.	Thymidine	233-236	triosephosphate isomerase 1	Homo sapiens	151-153
17098463-16	2007	Uracil accumulation was heavily reduced in the presence of TPI for Colo320TP1 and HaCaT cells, whereas 5FU-induced dUrd production by these cell lines increased (p<0.01).	Uracil	0-6	triosephosphate isomerase 1	Homo sapiens	59-62
17176070-1	2006	The importance of the fully conserved active site proline, Pro168, for the reaction mechanism of triosephosphate isomerase (TIM) has been investigated by studying the enzymatic and crystallographic properties of the P168A variant of trypanosomal TIM.	Proline	50-57	triosephosphate isomerase 1	Homo sapiens	97-122
17176070-1	2006	The importance of the fully conserved active site proline, Pro168, for the reaction mechanism of triosephosphate isomerase (TIM) has been investigated by studying the enzymatic and crystallographic properties of the P168A variant of trypanosomal TIM.	Proline	50-57	triosephosphate isomerase 1	Homo sapiens	124-127
17176070-5	2006	The crystal structures of unliganded and liganded (2PG) P168A show that the phosphate moiety of 2PG is bound similarly as in wild-type TIM, whereas the interactions of the carboxylic acid moiety with the side chain of the catalytic Glu167 differ.	Phosphates	76-85	triosephosphate isomerase 1	Homo sapiens	135-138
17176070-6	2006	The unique properties of the proline side chain at position 168 are required to transmit ligand binding to the conformational change of Glu167: the side chain of Glu167 flips from the inactive swung-out to the active swung-in conformation on ligand binding in wild-type TIM, whereas in the mutant this conformational change does not occur.	Proline	29-36	triosephosphate isomerase 1	Homo sapiens	270-273
16457948-9	2006	A TP inhibitor, TPI, abrogated the cytotoxic activity of 5"-DFUR, and attenuated the combined cytotoxicity of AZT and 5"-DFUR.	doxifluridine	57-64	triosephosphate isomerase 1	Homo sapiens	16-19
16457948-9	2006	A TP inhibitor, TPI, abrogated the cytotoxic activity of 5"-DFUR, and attenuated the combined cytotoxicity of AZT and 5"-DFUR.	Zidovudine	110-113	triosephosphate isomerase 1	Homo sapiens	16-19
16457948-9	2006	A TP inhibitor, TPI, abrogated the cytotoxic activity of 5"-DFUR, and attenuated the combined cytotoxicity of AZT and 5"-DFUR.	doxifluridine	118-125	triosephosphate isomerase 1	Homo sapiens	16-19
16978361-7	2006	Importantly, the apparent K(m) value of M. tuberculosis rTPI for the substrate glyceraldehyde-3-phosphate is 84 microM which is sevenfold higher than the value reported for human TPI.	Glyceraldehyde 3-Phosphate	79-105	triosephosphate isomerase 1	Homo sapiens	57-60
17183658-10	2006	Finally, we discovered that yeast cells expressing a TPI variant exhibiting reduced catalytic activity are more resistant against oxidative stress caused by the thiol-oxidizing reagent diamide.	Sulfhydryl Compounds	161-166	triosephosphate isomerase 1	Homo sapiens	53-56
17183658-10	2006	Finally, we discovered that yeast cells expressing a TPI variant exhibiting reduced catalytic activity are more resistant against oxidative stress caused by the thiol-oxidizing reagent diamide.	Diamide	185-192	triosephosphate isomerase 1	Homo sapiens	53-56
17424909-3	2006	The physiological function of TPI is to adjust the rapid equilibrium between dihydroxyacetone phosphate and glyceraldehyde-3-phosphate produced by aldolase in glycolysis, which is interconnected to the pentose phosphate pathway and to lipid metabolism via triosephosphates.	Dihydroxyacetone Phosphate	77-103	triosephosphate isomerase 1	Homo sapiens	30-33
17424909-3	2006	The physiological function of TPI is to adjust the rapid equilibrium between dihydroxyacetone phosphate and glyceraldehyde-3-phosphate produced by aldolase in glycolysis, which is interconnected to the pentose phosphate pathway and to lipid metabolism via triosephosphates.	Glyceraldehyde 3-Phosphate	108-134	triosephosphate isomerase 1	Homo sapiens	30-33
17424909-3	2006	The physiological function of TPI is to adjust the rapid equilibrium between dihydroxyacetone phosphate and glyceraldehyde-3-phosphate produced by aldolase in glycolysis, which is interconnected to the pentose phosphate pathway and to lipid metabolism via triosephosphates.	Pentosephosphates	202-219	triosephosphate isomerase 1	Homo sapiens	30-33
17424909-3	2006	The physiological function of TPI is to adjust the rapid equilibrium between dihydroxyacetone phosphate and glyceraldehyde-3-phosphate produced by aldolase in glycolysis, which is interconnected to the pentose phosphate pathway and to lipid metabolism via triosephosphates.	triosephosphates	256-272	triosephosphate isomerase 1	Homo sapiens	30-33
16953564-1	2006	Solution NMR spin relaxation experiments and classical MD simulations are used to study the dynamics of triosephosphate isomerase (TIM) in complex with glycerol 3-phosphate (G3P).	alpha-glycerophosphoric acid	174-177	triosephosphate isomerase 1	Homo sapiens	104-129
16953564-1	2006	Solution NMR spin relaxation experiments and classical MD simulations are used to study the dynamics of triosephosphate isomerase (TIM) in complex with glycerol 3-phosphate (G3P).	alpha-glycerophosphoric acid	152-172	triosephosphate isomerase 1	Homo sapiens	104-129
16953564-1	2006	Solution NMR spin relaxation experiments and classical MD simulations are used to study the dynamics of triosephosphate isomerase (TIM) in complex with glycerol 3-phosphate (G3P).	alpha-glycerophosphoric acid	152-172	triosephosphate isomerase 1	Homo sapiens	131-134
16953564-1	2006	Solution NMR spin relaxation experiments and classical MD simulations are used to study the dynamics of triosephosphate isomerase (TIM) in complex with glycerol 3-phosphate (G3P).	alpha-glycerophosphoric acid	174-177	triosephosphate isomerase 1	Homo sapiens	131-134
16953564-2	2006	Three regions in TIM exhibit conformational transitions on the micros-ms time scale as detected by chemical exchange broadening effects in NMR spectroscopy: residue Lys 84 on helix C, located at the dimeric interface; active site loop 6; and helix G. The results indicate that the conformational exchange process affecting the residues of loop 6 is the correlated opening and closing of the loop.	Lysine	165-168	triosephosphate isomerase 1	Homo sapiens	17-20
16741995-1	2006	QM and QM/MM energy calculations have been carried out on an atomic resolution structure of liganded triosephosphate isomerase (TIM) that has an active site proline (Pro168) in a planar conformation.	Proline	157-164	triosephosphate isomerase 1	Homo sapiens	101-126
16741995-1	2006	QM and QM/MM energy calculations have been carried out on an atomic resolution structure of liganded triosephosphate isomerase (TIM) that has an active site proline (Pro168) in a planar conformation.	Proline	157-164	triosephosphate isomerase 1	Homo sapiens	128-131
16741995-7	2006	Comparison of the proline conformation in different TIM X-ray structures, indicates that in the closed conformation of TIM the proline is planar or nearly planar, while in the open conformation it is down puckered.	Proline	18-25	triosephosphate isomerase 1	Homo sapiens	52-55
16741995-7	2006	Comparison of the proline conformation in different TIM X-ray structures, indicates that in the closed conformation of TIM the proline is planar or nearly planar, while in the open conformation it is down puckered.	Proline	18-25	triosephosphate isomerase 1	Homo sapiens	119-122
16741995-7	2006	Comparison of the proline conformation in different TIM X-ray structures, indicates that in the closed conformation of TIM the proline is planar or nearly planar, while in the open conformation it is down puckered.	Proline	127-134	triosephosphate isomerase 1	Homo sapiens	52-55
16741995-7	2006	Comparison of the proline conformation in different TIM X-ray structures, indicates that in the closed conformation of TIM the proline is planar or nearly planar, while in the open conformation it is down puckered.	Proline	127-134	triosephosphate isomerase 1	Homo sapiens	119-122
16198931-5	2005	METHODS: TPI was calculated from BUN and urea clearance.	Urea	41-45	triosephosphate isomerase 1	Homo sapiens	9-12
16330546-0	2006	Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.	Carbon	164-170	triosephosphate isomerase 1	Homo sapiens	129-132
16330546-0	2006	Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.	Carbon	171-177	triosephosphate isomerase 1	Homo sapiens	129-132
16330546-6	2006	Surprisingly, the residues forming this cation-binding site and most of their interaction partners are shared with three other TIM barrel enzymes that catalyze diverse carbon-carbon bond cleavage reactions believed to proceed through enolate intermediates (4-hydroxy-2-ketovalerate aldolase, 2-isopropylmalate synthase, and transcarboxylase 5S).	Carbon	168-174	triosephosphate isomerase 1	Homo sapiens	127-130
16330546-6	2006	Surprisingly, the residues forming this cation-binding site and most of their interaction partners are shared with three other TIM barrel enzymes that catalyze diverse carbon-carbon bond cleavage reactions believed to proceed through enolate intermediates (4-hydroxy-2-ketovalerate aldolase, 2-isopropylmalate synthase, and transcarboxylase 5S).	Carbon	175-181	triosephosphate isomerase 1	Homo sapiens	127-130
16330546-6	2006	Surprisingly, the residues forming this cation-binding site and most of their interaction partners are shared with three other TIM barrel enzymes that catalyze diverse carbon-carbon bond cleavage reactions believed to proceed through enolate intermediates (4-hydroxy-2-ketovalerate aldolase, 2-isopropylmalate synthase, and transcarboxylase 5S).	enolate	234-241	triosephosphate isomerase 1	Homo sapiens	127-130
16330546-7	2006	We propose the name "DRE-TIM metallolyases" for this newly identified enzyme family likely to employ a common catalytic reaction mechanism involving an invariant Asp-Arg-Glu (DRE) triplet.	Asp-Arg	162-169	triosephosphate isomerase 1	Homo sapiens	25-28
16330546-7	2006	We propose the name "DRE-TIM metallolyases" for this newly identified enzyme family likely to employ a common catalytic reaction mechanism involving an invariant Asp-Arg-Glu (DRE) triplet.	Glutamic Acid	170-173	triosephosphate isomerase 1	Homo sapiens	25-28
16833297-1	2005	Radical cations of trans-stilbene and substituted trans-stilbenes (stilbenes and the radical cations denote Sand S(*+), respectively) were generated from the resonant two-photon ionization (TPI) in acetonitrile with irradiation of one-laser (266- or 355-nm laser) and with simultaneous irradiation of two-color two-lasers (266- and 532-nm or 355- and 532-nm lasers) with the pulse width of 5 ns each.	Stilbenes	19-33	triosephosphate isomerase 1	Homo sapiens	190-193
16833297-1	2005	Radical cations of trans-stilbene and substituted trans-stilbenes (stilbenes and the radical cations denote Sand S(*+), respectively) were generated from the resonant two-photon ionization (TPI) in acetonitrile with irradiation of one-laser (266- or 355-nm laser) and with simultaneous irradiation of two-color two-lasers (266- and 532-nm or 355- and 532-nm lasers) with the pulse width of 5 ns each.	trans-stilbenes	50-65	triosephosphate isomerase 1	Homo sapiens	190-193
16833297-1	2005	Radical cations of trans-stilbene and substituted trans-stilbenes (stilbenes and the radical cations denote Sand S(*+), respectively) were generated from the resonant two-photon ionization (TPI) in acetonitrile with irradiation of one-laser (266- or 355-nm laser) and with simultaneous irradiation of two-color two-lasers (266- and 532-nm or 355- and 532-nm lasers) with the pulse width of 5 ns each.	Stilbenes	56-65	triosephosphate isomerase 1	Homo sapiens	190-193
16833297-1	2005	Radical cations of trans-stilbene and substituted trans-stilbenes (stilbenes and the radical cations denote Sand S(*+), respectively) were generated from the resonant two-photon ionization (TPI) in acetonitrile with irradiation of one-laser (266- or 355-nm laser) and with simultaneous irradiation of two-color two-lasers (266- and 532-nm or 355- and 532-nm lasers) with the pulse width of 5 ns each.	acetonitrile	198-210	triosephosphate isomerase 1	Homo sapiens	190-193
16010427-3	2005	We attempted to augment the antitumor activity of FTD by combining it with a potent and reversible inhibitor of TP, 5-chloro-6-(2-imino-propyrrolidin-1-yl) methyl-2, 4 (1H, 3H)-pyrimidinedione hydrochloride (TPI) in human tumor xenografts with a low sensitivity to 5-fluorouracil.	5-chloro-6-(2-imino-propyrrolidin-1-yl) methyl-2,4 (1H, 3H)-pyrimidinedione hydrochloride	116-206	triosephosphate isomerase 1	Homo sapiens	208-211
15707966-2	2005	Structural and energetical analysis of the complexes showed that large benzothiazoles could form more stable complexes with trypanosomal triosephosphate isomerase than with human triosephosphate isomerase.	Benzothiazoles	71-85	triosephosphate isomerase 1	Homo sapiens	137-162
15941051-1	2005	A highly sensitive analytical method was developed using GC/MS with temperature-programmable inlet on-column injection (TPI on-column GC/MS) for determining methyl dimethyldithiocarbamate (DMDC-methyl) and dimethyl ethylenebisdithiocarbamate (EBDC-dimethyl), which are methyl derivatives of alkali decomposed polycarbamate.	Dimethyldithiocarbamate	164-187	triosephosphate isomerase 1	Homo sapiens	120-123
15941051-1	2005	A highly sensitive analytical method was developed using GC/MS with temperature-programmable inlet on-column injection (TPI on-column GC/MS) for determining methyl dimethyldithiocarbamate (DMDC-methyl) and dimethyl ethylenebisdithiocarbamate (EBDC-dimethyl), which are methyl derivatives of alkali decomposed polycarbamate.	dichlorodimethylsilane	189-193	triosephosphate isomerase 1	Homo sapiens	120-123
15941051-1	2005	A highly sensitive analytical method was developed using GC/MS with temperature-programmable inlet on-column injection (TPI on-column GC/MS) for determining methyl dimethyldithiocarbamate (DMDC-methyl) and dimethyl ethylenebisdithiocarbamate (EBDC-dimethyl), which are methyl derivatives of alkali decomposed polycarbamate.	dimethyl ethylenebisdithiocarbamate	206-241	triosephosphate isomerase 1	Homo sapiens	120-123
15941051-1	2005	A highly sensitive analytical method was developed using GC/MS with temperature-programmable inlet on-column injection (TPI on-column GC/MS) for determining methyl dimethyldithiocarbamate (DMDC-methyl) and dimethyl ethylenebisdithiocarbamate (EBDC-dimethyl), which are methyl derivatives of alkali decomposed polycarbamate.	ebdc-dimethyl	243-256	triosephosphate isomerase 1	Homo sapiens	120-123
15941051-1	2005	A highly sensitive analytical method was developed using GC/MS with temperature-programmable inlet on-column injection (TPI on-column GC/MS) for determining methyl dimethyldithiocarbamate (DMDC-methyl) and dimethyl ethylenebisdithiocarbamate (EBDC-dimethyl), which are methyl derivatives of alkali decomposed polycarbamate.	Vitene	309-322	triosephosphate isomerase 1	Homo sapiens	120-123
15707966-2	2005	Structural and energetical analysis of the complexes showed that large benzothiazoles could form more stable complexes with trypanosomal triosephosphate isomerase than with human triosephosphate isomerase.	Benzothiazoles	71-85	triosephosphate isomerase 1	Homo sapiens	179-204
15685366-5	2005	Results revealed that TPA treatment in CNE2 cells could upregulate the expression of "triosephosphate isomerase" and "14-3-3 protein sigma" and downregulate the expression of "reticulocalbin 1 precursor", "nucleophosmin", "mitochondrial matrix protein p1 precursor", and "stathmin".	Tetradecanoylphorbol Acetate	22-25	triosephosphate isomerase 1	Homo sapiens	85-124
15149664-1	2004	To explore the possible binding sites at the interface of tripanosomal triosephosphate isomerase, fully flexible benzothiazoles were docked onto the dimer interface.	Benzothiazoles	113-127	triosephosphate isomerase 1	Homo sapiens	71-96
15321726-8	2004	The portion of the interface of TcTIM that binds the benzothiazole derivative and its equivalent region in human TIM differs in amino acid composition and hydrophobic packing.	benzothiazole	53-66	triosephosphate isomerase 1	Homo sapiens	34-37
15186830-6	2004	Compound 2 (TPI) has been selected for clinical evaluation based on its strong TP inhibition and excellent modulation of 2"-deoxy-5-(trifluoromethyl)uridine (F(3)dThd) pharmacokinetics.	Trifluridine	121-156	triosephosphate isomerase 1	Homo sapiens	12-15
15186830-6	2004	Compound 2 (TPI) has been selected for clinical evaluation based on its strong TP inhibition and excellent modulation of 2"-deoxy-5-(trifluoromethyl)uridine (F(3)dThd) pharmacokinetics.	Thymidine	162-166	triosephosphate isomerase 1	Homo sapiens	12-15
15186830-7	2004	As a result, TAS-102 (a combination of F(3)dThd and TPI) is currently in phase 1 clinical studies.	trifluridine tipiracil drug combination	13-20	triosephosphate isomerase 1	Homo sapiens	52-55
15499188-1	2004	TAS-102, a new oral drug, is composed of an antitumor drug, alpha,alpha,alpha-trifluorothymidine (FTD), and its metabolic inhibitor, 5-chloro-6-(2-iminopyrrolidine-1-yl)methyl-2,4(1H,3H)-pyrimidinedione hydrochloride (TPI).	trifluridine tipiracil drug combination	0-7	triosephosphate isomerase 1	Homo sapiens	218-221
15499188-1	2004	TAS-102, a new oral drug, is composed of an antitumor drug, alpha,alpha,alpha-trifluorothymidine (FTD), and its metabolic inhibitor, 5-chloro-6-(2-iminopyrrolidine-1-yl)methyl-2,4(1H,3H)-pyrimidinedione hydrochloride (TPI).	5-chloro-6-(2-iminopyrrolidine-1-yl)methyl-2,4(1h,3h)-pyrimidinedione hydrochloride	133-216	triosephosphate isomerase 1	Homo sapiens	218-221
14762718-1	2004	The glycolytic enzyme triosephosphate isomerase (TPI) catalyses the reversible conversion of dihydroxyacetone phosphate into glyceraldehyde-3-phosphate.	Dihydroxyacetone Phosphate	93-119	triosephosphate isomerase 1	Homo sapiens	22-47
14762718-1	2004	The glycolytic enzyme triosephosphate isomerase (TPI) catalyses the reversible conversion of dihydroxyacetone phosphate into glyceraldehyde-3-phosphate.	Dihydroxyacetone Phosphate	93-119	triosephosphate isomerase 1	Homo sapiens	49-52
14762718-3	2004	The temporal pattern of hypoxic TPI induction is very similar to that of genes triggered by the hypoxia-inducible transcription factor (HIF) and is mimicked characteristically by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor nuclear translocator (ARNT, here HIF-1beta) and in cells lacking HIF-1alpha protein.	Deferoxamine	193-205	triosephosphate isomerase 1	Homo sapiens	32-35
14762718-1	2004	The glycolytic enzyme triosephosphate isomerase (TPI) catalyses the reversible conversion of dihydroxyacetone phosphate into glyceraldehyde-3-phosphate.	Glyceraldehyde 3-Phosphate	125-151	triosephosphate isomerase 1	Homo sapiens	22-47
14762718-1	2004	The glycolytic enzyme triosephosphate isomerase (TPI) catalyses the reversible conversion of dihydroxyacetone phosphate into glyceraldehyde-3-phosphate.	Glyceraldehyde 3-Phosphate	125-151	triosephosphate isomerase 1	Homo sapiens	49-52
14762718-4	2004	We conclude from these findings that the expression of TPI is regulated via the HIF pathway and thus belongs to the family of classic oxygen-regulated genes.	Oxygen	134-140	triosephosphate isomerase 1	Homo sapiens	55-58
14762718-3	2004	The temporal pattern of hypoxic TPI induction is very similar to that of genes triggered by the hypoxia-inducible transcription factor (HIF) and is mimicked characteristically by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor nuclear translocator (ARNT, here HIF-1beta) and in cells lacking HIF-1alpha protein.	Cobalt	179-185	triosephosphate isomerase 1	Homo sapiens	32-35
14762718-5	2004	The physiological meaning of an increased expression of TPI in hypoxygenated tissues is probably to increase the flow of triosephosphates through the glycolytic cascade thus leading to an increase of anaerobic energy generation.	triosephosphates	121-137	triosephosphate isomerase 1	Homo sapiens	56-59
12707923-9	2003	Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses of the acidic isoforms of triosephosphate isomerase showed modifications of cysteine residues to cysteic acid.	Cysteine	143-151	triosephosphate isomerase 1	Homo sapiens	93-118
15001364-3	2004	The conjunction of this novel computational approach with the use of the recent near-atomic resolution TIM-DHAP Michaelis complex PDB structure, 1NEY.pdb, has enabled us to obtain robust qualitative and, where available, quantitative agreement with a wide range of experimental data.	Dihydroxyacetone Phosphate	107-111	triosephosphate isomerase 1	Homo sapiens	103-106
15262334-0	2004	The strong inhibition of triosephosphate isomerase by the natural beta-carbolines may explain their neurotoxic actions.	Carbolines	66-81	triosephosphate isomerase 1	Homo sapiens	25-50
14725767-3	2004	We determined the structure of HTP bound to the small molecule inhibitor 5-chloro-6-[1-(2-iminopyrrolidinyl) methyl] uracil hydrochloride (TPI).	5-chloro-6-(1-(2-iminopyrrolidinyl) methyl)uracil hydrochloride	73-137	triosephosphate isomerase 1	Homo sapiens	139-142
12707923-9	2003	Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses of the acidic isoforms of triosephosphate isomerase showed modifications of cysteine residues to cysteic acid.	Cysteic Acid	164-176	triosephosphate isomerase 1	Homo sapiens	93-118
12644837-1	2003	Platelet-derived endothelial cell growth factor (PD-ECGF)/thymidine phosphorylase (TP) catalyses the reversible phosphorolysis of thymidine to thymine and 2-deoxyribose-1-phosphate and is involved in the metabolism of fluoropyrimidines.	fluoropyrimidines	218-235	triosephosphate isomerase 1	Homo sapiens	83-85
12644837-3	2003	We studied the contribution of TP activity to the sensitivity for these fluoropyrimidines by modulating its activity and/or expression level in colon and lung cancer cells using a specific inhibitor of TP (TPI) or by overproduction of TP via stable transfection of human TP.	fluoropyrimidines	72-89	triosephosphate isomerase 1	Homo sapiens	31-33
12644837-1	2003	Platelet-derived endothelial cell growth factor (PD-ECGF)/thymidine phosphorylase (TP) catalyses the reversible phosphorolysis of thymidine to thymine and 2-deoxyribose-1-phosphate and is involved in the metabolism of fluoropyrimidines.	Thymidine	58-67	triosephosphate isomerase 1	Homo sapiens	83-85
12475328-3	2002	However, they catalyze different reactions; TIM catalyzes the isomerization of DHAP to glyceraldehyde 3-phosphate (GAP), while MGS catalyzes the elimination of phosphate from DHAP.	Dihydroxyacetone Phosphate	79-83	triosephosphate isomerase 1	Homo sapiens	44-47
12644837-1	2003	Platelet-derived endothelial cell growth factor (PD-ECGF)/thymidine phosphorylase (TP) catalyses the reversible phosphorolysis of thymidine to thymine and 2-deoxyribose-1-phosphate and is involved in the metabolism of fluoropyrimidines.	Thymine	143-150	triosephosphate isomerase 1	Homo sapiens	83-85
12644837-1	2003	Platelet-derived endothelial cell growth factor (PD-ECGF)/thymidine phosphorylase (TP) catalyses the reversible phosphorolysis of thymidine to thymine and 2-deoxyribose-1-phosphate and is involved in the metabolism of fluoropyrimidines.	2-deoxyribose 1-phosphate	155-180	triosephosphate isomerase 1	Homo sapiens	83-85
12509510-2	2003	We focus here on the initial proton transfer of the isomerization reaction catalyzed by triosephosphate isomerase and present the crystal structure of its Michaelis complex with the substrate dihydroxyacetone phosphate at near-atomic resolution.	Dihydroxyacetone Phosphate	192-218	triosephosphate isomerase 1	Homo sapiens	88-113
12475328-3	2002	However, they catalyze different reactions; TIM catalyzes the isomerization of DHAP to glyceraldehyde 3-phosphate (GAP), while MGS catalyzes the elimination of phosphate from DHAP.	Glyceraldehyde 3-Phosphate	87-113	triosephosphate isomerase 1	Homo sapiens	44-47
12475328-3	2002	However, they catalyze different reactions; TIM catalyzes the isomerization of DHAP to glyceraldehyde 3-phosphate (GAP), while MGS catalyzes the elimination of phosphate from DHAP.	Phosphates	104-113	triosephosphate isomerase 1	Homo sapiens	44-47
12475328-3	2002	However, they catalyze different reactions; TIM catalyzes the isomerization of DHAP to glyceraldehyde 3-phosphate (GAP), while MGS catalyzes the elimination of phosphate from DHAP.	Dihydroxyacetone Phosphate	175-179	triosephosphate isomerase 1	Homo sapiens	44-47
12475328-4	2002	Similar to previous suggestions, the calculations confirmed that GAP formation is prohibited in MGS due primarily to the reduced flexibility of the catalytic base (Asp 71) compared to that in TIM (Glu 165).	Glutamic Acid	197-200	triosephosphate isomerase 1	Homo sapiens	192-195
12475328-5	2002	For the suppression of phosphate elimination in TIM, the calculations show that the widely accepted stereoelectronic argument that invokes the different phosphoryl torsion angles observed in the X-ray structures of inhibitor complexes of the two enzymes is not as important as electrostatic contributions from the protein and water molecules surrounding the phosphoryl.	Phosphates	23-32	triosephosphate isomerase 1	Homo sapiens	48-51
12475328-5	2002	For the suppression of phosphate elimination in TIM, the calculations show that the widely accepted stereoelectronic argument that invokes the different phosphoryl torsion angles observed in the X-ray structures of inhibitor complexes of the two enzymes is not as important as electrostatic contributions from the protein and water molecules surrounding the phosphoryl.	Water	326-331	triosephosphate isomerase 1	Homo sapiens	48-51
11741702-3	2002	The method most commonly employed to determine phosphofructokinase-1 activity is based on oxidation of NADH by the use of aldolase, triosephosphate isomerase, and alpha-glycerophosphate dehydrogenase.	NAD	103-107	triosephosphate isomerase 1	Homo sapiens	132-157
12270704-4	2002	TIM from Entamoeba histolytica (EhTIM) has the interface cysteine residue and presents more than ten insertions when compared with the enzyme from other pathogens.	Cysteine	57-65	triosephosphate isomerase 1	Homo sapiens	0-3
12127988-6	2002	TcTIM has a cysteine (Cys 15) at the dimer interface, whereas human TIM has methionine in that position.	Cysteine	12-20	triosephosphate isomerase 1	Homo sapiens	2-5
12127988-7	2002	In M15C human TIM, the benzothiazole concentrations that caused half-maximal inactivation were much lower than in the wild type.	benzothiazole	23-36	triosephosphate isomerase 1	Homo sapiens	14-17
12359716-7	2002	Cofilin was translocated to the plasma membrane along with triose-phosphate isomerase by the Rho activator lysophosphatidic acid but not by the p160 Rho-associated kinase inhibitor Y-27632, suggesting that the phosphorylated form of cofilin bound to TPI interacts with Na,K-ATPase.	lysophosphatidic acid	107-128	triosephosphate isomerase 1	Homo sapiens	59-85
11697989-0	2001	Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase.	Phosphates	16-25	triosephosphate isomerase 1	Homo sapiens	90-115
11419952-1	2001	Product release is partially rate determining in the isomerization reaction catalyzed by Triosephosphate Isomerase, the conversion of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate, probably because an active-site loop movement is necessary to free the product from confinement in the active-site.	Dihydroxyacetone Phosphate	134-160	triosephosphate isomerase 1	Homo sapiens	89-114
11589711-1	2001	The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis.	2-(N-formyl-N-hydroxy)aminoethyl phosphonate	83-128	triosephosphate isomerase 1	Homo sapiens	36-61
11589711-1	2001	The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis.	2-(N-formyl-N-hydroxy)aminoethyl phosphonate	83-128	triosephosphate isomerase 1	Homo sapiens	63-66
11589711-1	2001	The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis.	indolepropanol phosphate	130-133	triosephosphate isomerase 1	Homo sapiens	36-61
11589711-1	2001	The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis.	indolepropanol phosphate	130-133	triosephosphate isomerase 1	Homo sapiens	63-66
11589711-4	2001	Comparison of the TIM-IPP and the TIM-PGH structures with other liganded and unliganded structures also highlights the conformational flexibility of the ligand and the active site, as well as the conserved mode of ligand binding.	phosphoglycolohydroxamate	38-41	triosephosphate isomerase 1	Homo sapiens	34-37
11419952-1	2001	Product release is partially rate determining in the isomerization reaction catalyzed by Triosephosphate Isomerase, the conversion of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate, probably because an active-site loop movement is necessary to free the product from confinement in the active-site.	d-glyceraldehyde 3-phosphate	164-192	triosephosphate isomerase 1	Homo sapiens	89-114
11389594-1	2001	Methylglyoxal synthase (MGS) and triosephosphate isomerase (TIM) share neither sequence nor structural similarities, yet the reactions catalyzed by both enzymes are similar, in that both initially convert dihydroxyacetone phosphate to a cis-enediolic intermediate.	Dihydroxyacetone Phosphate	205-231	triosephosphate isomerase 1	Homo sapiens	33-58
11034068-1	2000	We developed a novel inhibitor of thymidine phosphorylase (TP), 5-chloro-6-[1-(2-iminopyrrolidinyl) methyl] uracil hydrochloride (TPI), that is about 1000-fold more active than 6-amino-5-chlorouracil, one of the most potent TP inhibitors.	5-chloro-6-(1-(2-iminopyrrolidinyl) methyl)uracil hydrochloride	64-128	triosephosphate isomerase 1	Homo sapiens	130-133
11389594-1	2001	Methylglyoxal synthase (MGS) and triosephosphate isomerase (TIM) share neither sequence nor structural similarities, yet the reactions catalyzed by both enzymes are similar, in that both initially convert dihydroxyacetone phosphate to a cis-enediolic intermediate.	Dihydroxyacetone Phosphate	205-231	triosephosphate isomerase 1	Homo sapiens	60-63
11389594-2	2001	This enediolic intermediate is formed from the abstraction of the pro-S C3 proton of DHAP by Asp-71 of MGS or the pro-R C3 proton of DHAP by Glu-165 of TIM.	Dihydroxyacetone Phosphate	85-89	triosephosphate isomerase 1	Homo sapiens	152-155
11389594-2	2001	This enediolic intermediate is formed from the abstraction of the pro-S C3 proton of DHAP by Asp-71 of MGS or the pro-R C3 proton of DHAP by Glu-165 of TIM.	Aspartic Acid	93-96	triosephosphate isomerase 1	Homo sapiens	152-155
11389594-2	2001	This enediolic intermediate is formed from the abstraction of the pro-S C3 proton of DHAP by Asp-71 of MGS or the pro-R C3 proton of DHAP by Glu-165 of TIM.	Dihydroxyacetone Phosphate	133-137	triosephosphate isomerase 1	Homo sapiens	152-155
11389594-2	2001	This enediolic intermediate is formed from the abstraction of the pro-S C3 proton of DHAP by Asp-71 of MGS or the pro-R C3 proton of DHAP by Glu-165 of TIM.	Glutamic Acid	141-144	triosephosphate isomerase 1	Homo sapiens	152-155
11389594-3	2001	MGS then catalyzes the elimination of phosphate from this enediolic intermediate to form the enol of methylglyoxal, while TIM catalyzes proton donation to C2 to form D-glyceraldehyde phosphate.	d-glyceraldehyde phosphate	166-192	triosephosphate isomerase 1	Homo sapiens	122-125
11389594-4	2001	A competitive inhibitor of TIM, phosphoglycolohydroxamic acid (PGH) is found to be a tight binding competitive inhibitor of MGS with a K(i) of 39 nM.	phosphoglycolohydroxamate	63-66	triosephosphate isomerase 1	Homo sapiens	27-30
11151009-0	2001	Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity.	Phosphates	69-78	triosephosphate isomerase 1	Homo sapiens	104-129
11151009-1	2001	Loop 8 (residues 232-242) in triosephosphate isomerase (TIM) is a highly conserved loop that forms a tight binding pocket for the phosphate moiety of the substrate.	Phosphates	35-44	triosephosphate isomerase 1	Homo sapiens	56-59
11151009-3	2001	The tight phosphate-binding pocket explains the high substrate specificity of TIM being limited to the in vivo substrates dihydroxyacetone-phosphate and D-glyceraldehyde-3-phosphate.	Phosphates	10-19	triosephosphate isomerase 1	Homo sapiens	78-81
11151009-3	2001	The tight phosphate-binding pocket explains the high substrate specificity of TIM being limited to the in vivo substrates dihydroxyacetone-phosphate and D-glyceraldehyde-3-phosphate.	Dihydroxyacetone Phosphate	122-148	triosephosphate isomerase 1	Homo sapiens	78-81
11151009-3	2001	The tight phosphate-binding pocket explains the high substrate specificity of TIM being limited to the in vivo substrates dihydroxyacetone-phosphate and D-glyceraldehyde-3-phosphate.	d-glyceraldehyde 3-phosphate	153-181	triosephosphate isomerase 1	Homo sapiens	78-81
11151009-9	2001	The much wider phosphate-binding pocket of the new variant allows for the development of a new TIM variant with a different substrate specificity.	Phosphates	15-24	triosephosphate isomerase 1	Homo sapiens	95-98
11330647-6	2001	Triosephosphate isomerase (TPI) was inhibited by ACH, but not by CHOP and DCDF, irrespective of species.	alpha-Chlorohydrin	49-52	triosephosphate isomerase 1	Homo sapiens	0-25
11330647-6	2001	Triosephosphate isomerase (TPI) was inhibited by ACH, but not by CHOP and DCDF, irrespective of species.	alpha-Chlorohydrin	49-52	triosephosphate isomerase 1	Homo sapiens	27-30
11456876-3	2001	By contrast, the mechanism that involves intramolecular proton transfer in the enediolate was found to be energetically unfavorable due to electrostatic interactions with His 95, a conserved residue in TIM from different organisms.	Histidine	171-174	triosephosphate isomerase 1	Homo sapiens	202-205
11034068-1	2000	We developed a novel inhibitor of thymidine phosphorylase (TP), 5-chloro-6-[1-(2-iminopyrrolidinyl) methyl] uracil hydrochloride (TPI), that is about 1000-fold more active than 6-amino-5-chlorouracil, one of the most potent TP inhibitors.	6-Amino-5-chloropyrimidine-2,4(1H,3H)-dione	177-199	triosephosphate isomerase 1	Homo sapiens	130-133
11285859-6	2000	Because the method depends on the colorimetric determination of triose formed from fructose-1,6-diphosphate only by aldolase, glycerophosphate dehydrogenase/triosephosphate isomerase (GDH/TIM) and reduced nicotinamide adenine dinucleotide (NADH) which usually applied in multienzymatic method, are omitted in the modified method.	fructose-1,6-diphosphate	83-107	triosephosphate isomerase 1	Homo sapiens	188-191
10772880-0	2000	Diminished blood levels of reduced glutathione and alpha-tocopherol in two triosephosphate isomerase-deficient brothers.	alpha-Tocopherol	51-67	triosephosphate isomerase 1	Homo sapiens	75-100
10736423-8	2000	Combined oral administration of TPI significantly potentiated the antitumor activity of F(3)dThd on AZ-521 human stomach cancer xenografts in nude mice.	Thymidine	92-96	triosephosphate isomerase 1	Homo sapiens	32-35
10736423-8	2000	Combined oral administration of TPI significantly potentiated the antitumor activity of F(3)dThd on AZ-521 human stomach cancer xenografts in nude mice.	az-521	100-106	triosephosphate isomerase 1	Homo sapiens	32-35
10736423-9	2000	In conclusion, TPI may contribute not only to inhibition of TPase-mediated biological functions but also to potentiation of the biological activity of various 2"-deoxyuridine and thymidine derivatives by combining with them.	Deoxyuridine	159-174	triosephosphate isomerase 1	Homo sapiens	15-18
10736423-9	2000	In conclusion, TPI may contribute not only to inhibition of TPase-mediated biological functions but also to potentiation of the biological activity of various 2"-deoxyuridine and thymidine derivatives by combining with them.	Thymidine	179-188	triosephosphate isomerase 1	Homo sapiens	15-18
10715115-3	2000	Since 2PG is a competitive inhibitor of both MGS and triosephosphate isomerase (TIM), the carboxylate groups of each bound 2PG from this structure and the structure of 2PG bound to TIM were used to align and compare the active sites despite differences in their protein folds.	carboxylate	90-101	triosephosphate isomerase 1	Homo sapiens	80-83
10715115-4	2000	The distances between the functional groups of Asp 71, His 98, His 19, and the carboxylate oxygens of the 2PG molecule in MGS are similar to the corresponding distances between the functional groups of Glu 165, His 95, Lys 13, and the carboxylate oxygens of the 2PG molecule in TIM.	Aspartic Acid	47-50	triosephosphate isomerase 1	Homo sapiens	278-281
10715115-4	2000	The distances between the functional groups of Asp 71, His 98, His 19, and the carboxylate oxygens of the 2PG molecule in MGS are similar to the corresponding distances between the functional groups of Glu 165, His 95, Lys 13, and the carboxylate oxygens of the 2PG molecule in TIM.	Glutamic Acid	202-205	triosephosphate isomerase 1	Homo sapiens	278-281
10715115-4	2000	The distances between the functional groups of Asp 71, His 98, His 19, and the carboxylate oxygens of the 2PG molecule in MGS are similar to the corresponding distances between the functional groups of Glu 165, His 95, Lys 13, and the carboxylate oxygens of the 2PG molecule in TIM.	carboxylate	235-246	triosephosphate isomerase 1	Homo sapiens	278-281
10715115-6	2000	Consistent with the known stereochemical data, the catalytic base Asp 71 is positioned on the opposite face of the 2PG-carboxylate plane as Glu 165 of TIM.	Aspartic Acid	66-69	triosephosphate isomerase 1	Homo sapiens	151-154
10715115-6	2000	Consistent with the known stereochemical data, the catalytic base Asp 71 is positioned on the opposite face of the 2PG-carboxylate plane as Glu 165 of TIM.	2pg-carboxylate	115-130	triosephosphate isomerase 1	Homo sapiens	151-154
10715115-6	2000	Consistent with the known stereochemical data, the catalytic base Asp 71 is positioned on the opposite face of the 2PG-carboxylate plane as Glu 165 of TIM.	Glutamic Acid	140-143	triosephosphate isomerase 1	Homo sapiens	151-154
10715115-7	2000	Both His 98 of MGS and His 95 of TIM are in the plane of the carboxylate of 2PG, suggesting that these two residues are homologous in function.	carboxylate	61-72	triosephosphate isomerase 1	Homo sapiens	33-36
10715115-8	2000	While His 19 of MGS and Lys 13 of TIM appear on the opposite face of the 2PG carboxylate plane, their relative location to the 2PG molecule is quite different, suggesting that they probably have different functions.	Histidine	6-9	triosephosphate isomerase 1	Homo sapiens	34-37
10715115-8	2000	While His 19 of MGS and Lys 13 of TIM appear on the opposite face of the 2PG carboxylate plane, their relative location to the 2PG molecule is quite different, suggesting that they probably have different functions.	Lysine	24-27	triosephosphate isomerase 1	Homo sapiens	34-37
10715115-8	2000	While His 19 of MGS and Lys 13 of TIM appear on the opposite face of the 2PG carboxylate plane, their relative location to the 2PG molecule is quite different, suggesting that they probably have different functions.	carboxylate	77-88	triosephosphate isomerase 1	Homo sapiens	34-37
10910933-1	2000	Three French families with triose phosphate isomerase (TPI) deficiency were studied, and 2 new mutations giving rise to null alleles were observed: a frameshift mutation with deletion of the 86-87 TG dinucleotide in codon 29 (TPI Alfortville) and a T-->A transversion in nucleotide 2 of the initiation codon (TPI Paris).	Thioguanine	197-199	triosephosphate isomerase 1	Homo sapiens	27-53
10910933-1	2000	Three French families with triose phosphate isomerase (TPI) deficiency were studied, and 2 new mutations giving rise to null alleles were observed: a frameshift mutation with deletion of the 86-87 TG dinucleotide in codon 29 (TPI Alfortville) and a T-->A transversion in nucleotide 2 of the initiation codon (TPI Paris).	Thioguanine	197-199	triosephosphate isomerase 1	Homo sapiens	55-58
10910933-1	2000	Three French families with triose phosphate isomerase (TPI) deficiency were studied, and 2 new mutations giving rise to null alleles were observed: a frameshift mutation with deletion of the 86-87 TG dinucleotide in codon 29 (TPI Alfortville) and a T-->A transversion in nucleotide 2 of the initiation codon (TPI Paris).	Dinucleoside Phosphates	200-212	triosephosphate isomerase 1	Homo sapiens	27-53
10910933-1	2000	Three French families with triose phosphate isomerase (TPI) deficiency were studied, and 2 new mutations giving rise to null alleles were observed: a frameshift mutation with deletion of the 86-87 TG dinucleotide in codon 29 (TPI Alfortville) and a T-->A transversion in nucleotide 2 of the initiation codon (TPI Paris).	Dinucleoside Phosphates	200-212	triosephosphate isomerase 1	Homo sapiens	55-58
10772880-1	2000	The glutathione redox system and alpha-tocopherol, both of which are essential for maintaining the normal structure of biological membranes, some other lipid-soluble antioxidants (lycopene, beta-carotene, retinol), and lipid peroxidation, were investigated in the blood from two triosephosphate isomerase (TPI)-deficient brothers.	Glutathione	4-15	triosephosphate isomerase 1	Homo sapiens	279-304
10772880-1	2000	The glutathione redox system and alpha-tocopherol, both of which are essential for maintaining the normal structure of biological membranes, some other lipid-soluble antioxidants (lycopene, beta-carotene, retinol), and lipid peroxidation, were investigated in the blood from two triosephosphate isomerase (TPI)-deficient brothers.	Glutathione	4-15	triosephosphate isomerase 1	Homo sapiens	306-309
10772880-1	2000	The glutathione redox system and alpha-tocopherol, both of which are essential for maintaining the normal structure of biological membranes, some other lipid-soluble antioxidants (lycopene, beta-carotene, retinol), and lipid peroxidation, were investigated in the blood from two triosephosphate isomerase (TPI)-deficient brothers.	alpha-Tocopherol	33-49	triosephosphate isomerase 1	Homo sapiens	279-304
10772880-1	2000	The glutathione redox system and alpha-tocopherol, both of which are essential for maintaining the normal structure of biological membranes, some other lipid-soluble antioxidants (lycopene, beta-carotene, retinol), and lipid peroxidation, were investigated in the blood from two triosephosphate isomerase (TPI)-deficient brothers.	alpha-Tocopherol	33-49	triosephosphate isomerase 1	Homo sapiens	306-309
10556207-6	1999	Uptake of active enzyme by TPI-deficient cells resulted in reversal of intracellular substrate accumulation, with a reduction in dihydroxyacetone phosphate (DHAP) concentration to levels seen in TPI-competent cells.	Dihydroxyacetone Phosphate	129-155	triosephosphate isomerase 1	Homo sapiens	27-30
10655478-1	2000	In a Hungarian family with triosephosphate isomerase (TPI; D-glyceraldehyde-3-phosphate keto-isomerase, EC 5.3.1.1) deficiency, two germ-line identical, but phenotypically differing compound heterozygote brothers (one of them with neurological disorder) have been identified with the same very low (<5%) TPI activity and 20- or 40-fold higher erythrocyte dihydroxyacetone phosphate levels as compared with normal controls.	Dihydroxyacetone Phosphate	358-384	triosephosphate isomerase 1	Homo sapiens	54-57
10677844-1	2000	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and triosephosphate isomerase (TPI) are essential to glycolysis, the major route of carbohydrate breakdown in eukaryotes.	Carbohydrates	133-145	triosephosphate isomerase 1	Homo sapiens	53-78
10677844-1	2000	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and triosephosphate isomerase (TPI) are essential to glycolysis, the major route of carbohydrate breakdown in eukaryotes.	Carbohydrates	133-145	triosephosphate isomerase 1	Homo sapiens	80-83
10556207-6	1999	Uptake of active enzyme by TPI-deficient cells resulted in reversal of intracellular substrate accumulation, with a reduction in dihydroxyacetone phosphate (DHAP) concentration to levels seen in TPI-competent cells.	Dihydroxyacetone Phosphate	157-161	triosephosphate isomerase 1	Homo sapiens	27-30
10585501-12	1999	Moreover, when a synthetic peptide from this TIM segment was studied in vitro, it was able to aggregate and to form amyloid fibrils, as established by Congo red binding and electron microscopy.	Congo Red	151-160	triosephosphate isomerase 1	Homo sapiens	45-48
10450932-7	1999	In addition, when the percent transfer of TG and CSA were determined in the presence of TPI, the percent transfer of TG and CSA from only LDL to HDL were significantly decreased in T150 buffer and human plasma compared to controls.	Triglycerides	42-44	triosephosphate isomerase 1	Homo sapiens	88-91
10450932-7	1999	In addition, when the percent transfer of TG and CSA were determined in the presence of TPI, the percent transfer of TG and CSA from only LDL to HDL were significantly decreased in T150 buffer and human plasma compared to controls.	Cyclosporine	49-52	triosephosphate isomerase 1	Homo sapiens	88-91
10450932-7	1999	In addition, when the percent transfer of TG and CSA were determined in the presence of TPI, the percent transfer of TG and CSA from only LDL to HDL were significantly decreased in T150 buffer and human plasma compared to controls.	Triglycerides	117-119	triosephosphate isomerase 1	Homo sapiens	88-91
10049939-5	1999	A C to T mutation identified by cDNA sequencing caused a Thr to Ile conversion in TPI, which could be detected in a tryptic digest of tumor-derived TPI by mass spectrometry.	Threonine	57-60	triosephosphate isomerase 1	Homo sapiens	82-85
10049939-5	1999	A C to T mutation identified by cDNA sequencing caused a Thr to Ile conversion in TPI, which could be detected in a tryptic digest of tumor-derived TPI by mass spectrometry.	Threonine	57-60	triosephosphate isomerase 1	Homo sapiens	148-151
10049939-5	1999	A C to T mutation identified by cDNA sequencing caused a Thr to Ile conversion in TPI, which could be detected in a tryptic digest of tumor-derived TPI by mass spectrometry.	Isoleucine	64-67	triosephosphate isomerase 1	Homo sapiens	82-85
10049939-5	1999	A C to T mutation identified by cDNA sequencing caused a Thr to Ile conversion in TPI, which could be detected in a tryptic digest of tumor-derived TPI by mass spectrometry.	Isoleucine	64-67	triosephosphate isomerase 1	Homo sapiens	148-151
10412233-3	1998	The K(m) for papain with BAPNA as substrate and Kcat/K(m) values for TPI-1, TPI-3 and TPI-4 were 2.7 x 10(-6) M, 0.84 nM/sec; 3.2 x 10(-6) M, 0.75 nM/sec; and 3.6 x 10(-6) M, 0.72 nM/sec respectively.	Benzoylarginine Nitroanilide	25-30	triosephosphate isomerase 1	Homo sapiens	69-74
9864381-5	1999	Additional studies with the transcription inhibitor, actinomycin D, revealed a rapid degradation of TPI mRNA in controls compared to FFP-treated cells, indicating that the stability of the TPI transcript was affected by plasma.	Dactinomycin	53-66	triosephosphate isomerase 1	Homo sapiens	100-103
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	phosphoglycolohydroxamate	12-15	triosephosphate isomerase 1	Homo sapiens	229-232
9761683-10	1998	In addition, TcTIM has proline at position 24 in the first helix of the TIM barrel; this is absent in the other TIM.	Proline	23-30	triosephosphate isomerase 1	Homo sapiens	15-18
9761683-10	1998	In addition, TcTIM has proline at position 24 in the first helix of the TIM barrel; this is absent in the other TIM.	Proline	23-30	triosephosphate isomerase 1	Homo sapiens	72-75
9398185-13	1997	A low-barrier hydrogen bond from PGH NOH to Glu-165 suggests a dual role for Glu-165 in catalysis of proton transfer not only between the C1 and C2 carbons but also between the O1 and O2 oxygens in the interconversion of DHAP and GAP in wild type TIM.	Glutamic Acid	44-47	triosephosphate isomerase 1	Homo sapiens	247-250
9398185-0	1997	NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase.	Hydrogen	27-35	triosephosphate isomerase 1	Homo sapiens	64-89
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	76-102	triosephosphate isomerase 1	Homo sapiens	0-25
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	76-102	triosephosphate isomerase 1	Homo sapiens	27-30
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	104-108	triosephosphate isomerase 1	Homo sapiens	0-25
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	104-108	triosephosphate isomerase 1	Homo sapiens	27-30
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glyceraldehyde 3-Phosphate	114-140	triosephosphate isomerase 1	Homo sapiens	0-25
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glyceraldehyde 3-Phosphate	114-140	triosephosphate isomerase 1	Homo sapiens	27-30
9850739-1	1998	Triosephosphate isomerase (TPI, EC 5.3.1.1) is an ubiquitously expressed enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate in the energy-generating glycolytic pathway.	Dihydroxyacetone Phosphate	118-144	triosephosphate isomerase 1	Homo sapiens	0-25
9850739-1	1998	Triosephosphate isomerase (TPI, EC 5.3.1.1) is an ubiquitously expressed enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate in the energy-generating glycolytic pathway.	Dihydroxyacetone Phosphate	118-144	triosephosphate isomerase 1	Homo sapiens	27-30
9850739-1	1998	Triosephosphate isomerase (TPI, EC 5.3.1.1) is an ubiquitously expressed enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate in the energy-generating glycolytic pathway.	Dihydroxyacetone Phosphate	146-150	triosephosphate isomerase 1	Homo sapiens	0-25
9850739-1	1998	Triosephosphate isomerase (TPI, EC 5.3.1.1) is an ubiquitously expressed enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate in the energy-generating glycolytic pathway.	Dihydroxyacetone Phosphate	146-150	triosephosphate isomerase 1	Homo sapiens	27-30
9850739-1	1998	Triosephosphate isomerase (TPI, EC 5.3.1.1) is an ubiquitously expressed enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate in the energy-generating glycolytic pathway.	Glyceraldehyde 3-Phosphate	156-182	triosephosphate isomerase 1	Homo sapiens	0-25
9850739-1	1998	Triosephosphate isomerase (TPI, EC 5.3.1.1) is an ubiquitously expressed enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate in the energy-generating glycolytic pathway.	Glyceraldehyde 3-Phosphate	156-182	triosephosphate isomerase 1	Homo sapiens	27-30
9850739-2	1998	Inherited defects in the TPI gene are characterised biochemically by markedly reduced TPI enzyme activity in all tissues resulting in metabolic block in glycolysis, with accumulating DHAP particularly in red cells.	Dihydroxyacetone Phosphate	183-187	triosephosphate isomerase 1	Homo sapiens	25-28
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	76-102	triosephosphate isomerase 1	Homo sapiens	0-25
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	76-102	triosephosphate isomerase 1	Homo sapiens	27-30
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	104-108	triosephosphate isomerase 1	Homo sapiens	0-25
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Dihydroxyacetone Phosphate	104-108	triosephosphate isomerase 1	Homo sapiens	27-30
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glyceraldehyde 3-Phosphate	114-140	triosephosphate isomerase 1	Homo sapiens	0-25
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glyceraldehyde 3-Phosphate	114-140	triosephosphate isomerase 1	Homo sapiens	27-30
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glutamic Acid	153-156	triosephosphate isomerase 1	Homo sapiens	0-25
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glutamic Acid	153-156	triosephosphate isomerase 1	Homo sapiens	27-30
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Histidine	215-218	triosephosphate isomerase 1	Homo sapiens	0-25
9843453-1	1998	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Histidine	215-218	triosephosphate isomerase 1	Homo sapiens	27-30
9843453-5	1998	On the basis of NMR detection of a strong hydrogen bond between Glu-165 and the 1-OH of an analogue of the enediol intermediate [Harris, T. K., Abeygunawardana, C., and Mildvan, A. S. (1997) Biochemistry 36, 14661], we have suggested a "criss-cross" mechanism for TIM in which Glu-165 transfers a proton from C1 of DHAP to O2 of the enediol, and subsequently from O1 of the enediol to C2 of the product GAP.	Glutamic Acid	64-67	triosephosphate isomerase 1	Homo sapiens	264-267
9842650-1	1998	A discussion of a 5-year-old child with congenital hemolytic anemia and severe hypotonia caused by triosephosphate (TPI) deficiency is presented.	triosephosphate	99-114	triosephosphate isomerase 1	Homo sapiens	116-119
9576855-0	1998	Reactivation of triosephosphate isomerase from three trypanosomatids and human: effect of suramin.	Suramin	90-97	triosephosphate isomerase 1	Homo sapiens	16-41
9576855-6	1998	Since the life time of the monomer of T. brucei TIM is longer than that of the other enzymes, Suramin is a more effective inhibitor of the reactivation of TIM from T. brucei, particularly at monomer concentrations above 1 microg of protein per ml (monomer concentration approx.	Suramin	94-101	triosephosphate isomerase 1	Homo sapiens	48-51
9576855-6	1998	Since the life time of the monomer of T. brucei TIM is longer than that of the other enzymes, Suramin is a more effective inhibitor of the reactivation of TIM from T. brucei, particularly at monomer concentrations above 1 microg of protein per ml (monomer concentration approx.	Suramin	94-101	triosephosphate isomerase 1	Homo sapiens	155-158
9576855-8	1998	Compounds that are structurally related to Suramin also inhibit TIM reactivation; their effect was about five times more pronounced in the enzyme from T. brucei than in human TIM.	Suramin	43-50	triosephosphate isomerase 1	Homo sapiens	64-67
9576855-8	1998	Compounds that are structurally related to Suramin also inhibit TIM reactivation; their effect was about five times more pronounced in the enzyme from T. brucei than in human TIM.	Suramin	43-50	triosephosphate isomerase 1	Homo sapiens	175-178
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glutamic Acid	153-156	triosephosphate isomerase 1	Homo sapiens	0-25
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	15n	59-62	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Glutamic Acid	153-156	triosephosphate isomerase 1	Homo sapiens	27-30
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	phosphoglycolohydroxamate	63-66	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Histidine	215-218	triosephosphate isomerase 1	Homo sapiens	0-25
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	Hydrogen	82-84	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-1	1997	Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.	Histidine	215-218	triosephosphate isomerase 1	Homo sapiens	27-30
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	15n	59-62	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-2	1997	TIM and its complexes with the reactive intermediate analogs, phosphoglycolic acid (PGA) and phosphoglycolohydroxamic acid (PGH), were studied by 1H NMR at 600 MHz and at low temperature (-4.8 degrees C).	phosphoglycolate	62-82	triosephosphate isomerase 1	Homo sapiens	0-3
9398185-2	1997	TIM and its complexes with the reactive intermediate analogs, phosphoglycolic acid (PGA) and phosphoglycolohydroxamic acid (PGH), were studied by 1H NMR at 600 MHz and at low temperature (-4.8 degrees C).	phosphoglycolate	84-87	triosephosphate isomerase 1	Homo sapiens	0-3
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	15n	59-62	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-2	1997	TIM and its complexes with the reactive intermediate analogs, phosphoglycolic acid (PGA) and phosphoglycolohydroxamic acid (PGH), were studied by 1H NMR at 600 MHz and at low temperature (-4.8 degrees C).	phosphoglycolohydroxamate	93-122	triosephosphate isomerase 1	Homo sapiens	0-3
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	15n	59-62	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-2	1997	TIM and its complexes with the reactive intermediate analogs, phosphoglycolic acid (PGA) and phosphoglycolohydroxamic acid (PGH), were studied by 1H NMR at 600 MHz and at low temperature (-4.8 degrees C).	phosphoglycolohydroxamate	124-127	triosephosphate isomerase 1	Homo sapiens	0-3
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	15n	59-62	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-2	1997	TIM and its complexes with the reactive intermediate analogs, phosphoglycolic acid (PGA) and phosphoglycolohydroxamic acid (PGH), were studied by 1H NMR at 600 MHz and at low temperature (-4.8 degrees C).	Hydrogen	146-148	triosephosphate isomerase 1	Homo sapiens	0-3
9398185-3	1997	His-95 shows an N epsilon H resonance at 13.1 ppm which shifts to 13.3 ppm in the TIM-PGA complex and to 13.5 ppm in the TIM-PGH complex.	phosphoglycolohydroxamate	125-128	triosephosphate isomerase 1	Homo sapiens	121-124
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	phosphoglycolohydroxamate	63-66	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-4	1997	In the TIM-PGH complex, His-95 N epsilon H shows a slow, pH-independent exchange rate with water (kex = 80 s-1 at 30 degrees C, Eact = 19 kcal/mol), which is 44-fold slower than that of an exposed histidine suggesting partial shielding from bulk solvent, and a fractionation factor phi = 0.71 +/- 0.02 consistent with its donation of a normal hydrogen bond.	phosphoglycolohydroxamate	11-14	triosephosphate isomerase 1	Homo sapiens	7-10
9398185-4	1997	In the TIM-PGH complex, His-95 N epsilon H shows a slow, pH-independent exchange rate with water (kex = 80 s-1 at 30 degrees C, Eact = 19 kcal/mol), which is 44-fold slower than that of an exposed histidine suggesting partial shielding from bulk solvent, and a fractionation factor phi = 0.71 +/- 0.02 consistent with its donation of a normal hydrogen bond.	Histidine	24-27	triosephosphate isomerase 1	Homo sapiens	7-10
9398185-4	1997	In the TIM-PGH complex, His-95 N epsilon H shows a slow, pH-independent exchange rate with water (kex = 80 s-1 at 30 degrees C, Eact = 19 kcal/mol), which is 44-fold slower than that of an exposed histidine suggesting partial shielding from bulk solvent, and a fractionation factor phi = 0.71 +/- 0.02 consistent with its donation of a normal hydrogen bond.	Water	91-96	triosephosphate isomerase 1	Homo sapiens	7-10
9398185-10	1997	This resonance shows a pH-independent exchange rate with water (kex = 3900 s-1 at 30 degrees C, Eact = 8.9 kcal/mol) which may reflect the dissociation of the TIM-PGH complex, and meets the criteria for a low-barrier hydrogen bond on the basis of the significant downfield shift of 6.2 ppm from the NOH proton of the model compound acetohydroxamic acid, and a very low fractionation factor phi = 0.38 +/- 0.06.	Water	57-62	triosephosphate isomerase 1	Homo sapiens	159-162
9398185-10	1997	This resonance shows a pH-independent exchange rate with water (kex = 3900 s-1 at 30 degrees C, Eact = 8.9 kcal/mol) which may reflect the dissociation of the TIM-PGH complex, and meets the criteria for a low-barrier hydrogen bond on the basis of the significant downfield shift of 6.2 ppm from the NOH proton of the model compound acetohydroxamic acid, and a very low fractionation factor phi = 0.38 +/- 0.06.	phosphoglycolohydroxamate	163-166	triosephosphate isomerase 1	Homo sapiens	159-162
9398185-4	1997	In the TIM-PGH complex, His-95 N epsilon H shows a slow, pH-independent exchange rate with water (kex = 80 s-1 at 30 degrees C, Eact = 19 kcal/mol), which is 44-fold slower than that of an exposed histidine suggesting partial shielding from bulk solvent, and a fractionation factor phi = 0.71 +/- 0.02 consistent with its donation of a normal hydrogen bond.	Histidine	197-206	triosephosphate isomerase 1	Homo sapiens	7-10
9398185-10	1997	This resonance shows a pH-independent exchange rate with water (kex = 3900 s-1 at 30 degrees C, Eact = 8.9 kcal/mol) which may reflect the dissociation of the TIM-PGH complex, and meets the criteria for a low-barrier hydrogen bond on the basis of the significant downfield shift of 6.2 ppm from the NOH proton of the model compound acetohydroxamic acid, and a very low fractionation factor phi = 0.38 +/- 0.06.	Hydrogen	217-225	triosephosphate isomerase 1	Homo sapiens	159-162
9398185-4	1997	In the TIM-PGH complex, His-95 N epsilon H shows a slow, pH-independent exchange rate with water (kex = 80 s-1 at 30 degrees C, Eact = 19 kcal/mol), which is 44-fold slower than that of an exposed histidine suggesting partial shielding from bulk solvent, and a fractionation factor phi = 0.71 +/- 0.02 consistent with its donation of a normal hydrogen bond.	Hydrogen	343-351	triosephosphate isomerase 1	Homo sapiens	7-10
9398185-6	1997	The resonance at 14.9 ppm is absent and the resonance at 10.9 ppm is much weaker in the TIM complex of PGA, which lacks the hydroxamic acid (-NHOH) moiety.	phosphoglycolate	103-106	triosephosphate isomerase 1	Homo sapiens	88-91
9398185-10	1997	This resonance shows a pH-independent exchange rate with water (kex = 3900 s-1 at 30 degrees C, Eact = 8.9 kcal/mol) which may reflect the dissociation of the TIM-PGH complex, and meets the criteria for a low-barrier hydrogen bond on the basis of the significant downfield shift of 6.2 ppm from the NOH proton of the model compound acetohydroxamic acid, and a very low fractionation factor phi = 0.38 +/- 0.06.	2-amino-5-chlorobenzophenone N-hydroxyamidinohydrazone	299-302	triosephosphate isomerase 1	Homo sapiens	159-162
9398185-6	1997	The resonance at 14.9 ppm is absent and the resonance at 10.9 ppm is much weaker in the TIM complex of PGA, which lacks the hydroxamic acid (-NHOH) moiety.	Hydroxamic Acids	124-139	triosephosphate isomerase 1	Homo sapiens	88-91
9398185-10	1997	This resonance shows a pH-independent exchange rate with water (kex = 3900 s-1 at 30 degrees C, Eact = 8.9 kcal/mol) which may reflect the dissociation of the TIM-PGH complex, and meets the criteria for a low-barrier hydrogen bond on the basis of the significant downfield shift of 6.2 ppm from the NOH proton of the model compound acetohydroxamic acid, and a very low fractionation factor phi = 0.38 +/- 0.06.	acetohydroxamic acid	332-352	triosephosphate isomerase 1	Homo sapiens	159-162
9398185-6	1997	The resonance at 14.9 ppm is absent and the resonance at 10.9 ppm is much weaker in the TIM complex of PGA, which lacks the hydroxamic acid (-NHOH) moiety.	nhoh	142-146	triosephosphate isomerase 1	Homo sapiens	88-91
9398185-7	1997	15N-labeled PGH was synthesized and the NH proton of free [15N]PGH shows a single 1H-15N HMQC cross peak with delta (1H) = 10.3 ppm and delta (15N) = 168 ppm which shifts to delta (1H) = 10.9 ppm and delta (15N) = 174 ppm in the TIM complex of [15N]PGH.	15n	0-3	triosephosphate isomerase 1	Homo sapiens	229-232
9398185-11	1997	In the X-ray structure of the TIM-PGH complex [Davenport, R. C., Bash, P. A., Seaton, B.	phosphoglycolohydroxamate	34-37	triosephosphate isomerase 1	Homo sapiens	30-33
9398185-13	1997	A low-barrier hydrogen bond from PGH NOH to Glu-165 suggests a dual role for Glu-165 in catalysis of proton transfer not only between the C1 and C2 carbons but also between the O1 and O2 oxygens in the interconversion of DHAP and GAP in wild type TIM.	Hydrogen	14-22	triosephosphate isomerase 1	Homo sapiens	247-250
9398185-13	1997	A low-barrier hydrogen bond from PGH NOH to Glu-165 suggests a dual role for Glu-165 in catalysis of proton transfer not only between the C1 and C2 carbons but also between the O1 and O2 oxygens in the interconversion of DHAP and GAP in wild type TIM.	pgh noh	33-40	triosephosphate isomerase 1	Homo sapiens	247-250
9398185-13	1997	A low-barrier hydrogen bond from PGH NOH to Glu-165 suggests a dual role for Glu-165 in catalysis of proton transfer not only between the C1 and C2 carbons but also between the O1 and O2 oxygens in the interconversion of DHAP and GAP in wild type TIM.	Glutamic Acid	77-80	triosephosphate isomerase 1	Homo sapiens	247-250
9398185-13	1997	A low-barrier hydrogen bond from PGH NOH to Glu-165 suggests a dual role for Glu-165 in catalysis of proton transfer not only between the C1 and C2 carbons but also between the O1 and O2 oxygens in the interconversion of DHAP and GAP in wild type TIM.	Carbon	148-155	triosephosphate isomerase 1	Homo sapiens	247-250
9398185-13	1997	A low-barrier hydrogen bond from PGH NOH to Glu-165 suggests a dual role for Glu-165 in catalysis of proton transfer not only between the C1 and C2 carbons but also between the O1 and O2 oxygens in the interconversion of DHAP and GAP in wild type TIM.	Oxygen	187-194	triosephosphate isomerase 1	Homo sapiens	247-250
9398185-13	1997	A low-barrier hydrogen bond from PGH NOH to Glu-165 suggests a dual role for Glu-165 in catalysis of proton transfer not only between the C1 and C2 carbons but also between the O1 and O2 oxygens in the interconversion of DHAP and GAP in wild type TIM.	Dihydroxyacetone Phosphate	221-225	triosephosphate isomerase 1	Homo sapiens	247-250
9261072-8	1997	This leucine residue is completely exposed and together with the surrounding positively charged patch, may be responsible for binding TIM to the erythrocyte membrane.	Leucine	5-12	triosephosphate isomerase 1	Homo sapiens	134-137
9294216-3	1997	There were roughly 100% and 30% more 16:0/20:4 and 18:0/20:4 diacyl-phosphatidylcholine species in erythrocytes from the two TPI-deficient brothers than in the probes from healthy controls.	diacyl-phosphatidylcholine	61-87	triosephosphate isomerase 1	Homo sapiens	125-128
9261072-9	1997	Another interesting feature is the occurrence of a cysteine residue at the dimer interface of PfTIM (Cys13), in contrast to human TIM where this residue is a methionine.	Cysteine	51-59	triosephosphate isomerase 1	Homo sapiens	96-99
9261072-10	1997	Finally, residue 96 of human TIM (Ser96), which occurs near the active site, has been replaced by phenylalanine in PfTIM.	Phenylalanine	98-111	triosephosphate isomerase 1	Homo sapiens	29-32
9338582-2	1997	Among seven unrelated Northern European kindreds with clinical TPI deficiency studied, a single missense mutation at codon 104 (GAG;Glu-->GAC;Asp) predominated, accounting for 11/14 (79%) mutant alleles.	Glycosaminoglycans	128-131	triosephosphate isomerase 1	Homo sapiens	63-66
9049311-5	1997	Here, we provide evidence that a nonsense codon at position 1, 2 or 10 reduces the abundance of nucleus-associated TPI mRNA to an average of only 84% of normal because translation reinitiates at the methionine codon at position 14.	Methionine	199-209	triosephosphate isomerase 1	Homo sapiens	115-118
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Dihydroxyacetone Phosphate	107-133	triosephosphate isomerase 1	Homo sapiens	24-50
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Dihydroxyacetone Phosphate	107-133	triosephosphate isomerase 1	Homo sapiens	52-55
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Dihydroxyacetone Phosphate	135-139	triosephosphate isomerase 1	Homo sapiens	24-50
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Dihydroxyacetone Phosphate	135-139	triosephosphate isomerase 1	Homo sapiens	52-55
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Glyceraldehyde 3-Phosphate	145-171	triosephosphate isomerase 1	Homo sapiens	24-50
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Glyceraldehyde 3-Phosphate	145-171	triosephosphate isomerase 1	Homo sapiens	52-55
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Dihydroxyacetone Phosphate	226-230	triosephosphate isomerase 1	Homo sapiens	24-50
9125215-1	1997	Inherited deficiency of triose phosphate isomerase (TPI), the enzyme that catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate, is characterised by an accumulation of intracellular DHAP and markedly reduced enzyme activity in cells and tissues, resulting in progressive, usually fatal neuromuscular dysfunction.	Dihydroxyacetone Phosphate	226-230	triosephosphate isomerase 1	Homo sapiens	52-55
9099261-4	1997	In this report we develop first a more direct synthase assay which uses glyceraldehyde phosphate to suppress the aldolase and triose phosphate isomerase reactions.	Glyceraldehyde 3-Phosphate	72-96	triosephosphate isomerase 1	Homo sapiens	126-152
9338582-2	1997	Among seven unrelated Northern European kindreds with clinical TPI deficiency studied, a single missense mutation at codon 104 (GAG;Glu-->GAC;Asp) predominated, accounting for 11/14 (79%) mutant alleles.	Glutamic Acid	132-135	triosephosphate isomerase 1	Homo sapiens	63-66
9338582-2	1997	Among seven unrelated Northern European kindreds with clinical TPI deficiency studied, a single missense mutation at codon 104 (GAG;Glu-->GAC;Asp) predominated, accounting for 11/14 (79%) mutant alleles.	Aspartic Acid	145-148	triosephosphate isomerase 1	Homo sapiens	63-66
8672446-2	1996	In a previous work, a monomeric mutant of hTIM was engineered in which Met14 and Arg98, two interface residues, were changed to glutamine.	Glutamine	128-137	triosephosphate isomerase 1	Homo sapiens	42-46
8841131-2	1996	Secondary kH/kT kinetic isotope effects in H2O and kH/kT or kD/kT isotope effects in D2O have been measured for the triosephosphate isomerase-catalyzed conversion of dihydroxyacetone 3-phosphate (DHAP) to D-glyceraldehyde 3-phosphate.	Water	43-46	triosephosphate isomerase 1	Homo sapiens	116-141
8841131-2	1996	Secondary kH/kT kinetic isotope effects in H2O and kH/kT or kD/kT isotope effects in D2O have been measured for the triosephosphate isomerase-catalyzed conversion of dihydroxyacetone 3-phosphate (DHAP) to D-glyceraldehyde 3-phosphate.	Deuterium Oxide	85-88	triosephosphate isomerase 1	Homo sapiens	116-141
8841131-2	1996	Secondary kH/kT kinetic isotope effects in H2O and kH/kT or kD/kT isotope effects in D2O have been measured for the triosephosphate isomerase-catalyzed conversion of dihydroxyacetone 3-phosphate (DHAP) to D-glyceraldehyde 3-phosphate.	Dihydroxyacetone Phosphate	166-194	triosephosphate isomerase 1	Homo sapiens	116-141
8841131-2	1996	Secondary kH/kT kinetic isotope effects in H2O and kH/kT or kD/kT isotope effects in D2O have been measured for the triosephosphate isomerase-catalyzed conversion of dihydroxyacetone 3-phosphate (DHAP) to D-glyceraldehyde 3-phosphate.	Dihydroxyacetone Phosphate	196-200	triosephosphate isomerase 1	Homo sapiens	116-141
8841131-2	1996	Secondary kH/kT kinetic isotope effects in H2O and kH/kT or kD/kT isotope effects in D2O have been measured for the triosephosphate isomerase-catalyzed conversion of dihydroxyacetone 3-phosphate (DHAP) to D-glyceraldehyde 3-phosphate.	d-glyceraldehyde 3-phosphate	205-233	triosephosphate isomerase 1	Homo sapiens	116-141
8944178-10	1996	In contrast to the experimental data the theoretical calculations predict elevation in DHAP level at lower than 0.1% of the normal value of TPI activity.	Dihydroxyacetone Phosphate	87-91	triosephosphate isomerase 1	Homo sapiens	140-143
8944178-13	1996	We propose that the microcompartmentation of TPI that could further decrease the reduced isomerase activity of the deficient cells, is responsible for the high DHAP level.	Dihydroxyacetone Phosphate	160-164	triosephosphate isomerase 1	Homo sapiens	45-48
8811738-5	1996	The complexes of TIM with the substrate dihydroxyacetone phosphate (DHAP), five possible intermediates and the product glyceraldehyde-3-phosphate (GAP) were optimized in the active-site model at the 3-21G(*) level and energy profile for the proton abstraction from DHAP by the active-site Glu 167 was calculated at the MP2/3-21G(*)13-21G(*) level.	Dihydroxyacetone Phosphate	40-66	triosephosphate isomerase 1	Homo sapiens	17-20
8811738-5	1996	The complexes of TIM with the substrate dihydroxyacetone phosphate (DHAP), five possible intermediates and the product glyceraldehyde-3-phosphate (GAP) were optimized in the active-site model at the 3-21G(*) level and energy profile for the proton abstraction from DHAP by the active-site Glu 167 was calculated at the MP2/3-21G(*)13-21G(*) level.	Dihydroxyacetone Phosphate	68-72	triosephosphate isomerase 1	Homo sapiens	17-20
8811738-5	1996	The complexes of TIM with the substrate dihydroxyacetone phosphate (DHAP), five possible intermediates and the product glyceraldehyde-3-phosphate (GAP) were optimized in the active-site model at the 3-21G(*) level and energy profile for the proton abstraction from DHAP by the active-site Glu 167 was calculated at the MP2/3-21G(*)13-21G(*) level.	Glyceraldehyde 3-Phosphate	119-145	triosephosphate isomerase 1	Homo sapiens	17-20
8811738-5	1996	The complexes of TIM with the substrate dihydroxyacetone phosphate (DHAP), five possible intermediates and the product glyceraldehyde-3-phosphate (GAP) were optimized in the active-site model at the 3-21G(*) level and energy profile for the proton abstraction from DHAP by the active-site Glu 167 was calculated at the MP2/3-21G(*)13-21G(*) level.	Dihydroxyacetone Phosphate	265-269	triosephosphate isomerase 1	Homo sapiens	17-20
8811738-5	1996	The complexes of TIM with the substrate dihydroxyacetone phosphate (DHAP), five possible intermediates and the product glyceraldehyde-3-phosphate (GAP) were optimized in the active-site model at the 3-21G(*) level and energy profile for the proton abstraction from DHAP by the active-site Glu 167 was calculated at the MP2/3-21G(*)13-21G(*) level.	Glutamic Acid	289-292	triosephosphate isomerase 1	Homo sapiens	17-20
8609635-2	1996	Two hTIM mutants were produced, in which a glutamine residue was substituted for either Met14 or Arg98, both of which are interface residuces.	Glutamine	43-52	triosephosphate isomerase 1	Homo sapiens	4-8
8532677-7	1995	Evidence from published sequencing and mutational studies on selected members of the GAT superfamily (carbamoyl phosphate, imidazoleglycerol phosphate, GMP and CTP synthases) support both the secondary structure prediction and the TIM-barrel topology.	Carbamyl Phosphate	102-121	triosephosphate isomerase 1	Homo sapiens	231-234
8745400-6	1996	The best inhibitors of wild-type TIM are phosphoglycolohydroxamate (PGH) and 2-phosphoglycolate (2PG), with KI values of 8 microM and 26 microM, respectively.	phosphoglycolate	77-95	triosephosphate isomerase 1	Homo sapiens	33-36
8591044-7	1995	In the structures with inhibitor bound, the catalytic lysine (Lys13 in loop-1) and the catalytic histidine (His95 in loop-4) adopt conformations similar to those observed in wild-type TIM, but very different from the monoTIM structure.	Lysine	54-60	triosephosphate isomerase 1	Homo sapiens	184-187
8591044-7	1995	In the structures with inhibitor bound, the catalytic lysine (Lys13 in loop-1) and the catalytic histidine (His95 in loop-4) adopt conformations similar to those observed in wild-type TIM, but very different from the monoTIM structure.	Histidine	97-106	triosephosphate isomerase 1	Homo sapiens	184-187
8745400-2	1996	It is known that in TIM, three residues, Lys 13 (loop 1), His 95 (loop 4), and Glu 167 (loop 6) are the crucial catalytic residues.	Lysine	41-44	triosephosphate isomerase 1	Homo sapiens	20-23
8745400-2	1996	It is known that in TIM, three residues, Lys 13 (loop 1), His 95 (loop 4), and Glu 167 (loop 6) are the crucial catalytic residues.	Histidine	58-61	triosephosphate isomerase 1	Homo sapiens	20-23
8745400-2	1996	It is known that in TIM, three residues, Lys 13 (loop 1), His 95 (loop 4), and Glu 167 (loop 6) are the crucial catalytic residues.	Glutamic Acid	79-82	triosephosphate isomerase 1	Homo sapiens	20-23
8745400-6	1996	The best inhibitors of wild-type TIM are phosphoglycolohydroxamate (PGH) and 2-phosphoglycolate (2PG), with KI values of 8 microM and 26 microM, respectively.	phosphoglycolohydroxamate	41-66	triosephosphate isomerase 1	Homo sapiens	33-36
8745400-6	1996	The best inhibitors of wild-type TIM are phosphoglycolohydroxamate (PGH) and 2-phosphoglycolate (2PG), with KI values of 8 microM and 26 microM, respectively.	phosphoglycolohydroxamate	68-71	triosephosphate isomerase 1	Homo sapiens	33-36
7599123-1	1995	Using solid-state deuterium NMR, we have measured the motion of the flexible loop of triosephosphate isomerase (TIM) with and without substrate and transition-state analogs.	Deuterium	18-27	triosephosphate isomerase 1	Homo sapiens	85-110
7599123-1	1995	Using solid-state deuterium NMR, we have measured the motion of the flexible loop of triosephosphate isomerase (TIM) with and without substrate and transition-state analogs.	Deuterium	18-27	triosephosphate isomerase 1	Homo sapiens	112-115
7599123-2	1995	The measurements were carried out on a catalytically competent mutant of TIM W90Y W157F containing a single tryptophan (W168) in the flexible loop; W168 is the only strictly conserved tryptophan in the currently available TIM sequences.	Tryptophan	108-118	triosephosphate isomerase 1	Homo sapiens	73-76
7599123-2	1995	The measurements were carried out on a catalytically competent mutant of TIM W90Y W157F containing a single tryptophan (W168) in the flexible loop; W168 is the only strictly conserved tryptophan in the currently available TIM sequences.	Tryptophan	184-194	triosephosphate isomerase 1	Homo sapiens	73-76
7599123-3	1995	The solid-state NMR samples were prepared by precipitation using polyethylene glycol, and kinetic analysis of the PEG-precipitated TIM gave values for kcat, Km, and KI similar to those measured in solution for the substrate and substrate and transition-state analogs.	Polyethylene Glycols	114-117	triosephosphate isomerase 1	Homo sapiens	131-134
7599123-5	1995	Surprisingly, spectra of TIM ligated with a substrate analog, glycerol 3-phosphate (G3P), or with a tight-binding transition-state analog, phosphoglycolate (PGA), show that the loop moves with a rate similar to the rate in the empty enzyme and also has a similar population ratio for the two conformers.	alpha-glycerophosphoric acid	62-82	triosephosphate isomerase 1	Homo sapiens	25-28
7599123-5	1995	Surprisingly, spectra of TIM ligated with a substrate analog, glycerol 3-phosphate (G3P), or with a tight-binding transition-state analog, phosphoglycolate (PGA), show that the loop moves with a rate similar to the rate in the empty enzyme and also has a similar population ratio for the two conformers.	alpha-glycerophosphoric acid	84-87	triosephosphate isomerase 1	Homo sapiens	25-28
7599123-5	1995	Surprisingly, spectra of TIM ligated with a substrate analog, glycerol 3-phosphate (G3P), or with a tight-binding transition-state analog, phosphoglycolate (PGA), show that the loop moves with a rate similar to the rate in the empty enzyme and also has a similar population ratio for the two conformers.	phosphoglycolate	139-155	triosephosphate isomerase 1	Homo sapiens	25-28
7599123-5	1995	Surprisingly, spectra of TIM ligated with a substrate analog, glycerol 3-phosphate (G3P), or with a tight-binding transition-state analog, phosphoglycolate (PGA), show that the loop moves with a rate similar to the rate in the empty enzyme and also has a similar population ratio for the two conformers.	phosphoglycolate	157-160	triosephosphate isomerase 1	Homo sapiens	25-28
7599123-10	1995	The hypothesis that the spin-lattice relaxation of the alpha-deuteron is very slow would be consistent with the observed dynamics of the ring-deuterated TIM.	alpha-deuteron	55-69	triosephosphate isomerase 1	Homo sapiens	153-156
7558587-4	1995	Antibodies were generated against RC-3095 and Des-Tpi1-RC-3095, conjugated to bovine serum albumin with glutaraldehyde.	Glutaral	104-118	triosephosphate isomerase 1	Homo sapiens	50-54
8532677-7	1995	Evidence from published sequencing and mutational studies on selected members of the GAT superfamily (carbamoyl phosphate, imidazoleglycerol phosphate, GMP and CTP synthases) support both the secondary structure prediction and the TIM-barrel topology.	imidazoleglycerol phosphate	123-150	triosephosphate isomerase 1	Homo sapiens	231-234
7827080-3	1995	When [1,6-13C]fructose 1,6-bisphosphate or [1-13C]fructose 1,6-bisphosphate was utilized individually, gluconeogenic flux occurred without metabolism through aldolase and triosephosphate isomerase resulting in formation of [1,6-13C]-glucose and [1-13C]glucose respectively.	[1,6-13c]fructose 1,6-bisphosphate	5-39	triosephosphate isomerase 1	Homo sapiens	171-196
7628118-7	1995	Direct sequencing of the triosephosphate isomerase gene revealed homozygosity for the formerly described GAG-->GAC-mutation changing 104 Glu-->Asp.	Aspartic Acid	149-152	triosephosphate isomerase 1	Homo sapiens	25-50
7827080-3	1995	When [1,6-13C]fructose 1,6-bisphosphate or [1-13C]fructose 1,6-bisphosphate was utilized individually, gluconeogenic flux occurred without metabolism through aldolase and triosephosphate isomerase resulting in formation of [1,6-13C]-glucose and [1-13C]glucose respectively.	1,6-bisphosphate	23-39	triosephosphate isomerase 1	Homo sapiens	171-196
7816830-3	1995	Anisotropy measurements with n-(9-anthroyloxy) stearic and -palmitic acid fluorophores revealed increased motional freedom of the fatty acid chains in the external lipid layers of the intact erythrocytes from all members of the TPI-deficient family as compared with normal age-matched controls.	n-(9-anthroyloxy) stearic	29-54	triosephosphate isomerase 1	Homo sapiens	228-231
8061610-2	1994	The crystal structure of recombinant human triosephosphate isomerase (hTIM) has been determined complexed with the transition-state analogue 2-phosphoglycolate at a resolution of 2.8 A.	phosphoglycolate	141-159	triosephosphate isomerase 1	Homo sapiens	43-68
7816830-1	1995	Marked hypoalphalipoproteinemia was found together with relatively low serum cholesterol, triacylglycerol, and LDL levels in a triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1)-deficient Hungarian family, especially in the two compound-heterozygote brothers.	Cholesterol	77-88	triosephosphate isomerase 1	Homo sapiens	127-153
7816830-1	1995	Marked hypoalphalipoproteinemia was found together with relatively low serum cholesterol, triacylglycerol, and LDL levels in a triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1)-deficient Hungarian family, especially in the two compound-heterozygote brothers.	Cholesterol	77-88	triosephosphate isomerase 1	Homo sapiens	155-158
7816830-1	1995	Marked hypoalphalipoproteinemia was found together with relatively low serum cholesterol, triacylglycerol, and LDL levels in a triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1)-deficient Hungarian family, especially in the two compound-heterozygote brothers.	Triglycerides	90-105	triosephosphate isomerase 1	Homo sapiens	127-153
7816830-1	1995	Marked hypoalphalipoproteinemia was found together with relatively low serum cholesterol, triacylglycerol, and LDL levels in a triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1)-deficient Hungarian family, especially in the two compound-heterozygote brothers.	Triglycerides	90-105	triosephosphate isomerase 1	Homo sapiens	155-158
8848575-2	1995	The high phosphatase activity hydrolyses the ester to alpha-chlorohydrin which undergoes oxidation to (S)-3-chlorolactaldehyde, a specific inhibitor of sperm glyceraldehyde-3-phosphate dehydrogenase and triosephosphate isomerase, thereby exhibiting an anti-glycolytic action.	Esters	45-50	triosephosphate isomerase 1	Homo sapiens	203-228
8848575-2	1995	The high phosphatase activity hydrolyses the ester to alpha-chlorohydrin which undergoes oxidation to (S)-3-chlorolactaldehyde, a specific inhibitor of sperm glyceraldehyde-3-phosphate dehydrogenase and triosephosphate isomerase, thereby exhibiting an anti-glycolytic action.	alpha-Chlorohydrin	54-72	triosephosphate isomerase 1	Homo sapiens	203-228
8848575-2	1995	The high phosphatase activity hydrolyses the ester to alpha-chlorohydrin which undergoes oxidation to (S)-3-chlorolactaldehyde, a specific inhibitor of sperm glyceraldehyde-3-phosphate dehydrogenase and triosephosphate isomerase, thereby exhibiting an anti-glycolytic action.	3-chlorolactaldehyde	102-126	triosephosphate isomerase 1	Homo sapiens	203-228
8204630-0	1994	Deamidation of triosephosphate isomerase in reverse micelles: effects of water on catalysis and molecular wear and tear.	Water	73-78	triosephosphate isomerase 1	Homo sapiens	15-40
8204630-1	1994	The specific deamidation of asparagine-71 of triosephosphate isomerase increases upon substrate binding and catalysis.	Asparagine	28-38	triosephosphate isomerase 1	Homo sapiens	45-70
8204630-4	1994	In order to explore this interaction, triosephosphate isomerase was entrapped in reverse micelles with different water contents that support different catalytic rates.	Water	113-118	triosephosphate isomerase 1	Homo sapiens	38-63
8061610-2	1994	The crystal structure of recombinant human triosephosphate isomerase (hTIM) has been determined complexed with the transition-state analogue 2-phosphoglycolate at a resolution of 2.8 A.	phosphoglycolate	141-159	triosephosphate isomerase 1	Homo sapiens	70-74
8061610-15	1994	Inspection of the 3-dimensional structure of trypanosomal triosephosphate isomerase, which has a methionine at position 122, only increased the mystery of the effects of the Gly to Arg mutation in the human enzyme.	Methionine	97-107	triosephosphate isomerase 1	Homo sapiens	58-83
8061610-15	1994	Inspection of the 3-dimensional structure of trypanosomal triosephosphate isomerase, which has a methionine at position 122, only increased the mystery of the effects of the Gly to Arg mutation in the human enzyme.	Glycine	174-177	triosephosphate isomerase 1	Homo sapiens	58-83
8061610-15	1994	Inspection of the 3-dimensional structure of trypanosomal triosephosphate isomerase, which has a methionine at position 122, only increased the mystery of the effects of the Gly to Arg mutation in the human enzyme.	Arginine	181-184	triosephosphate isomerase 1	Homo sapiens	58-83
1390632-1	1992	To determine what drives the closure of the active-site loop in the reaction catalyzed by triosephosphate isomerase, several residues involved in hydrogen bonding between the loop and the bulk of the protein have been altered.	Hydrogen	146-154	triosephosphate isomerase 1	Homo sapiens	90-115
8503454-0	1993	Human triosephosphate isomerase deficiency resulting from mutation of Phe-240.	Phenylalanine	70-73	triosephosphate isomerase 1	Homo sapiens	6-31
1400336-5	1992	Covalent reaction of the active site Glu165 with the substrate analogue 3-chloroacetol phosphate (CAP) results in dimers with increased susceptibility to unfolding and inactivation by denaturants (i.e. the rates of inactivation and unfolding are (TPICAP)2 greater than (TPI-TPICAP) greater than (TPI)2).	3-chloroacetol phosphate	72-96	triosephosphate isomerase 1	Homo sapiens	247-250
1400336-5	1992	Covalent reaction of the active site Glu165 with the substrate analogue 3-chloroacetol phosphate (CAP) results in dimers with increased susceptibility to unfolding and inactivation by denaturants (i.e. the rates of inactivation and unfolding are (TPICAP)2 greater than (TPI-TPICAP) greater than (TPI)2).	3-chloroacetol phosphate	72-96	triosephosphate isomerase 1	Homo sapiens	270-273
1400336-5	1992	Covalent reaction of the active site Glu165 with the substrate analogue 3-chloroacetol phosphate (CAP) results in dimers with increased susceptibility to unfolding and inactivation by denaturants (i.e. the rates of inactivation and unfolding are (TPICAP)2 greater than (TPI-TPICAP) greater than (TPI)2).	cap	98-101	triosephosphate isomerase 1	Homo sapiens	247-250
1400336-5	1992	Covalent reaction of the active site Glu165 with the substrate analogue 3-chloroacetol phosphate (CAP) results in dimers with increased susceptibility to unfolding and inactivation by denaturants (i.e. the rates of inactivation and unfolding are (TPICAP)2 greater than (TPI-TPICAP) greater than (TPI)2).	cap	98-101	triosephosphate isomerase 1	Homo sapiens	270-273
8356028-9	1993	It is found that transfer to 0.4 M ammonium sulphate (equal to 80 times the Ki of sulphate for TIM), gives rise to significant sulphate binding at the active site of one dimer (termed molecule-2), and less significant binding at the active site of the other.	Ammonium Sulfate	35-52	triosephosphate isomerase 1	Homo sapiens	95-98
8356028-9	1993	It is found that transfer to 0.4 M ammonium sulphate (equal to 80 times the Ki of sulphate for TIM), gives rise to significant sulphate binding at the active site of one dimer (termed molecule-2), and less significant binding at the active site of the other.	Sulfates	44-52	triosephosphate isomerase 1	Homo sapiens	95-98
8356028-9	1993	It is found that transfer to 0.4 M ammonium sulphate (equal to 80 times the Ki of sulphate for TIM), gives rise to significant sulphate binding at the active site of one dimer (termed molecule-2), and less significant binding at the active site of the other.	Sulfates	82-90	triosephosphate isomerase 1	Homo sapiens	95-98
8356028-11	1993	In a mother liquor containing 40 microM phosphoglycolohydroxamate (equal to 10 times the Ki of phosphoglycolohydroxamate for TIM), an inhibitor molecule binds at the active site of only that dimer of which the flexible loop is free from crystal contacts (molecule-2).	phosphoglycolohydroxamate	40-65	triosephosphate isomerase 1	Homo sapiens	125-128
8356028-11	1993	In a mother liquor containing 40 microM phosphoglycolohydroxamate (equal to 10 times the Ki of phosphoglycolohydroxamate for TIM), an inhibitor molecule binds at the active site of only that dimer of which the flexible loop is free from crystal contacts (molecule-2).	phosphoglycolohydroxamate	95-120	triosephosphate isomerase 1	Homo sapiens	125-128
8476863-1	1993	In previous work, we have shown that the first (and, presumably, the second) pKa of the active-site histidine-95 in triosephosphate isomerase has been lowered by about 2 units [Lodi, P. J., & Knowles, J. R. (1991) Biochemistry 30, 6948-6956].	Histidine	100-109	triosephosphate isomerase 1	Homo sapiens	116-141
8444148-4	1993	Methylglyoxal formation from glycerone phosphate was increased in the presence of triose phosphate isomerase but this may be due to the faster non-enzymatic formation from the glyceraldehyde 3-phosphate isomerisation product.	Pyruvaldehyde	0-13	triosephosphate isomerase 1	Homo sapiens	82-108
8444148-4	1993	Methylglyoxal formation from glycerone phosphate was increased in the presence of triose phosphate isomerase but this may be due to the faster non-enzymatic formation from the glyceraldehyde 3-phosphate isomerisation product.	Dihydroxyacetone Phosphate	29-48	triosephosphate isomerase 1	Homo sapiens	82-108
8444148-4	1993	Methylglyoxal formation from glycerone phosphate was increased in the presence of triose phosphate isomerase but this may be due to the faster non-enzymatic formation from the glyceraldehyde 3-phosphate isomerisation product.	Glyceraldehyde 3-Phosphate	176-202	triosephosphate isomerase 1	Homo sapiens	82-108
1390633-0	1992	Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase.	Hydrogen	50-58	triosephosphate isomerase 1	Homo sapiens	109-134
1390633-1	1992	A residue essential for proper closure of the active-site loop in the reaction catalyzed by triosephosphate isomerase is tyrosine-208, the hydroxyl group of which forms a hydrogen bond with the amide nitrogen of alanine-176, a component of the loop.	Tyrosine	121-129	triosephosphate isomerase 1	Homo sapiens	92-117
1390633-1	1992	A residue essential for proper closure of the active-site loop in the reaction catalyzed by triosephosphate isomerase is tyrosine-208, the hydroxyl group of which forms a hydrogen bond with the amide nitrogen of alanine-176, a component of the loop.	Hydrogen	171-179	triosephosphate isomerase 1	Homo sapiens	92-117
1390633-1	1992	A residue essential for proper closure of the active-site loop in the reaction catalyzed by triosephosphate isomerase is tyrosine-208, the hydroxyl group of which forms a hydrogen bond with the amide nitrogen of alanine-176, a component of the loop.	Amides	194-199	triosephosphate isomerase 1	Homo sapiens	92-117
1390633-1	1992	A residue essential for proper closure of the active-site loop in the reaction catalyzed by triosephosphate isomerase is tyrosine-208, the hydroxyl group of which forms a hydrogen bond with the amide nitrogen of alanine-176, a component of the loop.	Nitrogen	200-208	triosephosphate isomerase 1	Homo sapiens	92-117
1390633-1	1992	A residue essential for proper closure of the active-site loop in the reaction catalyzed by triosephosphate isomerase is tyrosine-208, the hydroxyl group of which forms a hydrogen bond with the amide nitrogen of alanine-176, a component of the loop.	Alanine	212-219	triosephosphate isomerase 1	Homo sapiens	92-117
1521533-6	1992	The rate of TPI reactivation also increased with increasing protein concentration in the system with denatured TPI covalently derivatized at the catalytic site with the substrate analogue 3-chloroacetol phosphate.	3-chloroacetol phosphate	188-212	triosephosphate isomerase 1	Homo sapiens	111-114
1536574-3	1992	CAP binding accelerated the specific deamidation of Asn71 in mammalian TPI.	cap	0-3	triosephosphate isomerase 1	Homo sapiens	71-74
1521533-3	1992	In the transfer step, denatured TPI monomers distributed in single micelles, and guanidine hydrochloride was diluted more than 100 times.	Guanidine	81-104	triosephosphate isomerase 1	Homo sapiens	32-35
1521533-6	1992	The rate of TPI reactivation also increased with increasing protein concentration in the system with denatured TPI covalently derivatized at the catalytic site with the substrate analogue 3-chloroacetol phosphate.	3-chloroacetol phosphate	188-212	triosephosphate isomerase 1	Homo sapiens	12-15
18601147-1	1992	The process of thermal inactivation of triosephosphate isomerase covalently attached to a silica-based support activated with p-benzoquinone was found to be a complex one.	Silicon Dioxide	90-96	triosephosphate isomerase 1	Homo sapiens	39-64
18601147-1	1992	The process of thermal inactivation of triosephosphate isomerase covalently attached to a silica-based support activated with p-benzoquinone was found to be a complex one.	quinone	126-140	triosephosphate isomerase 1	Homo sapiens	39-64
1586170-5	1992	Covalent reaction of the active site Glu 165 with the substrate analogue 3-chloroacetol phosphate results in a conformational change (decrease in beta-sheet) which is similar in TPI from all three species.	Glutamic Acid	37-40	triosephosphate isomerase 1	Homo sapiens	178-181
1586170-5	1992	Covalent reaction of the active site Glu 165 with the substrate analogue 3-chloroacetol phosphate results in a conformational change (decrease in beta-sheet) which is similar in TPI from all three species.	3-chloroacetol phosphate	73-97	triosephosphate isomerase 1	Homo sapiens	178-181
1536574-4	1992	Transverse urea gradient gel electrophoretic analysis showed that the CAP-TPI dimer dissociates more readily than the native dimer.	Urea	11-15	triosephosphate isomerase 1	Homo sapiens	74-77
1895291-0	1991	Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate.	2-phosphoglycerate	174-192	triosephosphate isomerase 1	Homo sapiens	64-89
1290934-1	1992	A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM).	Dihydroxyacetone Phosphate	65-91	triosephosphate isomerase 1	Homo sapiens	160-186
1290934-1	1992	A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM).	Dihydroxyacetone Phosphate	65-91	triosephosphate isomerase 1	Homo sapiens	188-191
1290934-1	1992	A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM).	Dihydroxyacetone Phosphate	93-97	triosephosphate isomerase 1	Homo sapiens	160-186
1290934-1	1992	A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM).	Dihydroxyacetone Phosphate	93-97	triosephosphate isomerase 1	Homo sapiens	188-191
1290934-1	1992	A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM).	d-glyceraldehyde 3-phosphate	102-130	triosephosphate isomerase 1	Homo sapiens	160-186
1290934-1	1992	A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM).	d-glyceraldehyde 3-phosphate	102-130	triosephosphate isomerase 1	Homo sapiens	188-191
1573338-5	1992	Cyclandelate was clinically effective in the prophylactic treatment of migraine as shown by an average reduction of greater than 60% in three migraine parameters; frequency of attacks (FA 77.6%), total pain index (TPI 64.0%) and number of awakenings with headache (AwH 72.7%).	Cyclandelate	0-12	triosephosphate isomerase 1	Homo sapiens	214-217
1573338-7	1992	An average reduction of about 50% in FA, TPI and AwH was already observed in the cyclandelate group after 4-6 weeks suggesting an early onset of action.	Cyclandelate	81-93	triosephosphate isomerase 1	Homo sapiens	41-44
1729373-5	1992	Amino terminus sequences of tryptic peptides of the 28-kDa Ag had high (79-87%) sequence homology with the mammalian glycolytic/gluconeogenic enzyme triosephosphate isomerase (TPI).	Peptides	36-44	triosephosphate isomerase 1	Homo sapiens	149-174
1729373-5	1992	Amino terminus sequences of tryptic peptides of the 28-kDa Ag had high (79-87%) sequence homology with the mammalian glycolytic/gluconeogenic enzyme triosephosphate isomerase (TPI).	Peptides	36-44	triosephosphate isomerase 1	Homo sapiens	176-179
1895291-1	1991	In the continuation of a project aimed at the rational design of drugs against diseases caused by trypanosomes, the crystal structure of trypanosomal triosephosphate isomerase in complex with the active site inhibitor 2-phosphoglycerate has been determined.	2-phosphoglycerate	218-236	triosephosphate isomerase 1	Homo sapiens	150-175
1895291-8	1991	The crystallographic structure of the 2-PGA TIM complex shows that the ligand binds fully within the active site of TIM, with partners for all but one of the ligand"s strongly hydrogen bonding groups.	2-Propylglutaric acid	38-43	triosephosphate isomerase 1	Homo sapiens	44-47
1895291-8	1991	The crystallographic structure of the 2-PGA TIM complex shows that the ligand binds fully within the active site of TIM, with partners for all but one of the ligand"s strongly hydrogen bonding groups.	2-Propylglutaric acid	38-43	triosephosphate isomerase 1	Homo sapiens	116-119
1895291-8	1991	The crystallographic structure of the 2-PGA TIM complex shows that the ligand binds fully within the active site of TIM, with partners for all but one of the ligand"s strongly hydrogen bonding groups.	Hydrogen	176-184	triosephosphate isomerase 1	Homo sapiens	44-47
1895291-8	1991	The crystallographic structure of the 2-PGA TIM complex shows that the ligand binds fully within the active site of TIM, with partners for all but one of the ligand"s strongly hydrogen bonding groups.	Hydrogen	176-184	triosephosphate isomerase 1	Homo sapiens	116-119
1952062-0	1991	1H nuclear magnetic resonance assay of erythrocyte triosephosphate isomerase.	Hydrogen	0-2	triosephosphate isomerase 1	Homo sapiens	51-76
1952062-1	1991	A direct method for measuring the activity of erythrocyte triosephosphate isomerase using 1H NMR spectroscopy was developed.	Hydrogen	90-92	triosephosphate isomerase 1	Homo sapiens	58-83
1849541-0	1991	Affinity purification of antibodies from sera using polyvinylidenedifluoride (PVDF) membranes as coupling matrices for antigens presented by autoantibodies to triosephosphate isomerase.	polyvinylidene fluoride	52-76	triosephosphate isomerase 1	Homo sapiens	159-184
2069953-0	1991	Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications.	imidazole	8-17	triosephosphate isomerase 1	Homo sapiens	67-92
2069953-1	1991	To illuminate the role of histidine-95 in the catalytic reaction mediated by triosephosphate isomerase, 13C and 15N NMR titration studies have been carried out both on the wild-type enzyme and on a mutant isomerase in which the single remaining histidine (that at the active site) has been isotopically enriched in the imidazole ring.	Histidine	26-35	triosephosphate isomerase 1	Homo sapiens	77-102
2043623-1	1991	The glycolytic enzyme triosephosphate isomerase (TIM) catalyzes the interconversion of the three-carbon sugars dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (GAP) at a rate limited by the diffusion of substrate to the enzyme.	Carbon	97-103	triosephosphate isomerase 1	Homo sapiens	49-52
2043623-1	1991	The glycolytic enzyme triosephosphate isomerase (TIM) catalyzes the interconversion of the three-carbon sugars dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (GAP) at a rate limited by the diffusion of substrate to the enzyme.	Sugars	104-110	triosephosphate isomerase 1	Homo sapiens	49-52
2043623-1	1991	The glycolytic enzyme triosephosphate isomerase (TIM) catalyzes the interconversion of the three-carbon sugars dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (GAP) at a rate limited by the diffusion of substrate to the enzyme.	Dihydroxyacetone Phosphate	111-137	triosephosphate isomerase 1	Homo sapiens	49-52
2043623-1	1991	The glycolytic enzyme triosephosphate isomerase (TIM) catalyzes the interconversion of the three-carbon sugars dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (GAP) at a rate limited by the diffusion of substrate to the enzyme.	Dihydroxyacetone Phosphate	139-143	triosephosphate isomerase 1	Homo sapiens	49-52
2043623-1	1991	The glycolytic enzyme triosephosphate isomerase (TIM) catalyzes the interconversion of the three-carbon sugars dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (GAP) at a rate limited by the diffusion of substrate to the enzyme.	d-glyceraldehyde 3-phosphate	149-177	triosephosphate isomerase 1	Homo sapiens	49-52
2043623-2	1991	We have solved the three-dimensional structure of TIM complexed with a reactive intermediate analogue, phosphoglycolohydroxamate (PGH), at 1.9-A resolution and have refined the structure to an R-factor of 18%.	phosphoglycolohydroxamate	103-128	triosephosphate isomerase 1	Homo sapiens	50-53
2043623-2	1991	We have solved the three-dimensional structure of TIM complexed with a reactive intermediate analogue, phosphoglycolohydroxamate (PGH), at 1.9-A resolution and have refined the structure to an R-factor of 18%.	phosphoglycolohydroxamate	130-133	triosephosphate isomerase 1	Homo sapiens	50-53
2040290-2	1991	The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor SO-4(2) was determined by X-ray crystallography to a resolution of 0.24 nm.	so-4(2)	102-109	triosephosphate isomerase 1	Homo sapiens	35-60
2071606-5	1991	We have also quantitated TPI mRNA throughout the cell cycle following cell synchronization with aphidicolin.	Aphidicolin	96-107	triosephosphate isomerase 1	Homo sapiens	25-28
1849541-0	1991	Affinity purification of antibodies from sera using polyvinylidenedifluoride (PVDF) membranes as coupling matrices for antigens presented by autoantibodies to triosephosphate isomerase.	polyvinylidene fluoride	78-82	triosephosphate isomerase 1	Homo sapiens	159-184
2217142-5	1990	We performed simulations of wild-type TIM and the active site mutants with the substrate dihydroxyacetone phosphate bound both noncovalently and covalently.	Dihydroxyacetone Phosphate	89-115	triosephosphate isomerase 1	Homo sapiens	38-41
2260979-0	1990	Phosphorus-31 nuclear magnetic resonance spectroscopy reveals two conformational forms of chloroacetol phosphate-bound triosephosphate isomerase.	Phosphorus	0-10	triosephosphate isomerase 1	Homo sapiens	119-144
2260979-1	1990	Chloroacetol phosphate covalently reacts with Glu-165 in the catalytic center of triosephosphate isomerase.	chloroacetol phosphate	0-22	triosephosphate isomerase 1	Homo sapiens	81-106
2260979-1	1990	Chloroacetol phosphate covalently reacts with Glu-165 in the catalytic center of triosephosphate isomerase.	Glutamic Acid	46-49	triosephosphate isomerase 1	Homo sapiens	81-106
2260979-4	1990	Reassociation and redimerization of the triosephosphate isomerase-chloroacetol phosphate complex restores only the resonance at 5.5 ppm.	chloroacetol phosphate	66-88	triosephosphate isomerase 1	Homo sapiens	40-65
2241163-1	1990	The electrophoretic isoforms of mammalian triosephosphate isomerase (TPI; EC 5.3.1.1) are due to deamidation at two Asn-Gly sites (Asn15 and Asn71).	Asn-Gly	116-123	triosephosphate isomerase 1	Homo sapiens	42-67
2241163-1	1990	The electrophoretic isoforms of mammalian triosephosphate isomerase (TPI; EC 5.3.1.1) are due to deamidation at two Asn-Gly sites (Asn15 and Asn71).	Asn-Gly	116-123	triosephosphate isomerase 1	Homo sapiens	69-72
2339591-5	1990	The disturbed balance between glycerin-aldehyde phosphate and dihydroxyacetone phosphate, due to the deficiency of the TPI enzyme, is interpreted as the biochemical background of an impaired electron transport across the mitochondrial membrane, resulting in the coexistence of an impaired glycolytic pathway and an impaired mitochondrial metabolism of muscle cells.	Glycerol	30-38	triosephosphate isomerase 1	Homo sapiens	119-122
2339591-5	1990	The disturbed balance between glycerin-aldehyde phosphate and dihydroxyacetone phosphate, due to the deficiency of the TPI enzyme, is interpreted as the biochemical background of an impaired electron transport across the mitochondrial membrane, resulting in the coexistence of an impaired glycolytic pathway and an impaired mitochondrial metabolism of muscle cells.	aldehyde phosphate	39-57	triosephosphate isomerase 1	Homo sapiens	119-122
2339591-5	1990	The disturbed balance between glycerin-aldehyde phosphate and dihydroxyacetone phosphate, due to the deficiency of the TPI enzyme, is interpreted as the biochemical background of an impaired electron transport across the mitochondrial membrane, resulting in the coexistence of an impaired glycolytic pathway and an impaired mitochondrial metabolism of muscle cells.	Dihydroxyacetone Phosphate	62-88	triosephosphate isomerase 1	Homo sapiens	119-122
34096270-6	2021	In addition, TPI-An-Py can be applied to the detection of Cu2+ in real samples with satisfactory recoveries in the range of 100-112% in lake water and 98-101% in tap water.	cupric ion	58-62	triosephosphate isomerase 1	Homo sapiens	13-16
34848475-1	2021	BACKGROUND/AIM: Recently, trifluridine/tipiracil (FTD/TPI) treatment was established as a later-line treatment for metastatic colorectal cancer (mCRC).	Trifluridine	26-38	triosephosphate isomerase 1	Homo sapiens	54-57
34848475-1	2021	BACKGROUND/AIM: Recently, trifluridine/tipiracil (FTD/TPI) treatment was established as a later-line treatment for metastatic colorectal cancer (mCRC).	tipiracil	39-48	triosephosphate isomerase 1	Homo sapiens	54-57
34406678-1	2021	BACKGROUND: Trifluridine/tipiracil (FTD/TPI) and regorafenib prolong survival for patients with refractory metastatic colorectal cancer (mCRC); limited comparative effectiveness data exist.	Trifluridine	12-24	triosephosphate isomerase 1	Homo sapiens	40-43
34406678-1	2021	BACKGROUND: Trifluridine/tipiracil (FTD/TPI) and regorafenib prolong survival for patients with refractory metastatic colorectal cancer (mCRC); limited comparative effectiveness data exist.	tipiracil	25-34	triosephosphate isomerase 1	Homo sapiens	40-43
34097100-1	2021	PURPOSE: Trifluridine/tipiracil (FTD/TPI) is approved for advanced colorectal and gastric/gastroesophageal cancer; however, data in patients with renal impairment (RI) are limited.	Trifluridine	9-21	triosephosphate isomerase 1	Homo sapiens	37-40
34097100-1	2021	PURPOSE: Trifluridine/tipiracil (FTD/TPI) is approved for advanced colorectal and gastric/gastroesophageal cancer; however, data in patients with renal impairment (RI) are limited.	tipiracil	22-31	triosephosphate isomerase 1	Homo sapiens	37-40
33939414-5	2021	Triosephosphate isomerase (TIM), orotidine 5"-monophosphate decarboxylase (OMPDC), and glycerol 3-phosphate dehydrogenase (GPDH) show effective catalysis of reactions of phosphorylated substrates and strong phosphite dianion activation of reactions of phosphodianion truncated substrates, with rate constants kcat/Km (M-1 s-1) and kcat/KdKHPi (M-2 s-1), respectively.	phosphodianion	252-266	triosephosphate isomerase 1	Homo sapiens	0-25
33939414-5	2021	Triosephosphate isomerase (TIM), orotidine 5"-monophosphate decarboxylase (OMPDC), and glycerol 3-phosphate dehydrogenase (GPDH) show effective catalysis of reactions of phosphorylated substrates and strong phosphite dianion activation of reactions of phosphodianion truncated substrates, with rate constants kcat/Km (M-1 s-1) and kcat/KdKHPi (M-2 s-1), respectively.	phosphodianion	252-266	triosephosphate isomerase 1	Homo sapiens	27-30
33939414-9	2021	There is a good linear correlation, with a slope of 0.73, between values of the dissociation constants log Ki for release of the transition state analog phosphoglycolate (PGA) trianion and log kcat/Km for isomerization of GAP for wild-type and variants of TIM.	phosphoglycolate	153-169	triosephosphate isomerase 1	Homo sapiens	256-259
33939414-9	2021	There is a good linear correlation, with a slope of 0.73, between values of the dissociation constants log Ki for release of the transition state analog phosphoglycolate (PGA) trianion and log kcat/Km for isomerization of GAP for wild-type and variants of TIM.	phosphoglycolate	171-174	triosephosphate isomerase 1	Homo sapiens	256-259
33939414-9	2021	There is a good linear correlation, with a slope of 0.73, between values of the dissociation constants log Ki for release of the transition state analog phosphoglycolate (PGA) trianion and log kcat/Km for isomerization of GAP for wild-type and variants of TIM.	trianion	176-184	triosephosphate isomerase 1	Homo sapiens	256-259
33939414-10	2021	This correlation shows that the substituted amino acid side chains act to stabilize the complex between TIM and the PGA trianion and that ca.	pga trianion	116-128	triosephosphate isomerase 1	Homo sapiens	104-107
33939414-12	2021	The correlation provides evidence that these side chains function to enhance the basicity of the E165 side chain of TIM, which deprotonates the bound carbon acid substrate.	carbon acid	150-161	triosephosphate isomerase 1	Homo sapiens	116-119
33939414-13	2021	There is a good linear correlation, with a slope of 0.74, between the values of DeltaG  and DeltaG  determined by electron valence bond (EVB) calculations to model deprotonation of dihydroxyacetone phosphate (DHAP) in water and when bound to wild-type and variant forms of TIM to form the enediolate reaction intermediate.	Dihydroxyacetone Phosphate	181-207	triosephosphate isomerase 1	Homo sapiens	273-276
33939414-13	2021	There is a good linear correlation, with a slope of 0.74, between the values of DeltaG  and DeltaG  determined by electron valence bond (EVB) calculations to model deprotonation of dihydroxyacetone phosphate (DHAP) in water and when bound to wild-type and variant forms of TIM to form the enediolate reaction intermediate.	Dihydroxyacetone Phosphate	209-213	triosephosphate isomerase 1	Homo sapiens	273-276
33939414-13	2021	There is a good linear correlation, with a slope of 0.74, between the values of DeltaG  and DeltaG  determined by electron valence bond (EVB) calculations to model deprotonation of dihydroxyacetone phosphate (DHAP) in water and when bound to wild-type and variant forms of TIM to form the enediolate reaction intermediate.	Water	218-223	triosephosphate isomerase 1	Homo sapiens	273-276
33939414-14	2021	This correlation provides evidence that the stabilizing interactions of the transition state for TIM-catalyzed deprotonation of DHAP are optimized by placement of amino acid side chains in positions that provide for the maximum stabilization of the charged reaction intermediate, relative to the neutral substrate.	Dihydroxyacetone Phosphate	128-132	triosephosphate isomerase 1	Homo sapiens	97-100
34936872-4	2021	The most significant modification is the delta mass of 79.967 Da at serine 58 (Ser58) of triosephosphate isomerase (TPI), which is confirmed to be phosphorylation.	Serine	68-74	triosephosphate isomerase 1	Homo sapiens	89-114
34936872-4	2021	The most significant modification is the delta mass of 79.967 Da at serine 58 (Ser58) of triosephosphate isomerase (TPI), which is confirmed to be phosphorylation.	Serine	68-74	triosephosphate isomerase 1	Homo sapiens	116-119
34547581-1	2021	BACKGROUND: In preclinical studies trifluridine/tipiracil (FTD/TPI) plus oxaliplatin (Industriestrasse, Holzkirchen, Germany) sensitised microsatellite stable (MSS) metastatic colorectal cancer (mCRC) to anti-programmed cell death protein-1; the addition of oxaliplatin or bevacizumab (F Hoffmann- la ROCHE AG, Kaiseraugst, Switzerland) enhanced the antitumour effects of FTD/TPI.	Trifluridine	35-47	triosephosphate isomerase 1	Homo sapiens	63-66
34547581-1	2021	BACKGROUND: In preclinical studies trifluridine/tipiracil (FTD/TPI) plus oxaliplatin (Industriestrasse, Holzkirchen, Germany) sensitised microsatellite stable (MSS) metastatic colorectal cancer (mCRC) to anti-programmed cell death protein-1; the addition of oxaliplatin or bevacizumab (F Hoffmann- la ROCHE AG, Kaiseraugst, Switzerland) enhanced the antitumour effects of FTD/TPI.	Trifluridine	35-47	triosephosphate isomerase 1	Homo sapiens	376-379
34547581-1	2021	BACKGROUND: In preclinical studies trifluridine/tipiracil (FTD/TPI) plus oxaliplatin (Industriestrasse, Holzkirchen, Germany) sensitised microsatellite stable (MSS) metastatic colorectal cancer (mCRC) to anti-programmed cell death protein-1; the addition of oxaliplatin or bevacizumab (F Hoffmann- la ROCHE AG, Kaiseraugst, Switzerland) enhanced the antitumour effects of FTD/TPI.	tipiracil	48-57	triosephosphate isomerase 1	Homo sapiens	63-66
34547581-1	2021	BACKGROUND: In preclinical studies trifluridine/tipiracil (FTD/TPI) plus oxaliplatin (Industriestrasse, Holzkirchen, Germany) sensitised microsatellite stable (MSS) metastatic colorectal cancer (mCRC) to anti-programmed cell death protein-1; the addition of oxaliplatin or bevacizumab (F Hoffmann- la ROCHE AG, Kaiseraugst, Switzerland) enhanced the antitumour effects of FTD/TPI.	tipiracil	48-57	triosephosphate isomerase 1	Homo sapiens	376-379
34547581-1	2021	BACKGROUND: In preclinical studies trifluridine/tipiracil (FTD/TPI) plus oxaliplatin (Industriestrasse, Holzkirchen, Germany) sensitised microsatellite stable (MSS) metastatic colorectal cancer (mCRC) to anti-programmed cell death protein-1; the addition of oxaliplatin or bevacizumab (F Hoffmann- la ROCHE AG, Kaiseraugst, Switzerland) enhanced the antitumour effects of FTD/TPI.	Oxaliplatin	73-84	triosephosphate isomerase 1	Homo sapiens	376-379
34547581-1	2021	BACKGROUND: In preclinical studies trifluridine/tipiracil (FTD/TPI) plus oxaliplatin (Industriestrasse, Holzkirchen, Germany) sensitised microsatellite stable (MSS) metastatic colorectal cancer (mCRC) to anti-programmed cell death protein-1; the addition of oxaliplatin or bevacizumab (F Hoffmann- la ROCHE AG, Kaiseraugst, Switzerland) enhanced the antitumour effects of FTD/TPI.	Oxaliplatin	258-269	triosephosphate isomerase 1	Homo sapiens	376-379
34517794-10	2022	CONCLUSION: Benzothiazole, benzoxazole, benzimidazole, and sulfhydryl derivatives stand out as TIM inhibitors.	benzothiazole	12-25	triosephosphate isomerase 1	Homo sapiens	95-98
34517794-10	2022	CONCLUSION: Benzothiazole, benzoxazole, benzimidazole, and sulfhydryl derivatives stand out as TIM inhibitors.	Benzoxazoles	27-38	triosephosphate isomerase 1	Homo sapiens	95-98
34517794-10	2022	CONCLUSION: Benzothiazole, benzoxazole, benzimidazole, and sulfhydryl derivatives stand out as TIM inhibitors.	benzimidazole	40-53	triosephosphate isomerase 1	Homo sapiens	95-98
34517794-10	2022	CONCLUSION: Benzothiazole, benzoxazole, benzimidazole, and sulfhydryl derivatives stand out as TIM inhibitors.	Sulfhydryl Compounds	59-69	triosephosphate isomerase 1	Homo sapiens	95-98
34175675-2	2021	In the TAGS study, trifluridine/tipiracil (FTD/TPI) improved overall survival (OS) compared with placebo in heavily pre-treated patients.	Trifluridine	19-31	triosephosphate isomerase 1	Homo sapiens	47-50
34175675-2	2021	In the TAGS study, trifluridine/tipiracil (FTD/TPI) improved overall survival (OS) compared with placebo in heavily pre-treated patients.	tipiracil	32-41	triosephosphate isomerase 1	Homo sapiens	47-50
34096270-6	2021	In addition, TPI-An-Py can be applied to the detection of Cu2+ in real samples with satisfactory recoveries in the range of 100-112% in lake water and 98-101% in tap water.	Water	141-146	triosephosphate isomerase 1	Homo sapiens	13-16
34096270-6	2021	In addition, TPI-An-Py can be applied to the detection of Cu2+ in real samples with satisfactory recoveries in the range of 100-112% in lake water and 98-101% in tap water.	Water	166-171	triosephosphate isomerase 1	Homo sapiens	13-16
35474007-1	2022	INTRODUCTION: The RECOURSE trial demonstrated a modest benefit in overall survival (OS) for trifluridine/tipiracil (FTD/TPI) versus placebo in pretreated metastatic colorectal cancer (mCRC) patients.	Trifluridine	92-104	triosephosphate isomerase 1	Homo sapiens	120-123
34140692-4	2021	The nuclear acetate levels were controlled by glycolytic enzyme triosephosphate isomerase 1 (TPI1).	Acetates	12-19	triosephosphate isomerase 1	Homo sapiens	64-91
34140692-4	2021	The nuclear acetate levels were controlled by glycolytic enzyme triosephosphate isomerase 1 (TPI1).	Acetates	12-19	triosephosphate isomerase 1	Homo sapiens	93-97
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	Serine	122-125	triosephosphate isomerase 1	Homo sapiens	117-121
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	Dihydroxyacetone Phosphate	220-224	triosephosphate isomerase 1	Homo sapiens	117-121
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	Acetates	246-253	triosephosphate isomerase 1	Homo sapiens	117-121
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	Dihydroxyacetone Phosphate	275-279	triosephosphate isomerase 1	Homo sapiens	117-121
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	Dihydroxyacetone Phosphate	275-279	triosephosphate isomerase 1	Homo sapiens	168-172
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	Acetates	290-297	triosephosphate isomerase 1	Homo sapiens	117-121
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	Acetates	290-297	triosephosphate isomerase 1	Homo sapiens	168-172
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	1-acetyl-dhap	319-332	triosephosphate isomerase 1	Homo sapiens	117-121
34140692-5	2021	Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP.	1-acetyl-dhap	319-332	triosephosphate isomerase 1	Homo sapiens	168-172
35050435-3	2022	Therefore, we investigated the efficacy of trifluridine/tipiracil (FTD/TPI) in patients with esophageal cancer who are refractory or intolerant to 5-fluorouracil, platinum-containing drugs, and taxanes.	tipiracil	56-65	triosephosphate isomerase 1	Homo sapiens	71-74
35050435-3	2022	Therefore, we investigated the efficacy of trifluridine/tipiracil (FTD/TPI) in patients with esophageal cancer who are refractory or intolerant to 5-fluorouracil, platinum-containing drugs, and taxanes.	Taxoids	194-201	triosephosphate isomerase 1	Homo sapiens	71-74
35474007-1	2022	INTRODUCTION: The RECOURSE trial demonstrated a modest benefit in overall survival (OS) for trifluridine/tipiracil (FTD/TPI) versus placebo in pretreated metastatic colorectal cancer (mCRC) patients.	tipiracil	105-114	triosephosphate isomerase 1	Homo sapiens	120-123
34997449-1	2022	BACKGROUND: Trifluridine and tipiracil (FTD/TPI) demonstrated survival benefit vs placebo and manageable safety in previously treated patients with metastatic gastric/gastroesophageal junction cancer (mGC/GEJC) in the randomized, placebo-controlled, phase 3 TAGS study.	tipiracil	29-38	triosephosphate isomerase 1	Homo sapiens	44-47
35182029-2	2022	Currently, molecular targeting agents and late-line treatment with regorafenib and trifluridine/tipiracil (FTD/TPI) are available.	Trifluridine	83-95	triosephosphate isomerase 1	Homo sapiens	111-114
35182029-2	2022	Currently, molecular targeting agents and late-line treatment with regorafenib and trifluridine/tipiracil (FTD/TPI) are available.	tipiracil	96-105	triosephosphate isomerase 1	Homo sapiens	111-114
35315486-0	2022	Itavastatin and Resveratrol increase triosephosphate isomerase protein (TPI) in a newly identified variant, TPIQ181P, that confers TPI deficiency.	Resveratrol	16-27	triosephosphate isomerase 1	Homo sapiens	72-75
35278170-1	2022	BACKGROUND: Trifluridine/tipiracil (FTD/TPI) and irinotecan are treatment options for heavily pretreated patients with advanced gastric cancer, but their efficacies are limited.	Trifluridine	12-24	triosephosphate isomerase 1	Homo sapiens	40-43
35278170-1	2022	BACKGROUND: Trifluridine/tipiracil (FTD/TPI) and irinotecan are treatment options for heavily pretreated patients with advanced gastric cancer, but their efficacies are limited.	tipiracil	25-34	triosephosphate isomerase 1	Homo sapiens	40-43
3339589-3	1988	All three compounds caused the accumulation of fructose 1,6-bisphosphate and dihydroxyacetone phosphate from fructose but not from glycerol which led to the conclusion that inhibition of triosephosphate isomerase was also associated with the anti-glycolytic action of (S)-3-chlorolactaldehyde.	fructose-1,6-diphosphate	47-72	triosephosphate isomerase 1	Homo sapiens	187-212
35152873-5	2022	(v) In addition, an extensive examination of the effects of clozapine on non-cardiac cellular proteins demonstrate that clozapine can impair enzymes involved in cellular metabolism such as pyruvate kinase, mitochondrial malate dehydrogenase and other proteins including alpha-enolase, triosephosphate isomerase and cofilin, that might explain clozapine-induced reductions in myocardial energy generation for cell viability as well as contractile function.	Clozapine	60-69	triosephosphate isomerase 1	Homo sapiens	285-310
35152873-5	2022	(v) In addition, an extensive examination of the effects of clozapine on non-cardiac cellular proteins demonstrate that clozapine can impair enzymes involved in cellular metabolism such as pyruvate kinase, mitochondrial malate dehydrogenase and other proteins including alpha-enolase, triosephosphate isomerase and cofilin, that might explain clozapine-induced reductions in myocardial energy generation for cell viability as well as contractile function.	Clozapine	120-129	triosephosphate isomerase 1	Homo sapiens	285-310
35149429-1	2022	INTRODUCTION: Trifluridine/tipiracil (FTD/TPI) improved both overall and progression-free survival (OS, PFS) of patients with pre-treated metastatic colorectal cancer (mCRC) in the pivotal phase III RECOURSE trial.	Trifluridine	14-26	triosephosphate isomerase 1	Homo sapiens	42-45
35149429-1	2022	INTRODUCTION: Trifluridine/tipiracil (FTD/TPI) improved both overall and progression-free survival (OS, PFS) of patients with pre-treated metastatic colorectal cancer (mCRC) in the pivotal phase III RECOURSE trial.	tipiracil	27-36	triosephosphate isomerase 1	Homo sapiens	42-45
3365378-10	1988	These results show that the reaction catalyzed by the wild-type triosephosphate isomerase is limited by the rate at which glyceraldehyde phosphate encounters, or departs from, the active site.	Glyceraldehyde 3-Phosphate	122-146	triosephosphate isomerase 1	Homo sapiens	64-89
35246510-5	2022	TPI1 is a glycolytic enzyme that interconverts dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP).	Dihydroxyacetone Phosphate	47-73	triosephosphate isomerase 1	Homo sapiens	0-4
35246510-5	2022	TPI1 is a glycolytic enzyme that interconverts dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP).	Dihydroxyacetone Phosphate	75-79	triosephosphate isomerase 1	Homo sapiens	0-4
35246510-5	2022	TPI1 is a glycolytic enzyme that interconverts dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP).	Glyceraldehyde 3-Phosphate	84-110	triosephosphate isomerase 1	Homo sapiens	0-4
35246510-10	2022	Moreover, nuclear translocation of TPI1 is induced by extracellular stress (such as chemotherapy agents and peroxide), which facilitates the chemoresistance of cancer cells.	Peroxides	108-116	triosephosphate isomerase 1	Homo sapiens	35-39
35007726-3	2022	Therefore, a new class of boronic acid derivate was developed to elucidate the possible mechanistic link between PKM2 activation and TPI1 activity, which has a significant role in the redox balance in cancer.	Boronic Acids	26-38	triosephosphate isomerase 1	Homo sapiens	133-137
35118741-0	2022	Daidzin inhibits hepatocellular carcinoma survival by interfering with the glycolytic/gluconeogenic pathway through downregulation of TPI1.	daidzin	0-7	triosephosphate isomerase 1	Homo sapiens	134-138
35118741-10	2022	Bioinformatic analysis identified TPI1, a gene in the glycolysis pathway with prognostic value for hepatocellular carcinoma (HCC), and DDZ treatment downregulated this gene.	daidzin	135-138	triosephosphate isomerase 1	Homo sapiens	34-38
35118741-12	2022	This study shows that DDZ interfered with the survival and migration of hepatocellular carcinoma cells, likely via TPI1 and the gluconeogenesis pathway.	daidzin	22-25	triosephosphate isomerase 1	Homo sapiens	115-119
35049438-13	2022	At the same time, after alpha-solanine treatment, the expression of the energy metabolism pathway-related proteins including GPI, ALDOA, TPI1, PKLR, LDHA and ALDH3 was reduced.	alpha-solanine	24-38	triosephosphate isomerase 1	Homo sapiens	137-141
3339589-3	1988	All three compounds caused the accumulation of fructose 1,6-bisphosphate and dihydroxyacetone phosphate from fructose but not from glycerol which led to the conclusion that inhibition of triosephosphate isomerase was also associated with the anti-glycolytic action of (S)-3-chlorolactaldehyde.	Dihydroxyacetone Phosphate	77-103	triosephosphate isomerase 1	Homo sapiens	187-212
3339589-3	1988	All three compounds caused the accumulation of fructose 1,6-bisphosphate and dihydroxyacetone phosphate from fructose but not from glycerol which led to the conclusion that inhibition of triosephosphate isomerase was also associated with the anti-glycolytic action of (S)-3-chlorolactaldehyde.	Fructose	47-55	triosephosphate isomerase 1	Homo sapiens	187-212
3339589-3	1988	All three compounds caused the accumulation of fructose 1,6-bisphosphate and dihydroxyacetone phosphate from fructose but not from glycerol which led to the conclusion that inhibition of triosephosphate isomerase was also associated with the anti-glycolytic action of (S)-3-chlorolactaldehyde.	3-chlorolactaldehyde	268-292	triosephosphate isomerase 1	Homo sapiens	187-212
3427057-1	1987	Triosephosphate isomerase has been shown to exist in two unliganded forms, one of which binds and isomerizes (R)-glyceraldehyde 3-phosphate and the other of which binds and isomerizes dihydroxyacetone 3-phosphate.	(r)-glyceraldehyde 3-phosphate	109-139	triosephosphate isomerase 1	Homo sapiens	0-25
3427057-1	1987	Triosephosphate isomerase has been shown to exist in two unliganded forms, one of which binds and isomerizes (R)-glyceraldehyde 3-phosphate and the other of which binds and isomerizes dihydroxyacetone 3-phosphate.	Dihydroxyacetone Phosphate	184-212	triosephosphate isomerase 1	Homo sapiens	0-25
3740839-1	1986	The effects of pH, temperature, buffer ion, ionic strength, protein concentration, and substrate on the rates of specific, spontaneous deamidations of Asn-15 and Asn-71 of human triosephosphate isomerase were examined.	asn-15	151-157	triosephosphate isomerase 1	Homo sapiens	178-203
3606593-0	1987	Inhibition of triosephosphate isomerase in boar spermatozoa by (S)-3-chlorolactaldehyde.	3-chlorolactaldehyde	63-87	triosephosphate isomerase 1	Homo sapiens	14-39
3606593-3	1987	Examination of enzyme activities in mature boar spermatozoa incubated with 3-chloro-1-hydroxyacetone, which is metabolised in vitro to (S)-3-chlorolactaldehyde, confirmed that glyceraldehyde 3-phosphate dehydrogenase and triosephosphate isomerase were both inhibited to equivalent degrees by this metabolite.	1-hydroxy-3-chloroacetone	75-100	triosephosphate isomerase 1	Homo sapiens	221-246
3619568-2	1987	Triose phosphate isomerase catalyses dihydroxyacetone phosphate to glyceraldehyde 3 phosphate isomerism.	Dihydroxyacetone Phosphate	37-63	triosephosphate isomerase 1	Homo sapiens	0-26
3619568-2	1987	Triose phosphate isomerase catalyses dihydroxyacetone phosphate to glyceraldehyde 3 phosphate isomerism.	Glyceraldehyde 3-Phosphate	67-93	triosephosphate isomerase 1	Homo sapiens	0-26
2876430-4	1986	The importance of glutamate-104 to enzyme structure and function is implicated by its conservation in the TPI protein of all species that have been characterized to date.	Glutamic Acid	18-27	triosephosphate isomerase 1	Homo sapiens	106-109
2876430-5	1986	The glutamate-to-aspartate substitution results in a thermolabile enzyme as demonstrated by assays of TPI activity in cultured fibroblasts of each patient and cultured Chinese hamster ovary (CHO) cells that were stably transformed with the mutant alleles.	Glutamic Acid	4-13	triosephosphate isomerase 1	Homo sapiens	102-105
2876430-5	1986	The glutamate-to-aspartate substitution results in a thermolabile enzyme as demonstrated by assays of TPI activity in cultured fibroblasts of each patient and cultured Chinese hamster ovary (CHO) cells that were stably transformed with the mutant alleles.	Aspartic Acid	17-26	triosephosphate isomerase 1	Homo sapiens	102-105
3740839-1	1986	The effects of pH, temperature, buffer ion, ionic strength, protein concentration, and substrate on the rates of specific, spontaneous deamidations of Asn-15 and Asn-71 of human triosephosphate isomerase were examined.	Asparagine	151-154	triosephosphate isomerase 1	Homo sapiens	178-203
3964229-2	1986	TPI 2HR1, an anodally migrating variant, was less stable than normal in guanidine denaturation and thermodenaturation tests, although it exhibited normal kinetic properties.	Guanidine	72-81	triosephosphate isomerase 1	Homo sapiens	0-3
2990063-5	1985	The stimulation by thrombin of 32P-labelled human platelets induced about 30% decrease in 32P-TPI and about 220% increase in 32P-PA at the first 10 sec.	Phosphorus-32	31-34	triosephosphate isomerase 1	Homo sapiens	94-97
2417997-4	1985	The dihydroxyacetone phosphate is reversibly converted into D-glyceraldehyde-3-phosphate by exogenous and endogenous triose phosphate isomerase.	Dihydroxyacetone Phosphate	4-30	triosephosphate isomerase 1	Homo sapiens	117-143
2417997-4	1985	The dihydroxyacetone phosphate is reversibly converted into D-glyceraldehyde-3-phosphate by exogenous and endogenous triose phosphate isomerase.	d-glyceraldehyde 3-phosphate	60-88	triosephosphate isomerase 1	Homo sapiens	117-143
2999166-4	1985	While it has been suggested that an increased synthesis of phosphatidylinositol (PI) is coupled to the stimulation of DPI and TPI synthesis, we found that thrombin stimulated an early synthesis PI but EGF did not.	Phosphatidylinositols	59-79	triosephosphate isomerase 1	Homo sapiens	126-129
6434534-6	1984	The primary structure of human triosephosphate isomerase is constructed from the alignment of the tryptic peptides with the analysis of the overlapping chymotryptic peptides.	Peptides	106-114	triosephosphate isomerase 1	Homo sapiens	31-56
3004131-2	1985	The enzyme hydrolyzed endogenous substrates in the order DPI greater than TPI greater than PI in a Ca2+-dependent manner.	3-aminodiphenyleneiodium	57-60	triosephosphate isomerase 1	Homo sapiens	74-77
3995002-0	1985	Reaction of triosephosphate isomerase with L-glyceraldehyde 3-phosphate and triose 1,2-enediol 3-phosphate.	L-glyceraldehyde 3-phosphate	43-71	triosephosphate isomerase 1	Homo sapiens	12-37
3995002-0	1985	Reaction of triosephosphate isomerase with L-glyceraldehyde 3-phosphate and triose 1,2-enediol 3-phosphate.	triose 1,2-enediol 3-phosphate	76-106	triosephosphate isomerase 1	Homo sapiens	12-37
3995002-1	1985	Triosephosphate isomerase catalyzes the isomerization and/or racemization reactions of L-glyceraldehyde 3-phosphate (LGAP), the enantiomer of the physiological substrate.	L-glyceraldehyde 3-phosphate	87-115	triosephosphate isomerase 1	Homo sapiens	0-25
3995002-6	1985	Triosephosphate isomerase catalysis of the protonation of triose 1,2-enediol 3-phosphate was expected because of the strong evidence supporting an enediol reaction intermediate for the overall reaction catalyzed by isomerase.	1,2-enediol 3-phosphate	65-88	triosephosphate isomerase 1	Homo sapiens	0-25
2984954-1	1985	A method that allows the quantification of phosphatidylinositol (PI), phosphatidylinositol 4-phosphate (DPI), and phosphatidylinositol 4,5-biphosphate (TPI) on a nanomolar scale is presented.	Phosphatidylinositol 4,5-Diphosphate	114-150	triosephosphate isomerase 1	Homo sapiens	152-155
4065896-10	1985	Substantial increases of red cell dihydroxyacetone phosphate and of fructose 1,6-diphosphate, normal Km of TPI for glyceraldehyde phosphate, and thermoinstability of the enzyme were found.	Glyceraldehyde 3-Phosphate	115-139	triosephosphate isomerase 1	Homo sapiens	107-110
6320736-5	1984	TPI alone, or in mixture with PI, was a poor substrate for phospholipase C. Increasing the TPI/PI ratio from 0 to 0.21, on the other hand, inhibited both PI degradation (greater than or equal to 95%) and overall formation of 1,2-diacylglycerol (greater than or equal to 82%).	1,2-diacylglycerol	225-243	triosephosphate isomerase 1	Homo sapiens	91-94
6320736-9	1984	Analysis of phospholipids from unstimulated human platelets from five different donors revealed DPI/PI and TPI/PI ratios of 0.42 and 0.16, respectively.	Phospholipids	12-25	triosephosphate isomerase 1	Homo sapiens	107-110
6320736-11	1984	Changes in 33P-prelabeled phospholipids of intact platelets upon stimulation with thrombin indicated a transient decline in 33P label of both TPI and DPI (15 s) followed by an increase in [33P]phosphatidic acid but no change in [33P]PI.	Phosphorus-33	11-14	triosephosphate isomerase 1	Homo sapiens	142-145
6320736-11	1984	Changes in 33P-prelabeled phospholipids of intact platelets upon stimulation with thrombin indicated a transient decline in 33P label of both TPI and DPI (15 s) followed by an increase in [33P]phosphatidic acid but no change in [33P]PI.	Phospholipids	26-39	triosephosphate isomerase 1	Homo sapiens	142-145
6320736-11	1984	Changes in 33P-prelabeled phospholipids of intact platelets upon stimulation with thrombin indicated a transient decline in 33P label of both TPI and DPI (15 s) followed by an increase in [33P]phosphatidic acid but no change in [33P]PI.	Phosphorus-33	124-127	triosephosphate isomerase 1	Homo sapiens	142-145
6320736-11	1984	Changes in 33P-prelabeled phospholipids of intact platelets upon stimulation with thrombin indicated a transient decline in 33P label of both TPI and DPI (15 s) followed by an increase in [33P]phosphatidic acid but no change in [33P]PI.	Phosphorus-33	124-127	triosephosphate isomerase 1	Homo sapiens	142-145
6320736-11	1984	Changes in 33P-prelabeled phospholipids of intact platelets upon stimulation with thrombin indicated a transient decline in 33P label of both TPI and DPI (15 s) followed by an increase in [33P]phosphatidic acid but no change in [33P]PI.	Phosphorus-33	124-127	triosephosphate isomerase 1	Homo sapiens	142-145
6320736-13	1984	Furthermore, the results suggest that in human platelets TPI may serve as modulator for the formation of 1,2-diacylglycerol from inositol phospholipids.	1,2-diacylglycerol	105-123	triosephosphate isomerase 1	Homo sapiens	57-60
6320736-13	1984	Furthermore, the results suggest that in human platelets TPI may serve as modulator for the formation of 1,2-diacylglycerol from inositol phospholipids.	Phosphatidylinositols	129-151	triosephosphate isomerase 1	Homo sapiens	57-60
438213-4	1979	The alkyl ether lipid was degraded, and the DHAP backbone isolated as glycerol, converted to DHAP via glycerol 3-phosphate and treated with either aldolase or triose phosphate isomerase.	alkyl ether lipid	4-21	triosephosphate isomerase 1	Homo sapiens	159-185
6500570-3	1984	A total of 15,387 individuals living in Hiroshima and Nagasaki, of whom 10,864 are unrelated, were examined for erythrocyte triosephosphate isomerase (TPI) by starch gel electrophoresis using TEMM buffer, pH 7.4.	Starch	159-165	triosephosphate isomerase 1	Homo sapiens	151-154
6301436-2	1983	The addition of thrombin to [3H]glycerol-labeled platelets induced an initial loss and a subsequent increase of the radioactivity in phosphatidylinositol-4,5-bisphosphate (TPI) without any significant change in phosphatidylinositol-4-phosphate (DPI).	[3h]glycerol	28-40	triosephosphate isomerase 1	Homo sapiens	172-175
6301436-2	1983	The addition of thrombin to [3H]glycerol-labeled platelets induced an initial loss and a subsequent increase of the radioactivity in phosphatidylinositol-4,5-bisphosphate (TPI) without any significant change in phosphatidylinositol-4-phosphate (DPI).	Phosphatidylinositol 4,5-Diphosphate	133-170	triosephosphate isomerase 1	Homo sapiens	172-175
6301436-3	1983	A marked enhancement of [32P]Pi incorporation into TPI occurred in parallel with an increase in this lipid content, which was accompanied with a conccurent decrease in phosphatidylinositol (PI).	Phosphorus-32	25-28	triosephosphate isomerase 1	Homo sapiens	51-54
6301436-3	1983	A marked enhancement of [32P]Pi incorporation into TPI occurred in parallel with an increase in this lipid content, which was accompanied with a conccurent decrease in phosphatidylinositol (PI).	Phosphatidylinositols	168-188	triosephosphate isomerase 1	Homo sapiens	51-54
6301436-4	1983	The rate of this subsequent increase in TPI was smaller than that observed in [3H]arachidonic acid-labeled platelets, suggesting that formed TPI in activated platelets may contain much greater amount of arachidonate than preexisting TPI in resting platelets.	Arachidonic Acid	203-215	triosephosphate isomerase 1	Homo sapiens	141-144
6301436-4	1983	The rate of this subsequent increase in TPI was smaller than that observed in [3H]arachidonic acid-labeled platelets, suggesting that formed TPI in activated platelets may contain much greater amount of arachidonate than preexisting TPI in resting platelets.	Arachidonic Acid	203-215	triosephosphate isomerase 1	Homo sapiens	141-144
6301436-5	1983	These data indicate that thrombin causes a rapid change in TPI metabolism (initial degradation of preexisting TPI and subsequent production of arachidonate-rich TPI), which might be a primary candidate to modulate thrombin-induced function in human platelets.	Arachidonic Acid	143-155	triosephosphate isomerase 1	Homo sapiens	59-62
6269709-11	1981	It is concluded that the structure-activity relationship on TPI/PA formation correlates with a similar relationship obtained on excessive grooming behavior in vivo.	Protactinium	64-66	triosephosphate isomerase 1	Homo sapiens	60-63
6266033-15	1981	All experimental and clinical studies agree and insist on the fact that penicillin therapy must be given early in the infection, at a prolonged and high dose; results having to be estimated on the serological answers, especially with repeated TPI and FTA tests.	Penicillins	72-82	triosephosphate isomerase 1	Homo sapiens	243-246
7356939-1	1980	The infrared spectrum of dihydroxyacetone phosphate bound to triosephosphate isomerase has been measured.	Dihydroxyacetone Phosphate	25-51	triosephosphate isomerase 1	Homo sapiens	61-86
7044470-5	1982	Only 0.05% of patients, in whom repeat tests confirmed a positive TPHA but a negative FTA-ABS result, benefited from a TPI test.	Flutamide	86-89	triosephosphate isomerase 1	Homo sapiens	119-122
6446532-4	1980	The dihydroxyacetone phosphate is reversibly converted into D-glyceraldehyde-3-phosphate by exogenous and endogenous triosephosphate isomerase.	Dihydroxyacetone Phosphate	4-30	triosephosphate isomerase 1	Homo sapiens	117-142
6446532-4	1980	The dihydroxyacetone phosphate is reversibly converted into D-glyceraldehyde-3-phosphate by exogenous and endogenous triosephosphate isomerase.	d-glyceraldehyde 3-phosphate	60-88	triosephosphate isomerase 1	Homo sapiens	117-142
438213-4	1979	The alkyl ether lipid was degraded, and the DHAP backbone isolated as glycerol, converted to DHAP via glycerol 3-phosphate and treated with either aldolase or triose phosphate isomerase.	Dihydroxyacetone Phosphate	44-48	triosephosphate isomerase 1	Homo sapiens	159-185
438213-4	1979	The alkyl ether lipid was degraded, and the DHAP backbone isolated as glycerol, converted to DHAP via glycerol 3-phosphate and treated with either aldolase or triose phosphate isomerase.	Glycerol	70-78	triosephosphate isomerase 1	Homo sapiens	159-185
438213-4	1979	The alkyl ether lipid was degraded, and the DHAP backbone isolated as glycerol, converted to DHAP via glycerol 3-phosphate and treated with either aldolase or triose phosphate isomerase.	Dihydroxyacetone Phosphate	93-97	triosephosphate isomerase 1	Homo sapiens	159-185
9762143-3	1978	The utilization of inorganic pyrophosphate is measured by coupling the production of fructose-1,6-bisphosphate with the oxidation of NADH using fructose-bisphosphate aldolase (EC 4.1.2.13), triosephosphate isomerase (EC 5.3.1.1), and glycerol-3-phosphate dehydrogenase (NAD+)(EC 1.1.1.8).	inorganic pyrophosphate	19-42	triosephosphate isomerase 1	Homo sapiens	190-215
9762143-3	1978	The utilization of inorganic pyrophosphate is measured by coupling the production of fructose-1,6-bisphosphate with the oxidation of NADH using fructose-bisphosphate aldolase (EC 4.1.2.13), triosephosphate isomerase (EC 5.3.1.1), and glycerol-3-phosphate dehydrogenase (NAD+)(EC 1.1.1.8).	fructose-1,6-diphosphate	85-110	triosephosphate isomerase 1	Homo sapiens	190-215
9762143-3	1978	The utilization of inorganic pyrophosphate is measured by coupling the production of fructose-1,6-bisphosphate with the oxidation of NADH using fructose-bisphosphate aldolase (EC 4.1.2.13), triosephosphate isomerase (EC 5.3.1.1), and glycerol-3-phosphate dehydrogenase (NAD+)(EC 1.1.1.8).	NAD	133-137	triosephosphate isomerase 1	Homo sapiens	190-215
29623-0	1978	The form of 2-phosphoglycollic acid bound by triosephosphate isomerase.	2-phosphoglycollic acid	12-35	triosephosphate isomerase 1	Homo sapiens	45-70
738390-1	1978	Preparations of the enzymes glyceraldehyde-3-phosphate dehydrogenase and triosephosphate isomerase are shown to be inhibited by alpha-chlorohydrin phosphate (II) in a competitive and non-competitive manner, respectively.	alpha-chlorohydrin phosphate	128-156	triosephosphate isomerase 1	Homo sapiens	73-98
629780-12	1978	After incubation with 3mm-alpha-chlorohydrin, glyceraldehyde 3-phosphate dehydrogenase and triose phosphate isomerase activities were decreased by approx.	3mm-alpha-chlorohydrin	22-44	triosephosphate isomerase 1	Homo sapiens	91-117
629780-26	1978	An unknown metabolic product of alpha-chlorohydrin is suggested to inhibit glyceraldehyde 3-phosphate dehydrogenase and triose phosphate isomerase of spermatozoa.	alpha-Chlorohydrin	32-50	triosephosphate isomerase 1	Homo sapiens	120-146
669702-4	1978	Zymosan-stimulated superoxide radical (O-.2) formation, not previously studied in TPI-deficient granulocytes, was also within normal limits.	Zymosan	0-7	triosephosphate isomerase 1	Homo sapiens	82-85
669702-5	1978	Starchgel electrophoresis of TPI in both erythrocytes and leukocytes of the proposita and her parents was normal.	starchgel	0-9	triosephosphate isomerase 1	Homo sapiens	29-32
902906-0	1977	Triose phosphate isomerase: interactions with ligands studied by [31P]phosphorus nuclear magnetic resonance [proceedings].	ET bromodomain inhibitor	66-69	triosephosphate isomerase 1	Homo sapiens	0-26
889785-0	1977	Phosphorus-31 nuclear magnetic resonance of dihydroxyacetone phosphate in the presence of triosephosphate isomerase.	Phosphorus	0-10	triosephosphate isomerase 1	Homo sapiens	90-115
889785-0	1977	Phosphorus-31 nuclear magnetic resonance of dihydroxyacetone phosphate in the presence of triosephosphate isomerase.	Dihydroxyacetone Phosphate	44-70	triosephosphate isomerase 1	Homo sapiens	90-115
902906-0	1977	Triose phosphate isomerase: interactions with ligands studied by [31P]phosphorus nuclear magnetic resonance [proceedings].	Phosphorus	70-80	triosephosphate isomerase 1	Homo sapiens	0-26
999833-0	1976	Energetics of triosephosphate isomerase: the fate of the 1(R)-3H label of tritiated dihydroxyacetone phsophate in the isomerase reaction.	1(r)-3h	57-64	triosephosphate isomerase 1	Homo sapiens	14-39
838535-0	1977	A note on the two-dimensional representation of hydrogen bonding scheme in triose phosphate isomerase.	Hydrogen	48-56	triosephosphate isomerase 1	Homo sapiens	75-101
838535-1	1977	When the backbone hydrogen bonding scheme of the protein triose phosphate isomerase is represented in the two-dimensional map where the donor residue number (i) is taken along the x-axis and the acceptor residue number (j) is taken along the y-axis, the (i, j)-map shows a characteristic pattern of (beta alpha)8-super-secondary structure.	Hydrogen	18-26	triosephosphate isomerase 1	Homo sapiens	57-83
999835-0	1976	Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate glyceraldehyde 3-phosphate and in product.	Glyceraldehyde 3-Phosphate	88-114	triosephosphate isomerase 1	Homo sapiens	14-39
999835-1	1976	When the isomerization of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and the product become labeled.	d-glyceraldehyde 3-phosphate	26-54	triosephosphate isomerase 1	Homo sapiens	101-126
999835-1	1976	When the isomerization of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and the product become labeled.	Dihydroxyacetone Phosphate	58-84	triosephosphate isomerase 1	Homo sapiens	101-126
999833-0	1976	Energetics of triosephosphate isomerase: the fate of the 1(R)-3H label of tritiated dihydroxyacetone phsophate in the isomerase reaction.	tritiated dihydroxyacetone phsophate	74-110	triosephosphate isomerase 1	Homo sapiens	14-39
999835-1	1976	When the isomerization of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and the product become labeled.	Water	140-145	triosephosphate isomerase 1	Homo sapiens	101-126
999836-0	1976	Energetics of triosephosphate isomerase: deuterium isotope effects in the enzyme-catalyzed reaction.	Deuterium	41-50	triosephosphate isomerase 1	Homo sapiens	14-39
999836-1	1976	The effect of isotopic substitution of the specifically labilized hydrogen in the substrates of triosephosphate isomerase on the steady-state rates of the enzyme-catalyzed reaction has been examined.	Hydrogen	66-74	triosephosphate isomerase 1	Homo sapiens	96-121
999837-0	1976	Energetics of triosephosphate isomerase: the nature of the proton transfer between the catalytic base and solvent water.	Water	114-119	triosephosphate isomerase 1	Homo sapiens	14-39
999837-1	1976	The isomerization of specifically deuterium-labeled [1(R)-2H5dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate, catalyzed by the enzyme triosephosphate isomerase, has been studied.	Deuterium	34-43	triosephosphate isomerase 1	Homo sapiens	145-170
999837-1	1976	The isomerization of specifically deuterium-labeled [1(R)-2H5dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate, catalyzed by the enzyme triosephosphate isomerase, has been studied.	[1(r)-2h5dihydroxyacetone phosphate	52-87	triosephosphate isomerase 1	Homo sapiens	145-170
999837-1	1976	The isomerization of specifically deuterium-labeled [1(R)-2H5dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate, catalyzed by the enzyme triosephosphate isomerase, has been studied.	d-glyceraldehyde 3-phosphate	91-119	triosephosphate isomerase 1	Homo sapiens	145-170
999838-1	1976	The experimental results on the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate catalyzed by triosephosphate isomerase that are presented in the previous five papers are here collected and analyzed according to the theory presented in the first paper (Albery, W.J., Knowles, J.R. (1976), Biochemistry 15, the first of eight papers in a series in this issue).	Dihydroxyacetone Phosphate	51-77	triosephosphate isomerase 1	Homo sapiens	124-149
999838-1	1976	The experimental results on the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate catalyzed by triosephosphate isomerase that are presented in the previous five papers are here collected and analyzed according to the theory presented in the first paper (Albery, W.J., Knowles, J.R. (1976), Biochemistry 15, the first of eight papers in a series in this issue).	d-glyceraldehyde 3-phosphate	82-110	triosephosphate isomerase 1	Homo sapiens	124-149
613905-2	1977	In 1973, TPI carried out a world-wide survey to ascertain the data available on aflatoxin contamination of food and feedingstuffs (JONES, 1975).	Aflatoxins	80-89	triosephosphate isomerase 1	Homo sapiens	9-12
999834-0	1976	Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product.	Tritium	67-74	triosephosphate isomerase 1	Homo sapiens	14-39
999834-0	1976	Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product.	Dihydroxyacetone Phosphate	88-114	triosephosphate isomerase 1	Homo sapiens	14-39
999834-1	1976	When the isomerization of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and product become labeled.	Dihydroxyacetone Phosphate	26-52	triosephosphate isomerase 1	Homo sapiens	101-126
999834-1	1976	When the isomerization of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and product become labeled.	d-glyceraldehyde 3-phosphate	56-84	triosephosphate isomerase 1	Homo sapiens	101-126
999834-1	1976	When the isomerization of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and product become labeled.	Water	140-145	triosephosphate isomerase 1	Homo sapiens	101-126
999835-0	1976	Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate glyceraldehyde 3-phosphate and in product.	Tritium	67-74	triosephosphate isomerase 1	Homo sapiens	14-39
1017253-5	1976	TPI and MHA-TP tests appear helpful in detecting false-positive FTA-ABS results.	fta-abs	64-71	triosephosphate isomerase 1	Homo sapiens	0-3
1105415-2	1975	The percentages of agreement seen both in comparison of THPA with the TPI (94,5 p.cent) and the FTA abs test (97 p.cent) demonstrate its high degree of specificity and sensitivity.	2-methyl-4-carboxy-5-hydroxy-3,4,5,6-tetrahydropyrimidine	56-60	triosephosphate isomerase 1	Homo sapiens	70-73
1182110-1	1975	Tritiated sodium borohydride was used to reduce the substrates of triosephosphate isomerase in the presence of the enzyme, and the mixture of the four possible products (D-[1(R)-3H]; D-[1(S)-3H]-; D-[2-3H]-, and L-[2-3H]glycerol 3-phosphate) was analyzed.	tritiated sodium borohydride	0-28	triosephosphate isomerase 1	Homo sapiens	66-91
1182110-1	1975	Tritiated sodium borohydride was used to reduce the substrates of triosephosphate isomerase in the presence of the enzyme, and the mixture of the four possible products (D-[1(R)-3H]; D-[1(S)-3H]-; D-[2-3H]-, and L-[2-3H]glycerol 3-phosphate) was analyzed.	d-[1(r)-3h	170-180	triosephosphate isomerase 1	Homo sapiens	66-91
1182110-1	1975	Tritiated sodium borohydride was used to reduce the substrates of triosephosphate isomerase in the presence of the enzyme, and the mixture of the four possible products (D-[1(R)-3H]; D-[1(S)-3H]-; D-[2-3H]-, and L-[2-3H]glycerol 3-phosphate) was analyzed.	d-[1(s)-3h	183-193	triosephosphate isomerase 1	Homo sapiens	66-91
1182110-1	1975	Tritiated sodium borohydride was used to reduce the substrates of triosephosphate isomerase in the presence of the enzyme, and the mixture of the four possible products (D-[1(R)-3H]; D-[1(S)-3H]-; D-[2-3H]-, and L-[2-3H]glycerol 3-phosphate) was analyzed.	d-[2-3h]	197-205	triosephosphate isomerase 1	Homo sapiens	66-91
1182110-1	1975	Tritiated sodium borohydride was used to reduce the substrates of triosephosphate isomerase in the presence of the enzyme, and the mixture of the four possible products (D-[1(R)-3H]; D-[1(S)-3H]-; D-[2-3H]-, and L-[2-3H]glycerol 3-phosphate) was analyzed.	l-[2-3h]glycerol 3-phosphate	212-240	triosephosphate isomerase 1	Homo sapiens	66-91
5461000-0	1970	Changes in absorption spectrum and crystal structure of triose phosphate isomerase brought about by 2-phosphoglycollate, a potential transition state analogue.	2-phosphoglycollate	100-119	triosephosphate isomerase 1	Homo sapiens	56-82
16742819-2	1973	The concerted actions of glucose phosphate isomerase, phosphofructokinase, aldolase and triose phosphate isomerase catalysed the loss of (3)H from [5-(3)H,U-(14)C]glucose 6-phosphate.	Glucose-6-Phosphate	163-182	triosephosphate isomerase 1	Homo sapiens	88-114
4330197-7	1971	Keto-dihydroxyacetone phosphate is the primary reactive species in the reactions catalysed by alpha-glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase.	keto-dihydroxyacetone phosphate	0-31	triosephosphate isomerase 1	Homo sapiens	145-171
4375983-1	1974	In the presence of triose phosphate isomerase, the substrate dihydroxyacetone phosphate is reduced stereoselectively by NaBH(4).	Dihydroxyacetone Phosphate	61-87	triosephosphate isomerase 1	Homo sapiens	19-45
4375983-1	1974	In the presence of triose phosphate isomerase, the substrate dihydroxyacetone phosphate is reduced stereoselectively by NaBH(4).	sodium borohydride	120-124	triosephosphate isomerase 1	Homo sapiens	19-45
5428408-0	1970	Identification of site in triose phosphate isomerase labelled by glycidol phosphate.	glycidol phosphate	65-83	triosephosphate isomerase 1	Homo sapiens	26-52
13058935-2	1953	The occurrence of aldolase and triosephosphate isomerase in Aspergillus species and their relationship to kojic acid biosynthesis.	kojic acid	106-116	triosephosphate isomerase 1	Homo sapiens	31-56
4309306-0	1969	The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase.	d-glyceraldehyde 3-phosphate	29-57	triosephosphate isomerase 1	Homo sapiens	137-163
4309306-6	1969	Aldolase and triose phosphate isomerase both liberate d-glyceraldehyde 3-phosphate as the aldehyde.	d-glyceraldehyde 3-phosphate	54-82	triosephosphate isomerase 1	Homo sapiens	13-39
4309306-6	1969	Aldolase and triose phosphate isomerase both liberate d-glyceraldehyde 3-phosphate as the aldehyde.	Aldehydes	62-70	triosephosphate isomerase 1	Homo sapiens	13-39
14052778-0	1962	APPLICATION OF THE OIL TECHNIQUE IN THE ONE-DAY TPI TEST WITH LYSOZYME.	Oils	19-22	triosephosphate isomerase 1	Homo sapiens	48-51
33827020-8	2021	The decrease of TOC and UV-254 happened in HPO-A, HPO-N and TPI-A organic substance of EPS (mainly contained in TB-EPS fraction) indicated that the destruction of hydrophobic organic matter of EPS would stimulate the release of bound water, which was beneficial to dewater sludge.	exophthalmos producing substance	87-90	triosephosphate isomerase 1	Homo sapiens	60-63
33900864-1	2022	OBJECTIVE: To evaluate the cost-effectiveness of trifluridine/tipiracil (FTD/TPI) compared with best supportive care (BSC) for the treatment of patients with metastatic gastric cancer (mGC), including gastroesophageal junction adenocarcinoma (GEJ), who have received at least two prior therapies for metastatic disease and are eligible for third-line treatment, in Greece.	Trifluridine	49-61	triosephosphate isomerase 1	Homo sapiens	77-80
33569986-1	2021	Trifluridine/tipiracil (FTD/TPI) is an orally active formulation of trifluridine, a thymidine-based nucleoside analog, and tipiracil hydrochloride, a thymidine phosphorylase inhibitor that increases the bioavailability of trifluridine.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
33569986-1	2021	Trifluridine/tipiracil (FTD/TPI) is an orally active formulation of trifluridine, a thymidine-based nucleoside analog, and tipiracil hydrochloride, a thymidine phosphorylase inhibitor that increases the bioavailability of trifluridine.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
33569986-1	2021	Trifluridine/tipiracil (FTD/TPI) is an orally active formulation of trifluridine, a thymidine-based nucleoside analog, and tipiracil hydrochloride, a thymidine phosphorylase inhibitor that increases the bioavailability of trifluridine.	Trifluridine	68-80	triosephosphate isomerase 1	Homo sapiens	28-31
33569986-1	2021	Trifluridine/tipiracil (FTD/TPI) is an orally active formulation of trifluridine, a thymidine-based nucleoside analog, and tipiracil hydrochloride, a thymidine phosphorylase inhibitor that increases the bioavailability of trifluridine.	Thymidine	84-93	triosephosphate isomerase 1	Homo sapiens	28-31
33569986-1	2021	Trifluridine/tipiracil (FTD/TPI) is an orally active formulation of trifluridine, a thymidine-based nucleoside analog, and tipiracil hydrochloride, a thymidine phosphorylase inhibitor that increases the bioavailability of trifluridine.	Tipiracil hydrochloride	123-146	triosephosphate isomerase 1	Homo sapiens	28-31
33993741-1	2021	Aim: To determine a recommended Phase II dose of the oral fluoropyrimidine trifluridine/tipiracil (FTD/TPI) combined with the multi-kinase inhibitor regorafenib (REG) in refractory metastatic colorectal cancer patients.	2-fluoropyrimidine	58-74	triosephosphate isomerase 1	Homo sapiens	103-106
33993741-1	2021	Aim: To determine a recommended Phase II dose of the oral fluoropyrimidine trifluridine/tipiracil (FTD/TPI) combined with the multi-kinase inhibitor regorafenib (REG) in refractory metastatic colorectal cancer patients.	Trifluridine	75-87	triosephosphate isomerase 1	Homo sapiens	103-106
33993741-1	2021	Aim: To determine a recommended Phase II dose of the oral fluoropyrimidine trifluridine/tipiracil (FTD/TPI) combined with the multi-kinase inhibitor regorafenib (REG) in refractory metastatic colorectal cancer patients.	tipiracil	88-97	triosephosphate isomerase 1	Homo sapiens	103-106
33914537-8	2021	The method implemented in GENESIS is applied to an enzyme, triosephosphate isomerase, which converts dihyroxyacetone phosphate to glyceraldehyde 3-phosphate in four proton-transfer processes.	dihyroxyacetone phosphate	101-126	triosephosphate isomerase 1	Homo sapiens	59-84
33914537-8	2021	The method implemented in GENESIS is applied to an enzyme, triosephosphate isomerase, which converts dihyroxyacetone phosphate to glyceraldehyde 3-phosphate in four proton-transfer processes.	Glyceraldehyde 3-Phosphate	130-156	triosephosphate isomerase 1	Homo sapiens	59-84
33464133-1	2021	Aim: To help to remove misperception of an appropriate position of trifluridine/tipiracil (FTD/TPI) in the treatment of metastatic colorectal cancer.	Trifluridine	67-79	triosephosphate isomerase 1	Homo sapiens	95-98
33952483-1	2021	BACKGROUND/AIM: Regorafenib (REG) and trifluridine/tipiracil (FTD/TPI) have have been shown to improve overall survival in patients with refractory metastatic colorectal cancer.	Trifluridine	38-50	triosephosphate isomerase 1	Homo sapiens	66-69
33952483-1	2021	BACKGROUND/AIM: Regorafenib (REG) and trifluridine/tipiracil (FTD/TPI) have have been shown to improve overall survival in patients with refractory metastatic colorectal cancer.	tipiracil	51-60	triosephosphate isomerase 1	Homo sapiens	66-69
33464133-1	2021	Aim: To help to remove misperception of an appropriate position of trifluridine/tipiracil (FTD/TPI) in the treatment of metastatic colorectal cancer.	tipiracil	80-89	triosephosphate isomerase 1	Homo sapiens	95-98
33744811-1	2021	BACKGROUND: Although the efficacy of trifluridine/tipiracil (FTD/TPI) plus bevacizumab (BEV) against metastatic colorectal cancer (mCRC) has been demonstrated, little is known about its effectiveness upon disease stratification by RAS mutations.	Trifluridine	37-49	triosephosphate isomerase 1	Homo sapiens	65-68
33995592-10	2021	Other oral fluoropyrimidines, such as FTD/TPI, are effective in patients with mCRC who are refractory, intolerant or ineligible for 5-FU.	fluoropyrimidines	11-28	triosephosphate isomerase 1	Homo sapiens	42-45
33995592-10	2021	Other oral fluoropyrimidines, such as FTD/TPI, are effective in patients with mCRC who are refractory, intolerant or ineligible for 5-FU.	Fluorouracil	132-136	triosephosphate isomerase 1	Homo sapiens	42-45
33780084-1	2021	Trifluridine/tipiracil (FTD/TPI) is an orally administrated anticancer drug with efficacy validated for patients with metastatic colorectal cancer (mCRC) or gastric cancer.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
33780084-1	2021	Trifluridine/tipiracil (FTD/TPI) is an orally administrated anticancer drug with efficacy validated for patients with metastatic colorectal cancer (mCRC) or gastric cancer.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
33780084-3	2021	Using specific antibodies against bromodeoxyuridine, FTD incorporation into DNA is detected in tumors and peripheral blood mononuclear cells (PBMCs) of patients with mCRC who are administered FTD/TPI.	Bromodeoxyuridine	34-51	triosephosphate isomerase 1	Homo sapiens	196-199
33713215-2	2021	Trifluridine/tipiracil (FTD/TPI) was approved for previously treated metastatic GC or GEJC (mGC/mGEJC) based on results of the phase 3 TAGS trial.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
33713215-2	2021	Trifluridine/tipiracil (FTD/TPI) was approved for previously treated metastatic GC or GEJC (mGC/mGEJC) based on results of the phase 3 TAGS trial.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
33385116-4	2021	Palmitic amide promoted virus infection by enhancing host glycolysis by binding to triosephosphate isomerase to enhance its enzymatic activity.	hexadecanamide	0-14	triosephosphate isomerase 1	Homo sapiens	83-108
33573542-3	2022	RESULTS: Initially, the mechanism of action of quinoxaline 1,4-di-N-oxide derivatives against bacteria, tumoural cell lines, and parasites has been described as nonspecific, but recently, the results against different organisms have shown that these compounds have an inhibitory action on specific targets such as trypanothione reductase, triosephosphate isomerase, and other essential enzymes.	quindoxin	47-73	triosephosphate isomerase 1	Homo sapiens	339-364
33544407-2	2021	In MSS CRC xenograft models, trifluridine/tipiracil (FTD/TPI) plus programed death 1 inhibitors resulted in synergistic antitumor activity and increased tumor immunogenicity.	Trifluridine	29-41	triosephosphate isomerase 1	Homo sapiens	57-60
33544407-2	2021	In MSS CRC xenograft models, trifluridine/tipiracil (FTD/TPI) plus programed death 1 inhibitors resulted in synergistic antitumor activity and increased tumor immunogenicity.	tipiracil	42-51	triosephosphate isomerase 1	Homo sapiens	57-60
33249761-1	2021	BACKGROUND: A previous Phase I/II study demonstrated that TAS-102 (trifluridine/tipiracil [FTD/TPI]) plus bevacizumab (Bev) has encouraging efficacy and controllable safety for patients with previously treated metastatic colorectal cancer.	trifluridine tipiracil drug combination	58-65	triosephosphate isomerase 1	Homo sapiens	95-98
33249761-1	2021	BACKGROUND: A previous Phase I/II study demonstrated that TAS-102 (trifluridine/tipiracil [FTD/TPI]) plus bevacizumab (Bev) has encouraging efficacy and controllable safety for patients with previously treated metastatic colorectal cancer.	trifluridine tipiracil drug combination	67-89	triosephosphate isomerase 1	Homo sapiens	95-98
33249761-13	2021	Capecitabine/bevacizumab can be selected as a subsequent maintenance therapy without irinotecan and oxaliplatin because FTD/TPI has no cross-resistance with 5-fluorouracil.	Capecitabine	0-12	triosephosphate isomerase 1	Homo sapiens	124-127
32816155-1	2020	PURPOSE: Trifluridine/tipiracil (FTD/TPI) improves the overall survival (OS) of metastatic colorectal cancer (mCRC) patients.	Trifluridine	9-21	triosephosphate isomerase 1	Homo sapiens	37-40
33089343-7	2020	RESULTS: Triosephosphate isomerise (TPI1) was significantly up-regulated in ICC tissues and Kaplan-Meier analysis reveals that higher TPI1 expression was strongly correlated with higher recurrence rate of ICC patients.	triosephosphate	9-24	triosephosphate isomerase 1	Homo sapiens	36-40
33089343-7	2020	RESULTS: Triosephosphate isomerise (TPI1) was significantly up-regulated in ICC tissues and Kaplan-Meier analysis reveals that higher TPI1 expression was strongly correlated with higher recurrence rate of ICC patients.	triosephosphate	9-24	triosephosphate isomerase 1	Homo sapiens	134-138
32891715-1	2020	Trifluridine/tipiracil (FTD/TPI; marketed as Lonsurf ) has shown clinically relevant activity after fluoropyrimidine failure in colorectal cancer and may thus be of increased efficacy compared with current standard capecitabine chemoradiation.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
32891715-1	2020	Trifluridine/tipiracil (FTD/TPI; marketed as Lonsurf ) has shown clinically relevant activity after fluoropyrimidine failure in colorectal cancer and may thus be of increased efficacy compared with current standard capecitabine chemoradiation.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
32891715-1	2020	Trifluridine/tipiracil (FTD/TPI; marketed as Lonsurf ) has shown clinically relevant activity after fluoropyrimidine failure in colorectal cancer and may thus be of increased efficacy compared with current standard capecitabine chemoradiation.	Capecitabine	215-227	triosephosphate isomerase 1	Homo sapiens	28-31
32891715-7	2020	Prolonged S phase arrest, persistent gammaH2AX signalling, endoreplication and polyploidy may contribute to the cytotoxicity of FTD/TPI.	gammah2ax	37-46	triosephosphate isomerase 1	Homo sapiens	132-135
33021466-1	2021	BACKGROUND: The RECOURSE trial (Study of TAS-102 in Patients With Metastatic Colorectal Cancer Refractory to Standard Chemotherapies) demonstrated an overall survival (OS) benefit of trifluridine/tipiracil (FTD/TPI) vs placebo in refractory metastatic colorectal cancer (mCRC).	trifluridine tipiracil drug combination	41-48	triosephosphate isomerase 1	Homo sapiens	211-214
33021466-1	2021	BACKGROUND: The RECOURSE trial (Study of TAS-102 in Patients With Metastatic Colorectal Cancer Refractory to Standard Chemotherapies) demonstrated an overall survival (OS) benefit of trifluridine/tipiracil (FTD/TPI) vs placebo in refractory metastatic colorectal cancer (mCRC).	Trifluridine	183-195	triosephosphate isomerase 1	Homo sapiens	211-214
33021466-1	2021	BACKGROUND: The RECOURSE trial (Study of TAS-102 in Patients With Metastatic Colorectal Cancer Refractory to Standard Chemotherapies) demonstrated an overall survival (OS) benefit of trifluridine/tipiracil (FTD/TPI) vs placebo in refractory metastatic colorectal cancer (mCRC).	tipiracil	196-205	triosephosphate isomerase 1	Homo sapiens	211-214
33173384-2	2020	The present study was initiated to address the lack of published prospective data about the qol benefits of trifluridine/tipiracil (ftd/tpi) compared with best supportive care (bsc) in patients with refractory metastatic colorectal cancer (mcrc).	Trifluridine	108-120	triosephosphate isomerase 1	Homo sapiens	136-139
33173384-2	2020	The present study was initiated to address the lack of published prospective data about the qol benefits of trifluridine/tipiracil (ftd/tpi) compared with best supportive care (bsc) in patients with refractory metastatic colorectal cancer (mcrc).	tipiracil	121-130	triosephosphate isomerase 1	Homo sapiens	136-139
32816155-1	2020	PURPOSE: Trifluridine/tipiracil (FTD/TPI) improves the overall survival (OS) of metastatic colorectal cancer (mCRC) patients.	tipiracil	22-31	triosephosphate isomerase 1	Homo sapiens	37-40
32485527-1	2020	TAS-102 is a preconstituted drug combination comprising an oral fluoropyrimidine (trifluridine, TFT) and a potent inhibitor of thymidine phosphorylase (tipiracil hydrochloride, TPI).	trifluridine tipiracil drug combination	0-7	triosephosphate isomerase 1	Homo sapiens	177-180
32882836-4	2020	The in vitro efficacy compounds against Giardia, as well as its effect on the inhibition of triosephosphate isomerase (TPI) recombinant, were investigated, the inactivation assays were performed with 0.2 mg/mL of the enzyme incubating for 2 h at 37  C in TE buffer, pH 7.4 with increasing concentrations of the compounds.	Tellurium	255-257	triosephosphate isomerase 1	Homo sapiens	119-122
32530932-1	2020	Regorafenib (REG) and trifluridine/tipiracil (FTD/TPI) showed survival benefits in metastatic colorectal cancer patients previously treated with standard chemotherapies; therefore, we compared the efficacy and safety of these two treatments.	Trifluridine	22-34	triosephosphate isomerase 1	Homo sapiens	50-53
32679775-7	2020	The highly increased permeability and loss of noncovalent interactions of deamidated TIM were found to play a central role in the process of selective enzyme inactivation and methylglyoxal production.	Pyruvaldehyde	175-188	triosephosphate isomerase 1	Homo sapiens	85-88
32530932-1	2020	Regorafenib (REG) and trifluridine/tipiracil (FTD/TPI) showed survival benefits in metastatic colorectal cancer patients previously treated with standard chemotherapies; therefore, we compared the efficacy and safety of these two treatments.	tipiracil	35-44	triosephosphate isomerase 1	Homo sapiens	50-53
31924737-1	2020	PURPOSE: This two-part phase Ib trial determined the maximum tolerated dose (MTD) of the combination of trifluridine/tipiracil (FTD/TPI) and irinotecan in patients with advanced gastrointestinal tumors, and evaluated the safety, pharmacokinetics, and antitumor activity of the FTD/TPI, irinotecan, and bevacizumab triplet combination in previously treated metastatic colorectal cancer (mCRC).	Trifluridine	104-116	triosephosphate isomerase 1	Homo sapiens	132-135
32371587-4	2020	Here, we propose a novel therapeutic strategy based on synthetic lethality combining trifluridine/tipiracil (FTD/TPI) and prexasertib (CHK1 inhibitor) as a treatment for ESCC.	Trifluridine	85-97	triosephosphate isomerase 1	Homo sapiens	113-116
32371587-4	2020	Here, we propose a novel therapeutic strategy based on synthetic lethality combining trifluridine/tipiracil (FTD/TPI) and prexasertib (CHK1 inhibitor) as a treatment for ESCC.	tipiracil	98-107	triosephosphate isomerase 1	Homo sapiens	113-116
31826977-1	2020	LESSONS LEARNED: Trifluridine/tipiracil (FTD/TPI) shows promising antitumor activity in heavily pretreated patients with advanced biliary tract carcinoma, including patients with 5-fluorouracil refractory tumors.FTD/TPI has an acceptable safety profile and should be studied further in patients with advanced biliary tract carcinoma after progression on standard first-line therapy.	Trifluridine	17-29	triosephosphate isomerase 1	Homo sapiens	45-48
31826977-1	2020	LESSONS LEARNED: Trifluridine/tipiracil (FTD/TPI) shows promising antitumor activity in heavily pretreated patients with advanced biliary tract carcinoma, including patients with 5-fluorouracil refractory tumors.FTD/TPI has an acceptable safety profile and should be studied further in patients with advanced biliary tract carcinoma after progression on standard first-line therapy.	Trifluridine	17-29	triosephosphate isomerase 1	Homo sapiens	216-219
31826977-1	2020	LESSONS LEARNED: Trifluridine/tipiracil (FTD/TPI) shows promising antitumor activity in heavily pretreated patients with advanced biliary tract carcinoma, including patients with 5-fluorouracil refractory tumors.FTD/TPI has an acceptable safety profile and should be studied further in patients with advanced biliary tract carcinoma after progression on standard first-line therapy.	tipiracil	30-39	triosephosphate isomerase 1	Homo sapiens	45-48
31826977-1	2020	LESSONS LEARNED: Trifluridine/tipiracil (FTD/TPI) shows promising antitumor activity in heavily pretreated patients with advanced biliary tract carcinoma, including patients with 5-fluorouracil refractory tumors.FTD/TPI has an acceptable safety profile and should be studied further in patients with advanced biliary tract carcinoma after progression on standard first-line therapy.	tipiracil	30-39	triosephosphate isomerase 1	Homo sapiens	216-219
31826977-1	2020	LESSONS LEARNED: Trifluridine/tipiracil (FTD/TPI) shows promising antitumor activity in heavily pretreated patients with advanced biliary tract carcinoma, including patients with 5-fluorouracil refractory tumors.FTD/TPI has an acceptable safety profile and should be studied further in patients with advanced biliary tract carcinoma after progression on standard first-line therapy.	Fluorouracil	179-193	triosephosphate isomerase 1	Homo sapiens	45-48
32308505-1	2020	Purpose: Trifluridine/tipiracil (FTD/TPI) is approved in Japan, the United States (US), and Europe for metastatic colorectal cancer (mCRC) refractory to standard therapies.	trifluridine tipiracil drug combination	9-31	triosephosphate isomerase 1	Homo sapiens	37-40
32322913-1	2020	PURPOSE: Trifluridine (FTD) is the active component of the nucleoside chemotherapeutic drug trifluridine/tipiracil (FTD/TPI), which is approved worldwide for the treatment of patients with metastatic gastrointestinal cancer.	Trifluridine	9-21	triosephosphate isomerase 1	Homo sapiens	120-123
32322913-1	2020	PURPOSE: Trifluridine (FTD) is the active component of the nucleoside chemotherapeutic drug trifluridine/tipiracil (FTD/TPI), which is approved worldwide for the treatment of patients with metastatic gastrointestinal cancer.	Nucleosides	59-69	triosephosphate isomerase 1	Homo sapiens	120-123
32322913-1	2020	PURPOSE: Trifluridine (FTD) is the active component of the nucleoside chemotherapeutic drug trifluridine/tipiracil (FTD/TPI), which is approved worldwide for the treatment of patients with metastatic gastrointestinal cancer.	trifluridine tipiracil drug combination	92-114	triosephosphate isomerase 1	Homo sapiens	120-123
31826977-3	2020	Trifluridine/tipiracil (FTD/TPI) has activity in both fluoropyrimidine-sensitive and -resistant tumors, which led us to conduct a single arm phase II trial to evaluate the safety and efficacy of FTD/TPI for patients previously treated for advanced BTC.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
31826977-3	2020	Trifluridine/tipiracil (FTD/TPI) has activity in both fluoropyrimidine-sensitive and -resistant tumors, which led us to conduct a single arm phase II trial to evaluate the safety and efficacy of FTD/TPI for patients previously treated for advanced BTC.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	199-202
31826977-3	2020	Trifluridine/tipiracil (FTD/TPI) has activity in both fluoropyrimidine-sensitive and -resistant tumors, which led us to conduct a single arm phase II trial to evaluate the safety and efficacy of FTD/TPI for patients previously treated for advanced BTC.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
31826977-3	2020	Trifluridine/tipiracil (FTD/TPI) has activity in both fluoropyrimidine-sensitive and -resistant tumors, which led us to conduct a single arm phase II trial to evaluate the safety and efficacy of FTD/TPI for patients previously treated for advanced BTC.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	199-202
31826977-3	2020	Trifluridine/tipiracil (FTD/TPI) has activity in both fluoropyrimidine-sensitive and -resistant tumors, which led us to conduct a single arm phase II trial to evaluate the safety and efficacy of FTD/TPI for patients previously treated for advanced BTC.	5-fluoropyrimidine	54-70	triosephosphate isomerase 1	Homo sapiens	28-31
31924737-1	2020	PURPOSE: This two-part phase Ib trial determined the maximum tolerated dose (MTD) of the combination of trifluridine/tipiracil (FTD/TPI) and irinotecan in patients with advanced gastrointestinal tumors, and evaluated the safety, pharmacokinetics, and antitumor activity of the FTD/TPI, irinotecan, and bevacizumab triplet combination in previously treated metastatic colorectal cancer (mCRC).	Trifluridine	104-116	triosephosphate isomerase 1	Homo sapiens	281-284
31924737-12	2020	CONCLUSIONS: Tolerability and activity observed in this phase I trial support further investigation of the FTD/TPI-irinotecan-bevacizumab combination in previously treated mCRC.	Irinotecan	115-125	triosephosphate isomerase 1	Homo sapiens	111-114
31364707-5	2020	Its application to an empirical data set of the triosephosphate isomerase (TIM)-barrel superfamily suggests rapid evolution of protein-mediated pyrimidine biosynthesis, likely taking place after the RNA world.	pyrimidine	144-154	triosephosphate isomerase 1	Homo sapiens	48-73
31838590-1	2020	BACKGROUND: Although regorafenib or trifluridine/tipiracil (FTD/TPI) has been recognized as a later-line standard treatment in patients with metastatic colorectal cancer (mCRC), not all patients have beneficial outcomes.	regorafenib	21-32	triosephosphate isomerase 1	Homo sapiens	64-67
31838590-1	2020	BACKGROUND: Although regorafenib or trifluridine/tipiracil (FTD/TPI) has been recognized as a later-line standard treatment in patients with metastatic colorectal cancer (mCRC), not all patients have beneficial outcomes.	Trifluridine	36-48	triosephosphate isomerase 1	Homo sapiens	64-67
31838590-1	2020	BACKGROUND: Although regorafenib or trifluridine/tipiracil (FTD/TPI) has been recognized as a later-line standard treatment in patients with metastatic colorectal cancer (mCRC), not all patients have beneficial outcomes.	tipiracil	49-58	triosephosphate isomerase 1	Homo sapiens	64-67
31364707-5	2020	Its application to an empirical data set of the triosephosphate isomerase (TIM)-barrel superfamily suggests rapid evolution of protein-mediated pyrimidine biosynthesis, likely taking place after the RNA world.	pyrimidine	144-154	triosephosphate isomerase 1	Homo sapiens	75-78
31600365-1	2020	Importance: Trifluridine/tipiracil (FTD/TPI) treatment has shown clinical benefit in patients with pretreated metastatic gastric cancer or gastroesophageal junction cancer (mGC/GEJC).	Trifluridine	12-24	triosephosphate isomerase 1	Homo sapiens	40-43
31874685-4	2020	In this study, a scaffoldin-mediated two-enzyme complex containing triosephosphate isomerase (TIM) and fructose-1,6-bisphosphate aldolase/phosphatase (FBPA) was constructed, and the initial production rate of fructose 6-phosphate (F6P) was determined with different types of fine-tuning linkers.	fructose-6-phosphate	209-229	triosephosphate isomerase 1	Homo sapiens	67-92
31874685-4	2020	In this study, a scaffoldin-mediated two-enzyme complex containing triosephosphate isomerase (TIM) and fructose-1,6-bisphosphate aldolase/phosphatase (FBPA) was constructed, and the initial production rate of fructose 6-phosphate (F6P) was determined with different types of fine-tuning linkers.	fructose-6-phosphate	209-229	triosephosphate isomerase 1	Homo sapiens	94-97
31874685-4	2020	In this study, a scaffoldin-mediated two-enzyme complex containing triosephosphate isomerase (TIM) and fructose-1,6-bisphosphate aldolase/phosphatase (FBPA) was constructed, and the initial production rate of fructose 6-phosphate (F6P) was determined with different types of fine-tuning linkers.	fructose-6-phosphate	231-234	triosephosphate isomerase 1	Homo sapiens	67-92
31874685-4	2020	In this study, a scaffoldin-mediated two-enzyme complex containing triosephosphate isomerase (TIM) and fructose-1,6-bisphosphate aldolase/phosphatase (FBPA) was constructed, and the initial production rate of fructose 6-phosphate (F6P) was determined with different types of fine-tuning linkers.	fructose-6-phosphate	231-234	triosephosphate isomerase 1	Homo sapiens	94-97
31874685-8	2020	The synthetic enzyme complex with the semirigid linker FRRRF in scaffoldin showed the highest initial F6P production rate of 10.16 muM/min, which indicates that the linker"s amino acid composition in scaffoldin may lead to significant changes in the spatial architecture of the TIM-FBPA complex and consequently affect the initial reaction rate.	fructose-6-phosphate	102-105	triosephosphate isomerase 1	Homo sapiens	278-281
30838483-2	2020	We conducted a phase I study to determine the maximum tolerated dose of oxaliplatin plus trifluridine/tipiracil (FTD/TPI) in patients with refractory mCRC.	Oxaliplatin	72-83	triosephosphate isomerase 1	Homo sapiens	117-120
30838483-2	2020	We conducted a phase I study to determine the maximum tolerated dose of oxaliplatin plus trifluridine/tipiracil (FTD/TPI) in patients with refractory mCRC.	Trifluridine	89-101	triosephosphate isomerase 1	Homo sapiens	117-120
30838483-2	2020	We conducted a phase I study to determine the maximum tolerated dose of oxaliplatin plus trifluridine/tipiracil (FTD/TPI) in patients with refractory mCRC.	tipiracil	102-111	triosephosphate isomerase 1	Homo sapiens	117-120
31600365-1	2020	Importance: Trifluridine/tipiracil (FTD/TPI) treatment has shown clinical benefit in patients with pretreated metastatic gastric cancer or gastroesophageal junction cancer (mGC/GEJC).	tipiracil	25-34	triosephosphate isomerase 1	Homo sapiens	40-43
29621041-9	2019	Triamcinolone was used at 90.2% (230/255) of the TPI visits.	Triamcinolone	0-13	triosephosphate isomerase 1	Homo sapiens	49-52
31591140-1	2020	BACKGROUND: Trifluridine and tipiracil (FTD + TPI) and regorafenib (REG) are approved treatments for the treatment of refractory metastatic colorectal cancer (mCRC).	tipiracil	29-38	triosephosphate isomerase 1	Homo sapiens	46-49
31591140-12	2020	IMPLICATIONS FOR PRACTICE: Trifluridine plus tipiracil (FTD + TPI) and regorafenib (REG) prolong survival in refractory metastatic colorectal cancer (mCRC) but have different tolerability profiles.	tipiracil	45-54	triosephosphate isomerase 1	Homo sapiens	62-65
31668066-1	2019	The triosephosphate isomerase (TIM), Scy p 8, is a crab allergen and shows cross-reactivity in the shellfish.	triosephosphate	4-19	triosephosphate isomerase 1	Homo sapiens	31-34
31668066-1	2019	The triosephosphate isomerase (TIM), Scy p 8, is a crab allergen and shows cross-reactivity in the shellfish.	scy p 8	37-44	triosephosphate isomerase 1	Homo sapiens	31-34
32392174-1	2019	BACKGROUND: Although regorafenib (REG) and trifluridine/tipiracil (FTD/TPI) have been recognised as standard treatments in metastatic colorectal cancer (mCRC), the best option remains unclear.	tipiracil	56-65	triosephosphate isomerase 1	Homo sapiens	71-74
31611243-1	2019	Trifluridine/tipiracil (FTD/TPI) is a new antimetabolite agent used to treat chemorefractory metastatic colorectal cancer.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
31611243-1	2019	Trifluridine/tipiracil (FTD/TPI) is a new antimetabolite agent used to treat chemorefractory metastatic colorectal cancer.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
31508957-6	2019	TIM utilizes the cationic side chain of K12 to provide direct electrostatic stabilization of the enolate oxyanion, and the nonpolar side chains of P166, I170 and L230 are utilized for the construction of an active site cavity that provides optimal stabilization of the enediolate phosphate intermediate relative to the carbon acid substrate.	enolate oxyanion	97-113	triosephosphate isomerase 1	Homo sapiens	0-3
31508957-6	2019	TIM utilizes the cationic side chain of K12 to provide direct electrostatic stabilization of the enolate oxyanion, and the nonpolar side chains of P166, I170 and L230 are utilized for the construction of an active site cavity that provides optimal stabilization of the enediolate phosphate intermediate relative to the carbon acid substrate.	Phosphates	280-289	triosephosphate isomerase 1	Homo sapiens	0-3
31508957-6	2019	TIM utilizes the cationic side chain of K12 to provide direct electrostatic stabilization of the enolate oxyanion, and the nonpolar side chains of P166, I170 and L230 are utilized for the construction of an active site cavity that provides optimal stabilization of the enediolate phosphate intermediate relative to the carbon acid substrate.	carbon acid	319-330	triosephosphate isomerase 1	Homo sapiens	0-3
31491983-9	2019	The experimental results showed that volumetric water contents compensated by ground temperature showed good agreement with the volumetric water contents estimated from the gravimetric water contents of the soil samples and TPI.	Water	48-53	triosephosphate isomerase 1	Homo sapiens	224-227
31491983-9	2019	The experimental results showed that volumetric water contents compensated by ground temperature showed good agreement with the volumetric water contents estimated from the gravimetric water contents of the soil samples and TPI.	Water	139-144	triosephosphate isomerase 1	Homo sapiens	224-227
31491983-9	2019	The experimental results showed that volumetric water contents compensated by ground temperature showed good agreement with the volumetric water contents estimated from the gravimetric water contents of the soil samples and TPI.	Water	139-144	triosephosphate isomerase 1	Homo sapiens	224-227
30628113-1	2019	AIMS: Trifluridine/tipiracil (FTD/TPI) prolongs survival in refractory metastatic colorectal cancer, but limited data exist on its use in patients with hepatic impairment.	Trifluridine	6-18	triosephosphate isomerase 1	Homo sapiens	34-37
31291107-4	2019	PtmU3 adopts an unprecedented triosephosphate isomerase (TIM) barrel structural fold for this class of enzymes and possesses a noncanonical diiron active site architecture with a saturated six-coordinate iron center lacking a mu-oxo bridge.	Iron	142-146	triosephosphate isomerase 1	Homo sapiens	57-60
31291107-5	2019	This study reveals the first member of a previously unidentified superfamily of TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature"s repertoire of nonheme diiron monooxygenases and TIM-barrel-fold enzymes.	Metals	108-113	triosephosphate isomerase 1	Homo sapiens	80-83
31291107-5	2019	This study reveals the first member of a previously unidentified superfamily of TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature"s repertoire of nonheme diiron monooxygenases and TIM-barrel-fold enzymes.	Metals	108-113	triosephosphate isomerase 1	Homo sapiens	295-298
31291107-5	2019	This study reveals the first member of a previously unidentified superfamily of TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature"s repertoire of nonheme diiron monooxygenases and TIM-barrel-fold enzymes.	Oxygen	124-132	triosephosphate isomerase 1	Homo sapiens	80-83
31291107-5	2019	This study reveals the first member of a previously unidentified superfamily of TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature"s repertoire of nonheme diiron monooxygenases and TIM-barrel-fold enzymes.	Oxygen	124-132	triosephosphate isomerase 1	Homo sapiens	295-298
30902310-3	2019	In particular, ascorbic acid inhibited HPA activity via non-competitive antagonism from two allosteric sites, by channeling the inhibition towards the active site cavity via the triose-phosphate isomerase (TIM) barrel.	Ascorbic Acid	15-28	triosephosphate isomerase 1	Homo sapiens	178-204
30902310-3	2019	In particular, ascorbic acid inhibited HPA activity via non-competitive antagonism from two allosteric sites, by channeling the inhibition towards the active site cavity via the triose-phosphate isomerase (TIM) barrel.	Ascorbic Acid	15-28	triosephosphate isomerase 1	Homo sapiens	206-209
30780136-0	2019	A novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer nanocomposite and its multifunctional properties.	graphene oxide	8-22	triosephosphate isomerase 1	Homo sapiens	50-53
30780136-0	2019	A novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer nanocomposite and its multifunctional properties.	trans-1,4-polyisoprene	23-45	triosephosphate isomerase 1	Homo sapiens	50-53
30780136-0	2019	A novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer nanocomposite and its multifunctional properties.	Polymers	68-75	triosephosphate isomerase 1	Homo sapiens	50-53
30780136-1	2019	In this work, we have synthesized a novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer (SMP) nanocomposite by adding GO (0.0-1.5 phr) to bulk TPI polymer to enhance its mechanical properties.	graphene oxide	42-56	triosephosphate isomerase 1	Homo sapiens	84-87
30780136-1	2019	In this work, we have synthesized a novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer (SMP) nanocomposite by adding GO (0.0-1.5 phr) to bulk TPI polymer to enhance its mechanical properties.	graphene oxide	42-56	triosephosphate isomerase 1	Homo sapiens	165-168
30780136-1	2019	In this work, we have synthesized a novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer (SMP) nanocomposite by adding GO (0.0-1.5 phr) to bulk TPI polymer to enhance its mechanical properties.	trans-1,4-polyisoprene	57-79	triosephosphate isomerase 1	Homo sapiens	84-87
30780136-1	2019	In this work, we have synthesized a novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer (SMP) nanocomposite by adding GO (0.0-1.5 phr) to bulk TPI polymer to enhance its mechanical properties.	trans-1,4-polyisoprene	57-79	triosephosphate isomerase 1	Homo sapiens	165-168
30780136-1	2019	In this work, we have synthesized a novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer (SMP) nanocomposite by adding GO (0.0-1.5 phr) to bulk TPI polymer to enhance its mechanical properties.	Polymers	102-109	triosephosphate isomerase 1	Homo sapiens	84-87
30780136-1	2019	In this work, we have synthesized a novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer (SMP) nanocomposite by adding GO (0.0-1.5 phr) to bulk TPI polymer to enhance its mechanical properties.	smp	111-114	triosephosphate isomerase 1	Homo sapiens	84-87
30780136-1	2019	In this work, we have synthesized a novel graphene oxide/trans-1,4-polyisoprene (GO/TPI) shape memory polymer (SMP) nanocomposite by adding GO (0.0-1.5 phr) to bulk TPI polymer to enhance its mechanical properties.	smp	111-114	triosephosphate isomerase 1	Homo sapiens	165-168
30628113-1	2019	AIMS: Trifluridine/tipiracil (FTD/TPI) prolongs survival in refractory metastatic colorectal cancer, but limited data exist on its use in patients with hepatic impairment.	tipiracil	19-28	triosephosphate isomerase 1	Homo sapiens	34-37
30601716-6	2019	Cadmium-induced aggregation was limited to newly synthesized Tpi1 that was recruited to foci containing the disaggregase Hsp104 and the peroxiredoxin chaperone Tsa1.	Cadmium	0-7	triosephosphate isomerase 1	Homo sapiens	61-65
31138881-1	2019	Trifluridine (FTD), a tri-fluorinated thymidine analogue, is a key component of the oral antitumor drug FTD/TPI (also known as TAS-102), which is used to treat refractory metastatic colorectal cancer.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	108-111
31138881-1	2019	Trifluridine (FTD), a tri-fluorinated thymidine analogue, is a key component of the oral antitumor drug FTD/TPI (also known as TAS-102), which is used to treat refractory metastatic colorectal cancer.	Thymidine	38-47	triosephosphate isomerase 1	Homo sapiens	108-111
30911085-6	2019	We show that the drug interferes with triosephosphate isomerase (TPI) causing release of methylglyoxal (MG).	Pyruvaldehyde	89-102	triosephosphate isomerase 1	Homo sapiens	65-68
30911085-12	2019	Fludioxonil directly inhibited TPI and also caused it to release methylglyoxal in vitro.	fludioxonil	0-11	triosephosphate isomerase 1	Homo sapiens	31-34
30911085-13	2019	Thus, TPI is a drug target of the phenylpyrrole class of fungicides, inducing elevated MG which alters HHK activity, likely converting the kinase to a phosphatase that acts on Ypd1 to trigger HOG pathway activation and fungal cell death.	2-Phenyl-1H-pyrrole	34-47	triosephosphate isomerase 1	Homo sapiens	6-9
30897744-1	2019	The screening of more than 30 million compounds derived from 81 small molecule libraries built on 81 distinct scaffolds identified pyrrolidine bis-cyclic guanidine library (TPI-1955) to be one of the most active and selective antiplasmodial libraries.	pyrrolidine bis-cyclic guanidine	131-163	triosephosphate isomerase 1	Homo sapiens	173-176
31136618-7	2019	Finally, we found that universal reactions are also associated with ancestral domains, such as those related to phosphorus-containing groups with a phosphate group as acceptor or those related to the ribulose-phosphate binding barrel, triosephosphate isomerase, and D-ribose-5-phosphate isomerase (RpiA) lid domain, among others.	Phosphorus	112-122	triosephosphate isomerase 1	Homo sapiens	235-260
31136618-7	2019	Finally, we found that universal reactions are also associated with ancestral domains, such as those related to phosphorus-containing groups with a phosphate group as acceptor or those related to the ribulose-phosphate binding barrel, triosephosphate isomerase, and D-ribose-5-phosphate isomerase (RpiA) lid domain, among others.	Phosphates	148-157	triosephosphate isomerase 1	Homo sapiens	235-260
30848893-6	2019	The biological functional assessments revealed that the modifications inhibited the activity of TPIS and induced the activity of ENOA, in vitro and in vivo, followed by an increase in the level of cellular methylglyoxal, advanced glycation end products, and reactive oxygen species/superoxide, and the induction of mitochondrial dysfunction, which further inhibited oxidative phosphorylation and stimulated glycolysis.	Reactive Oxygen Species	258-281	triosephosphate isomerase 1	Homo sapiens	96-100
30848893-6	2019	The biological functional assessments revealed that the modifications inhibited the activity of TPIS and induced the activity of ENOA, in vitro and in vivo, followed by an increase in the level of cellular methylglyoxal, advanced glycation end products, and reactive oxygen species/superoxide, and the induction of mitochondrial dysfunction, which further inhibited oxidative phosphorylation and stimulated glycolysis.	Superoxides	282-292	triosephosphate isomerase 1	Homo sapiens	96-100
30601716-7	2019	Misfolding of nascent Tpi1 in response to both cadmium and glucose-depletion stress required both cysteines, implying that thiol status in this protein directly influences folding.	Cadmium	47-54	triosephosphate isomerase 1	Homo sapiens	22-26
30601716-7	2019	Misfolding of nascent Tpi1 in response to both cadmium and glucose-depletion stress required both cysteines, implying that thiol status in this protein directly influences folding.	Glucose	59-66	triosephosphate isomerase 1	Homo sapiens	22-26
30601716-7	2019	Misfolding of nascent Tpi1 in response to both cadmium and glucose-depletion stress required both cysteines, implying that thiol status in this protein directly influences folding.	Cysteine	98-107	triosephosphate isomerase 1	Homo sapiens	22-26
30601716-7	2019	Misfolding of nascent Tpi1 in response to both cadmium and glucose-depletion stress required both cysteines, implying that thiol status in this protein directly influences folding.	Sulfhydryl Compounds	123-128	triosephosphate isomerase 1	Homo sapiens	22-26
30601716-9	2019	Moreover, human TPI, mutations in which cause a glycolytic deficiency syndrome, also forms aggregates in response to cadmium treatment, suggesting that this conserved enzyme is folding-labile and may be a useful endogenous model for investigating thiol-specific proteotoxicity.	Cadmium	117-124	triosephosphate isomerase 1	Homo sapiens	16-19
30601716-9	2019	Moreover, human TPI, mutations in which cause a glycolytic deficiency syndrome, also forms aggregates in response to cadmium treatment, suggesting that this conserved enzyme is folding-labile and may be a useful endogenous model for investigating thiol-specific proteotoxicity.	Sulfhydryl Compounds	247-252	triosephosphate isomerase 1	Homo sapiens	16-19
30547679-8	2019	In terms of health outcomes, FTD/TPI was associated with 0.25 and 0.11 increment in LYs compared with BSC and regorafenib, respectively.	Lysine	84-87	triosephosphate isomerase 1	Homo sapiens	33-36
30873387-14	2019	Our sera proteomic analysis confirms that TPI1 serum levels increase in poor prognosis gemcitabine-treated patients.	gemcitabine	87-98	triosephosphate isomerase 1	Homo sapiens	42-46
30547679-8	2019	In terms of health outcomes, FTD/TPI was associated with 0.25 and 0.11 increment in LYs compared with BSC and regorafenib, respectively.	regorafenib	110-121	triosephosphate isomerase 1	Homo sapiens	33-36
30547679-9	2019	Furthermore, FTD/TPI was associated with 0.17, and 0.07 increment in QALYs compared with BSC and regorafenib, resulting in ICERs of $32,759 per LY gained and $49,326 per QALY gained versus BSC.	regorafenib	97-108	triosephosphate isomerase 1	Homo sapiens	17-20
30445951-1	2018	BACKGROUND: Trifluridine/tipiracil (TAS-102, Lonsurf ), a novel oral anti-tumor agent combining an anti-neoplastic thymidine-based nucleoside analogue (trifluridine, FTD) with a thymidine phosphorylase inhibitor (tipiracil hydrochloride, TPI) presents a new treatment option for metastatic colorectal cancer (mCRC) patients refractory or intolerant to standard therapies.	Trifluridine	12-24	triosephosphate isomerase 1	Homo sapiens	238-241
30370845-1	2019	Triosephosphate isomerase is the fifth enzyme in glycolysis and its canonical function is the reversible isomerization of glyceraldehyde-3-phosphate and dihydroxyacetone phosphate.	Glyceraldehyde 3-Phosphate	122-148	triosephosphate isomerase 1	Homo sapiens	0-25
30370845-1	2019	Triosephosphate isomerase is the fifth enzyme in glycolysis and its canonical function is the reversible isomerization of glyceraldehyde-3-phosphate and dihydroxyacetone phosphate.	Dihydroxyacetone Phosphate	153-179	triosephosphate isomerase 1	Homo sapiens	0-25
30350179-1	2018	PURPOSE: Trifluridine/tipiracil (FTD/TPI; TAS-102, Lonsurf ), a novel form of chemotherapy for metastatic colorectal cancer (mCRC), has shown clinical benefit in the global, phase III RECOURSE trial, regardless of patient age.	Trifluridine	9-21	triosephosphate isomerase 1	Homo sapiens	37-40
30350179-1	2018	PURPOSE: Trifluridine/tipiracil (FTD/TPI; TAS-102, Lonsurf ), a novel form of chemotherapy for metastatic colorectal cancer (mCRC), has shown clinical benefit in the global, phase III RECOURSE trial, regardless of patient age.	tipiracil	22-31	triosephosphate isomerase 1	Homo sapiens	37-40
30627095-9	2018	The success in these present cases indicates that FTD/TPI+Bmab as a second- or third-line treatment is a therapeutic option for elderly patients with mCRC who are not eligible for intensive chemotherapy, even after failure of treatment with 5-FU.	Fluorouracil	241-245	triosephosphate isomerase 1	Homo sapiens	54-57
30445951-1	2018	BACKGROUND: Trifluridine/tipiracil (TAS-102, Lonsurf ), a novel oral anti-tumor agent combining an anti-neoplastic thymidine-based nucleoside analogue (trifluridine, FTD) with a thymidine phosphorylase inhibitor (tipiracil hydrochloride, TPI) presents a new treatment option for metastatic colorectal cancer (mCRC) patients refractory or intolerant to standard therapies.	tipiracil	25-34	triosephosphate isomerase 1	Homo sapiens	238-241
30445951-1	2018	BACKGROUND: Trifluridine/tipiracil (TAS-102, Lonsurf ), a novel oral anti-tumor agent combining an anti-neoplastic thymidine-based nucleoside analogue (trifluridine, FTD) with a thymidine phosphorylase inhibitor (tipiracil hydrochloride, TPI) presents a new treatment option for metastatic colorectal cancer (mCRC) patients refractory or intolerant to standard therapies.	trifluridine tipiracil drug combination	36-43	triosephosphate isomerase 1	Homo sapiens	238-241
30257515-1	2018	Salvage chemotherapy for refractory metastatic colorectal cancer using trifluridine/tipiracil (FTD/TPI) and regorafenib has shown survival benefits.	Trifluridine	71-83	triosephosphate isomerase 1	Homo sapiens	99-102
29856481-9	2018	The physiological significance of the TPI and miR-22/28 interaction for the glycolytic influx was confirmed by the l-lactate production in the HCT-116+/+ cells.	L-lactate	115-124	triosephosphate isomerase 1	Homo sapiens	38-41
30257515-1	2018	Salvage chemotherapy for refractory metastatic colorectal cancer using trifluridine/tipiracil (FTD/TPI) and regorafenib has shown survival benefits.	tipiracil	84-93	triosephosphate isomerase 1	Homo sapiens	99-102
30257515-9	2018	Treatment results following regorafenib administration subsequent to FTD or FTD/TPI suggest that sequential therapy with FTD/TPI prior to regorafenib may be effective in a clinical setting.	regorafenib	28-39	triosephosphate isomerase 1	Homo sapiens	125-128
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	Glyceraldehyde 3-Phosphate	77-103	triosephosphate isomerase 1	Homo sapiens	126-151
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	Glyceraldehyde 3-Phosphate	77-103	triosephosphate isomerase 1	Homo sapiens	153-156
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	Glyceraldehyde 3-Phosphate	77-103	triosephosphate isomerase 1	Homo sapiens	201-204
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	phosphoglycolate	253-269	triosephosphate isomerase 1	Homo sapiens	126-151
29627155-9	2018	Proteomic studies on the 20 micromol/L FTI-277 and 5 micromol/L alendronate +20 micromol/L FTI-277 treated cells revealed altered expression of different proteins including peroxiredoxin 2 (Prx2), glutathione S transferase 1 (GSTP1), Rho GTPase activating protein (RhoGAP), triosephosphate isomerase (TPI), and heat shock protein 60 (HSP60).	Alendronate	64-75	triosephosphate isomerase 1	Homo sapiens	274-299
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	phosphoglycolate	253-269	triosephosphate isomerase 1	Homo sapiens	153-156
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	phosphoglycolate	253-269	triosephosphate isomerase 1	Homo sapiens	201-204
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	Phosphates	270-278	triosephosphate isomerase 1	Homo sapiens	126-151
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	Phosphates	270-278	triosephosphate isomerase 1	Homo sapiens	153-156
29862813-1	2018	We report pH rate profiles for kcat and Km for the isomerization reaction of glyceraldehyde 3-phosphate catalyzed by wildtype triosephosphate isomerase (TIM) from three organisms and by ten mutants of TIM; and, for Ki for inhibition of this reaction by phosphoglycolate trianion (I3-).	Phosphates	270-278	triosephosphate isomerase 1	Homo sapiens	201-204
29862813-2	2018	The pH profiles for Ki show that the binding of I3- to TIM (E) to form EH I3- is accompanied by uptake of a proton by the carboxylate side-chain of E165, whose function is to abstract a proton from substrate.	carboxylate	122-133	triosephosphate isomerase 1	Homo sapiens	55-58
29862813-4	2018	The linear free energy correlation, with slope of 0.73 ( r2 = 0.96), between kcat/ Km for TIM-catalyzed isomerization and the disassociation constant of PGA trianion for TIM shows that EH I3- and the transition state are stabilized by similar interactions with the protein catalyst.	pga trianion	153-165	triosephosphate isomerase 1	Homo sapiens	90-93
29862813-4	2018	The linear free energy correlation, with slope of 0.73 ( r2 = 0.96), between kcat/ Km for TIM-catalyzed isomerization and the disassociation constant of PGA trianion for TIM shows that EH I3- and the transition state are stabilized by similar interactions with the protein catalyst.	pga trianion	153-165	triosephosphate isomerase 1	Homo sapiens	170-173
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Dihydroxyacetone Phosphate	91-117	triosephosphate isomerase 1	Homo sapiens	0-25
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Dihydroxyacetone Phosphate	91-117	triosephosphate isomerase 1	Homo sapiens	27-30
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Dihydroxyacetone Phosphate	119-123	triosephosphate isomerase 1	Homo sapiens	0-25
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Dihydroxyacetone Phosphate	119-123	triosephosphate isomerase 1	Homo sapiens	27-30
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Glyceraldehyde 3-Phosphate	128-154	triosephosphate isomerase 1	Homo sapiens	0-25
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Glyceraldehyde 3-Phosphate	128-154	triosephosphate isomerase 1	Homo sapiens	27-30
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Glyceraldehyde 3-Phosphate	156-159	triosephosphate isomerase 1	Homo sapiens	0-25
29678765-1	2018	Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies.	Glyceraldehyde 3-Phosphate	156-159	triosephosphate isomerase 1	Homo sapiens	27-30
29627155-9	2018	Proteomic studies on the 20 micromol/L FTI-277 and 5 micromol/L alendronate +20 micromol/L FTI-277 treated cells revealed altered expression of different proteins including peroxiredoxin 2 (Prx2), glutathione S transferase 1 (GSTP1), Rho GTPase activating protein (RhoGAP), triosephosphate isomerase (TPI), and heat shock protein 60 (HSP60).	Alendronate	64-75	triosephosphate isomerase 1	Homo sapiens	301-304
29396807-0	2018	The CNS penetrating taxane TPI 287 and the AURKA inhibitor alisertib induce synergistic apoptosis in glioblastoma cells.	taxane	20-26	triosephosphate isomerase 1	Homo sapiens	27-30
29396807-3	2018	Unlike current clinically used taxane drugs, the novel taxane TPI 287 penetrates the CNS.	taxane	31-37	triosephosphate isomerase 1	Homo sapiens	62-65
29396807-3	2018	Unlike current clinically used taxane drugs, the novel taxane TPI 287 penetrates the CNS.	taxane	55-61	triosephosphate isomerase 1	Homo sapiens	62-65
29396807-7	2018	TPI 287 not only potentiated the cytotoxicity of the AURKA inhibitors alisertib, MLN8054 and TC-A2317, but was often potently synergistic.	MLN 8237	70-79	triosephosphate isomerase 1	Homo sapiens	0-3
29396807-7	2018	TPI 287 not only potentiated the cytotoxicity of the AURKA inhibitors alisertib, MLN8054 and TC-A2317, but was often potently synergistic.	MLN8054	81-88	triosephosphate isomerase 1	Homo sapiens	0-3
29396807-7	2018	TPI 287 not only potentiated the cytotoxicity of the AURKA inhibitors alisertib, MLN8054 and TC-A2317, but was often potently synergistic.	tc-a2317	93-101	triosephosphate isomerase 1	Homo sapiens	0-3
29568368-1	2018	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) is a combination of the antineoplastic thymidine analog, FTD, and thymidine phosphorylase inhibitor, TPI (molar ratio 1:0.5).	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
29516737-1	2018	We have previously performed empirical valence bond calculations of the kinetic activation barriers, Delta G calc, for the deprotonation of complexes between TIM and the whole substrate glyceraldehyde-3-phosphate (GAP, Kulkarni et al.	Glyceraldehyde 3-Phosphate	186-212	triosephosphate isomerase 1	Homo sapiens	158-161
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	Water	58-63	triosephosphate isomerase 1	Homo sapiens	99-124
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	Water	58-63	triosephosphate isomerase 1	Homo sapiens	126-129
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	Water	58-63	triosephosphate isomerase 1	Homo sapiens	334-337
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	Water	58-63	triosephosphate isomerase 1	Homo sapiens	334-337
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	phosphoglycolohydroxamate	231-234	triosephosphate isomerase 1	Homo sapiens	99-124
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	phosphoglycolohydroxamate	231-234	triosephosphate isomerase 1	Homo sapiens	126-129
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	phosphoglycolohydroxamate	350-353	triosephosphate isomerase 1	Homo sapiens	99-124
29307720-1	2018	In this work, we examine the hypothesis about how trapped water molecules at the interface between triosephosphate isomerase (TIM) and either of two phosphorylated inhibitors, 2-phosphoglycolate (2PG) or phosphoglycolohydroxamate (PGH), can explain the anomalous highly negative binding heat capacities (DeltaCp,b) of both complexes, TIM-2PG and TIM-PGH.	phosphoglycolohydroxamate	350-353	triosephosphate isomerase 1	Homo sapiens	126-129
29307720-7	2018	These effects were also observed in the TIM-2PG complex using sucrose as stressor.	Sucrose	62-69	triosephosphate isomerase 1	Homo sapiens	40-43
29307720-8	2018	Our results strongly suggest that some water molecules became immobilized when the TIM-inhibitor complexes were formed.	Water	39-44	triosephosphate isomerase 1	Homo sapiens	83-86
29307720-9	2018	A computational analysis of the hydration state of the binding site of TIM in both its free state and its complexed form with 2PG or PGH, based on molecular dynamics (MD) simulations in explicit solvent, showed that the binding site effectively immobilized additional water molecules after binding these inhibitors.	phosphoglycolohydroxamate	133-136	triosephosphate isomerase 1	Homo sapiens	71-74
29307720-9	2018	A computational analysis of the hydration state of the binding site of TIM in both its free state and its complexed form with 2PG or PGH, based on molecular dynamics (MD) simulations in explicit solvent, showed that the binding site effectively immobilized additional water molecules after binding these inhibitors.	Water	268-273	triosephosphate isomerase 1	Homo sapiens	71-74
29568368-1	2018	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) is a combination of the antineoplastic thymidine analog, FTD, and thymidine phosphorylase inhibitor, TPI (molar ratio 1:0.5).	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	165-168
29568368-1	2018	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) is a combination of the antineoplastic thymidine analog, FTD, and thymidine phosphorylase inhibitor, TPI (molar ratio 1:0.5).	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
29568368-1	2018	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) is a combination of the antineoplastic thymidine analog, FTD, and thymidine phosphorylase inhibitor, TPI (molar ratio 1:0.5).	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	165-168
29568368-1	2018	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) is a combination of the antineoplastic thymidine analog, FTD, and thymidine phosphorylase inhibitor, TPI (molar ratio 1:0.5).	trifluridine tipiracil drug combination	55-62	triosephosphate isomerase 1	Homo sapiens	28-31
29568368-1	2018	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) is a combination of the antineoplastic thymidine analog, FTD, and thymidine phosphorylase inhibitor, TPI (molar ratio 1:0.5).	trifluridine tipiracil drug combination	55-62	triosephosphate isomerase 1	Homo sapiens	165-168
29568368-1	2018	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) is a combination of the antineoplastic thymidine analog, FTD, and thymidine phosphorylase inhibitor, TPI (molar ratio 1:0.5).	Thymidine	103-112	triosephosphate isomerase 1	Homo sapiens	28-31
29568368-3	2018	We evaluated the in vitro and in vivo efficacy and mechanisms of action of FTD and FTD/TPI against 5-fluorouracil (5-FU)-resistant MKN45/5FU, MKN74/5FU, and KATOIII/5FU human gastric cancer cells overexpressing thymidylate synthase (TS) and their respective parent cell lines.	Fluorouracil	99-113	triosephosphate isomerase 1	Homo sapiens	87-90
29568368-3	2018	We evaluated the in vitro and in vivo efficacy and mechanisms of action of FTD and FTD/TPI against 5-fluorouracil (5-FU)-resistant MKN45/5FU, MKN74/5FU, and KATOIII/5FU human gastric cancer cells overexpressing thymidylate synthase (TS) and their respective parent cell lines.	Fluorouracil	115-119	triosephosphate isomerase 1	Homo sapiens	87-90
29568368-10	2018	Thus, FTD/TPI is a promising chemotherapeutic agent against gastric cancers recurring following 5-FU therapy.	Fluorouracil	96-100	triosephosphate isomerase 1	Homo sapiens	10-13
29102632-3	2018	Tubulin Polymerization Inhibitor I (TPI1), a benzylidene derivative of 9(10H)-anthracenone, is a CBSI that inhibits the assembly of microtubules.	benzylidene	45-56	triosephosphate isomerase 1	Homo sapiens	36-40
29515409-1	2018	Trifluridine/tipiracil (FTD/TPI) significantly improves overall survival in patients with metastatic colorectal cancer (mCRC).	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
29515409-1	2018	Trifluridine/tipiracil (FTD/TPI) significantly improves overall survival in patients with metastatic colorectal cancer (mCRC).	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
29102632-3	2018	Tubulin Polymerization Inhibitor I (TPI1), a benzylidene derivative of 9(10H)-anthracenone, is a CBSI that inhibits the assembly of microtubules.	(10h)-anthracenone	72-90	triosephosphate isomerase 1	Homo sapiens	36-40
29102632-5	2018	Here we report a 2.3 A crystal structure of tubulin complexed with TPI1, the first structure of anthracenone family agents.	Anthracenone	96-108	triosephosphate isomerase 1	Homo sapiens	67-71
29102632-6	2018	This complex structure reveals the interactions between TPI1 and tubulin, and thus provides insights into the development of new anthracenone derivatives targeting the colchicine binding site.	Anthracenone	129-141	triosephosphate isomerase 1	Homo sapiens	56-60
29102632-6	2018	This complex structure reveals the interactions between TPI1 and tubulin, and thus provides insights into the development of new anthracenone derivatives targeting the colchicine binding site.	Colchicine	168-178	triosephosphate isomerase 1	Homo sapiens	56-60
29186784-4	2017	In this context, T. brucei depends on glycolysis as the unique source for ATP supply; therefore, the enzyme triosephosphate isomerase (TIM) is an attractive target for drug design.	Adenosine Triphosphate	74-77	triosephosphate isomerase 1	Homo sapiens	135-138
29312810-1	2017	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) with a molar ratio of 1:0.5, is a novel combination of FTD, an antineoplastic thymidine analog, and TPI, an inhibitor of thymidine phosphorylase.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	28-31
29312810-1	2017	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) with a molar ratio of 1:0.5, is a novel combination of FTD, an antineoplastic thymidine analog, and TPI, an inhibitor of thymidine phosphorylase.	Trifluridine	0-12	triosephosphate isomerase 1	Homo sapiens	164-167
29312810-1	2017	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) with a molar ratio of 1:0.5, is a novel combination of FTD, an antineoplastic thymidine analog, and TPI, an inhibitor of thymidine phosphorylase.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	28-31
29312810-1	2017	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) with a molar ratio of 1:0.5, is a novel combination of FTD, an antineoplastic thymidine analog, and TPI, an inhibitor of thymidine phosphorylase.	tipiracil	13-22	triosephosphate isomerase 1	Homo sapiens	164-167
29312810-1	2017	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) with a molar ratio of 1:0.5, is a novel combination of FTD, an antineoplastic thymidine analog, and TPI, an inhibitor of thymidine phosphorylase.	trifluridine tipiracil drug combination	55-62	triosephosphate isomerase 1	Homo sapiens	28-31
29312810-1	2017	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) with a molar ratio of 1:0.5, is a novel combination of FTD, an antineoplastic thymidine analog, and TPI, an inhibitor of thymidine phosphorylase.	trifluridine tipiracil drug combination	55-62	triosephosphate isomerase 1	Homo sapiens	164-167
29312810-1	2017	Trifluridine/tipiracil (FTD/TPI or TFTD, also known as TAS-102) with a molar ratio of 1:0.5, is a novel combination of FTD, an antineoplastic thymidine analog, and TPI, an inhibitor of thymidine phosphorylase.	Thymidine	142-151	triosephosphate isomerase 1	Homo sapiens	28-31
29312810-8	2017	Thus, the sequential treatment with SN-38 followed by FTD may be useful for the combination therapy of FTD/TPI and CPT-11 against relapsed colorectal cancer after 5-FU-based chemotherapy.	Irinotecan	36-41	triosephosphate isomerase 1	Homo sapiens	107-110
28587945-1	2017	A novel compound TPI-H containing triphenylimidazole chromophore is synthesized and employed as fluorescent probe for sequential detection of Cu2+ and S2-.	triphenylimidazole	34-52	triosephosphate isomerase 1	Homo sapiens	17-20
28990791-1	2017	Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate.	Dihydroxyacetone Phosphate	70-96	triosephosphate isomerase 1	Homo sapiens	0-25
28990791-1	2017	Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate.	Dihydroxyacetone Phosphate	70-96	triosephosphate isomerase 1	Homo sapiens	27-30
28990791-1	2017	Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate.	Dihydroxyacetone Phosphate	98-102	triosephosphate isomerase 1	Homo sapiens	0-25
28990791-1	2017	Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate.	Dihydroxyacetone Phosphate	98-102	triosephosphate isomerase 1	Homo sapiens	27-30
28990791-1	2017	Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate.	d-glyceraldehyde 3-phosphate	108-136	triosephosphate isomerase 1	Homo sapiens	0-25
28990791-1	2017	Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate.	d-glyceraldehyde 3-phosphate	108-136	triosephosphate isomerase 1	Homo sapiens	27-30
28990791-7	2017	We have found that in the enzyme-substrate reaction mixture with TIM from different organisms the number of substates and their population distribution within the DHAP side of the Michaelis complex may be different.	Dihydroxyacetone Phosphate	163-167	triosephosphate isomerase 1	Homo sapiens	65-68
28990791-8	2017	These discoveries provide a rare opportunity to probe the interconversion dynamics of these DHAP substates and form the bases for the future studies to determine if the TIM-catalyzed reaction follows a simple linear reaction pathway, as previously believed, or follows parallel reaction pathways, as suggested in another enzyme system that also shows a set of substates in the Michaelis complex.	Dihydroxyacetone Phosphate	92-96	triosephosphate isomerase 1	Homo sapiens	169-172
28587945-1	2017	A novel compound TPI-H containing triphenylimidazole chromophore is synthesized and employed as fluorescent probe for sequential detection of Cu2+ and S2-.	cupric ion	142-146	triosephosphate isomerase 1	Homo sapiens	17-20
28587945-2	2017	With three binding sites in its molecular structure, TPI-H exhibits highly selective binding towards Cu2+ and results in an apparent fluorescence "on-off" behavior.	cupric ion	101-105	triosephosphate isomerase 1	Homo sapiens	53-56
28587945-4	2017	Furthermore, the in-situ generated ensemble between TPI-H and Cu2+ (TPI-H-Cu(II)) can be used to detect S2- with a low detection limit of 15.6nM through Cu2+ displacement method.	cupric ion	62-66	triosephosphate isomerase 1	Homo sapiens	52-55
28587945-4	2017	Furthermore, the in-situ generated ensemble between TPI-H and Cu2+ (TPI-H-Cu(II)) can be used to detect S2- with a low detection limit of 15.6nM through Cu2+ displacement method.	cupric ion	62-66	triosephosphate isomerase 1	Homo sapiens	68-71
28587945-4	2017	Furthermore, the in-situ generated ensemble between TPI-H and Cu2+ (TPI-H-Cu(II)) can be used to detect S2- with a low detection limit of 15.6nM through Cu2+ displacement method.	Copper	62-64	triosephosphate isomerase 1	Homo sapiens	52-55
28587945-4	2017	Furthermore, the in-situ generated ensemble between TPI-H and Cu2+ (TPI-H-Cu(II)) can be used to detect S2- with a low detection limit of 15.6nM through Cu2+ displacement method.	Copper	62-64	triosephosphate isomerase 1	Homo sapiens	68-71
28587945-4	2017	Furthermore, the in-situ generated ensemble between TPI-H and Cu2+ (TPI-H-Cu(II)) can be used to detect S2- with a low detection limit of 15.6nM through Cu2+ displacement method.	cupric ion	153-157	triosephosphate isomerase 1	Homo sapiens	52-55
28587945-4	2017	Furthermore, the in-situ generated ensemble between TPI-H and Cu2+ (TPI-H-Cu(II)) can be used to detect S2- with a low detection limit of 15.6nM through Cu2+ displacement method.	cupric ion	153-157	triosephosphate isomerase 1	Homo sapiens	68-71
28126554-1	2017	Triosephosphate isomerase (TPI) is a vital enzyme in the glycolytic pathway, which can catalyze the interconversion of glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Glyceraldehyde 3-Phosphate	119-145	triosephosphate isomerase 1	Homo sapiens	0-25
28378917-2	2017	TIM is responsible for obtaining net ATP from glycolysis and producing an extra pyruvate molecule for each glucose molecule, under aerobic and anaerobic conditions.	Adenosine Triphosphate	37-40	triosephosphate isomerase 1	Homo sapiens	0-3
28378917-2	2017	TIM is responsible for obtaining net ATP from glycolysis and producing an extra pyruvate molecule for each glucose molecule, under aerobic and anaerobic conditions.	Pyruvic Acid	80-88	triosephosphate isomerase 1	Homo sapiens	0-3
28378917-2	2017	TIM is responsible for obtaining net ATP from glycolysis and producing an extra pyruvate molecule for each glucose molecule, under aerobic and anaerobic conditions.	Glucose	107-114	triosephosphate isomerase 1	Homo sapiens	0-3
28683550-1	2017	Triosephosphate isomerase (TIM) is a proficient catalyst of the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde phosphate (GAP), via general base catalysis by E165.	Dihydroxyacetone Phosphate	92-118	triosephosphate isomerase 1	Homo sapiens	0-25
28683550-1	2017	Triosephosphate isomerase (TIM) is a proficient catalyst of the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde phosphate (GAP), via general base catalysis by E165.	Dihydroxyacetone Phosphate	92-118	triosephosphate isomerase 1	Homo sapiens	27-30
28683550-1	2017	Triosephosphate isomerase (TIM) is a proficient catalyst of the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde phosphate (GAP), via general base catalysis by E165.	Dihydroxyacetone Phosphate	120-124	triosephosphate isomerase 1	Homo sapiens	0-25
28683550-1	2017	Triosephosphate isomerase (TIM) is a proficient catalyst of the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde phosphate (GAP), via general base catalysis by E165.	Dihydroxyacetone Phosphate	120-124	triosephosphate isomerase 1	Homo sapiens	27-30
28683550-1	2017	Triosephosphate isomerase (TIM) is a proficient catalyst of the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde phosphate (GAP), via general base catalysis by E165.	d-glyceraldehyde phosphate	129-155	triosephosphate isomerase 1	Homo sapiens	0-25
28683550-1	2017	Triosephosphate isomerase (TIM) is a proficient catalyst of the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde phosphate (GAP), via general base catalysis by E165.	d-glyceraldehyde phosphate	129-155	triosephosphate isomerase 1	Homo sapiens	27-30
28683550-3	2017	TIM is activated through an energetically demanding conformational change, which helps position the side chains of two key hydrophobic residues (I170 and L230), over the carboxylate side chain of E165.	carboxylate	170-181	triosephosphate isomerase 1	Homo sapiens	0-3
28683550-5	2017	Truncation of these residues to alanine causes significant falloffs in TIM"s catalytic activity, but experiments have failed to provide a full description of the action of this clamp in promoting substrate deprotonation.	Alanine	32-39	triosephosphate isomerase 1	Homo sapiens	71-74
28683550-6	2017	We perform here detailed empirical valence bond calculations of the TIM-catalyzed deprotonation of DHAP and GAP by both wild-type TIM and its I170A, L230A, and I170A/L230A mutants, obtaining exceptional quantitative agreement with experiment.	Dihydroxyacetone Phosphate	99-103	triosephosphate isomerase 1	Homo sapiens	68-71
28683550-6	2017	We perform here detailed empirical valence bond calculations of the TIM-catalyzed deprotonation of DHAP and GAP by both wild-type TIM and its I170A, L230A, and I170A/L230A mutants, obtaining exceptional quantitative agreement with experiment.	Dihydroxyacetone Phosphate	99-103	triosephosphate isomerase 1	Homo sapiens	130-133
28126554-1	2017	Triosephosphate isomerase (TPI) is a vital enzyme in the glycolytic pathway, which can catalyze the interconversion of glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Glyceraldehyde 3-Phosphate	119-145	triosephosphate isomerase 1	Homo sapiens	27-30
28126554-1	2017	Triosephosphate isomerase (TPI) is a vital enzyme in the glycolytic pathway, which can catalyze the interconversion of glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	156-182	triosephosphate isomerase 1	Homo sapiens	0-25
28126554-1	2017	Triosephosphate isomerase (TPI) is a vital enzyme in the glycolytic pathway, which can catalyze the interconversion of glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	156-182	triosephosphate isomerase 1	Homo sapiens	27-30
28126554-1	2017	Triosephosphate isomerase (TPI) is a vital enzyme in the glycolytic pathway, which can catalyze the interconversion of glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	184-188	triosephosphate isomerase 1	Homo sapiens	0-25
28126554-1	2017	Triosephosphate isomerase (TPI) is a vital enzyme in the glycolytic pathway, which can catalyze the interconversion of glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	184-188	triosephosphate isomerase 1	Homo sapiens	27-30
28422389-3	2017	Both of desferrioxamine and catechin could inhibit TIM nitration induced by heme-H2 O2 -NaNO2 and SIN-1 and protein oxidation induced by SIN-1, but promoted heme-H2 O2 -NaNO2 -induced protein oxidation.	Deferoxamine	8-23	triosephosphate isomerase 1	Homo sapiens	51-54
28422389-0	2017	Triosephosphate isomerase tyrosine nitration induced by heme-NaNO2 -H2 O2 or peroxynitrite: Effects of different natural phenolic compounds.	Tyrosine	26-34	triosephosphate isomerase 1	Homo sapiens	0-25
28422389-0	2017	Triosephosphate isomerase tyrosine nitration induced by heme-NaNO2 -H2 O2 or peroxynitrite: Effects of different natural phenolic compounds.	heme-nano2 -h2 o2	56-73	triosephosphate isomerase 1	Homo sapiens	0-25
28422389-0	2017	Triosephosphate isomerase tyrosine nitration induced by heme-NaNO2 -H2 O2 or peroxynitrite: Effects of different natural phenolic compounds.	Peroxynitrous Acid	77-90	triosephosphate isomerase 1	Homo sapiens	0-25
28422389-3	2017	Both of desferrioxamine and catechin could inhibit TIM nitration induced by heme-H2 O2 -NaNO2 and SIN-1 and protein oxidation induced by SIN-1, but promoted heme-H2 O2 -NaNO2 -induced protein oxidation.	Catechin	28-36	triosephosphate isomerase 1	Homo sapiens	51-54
28422389-3	2017	Both of desferrioxamine and catechin could inhibit TIM nitration induced by heme-H2 O2 -NaNO2 and SIN-1 and protein oxidation induced by SIN-1, but promoted heme-H2 O2 -NaNO2 -induced protein oxidation.	Heme	76-80	triosephosphate isomerase 1	Homo sapiens	51-54
28422389-3	2017	Both of desferrioxamine and catechin could inhibit TIM nitration induced by heme-H2 O2 -NaNO2 and SIN-1 and protein oxidation induced by SIN-1, but promoted heme-H2 O2 -NaNO2 -induced protein oxidation.	Hydrogen Peroxide	81-86	triosephosphate isomerase 1	Homo sapiens	51-54
28422389-3	2017	Both of desferrioxamine and catechin could inhibit TIM nitration induced by heme-H2 O2 -NaNO2 and SIN-1 and protein oxidation induced by SIN-1, but promoted heme-H2 O2 -NaNO2 -induced protein oxidation.	Hydrogen	81-83	triosephosphate isomerase 1	Homo sapiens	51-54
28422389-3	2017	Both of desferrioxamine and catechin could inhibit TIM nitration induced by heme-H2 O2 -NaNO2 and SIN-1 and protein oxidation induced by SIN-1, but promoted heme-H2 O2 -NaNO2 -induced protein oxidation.	Oxygen	84-86	triosephosphate isomerase 1	Homo sapiens	51-54
27543073-1	2017	Here we describe the long-term outcomes of type I thyroplasty (TP-I) with silicone block implantation through histopathological assessments in a male patient who underwent pharyngolaryngectomy for secondary hypopharyngeal carcinoma 7 years after silicone implantation.	Silicones	74-82	triosephosphate isomerase 1	Homo sapiens	43-67
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Hydrogen	108-110	triosephosphate isomerase 1	Homo sapiens	51-76
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Hydrogen	108-110	triosephosphate isomerase 1	Homo sapiens	78-81
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Oxygen	111-113	triosephosphate isomerase 1	Homo sapiens	51-76
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Oxygen	111-113	triosephosphate isomerase 1	Homo sapiens	78-81
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Tyrosine	199-207	triosephosphate isomerase 1	Homo sapiens	51-76
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Tyrosine	199-207	triosephosphate isomerase 1	Homo sapiens	78-81
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	linsidomine	221-258	triosephosphate isomerase 1	Homo sapiens	51-76
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	linsidomine	221-258	triosephosphate isomerase 1	Homo sapiens	78-81
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Peroxynitrous Acid	269-282	triosephosphate isomerase 1	Homo sapiens	51-76
28422389-2	2017	Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme-H2 O2 -NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor).	Peroxynitrous Acid	269-282	triosephosphate isomerase 1	Homo sapiens	78-81
27543073-1	2017	Here we describe the long-term outcomes of type I thyroplasty (TP-I) with silicone block implantation through histopathological assessments in a male patient who underwent pharyngolaryngectomy for secondary hypopharyngeal carcinoma 7 years after silicone implantation.	Silicones	246-254	triosephosphate isomerase 1	Homo sapiens	43-67
27780759-6	2017	We further studied guanidinium chloride (GdmCl)-induced denaturation of TIM-beta-globin complex by monitoring changes in the mean residue ellipticity at 222nm ([theta]222) and difference absorption coefficient at 406nm (Deltaepsilon406) at pH 7.5 and 25 C. We have observed that GdmCl-induced denaturation is reversible.	Guanidine	19-39	triosephosphate isomerase 1	Homo sapiens	72-75
27903763-12	2017	Phosphite dianion plays the active role of holding TIM in a high-energy closed active form, but acts as passive spectator in showing no effect on transition-state structure.	Phosphites	0-9	triosephosphate isomerase 1	Homo sapiens	51-54
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	Dihydroxyacetone Phosphate	75-101	triosephosphate isomerase 1	Homo sapiens	0-27
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	Dihydroxyacetone Phosphate	75-101	triosephosphate isomerase 1	Homo sapiens	29-33
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	Dihydroxyacetone Phosphate	103-107	triosephosphate isomerase 1	Homo sapiens	0-27
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	Dihydroxyacetone Phosphate	103-107	triosephosphate isomerase 1	Homo sapiens	29-33
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	d-glyceraldehyde 3-phosphate	113-141	triosephosphate isomerase 1	Homo sapiens	0-27
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	d-glyceraldehyde 3-phosphate	113-141	triosephosphate isomerase 1	Homo sapiens	29-33
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	3-phosphoglycerate	143-146	triosephosphate isomerase 1	Homo sapiens	0-27
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	3-phosphoglycerate	143-146	triosephosphate isomerase 1	Homo sapiens	29-33
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	Carbohydrates	212-224	triosephosphate isomerase 1	Homo sapiens	0-27
27908734-2	2017	Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism.	Carbohydrates	212-224	triosephosphate isomerase 1	Homo sapiens	29-33
27780759-6	2017	We further studied guanidinium chloride (GdmCl)-induced denaturation of TIM-beta-globin complex by monitoring changes in the mean residue ellipticity at 222nm ([theta]222) and difference absorption coefficient at 406nm (Deltaepsilon406) at pH 7.5 and 25 C. We have observed that GdmCl-induced denaturation is reversible.	Guanidine	41-46	triosephosphate isomerase 1	Homo sapiens	72-75
27647935-4	2016	While having a minute effect on the photosynthetic electron transport and oxygen photoreduction, ornidazole hinders the activity of two Calvin cycle enzymes, triose-phosphate isomerase (TPI) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).	Ornidazole	97-107	triosephosphate isomerase 1	Homo sapiens	158-184
27647935-4	2016	While having a minute effect on the photosynthetic electron transport and oxygen photoreduction, ornidazole hinders the activity of two Calvin cycle enzymes, triose-phosphate isomerase (TPI) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).	Ornidazole	97-107	triosephosphate isomerase 1	Homo sapiens	186-189
27647935-7	2016	Notably, TPI was inhibited by ornidazole in the dark or when electron transport was blocked by dichloromethyl diphenylurea, indicating that this inhibition was unrelated to the electron transport machinery.	Ornidazole	30-40	triosephosphate isomerase 1	Homo sapiens	9-12
27647935-7	2016	Notably, TPI was inhibited by ornidazole in the dark or when electron transport was blocked by dichloromethyl diphenylurea, indicating that this inhibition was unrelated to the electron transport machinery.	dichloromethyl diphenylurea	95-122	triosephosphate isomerase 1	Homo sapiens	9-12
26898502-5	2016	We report that multiple thiol-containing proteins involved in metabolism and glycolysis; fructose bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and creatine kinase, together with a number of chaperone, antioxidant and structural proteins, were modified in a reversible manner in macrophages treated with HOSCN.	Sulfhydryl Compounds	24-29	triosephosphate isomerase 1	Homo sapiens	121-146
27540836-1	2016	TPI 287 is a synthetic taxane derivative with structural modifications allowing for central nervous system penetration and potential circumvention of multidrug resistance efflux pump mechanisms.	taxane	23-29	triosephosphate isomerase 1	Homo sapiens	0-3
27559985-2	2016	Herein, we fabricated a new generation of smart adsorbents through grafting photoresponsive molecules, namely, 4-(3-triethoxysilylpropyl-ureido)azobenzene (AB-TPI), onto pore orifices of the support mesoporous silica.	4-(3-triethoxysilylpropyl-ureido)azobenzene	111-154	triosephosphate isomerase 1	Homo sapiens	159-162
27559985-2	2016	Herein, we fabricated a new generation of smart adsorbents through grafting photoresponsive molecules, namely, 4-(3-triethoxysilylpropyl-ureido)azobenzene (AB-TPI), onto pore orifices of the support mesoporous silica.	Silicon Dioxide	210-216	triosephosphate isomerase 1	Homo sapiens	159-162
26733481-5	2016	We show that TIM barrel enzymes corresponding to the most taxonomically broad superfamilies also have the broadest range of functions, often aided by metal and nucleotide-derived cofactors that are thought to reflect an earlier stage of metabolic evolution.	Metals	150-155	triosephosphate isomerase 1	Homo sapiens	13-16
26677869-1	2016	TAS-102 is a new oral anti-tumor drug, composed of a thymidine-based nucleoside analog (trifluridine: FTD) and a thymidine phosphorylase inhibitor (tipiracil hydrochloride: TPI).	trifluridine tipiracil drug combination	0-7	triosephosphate isomerase 1	Homo sapiens	173-176
26677869-1	2016	TAS-102 is a new oral anti-tumor drug, composed of a thymidine-based nucleoside analog (trifluridine: FTD) and a thymidine phosphorylase inhibitor (tipiracil hydrochloride: TPI).	Tipiracil hydrochloride	148-171	triosephosphate isomerase 1	Homo sapiens	173-176
29123462-2	2015	Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis.	d-glyceraldehyde 3-phosphate	74-102	triosephosphate isomerase 1	Homo sapiens	0-25
26570983-1	2015	The side chains of Y208 and S211 from loop 7 of triosephosphate isomerase (TIM) form hydrogen bonds to backbone amides and carbonyls from loop 6 to stabilize the caged enzyme-substrate complex.	Hydrogen	85-93	triosephosphate isomerase 1	Homo sapiens	48-73
26570983-1	2015	The side chains of Y208 and S211 from loop 7 of triosephosphate isomerase (TIM) form hydrogen bonds to backbone amides and carbonyls from loop 6 to stabilize the caged enzyme-substrate complex.	Hydrogen	85-93	triosephosphate isomerase 1	Homo sapiens	75-78
26570983-1	2015	The side chains of Y208 and S211 from loop 7 of triosephosphate isomerase (TIM) form hydrogen bonds to backbone amides and carbonyls from loop 6 to stabilize the caged enzyme-substrate complex.	Amides	112-118	triosephosphate isomerase 1	Homo sapiens	48-73
26570983-1	2015	The side chains of Y208 and S211 from loop 7 of triosephosphate isomerase (TIM) form hydrogen bonds to backbone amides and carbonyls from loop 6 to stabilize the caged enzyme-substrate complex.	Amides	112-118	triosephosphate isomerase 1	Homo sapiens	75-78
26570983-4	2015	The second linear logarithmic correlation [slope = 0.53 +- 0.16] between k(cat) for isomerization of GAP and K(d)( ) for phosphite dianion binding to the transition state for wildtype and many mutant TIM-catalyzed reactions of substrate pieces shows that ca.	Phosphites	121-130	triosephosphate isomerase 1	Homo sapiens	200-203
26570983-5	2015	50% of the wildtype TIM dianion binding energy, eliminated by these mutations, is expressed at the wildtype Michaelis complex, and ca.	dianion	24-31	triosephosphate isomerase 1	Homo sapiens	20-23
26535029-9	2015	Immunoblotting confirmed the up-regulation of Eno1 and Tpi1 in PaKiT03 cells following Poly I:C transfection.	Poly I-C	87-95	triosephosphate isomerase 1	Homo sapiens	55-59
29123462-2	2015	Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis.	Dihydroxyacetone Phosphate	112-138	triosephosphate isomerase 1	Homo sapiens	0-25
29123462-2	2015	Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis.	Dihydroxyacetone Phosphate	112-138	triosephosphate isomerase 1	Homo sapiens	27-30
29123462-2	2015	Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis.	Dihydroxyacetone Phosphate	140-144	triosephosphate isomerase 1	Homo sapiens	0-25
29123462-2	2015	Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis.	Dihydroxyacetone Phosphate	140-144	triosephosphate isomerase 1	Homo sapiens	27-30
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Glyceraldehyde 3-Phosphate	99-125	triosephosphate isomerase 1	Homo sapiens	0-25
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Glyceraldehyde 3-Phosphate	99-125	triosephosphate isomerase 1	Homo sapiens	27-30
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Glyceraldehyde 3-Phosphate	127-130	triosephosphate isomerase 1	Homo sapiens	0-25
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Glyceraldehyde 3-Phosphate	127-130	triosephosphate isomerase 1	Homo sapiens	27-30
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	136-162	triosephosphate isomerase 1	Homo sapiens	0-25
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	136-162	triosephosphate isomerase 1	Homo sapiens	27-30
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	164-168	triosephosphate isomerase 1	Homo sapiens	0-25
26602120-1	2016	Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	164-168	triosephosphate isomerase 1	Homo sapiens	27-30
26557901-6	2015	TAS-102, a combination of trifluorothymidine and the thymidine phosphorylase inhibitor TPI in a 1:0.5 ratio, is a novel oral formulation, which is active in 5FU-resistant models, both in vitro and in xenograft models.	trifluridine tipiracil drug combination	0-7	triosephosphate isomerase 1	Homo sapiens	87-90
29123462-2	2015	Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis.	d-glyceraldehyde 3-phosphate	74-102	triosephosphate isomerase 1	Homo sapiens	27-30
26353595-0	2015	Interaction of Silver Nanoparticles with Triosephosphate Isomerase from Human and Malarial Parasite (Plasmodium falciparum): A Comparative Study.	Silver	15-21	triosephosphate isomerase 1	Homo sapiens	41-66
26353595-3	2015	PfTIM had an optimal pH and temperature, K(m) and V(max) of 5.25, 25 degrees C, 12.8 mM and 1.13 mumol x mL(-1) min(-1) respectively while for hTIM the pH and temperature optima, K(m) and V(max) were 6.75, 30 degrees C; 8.2 mM and 1.35 mumol x ml(-1) min(-1).	pftim	0-5	triosephosphate isomerase 1	Homo sapiens	143-147
26353595-4	2015	Polyvinylpyrrolidone stabilised silver nanoparticles (60 nM; 2-6 nm diameter) selectively inhibited PfTIM with a 7-fold decrease in enzyme catalytic efficiency (K(cat)/K(m)) over hTIM.	Povidone	0-20	triosephosphate isomerase 1	Homo sapiens	179-183
26353595-4	2015	Polyvinylpyrrolidone stabilised silver nanoparticles (60 nM; 2-6 nm diameter) selectively inhibited PfTIM with a 7-fold decrease in enzyme catalytic efficiency (K(cat)/K(m)) over hTIM.	pftim	100-105	triosephosphate isomerase 1	Homo sapiens	179-183
25602614-0	2015	Why does Asn71 deamidate faster than Asn15 in the enzyme triosephosphate isomerase?	asn71 deamidate	9-24	triosephosphate isomerase 1	Homo sapiens	57-82
25716517-0	2015	A new inorganic-organic hybrid material Al-SBA-15-TPI/H6P2W18O62 catalyzed one-pot, three-component synthesis of 2H-indazolo[2,1-b]phthalazine-triones.	h6p2w18o62	54-64	triosephosphate isomerase 1	Homo sapiens	50-53
25716517-0	2015	A new inorganic-organic hybrid material Al-SBA-15-TPI/H6P2W18O62 catalyzed one-pot, three-component synthesis of 2H-indazolo[2,1-b]phthalazine-triones.	2h-indazolo[2,1-b]phthalazine-triones	113-150	triosephosphate isomerase 1	Homo sapiens	50-53
25716517-1	2015	A new inorganic-organic hybrid material Al-SBA-15-TPI/H6P2W18O62 was prepared and fully characterized by SEM, XRD, FT-IR, TGA-DTA, and UV-Vis spectroscopic techniques.	h6p2w18o62	54-64	triosephosphate isomerase 1	Homo sapiens	50-53
25602614-6	2015	The kinetics of asparagine dipeptide and two deamidation sites in mammalian TPI are also investigated using quantum mechanical/molecular mechanical tools with the umbrella sampling technique.	Asparagine	16-26	triosephosphate isomerase 1	Homo sapiens	76-79
25602614-6	2015	The kinetics of asparagine dipeptide and two deamidation sites in mammalian TPI are also investigated using quantum mechanical/molecular mechanical tools with the umbrella sampling technique.	Dipeptides	27-36	triosephosphate isomerase 1	Homo sapiens	76-79
25602614-8	2015	Our findings show that all the descriptors add up to favor the primary deamidation site over the secondary one in mammalian TPI: Asn71 deamidates faster because it is more solvent accessible, the adjacent glycine NH backbone acidity is enhanced, and the Asn side chain has a preferential near attack conformation.	Glycine	205-212	triosephosphate isomerase 1	Homo sapiens	124-127
25602614-8	2015	Our findings show that all the descriptors add up to favor the primary deamidation site over the secondary one in mammalian TPI: Asn71 deamidates faster because it is more solvent accessible, the adjacent glycine NH backbone acidity is enhanced, and the Asn side chain has a preferential near attack conformation.	Asparagine	129-132	triosephosphate isomerase 1	Homo sapiens	124-127
25102327-2	2014	It produces protein nitrotyrosination, after the reaction with nitric oxide to form peroxynitrite, being triosephosphate isomerase (TPI) one of the most affected proteins.	Nitric Oxide	63-75	triosephosphate isomerase 1	Homo sapiens	105-130
25901475-3	2015	Recently, TAS-102 (composed of FTD and tipiracil hydrochloride, TPI) was shown to prolong the survival of patients with colorectal cancer who received a median of 2 prior therapies, including 5-FU.	trifluridine tipiracil drug combination	10-17	triosephosphate isomerase 1	Homo sapiens	64-67
25901475-3	2015	Recently, TAS-102 (composed of FTD and tipiracil hydrochloride, TPI) was shown to prolong the survival of patients with colorectal cancer who received a median of 2 prior therapies, including 5-FU.	Fluorouracil	192-196	triosephosphate isomerase 1	Homo sapiens	64-67
25605932-6	2015	At one end of the HydG (betaalpha)8 triosephosphate isomerase (TIM) barrel, a canonical [4Fe-4S] cluster binds SAM in close proximity to the proposed tyrosine binding site.	Tyrosine	150-158	triosephosphate isomerase 1	Homo sapiens	36-61
25605932-6	2015	At one end of the HydG (betaalpha)8 triosephosphate isomerase (TIM) barrel, a canonical [4Fe-4S] cluster binds SAM in close proximity to the proposed tyrosine binding site.	Tyrosine	150-158	triosephosphate isomerase 1	Homo sapiens	63-66
25223993-0	2014	Giardial triosephosphate isomerase as possible target of the cytotoxic effect of omeprazole in Giardia lamblia.	Omeprazole	81-91	triosephosphate isomerase 1	Homo sapiens	9-34
25223993-3	2014	We used recombinant technology and enzyme inactivation to demonstrate the capacity of omeprazole to inactivate giardial triosephosphate isomerase, with no adverse effects on its human counterpart.	Omeprazole	86-96	triosephosphate isomerase 1	Homo sapiens	120-145
25223993-4	2014	To establish the specific target in the enzyme, we used single mutants of every cysteine residue in triosephosphate isomerase.	Cysteine	80-88	triosephosphate isomerase 1	Homo sapiens	100-125
25223993-5	2014	The effect on cellular triosephosphate isomerase was evaluated by following the remnant enzyme activity on trophozoites treated with omeprazole.	Omeprazole	133-143	triosephosphate isomerase 1	Homo sapiens	23-48
25223993-8	2014	Our results demonstrate that omeprazole inhibits giardial triosephosphate isomerase in a species-specific manner through interaction with cysteine at position 222.	Omeprazole	29-39	triosephosphate isomerase 1	Homo sapiens	58-83
25223993-8	2014	Our results demonstrate that omeprazole inhibits giardial triosephosphate isomerase in a species-specific manner through interaction with cysteine at position 222.	Cysteine	138-146	triosephosphate isomerase 1	Homo sapiens	58-83
25223993-9	2014	Omeprazole enters the cytoplasmic compartment of the trophozoites and inhibits cellular triosephosphate isomerase activity in a dose-dependent manner.	Omeprazole	0-10	triosephosphate isomerase 1	Homo sapiens	88-113
25223993-11	2014	G. lamblia triosephosphate isomerase (GlTIM) is a cytoplasmic protein which can help analyses of how omeprazole works against the proteins of this parasite and in the effort to understand its mechanism of cytotoxicity.	Omeprazole	101-111	triosephosphate isomerase 1	Homo sapiens	11-36
25223993-12	2014	Our results demonstrate the mechanism of giardial triosephosphate isomerase inhibition by omeprazole and show that this drug is effective in vitro against drug-resistant and drug-susceptible strains of G. lamblia.	Omeprazole	90-100	triosephosphate isomerase 1	Homo sapiens	50-75
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	Hydrogen	246-254	triosephosphate isomerase 1	Homo sapiens	61-64
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	Hydrogen	246-254	triosephosphate isomerase 1	Homo sapiens	75-100
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	Dihydroxyacetone Phosphate	270-296	triosephosphate isomerase 1	Homo sapiens	61-64
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	Dihydroxyacetone Phosphate	270-296	triosephosphate isomerase 1	Homo sapiens	75-100
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	Dihydroxyacetone Phosphate	298-302	triosephosphate isomerase 1	Homo sapiens	61-64
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	Dihydroxyacetone Phosphate	298-302	triosephosphate isomerase 1	Homo sapiens	75-100
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	d-glyceraldehyde 3-phosphate	307-335	triosephosphate isomerase 1	Homo sapiens	61-64
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	d-glyceraldehyde 3-phosphate	307-335	triosephosphate isomerase 1	Homo sapiens	75-100
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	DGAP	337-341	triosephosphate isomerase 1	Homo sapiens	61-64
25092608-2	2014	The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP).	DGAP	337-341	triosephosphate isomerase 1	Homo sapiens	75-100
25092608-5	2014	(d) The mechanism by which a ligand-gated conformational change, dominated by motion of loops 6 and 7, activates TIM for catalysis of deprotonation of DHAP or DGAP.	Dihydroxyacetone Phosphate	151-155	triosephosphate isomerase 1	Homo sapiens	113-116
25092608-5	2014	(d) The mechanism by which a ligand-gated conformational change, dominated by motion of loops 6 and 7, activates TIM for catalysis of deprotonation of DHAP or DGAP.	DGAP	159-163	triosephosphate isomerase 1	Homo sapiens	113-116
24919440-5	2014	RESULTS: By using integrated two datasets, we discovered that the biomarkers involved in the glycolysis pathway are highly enriched, including 4 genes (ENO1, TPI1, PKG1 and LDHC) and 2 metabolites (lactate and pyruvate).	Lactic Acid	198-205	triosephosphate isomerase 1	Homo sapiens	158-162
24919440-5	2014	RESULTS: By using integrated two datasets, we discovered that the biomarkers involved in the glycolysis pathway are highly enriched, including 4 genes (ENO1, TPI1, PKG1 and LDHC) and 2 metabolites (lactate and pyruvate).	Pyruvic Acid	210-218	triosephosphate isomerase 1	Homo sapiens	158-162
25102327-2	2014	It produces protein nitrotyrosination, after the reaction with nitric oxide to form peroxynitrite, being triosephosphate isomerase (TPI) one of the most affected proteins.	Nitric Oxide	63-75	triosephosphate isomerase 1	Homo sapiens	132-135
25102327-2	2014	It produces protein nitrotyrosination, after the reaction with nitric oxide to form peroxynitrite, being triosephosphate isomerase (TPI) one of the most affected proteins.	Peroxynitrous Acid	84-97	triosephosphate isomerase 1	Homo sapiens	105-130
25102327-2	2014	It produces protein nitrotyrosination, after the reaction with nitric oxide to form peroxynitrite, being triosephosphate isomerase (TPI) one of the most affected proteins.	Peroxynitrous Acid	84-97	triosephosphate isomerase 1	Homo sapiens	132-135
25102327-3	2014	TPI is a glycolytic enzyme that catalyzes the interconversion between glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Glyceraldehyde 3-Phosphate	70-96	triosephosphate isomerase 1	Homo sapiens	0-3
25102327-3	2014	TPI is a glycolytic enzyme that catalyzes the interconversion between glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	107-133	triosephosphate isomerase 1	Homo sapiens	0-3
25102327-3	2014	TPI is a glycolytic enzyme that catalyzes the interconversion between glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).	Dihydroxyacetone Phosphate	135-139	triosephosphate isomerase 1	Homo sapiens	0-3
25102327-4	2014	Methylglyoxal (MG) is a by-product of TPI activity whose production is triggered when TPI is nitrotyrosinated.	Pyruvaldehyde	0-13	triosephosphate isomerase 1	Homo sapiens	38-41
25102327-4	2014	Methylglyoxal (MG) is a by-product of TPI activity whose production is triggered when TPI is nitrotyrosinated.	Pyruvaldehyde	0-13	triosephosphate isomerase 1	Homo sapiens	86-89
25102327-4	2014	Methylglyoxal (MG) is a by-product of TPI activity whose production is triggered when TPI is nitrotyrosinated.	Pyruvaldehyde	15-17	triosephosphate isomerase 1	Homo sapiens	38-41
25102327-4	2014	Methylglyoxal (MG) is a by-product of TPI activity whose production is triggered when TPI is nitrotyrosinated.	Pyruvaldehyde	15-17	triosephosphate isomerase 1	Homo sapiens	86-89
25102327-4	2014	Methylglyoxal (MG) is a by-product of TPI activity whose production is triggered when TPI is nitrotyrosinated.	nitrotyrosinated	93-109	triosephosphate isomerase 1	Homo sapiens	38-41
25102327-4	2014	Methylglyoxal (MG) is a by-product of TPI activity whose production is triggered when TPI is nitrotyrosinated.	nitrotyrosinated	93-109	triosephosphate isomerase 1	Homo sapiens	86-89
25102327-7	2014	Moreover glycation was also observed when neuroblastoma cells overexpressed mutated TPI where Tyr165 or Tyr209, the two tyrosines close to the catalytic center, were changed by Phe in order to mimic the effect of nitrotyrosination.	Tyrosine	120-129	triosephosphate isomerase 1	Homo sapiens	84-87
25102327-7	2014	Moreover glycation was also observed when neuroblastoma cells overexpressed mutated TPI where Tyr165 or Tyr209, the two tyrosines close to the catalytic center, were changed by Phe in order to mimic the effect of nitrotyrosination.	Phenylalanine	177-180	triosephosphate isomerase 1	Homo sapiens	84-87
25102327-7	2014	Moreover glycation was also observed when neuroblastoma cells overexpressed mutated TPI where Tyr165 or Tyr209, the two tyrosines close to the catalytic center, were changed by Phe in order to mimic the effect of nitrotyrosination.	nitrotyrosination	213-230	triosephosphate isomerase 1	Homo sapiens	84-87
25206290-9	2014	The identified down-regulated proteins in CAPE-treated colorectal cancer cells were Triosephosphate Isomerase (Tim), Proteasome subunit alpha 4 (PSMA4) protein, Guanine nucleotide binding protein beta, Phosphoserine aminotransferase 1 (PSAT1), PSMA1, Myosin XVIIIB and Tryptophanyl-tRNA synthetase.	caffeic acid phenethyl ester	42-46	triosephosphate isomerase 1	Homo sapiens	84-109
25206290-9	2014	The identified down-regulated proteins in CAPE-treated colorectal cancer cells were Triosephosphate Isomerase (Tim), Proteasome subunit alpha 4 (PSMA4) protein, Guanine nucleotide binding protein beta, Phosphoserine aminotransferase 1 (PSAT1), PSMA1, Myosin XVIIIB and Tryptophanyl-tRNA synthetase.	caffeic acid phenethyl ester	42-46	triosephosphate isomerase 1	Homo sapiens	111-114
24373348-4	2014	We found that triosephosphate isomerase (TPI), a glycolytic enzyme produced by Staphylococcus aureus, bound to mannooligosaccharides from the pathogenic capsulated fungus Cryptococcus neoformans and human plasminogen, suggesting that TPI is a moonlighting protein.	mannooligosaccharides	111-132	triosephosphate isomerase 1	Homo sapiens	234-237
24699188-2	2014	There is a correlation between the burden to enzymatic catalysis of deprotonation of carbon acids and the substrate immobilization at solvent-occluded active sites for ketosteroid isomerase (KSI--small burden, substrate pKa=13), triosephosphate isomerase (TIM, substrate pKa 18) and diaminopimelate epimerase (DAP epimerase, large burden, substrate pKa 29) catalyzed reaction.	carbon acids	85-97	triosephosphate isomerase 1	Homo sapiens	229-254
24699188-2	2014	There is a correlation between the burden to enzymatic catalysis of deprotonation of carbon acids and the substrate immobilization at solvent-occluded active sites for ketosteroid isomerase (KSI--small burden, substrate pKa=13), triosephosphate isomerase (TIM, substrate pKa 18) and diaminopimelate epimerase (DAP epimerase, large burden, substrate pKa 29) catalyzed reaction.	carbon acids	85-97	triosephosphate isomerase 1	Homo sapiens	256-259
24614897-0	2014	Methylglyoxal produced by amyloid-beta peptide-induced nitrotyrosination of triosephosphate isomerase triggers neuronal death in Alzheimer"s disease.	Pyruvaldehyde	0-13	triosephosphate isomerase 1	Homo sapiens	76-101
24729658-0	2014	Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.	Carbon	45-51	triosephosphate isomerase 1	Homo sapiens	65-90
24729658-0	2014	Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.	phosphite dianion	113-130	triosephosphate isomerase 1	Homo sapiens	65-90
24729658-1	2014	The mechanistic imperatives for catalysis of deprotonation of alpha-carbonyl carbon by triosephosphate isomerase (TIM) are discussed.	Carbon	68-74	triosephosphate isomerase 1	Homo sapiens	87-112
24729658-1	2014	The mechanistic imperatives for catalysis of deprotonation of alpha-carbonyl carbon by triosephosphate isomerase (TIM) are discussed.	Carbon	68-74	triosephosphate isomerase 1	Homo sapiens	114-117
24729658-3	2014	Binding energies of 2 and 6 kcal/mol, respectively, have been determined for formation of phosphite dianion complexes to TIM and to the transition state for TIM-catalyzed deprotonation of the truncated substrate glycolaldehyde [T. L. Amyes, J. P. Richard, Biochemistry2007, 46, 5841].	phosphite dianion	90-107	triosephosphate isomerase 1	Homo sapiens	121-124
24729658-3	2014	Binding energies of 2 and 6 kcal/mol, respectively, have been determined for formation of phosphite dianion complexes to TIM and to the transition state for TIM-catalyzed deprotonation of the truncated substrate glycolaldehyde [T. L. Amyes, J. P. Richard, Biochemistry2007, 46, 5841].	phosphite dianion	90-107	triosephosphate isomerase 1	Homo sapiens	157-160
24729658-3	2014	Binding energies of 2 and 6 kcal/mol, respectively, have been determined for formation of phosphite dianion complexes to TIM and to the transition state for TIM-catalyzed deprotonation of the truncated substrate glycolaldehyde [T. L. Amyes, J. P. Richard, Biochemistry2007, 46, 5841].	glycolaldehyde	212-226	triosephosphate isomerase 1	Homo sapiens	157-160
24729658-3	2014	Binding energies of 2 and 6 kcal/mol, respectively, have been determined for formation of phosphite dianion complexes to TIM and to the transition state for TIM-catalyzed deprotonation of the truncated substrate glycolaldehyde [T. L. Amyes, J. P. Richard, Biochemistry2007, 46, 5841].	amyes	234-239	triosephosphate isomerase 1	Homo sapiens	121-124
24729658-3	2014	Binding energies of 2 and 6 kcal/mol, respectively, have been determined for formation of phosphite dianion complexes to TIM and to the transition state for TIM-catalyzed deprotonation of the truncated substrate glycolaldehyde [T. L. Amyes, J. P. Richard, Biochemistry2007, 46, 5841].	amyes	234-239	triosephosphate isomerase 1	Homo sapiens	157-160
24729658-4	2014	We propose that the phosphite dianion binding energy, which is specifically expressed at the transition state complex, is utilized to stabilize a rare catalytically active loop-closed form of TIM.	phosphite dianion	20-37	triosephosphate isomerase 1	Homo sapiens	192-195
24729658-6	2014	Evidence is presented that the hydrophobic side chain of Ile172 assists in activating TIM for catalysis of substrate deprotonation through an enhancement of the basicity of the carboxylate side-chain of Glu167.	carboxylate	177-188	triosephosphate isomerase 1	Homo sapiens	86-89
24729658-7	2014	Our experiments link the two imperatives for TIM-catalyzed deprotonation of carbon by providing evidence that the phosphodianion binding energy is utilized to drive an enzyme conformational change, which results in a reduction in the thermodynamic barrier to deprotonation of the carbon acid substrate at TIM compared with the barrier for deprotonation in water.	Carbon	76-82	triosephosphate isomerase 1	Homo sapiens	45-48
24729658-7	2014	Our experiments link the two imperatives for TIM-catalyzed deprotonation of carbon by providing evidence that the phosphodianion binding energy is utilized to drive an enzyme conformational change, which results in a reduction in the thermodynamic barrier to deprotonation of the carbon acid substrate at TIM compared with the barrier for deprotonation in water.	Carbon	76-82	triosephosphate isomerase 1	Homo sapiens	305-308
24729658-7	2014	Our experiments link the two imperatives for TIM-catalyzed deprotonation of carbon by providing evidence that the phosphodianion binding energy is utilized to drive an enzyme conformational change, which results in a reduction in the thermodynamic barrier to deprotonation of the carbon acid substrate at TIM compared with the barrier for deprotonation in water.	carbon acid	280-291	triosephosphate isomerase 1	Homo sapiens	45-48
24729658-7	2014	Our experiments link the two imperatives for TIM-catalyzed deprotonation of carbon by providing evidence that the phosphodianion binding energy is utilized to drive an enzyme conformational change, which results in a reduction in the thermodynamic barrier to deprotonation of the carbon acid substrate at TIM compared with the barrier for deprotonation in water.	carbon acid	280-291	triosephosphate isomerase 1	Homo sapiens	305-308
24729658-7	2014	Our experiments link the two imperatives for TIM-catalyzed deprotonation of carbon by providing evidence that the phosphodianion binding energy is utilized to drive an enzyme conformational change, which results in a reduction in the thermodynamic barrier to deprotonation of the carbon acid substrate at TIM compared with the barrier for deprotonation in water.	Water	356-361	triosephosphate isomerase 1	Homo sapiens	45-48
24729658-7	2014	Our experiments link the two imperatives for TIM-catalyzed deprotonation of carbon by providing evidence that the phosphodianion binding energy is utilized to drive an enzyme conformational change, which results in a reduction in the thermodynamic barrier to deprotonation of the carbon acid substrate at TIM compared with the barrier for deprotonation in water.	Water	356-361	triosephosphate isomerase 1	Homo sapiens	305-308
25516320-10	2014	Overall, TPI was associated with MAC (r=0.372, p<0.001), cAMA (r=0.337, p<0.001), and MAMC (r=0.351, p<0.001).	mamc	92-96	triosephosphate isomerase 1	Homo sapiens	9-12
25516320-11	2014	TPI-IDW was also associated with MAC (r=0.304, p<0.001), cAMA (r=0.202, p<0.001), and MAMC (r=0.200, p<0.001) but not for TPI normalized to actual body weight.	mamc	92-96	triosephosphate isomerase 1	Homo sapiens	0-3
25516320-12	2014	When examined separately, TPI was associated with MAC, cAMA, and MAMC in both CKD and healthy participants, but was associated with TPI-IDW only in CKD patients.	mamc	65-69	triosephosphate isomerase 1	Homo sapiens	26-29
25383217-10	2014	Docking and molecular dynamics (MD) suggested that the inhibitor made hydrogen bond contacts with TIM catalytic residues.	Hydrogen	70-78	triosephosphate isomerase 1	Homo sapiens	98-101
24614897-5	2014	We found an increased production of methylglyoxal (MG), a toxic byproduct of the inefficient nitro-TPI function.	Pyruvaldehyde	36-49	triosephosphate isomerase 1	Homo sapiens	99-102
24614897-5	2014	We found an increased production of methylglyoxal (MG), a toxic byproduct of the inefficient nitro-TPI function.	Pyruvaldehyde	51-53	triosephosphate isomerase 1	Homo sapiens	99-102
24614897-5	2014	We found an increased production of methylglyoxal (MG), a toxic byproduct of the inefficient nitro-TPI function.	nitro	93-98	triosephosphate isomerase 1	Homo sapiens	99-102
24614897-8	2014	Neuroblastoma cells transfected with the double mutant TPI consistently triggered MG production and a decrease in cell viability due to apoptotic mechanisms.	Pyruvaldehyde	82-84	triosephosphate isomerase 1	Homo sapiens	55-58
24614897-10	2014	This occurs because of TPI nitrotyrosination, which affects both tyrosines associated with the catalytic center.	Tyrosine	65-74	triosephosphate isomerase 1	Homo sapiens	23-26
23626684-3	2013	As a step toward designing a hybrid organic-inorganic ATP-generating system, we implemented a biomimetic site-specific immobilization strategy to tether two glycolytic enzymes representing different functional enzyme families: triose phosphoisomerase (TPI; an isomerase) and glyceraldehyde 3-phosphate dehydrogenase (GAPDHS; an oxidoreductase).	Adenosine Triphosphate	54-57	triosephosphate isomerase 1	Homo sapiens	227-250
23973283-1	2013	Triose phosphate isomerase (TPI) catalyses the interconversion of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate, a reaction in the glycolytic pathway.	Dihydroxyacetone Phosphate	66-92	triosephosphate isomerase 1	Homo sapiens	28-31
23973283-1	2013	Triose phosphate isomerase (TPI) catalyses the interconversion of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate, a reaction in the glycolytic pathway.	Glyceraldehyde 3-Phosphate	97-123	triosephosphate isomerase 1	Homo sapiens	28-31
23973283-5	2013	F. hepatica TPI is predicted to have a beta-barrel structure and key active site residues (Lys-14, His-95 and Glu-165) are conserved.	Lysine	91-94	triosephosphate isomerase 1	Homo sapiens	12-15
23973283-5	2013	F. hepatica TPI is predicted to have a beta-barrel structure and key active site residues (Lys-14, His-95 and Glu-165) are conserved.	Histidine	99-102	triosephosphate isomerase 1	Homo sapiens	12-15
23973283-5	2013	F. hepatica TPI is predicted to have a beta-barrel structure and key active site residues (Lys-14, His-95 and Glu-165) are conserved.	Glutamic Acid	110-113	triosephosphate isomerase 1	Homo sapiens	12-15
23973283-8	2013	Kinetic studies showed that F. hepatica TPI demonstrates Michaelis-Menten kinetics in both directions, with Km values for dihydroxyacetone phosphate and glyceraldehyde 3-phosphate of 2.3 mM and 0.66 mM respectively.	Dihydroxyacetone Phosphate	122-148	triosephosphate isomerase 1	Homo sapiens	40-43
23973283-8	2013	Kinetic studies showed that F. hepatica TPI demonstrates Michaelis-Menten kinetics in both directions, with Km values for dihydroxyacetone phosphate and glyceraldehyde 3-phosphate of 2.3 mM and 0.66 mM respectively.	Glyceraldehyde 3-Phosphate	153-179	triosephosphate isomerase 1	Homo sapiens	40-43
23946162-1	2013	A procedure for the synthesis of a(11)C-labeled oligopeptide containing [1-(11)C]1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid ([1-(11)C]Tpi) from the corresponding Trp HCl-containing peptides has been developed involving a Pictet-Spengler reaction with [(11) C]formaldehyde.	[1-(11)c]1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid	72-132	triosephosphate isomerase 1	Homo sapiens	143-146
23946162-2	2013	The synthesis of [1-(11)C]Tpi from Trp and [(11)C]formaldehyde was examined as a model reaction with the aim of developing a facile and effective method for the labeling of peptides with carbon-11.	Tryptophan	35-38	triosephosphate isomerase 1	Homo sapiens	26-29
23946162-2	2013	The synthesis of [1-(11)C]Tpi from Trp and [(11)C]formaldehyde was examined as a model reaction with the aim of developing a facile and effective method for the labeling of peptides with carbon-11.	[(11)c]formaldehyde	43-62	triosephosphate isomerase 1	Homo sapiens	26-29
23946162-2	2013	The synthesis of [1-(11)C]Tpi from Trp and [(11)C]formaldehyde was examined as a model reaction with the aim of developing a facile and effective method for the labeling of peptides with carbon-11.	Carbon-11	187-196	triosephosphate isomerase 1	Homo sapiens	26-29
23946162-3	2013	The Pictet-Spengler reaction of Trp and [(11)C]formaldehyde in acidic media (TsOH or HCl) afforded the desired [1-(11)C]Tpi in a moderate radiochemical yield.	Tryptophan	32-35	triosephosphate isomerase 1	Homo sapiens	120-123
23946162-3	2013	The Pictet-Spengler reaction of Trp and [(11)C]formaldehyde in acidic media (TsOH or HCl) afforded the desired [1-(11)C]Tpi in a moderate radiochemical yield.	Formaldehyde	47-59	triosephosphate isomerase 1	Homo sapiens	120-123
23946162-3	2013	The Pictet-Spengler reaction of Trp and [(11)C]formaldehyde in acidic media (TsOH or HCl) afforded the desired [1-(11)C]Tpi in a moderate radiochemical yield.	4-toluenesulfonic acid	77-81	triosephosphate isomerase 1	Homo sapiens	120-123
23946162-3	2013	The Pictet-Spengler reaction of Trp and [(11)C]formaldehyde in acidic media (TsOH or HCl) afforded the desired [1-(11)C]Tpi in a moderate radiochemical yield.	Hydrochloric Acid	85-88	triosephosphate isomerase 1	Homo sapiens	120-123
23768753-6	2013	Because two proteins, acrosin binding protein (ACRBP) and triosephosphate isomerase (TPI), presented the highest significant differences between GFE and PFE groups in two-dimensional difference gel electrophoresis assessment, Western blot analyses for ACRBP and TPI were also performed for validation.	perfluoroethylcyclohexane	153-156	triosephosphate isomerase 1	Homo sapiens	58-83
23768753-6	2013	Because two proteins, acrosin binding protein (ACRBP) and triosephosphate isomerase (TPI), presented the highest significant differences between GFE and PFE groups in two-dimensional difference gel electrophoresis assessment, Western blot analyses for ACRBP and TPI were also performed for validation.	perfluoroethylcyclohexane	153-156	triosephosphate isomerase 1	Homo sapiens	85-88
23768753-6	2013	Because two proteins, acrosin binding protein (ACRBP) and triosephosphate isomerase (TPI), presented the highest significant differences between GFE and PFE groups in two-dimensional difference gel electrophoresis assessment, Western blot analyses for ACRBP and TPI were also performed for validation.	perfluoroethylcyclohexane	153-156	triosephosphate isomerase 1	Homo sapiens	262-265
23318931-1	2013	Triose phosphate isomerase (TPI) is responsible for the interconversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate in glycolysis.	Dihydroxyacetone Phosphate	75-101	triosephosphate isomerase 1	Homo sapiens	0-26
23318931-1	2013	Triose phosphate isomerase (TPI) is responsible for the interconversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate in glycolysis.	Dihydroxyacetone Phosphate	75-101	triosephosphate isomerase 1	Homo sapiens	28-31
23318931-1	2013	Triose phosphate isomerase (TPI) is responsible for the interconversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate in glycolysis.	Glyceraldehyde 3-Phosphate	105-131	triosephosphate isomerase 1	Homo sapiens	0-26
23318931-1	2013	Triose phosphate isomerase (TPI) is responsible for the interconversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate in glycolysis.	Glyceraldehyde 3-Phosphate	105-131	triosephosphate isomerase 1	Homo sapiens	28-31
23318931-5	2013	Our data show that TPI(sugarkill) animals exhibit higher levels of the oxidized forms of NAD(+), NADP(+) and glutathione in an age-dependent manner.	NAD	89-95	triosephosphate isomerase 1	Homo sapiens	19-22
23318931-5	2013	Our data show that TPI(sugarkill) animals exhibit higher levels of the oxidized forms of NAD(+), NADP(+) and glutathione in an age-dependent manner.	NADP	97-104	triosephosphate isomerase 1	Homo sapiens	19-22
23318931-5	2013	Our data show that TPI(sugarkill) animals exhibit higher levels of the oxidized forms of NAD(+), NADP(+) and glutathione in an age-dependent manner.	Glutathione	109-120	triosephosphate isomerase 1	Homo sapiens	19-22
32261114-6	2013	The three-enzyme metabolon comprised of dockerin-containing triosephosphate isomerase, aldolase, and fructose 1,6-bisphosphatase was self-assembled because of the high-affinity interaction between cohesins and dockerins.	dockerin	40-48	triosephosphate isomerase 1	Homo sapiens	60-85
32261114-6	2013	The three-enzyme metabolon comprised of dockerin-containing triosephosphate isomerase, aldolase, and fructose 1,6-bisphosphatase was self-assembled because of the high-affinity interaction between cohesins and dockerins.	dockerins	210-219	triosephosphate isomerase 1	Homo sapiens	60-85
23768753-6	2013	Because two proteins, acrosin binding protein (ACRBP) and triosephosphate isomerase (TPI), presented the highest significant differences between GFE and PFE groups in two-dimensional difference gel electrophoresis assessment, Western blot analyses for ACRBP and TPI were also performed for validation.	1-(3,4-dichlorophenyl)-6,6-dimethyl-1,3,5-triazine-2,4-diamine	145-148	triosephosphate isomerase 1	Homo sapiens	58-83
23768753-6	2013	Because two proteins, acrosin binding protein (ACRBP) and triosephosphate isomerase (TPI), presented the highest significant differences between GFE and PFE groups in two-dimensional difference gel electrophoresis assessment, Western blot analyses for ACRBP and TPI were also performed for validation.	1-(3,4-dichlorophenyl)-6,6-dimethyl-1,3,5-triazine-2,4-diamine	145-148	triosephosphate isomerase 1	Homo sapiens	85-88
23768753-6	2013	Because two proteins, acrosin binding protein (ACRBP) and triosephosphate isomerase (TPI), presented the highest significant differences between GFE and PFE groups in two-dimensional difference gel electrophoresis assessment, Western blot analyses for ACRBP and TPI were also performed for validation.	1-(3,4-dichlorophenyl)-6,6-dimethyl-1,3,5-triazine-2,4-diamine	145-148	triosephosphate isomerase 1	Homo sapiens	262-265
23778534-5	2013	The results revealed that triosephosphate isomerase and ADP-sugar pyrophosphatase were downregulated, while peroxiredoxin-2, thioredoxin-dependent peroxide reductase, mitochondrial (Prx-3), peroxiredoxin-6, EGF-containing fibulin-like extracellular matrix protein 1, vimentin and Rab GDP dissociation inhibitor alpha were upregulated in the H2O2-treated EPCs.	Hydrogen Peroxide	341-345	triosephosphate isomerase 1	Homo sapiens	26-51
23526702-4	2013	In the present study, we have synthesized four analogues of P5U and urantide in which the Trp(7) residue was replaced by the highly constrained L-Tpi and D-Tpi residues.	p5u	60-63	triosephosphate isomerase 1	Homo sapiens	146-149
23526702-4	2013	In the present study, we have synthesized four analogues of P5U and urantide in which the Trp(7) residue was replaced by the highly constrained L-Tpi and D-Tpi residues.	p5u	60-63	triosephosphate isomerase 1	Homo sapiens	156-159
23526702-4	2013	In the present study, we have synthesized four analogues of P5U and urantide in which the Trp(7) residue was replaced by the highly constrained L-Tpi and D-Tpi residues.	urotensin II (4-11), Pen(5)-Trp(7)-Orn(8)-	68-76	triosephosphate isomerase 1	Homo sapiens	146-149
23526702-4	2013	In the present study, we have synthesized four analogues of P5U and urantide in which the Trp(7) residue was replaced by the highly constrained L-Tpi and D-Tpi residues.	urotensin II (4-11), Pen(5)-Trp(7)-Orn(8)-	68-76	triosephosphate isomerase 1	Homo sapiens	156-159
23526702-5	2013	The replacement of the Trp(7) by Tpi led to active analogues.	Tryptophan	23-26	triosephosphate isomerase 1	Homo sapiens	33-36
23626684-3	2013	As a step toward designing a hybrid organic-inorganic ATP-generating system, we implemented a biomimetic site-specific immobilization strategy to tether two glycolytic enzymes representing different functional enzyme families: triose phosphoisomerase (TPI; an isomerase) and glyceraldehyde 3-phosphate dehydrogenase (GAPDHS; an oxidoreductase).	Adenosine Triphosphate	54-57	triosephosphate isomerase 1	Homo sapiens	252-255
24564410-0	2013	Structural analysis on mutation residues and interfacial water molecules for human TIM disease understanding.	Water	57-62	triosephosphate isomerase 1	Homo sapiens	83-86
23853766-7	2013	TPI significantly correlated with age, Cys, CKD-EPI (cystatin), and IMT, whereas DPI significantly depended on Cystain, CKD-EPI (cystatin; cystatin-creatinine), IMT, NT-proBNP, and troponin I.	Cysteine	39-42	triosephosphate isomerase 1	Homo sapiens	0-3
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Sulfhydryl Compounds	82-87	triosephosphate isomerase 1	Homo sapiens	202-227
23233058-6	2013	One of the most nitrotyrosinated proteins in AD is the enzyme triosephosphate isomerase (TPI) that isomerises trioses, regulating glucose consumption by both phosphate pentose and glycolytic pathways and thereby pyruvate production.	Glucose	130-137	triosephosphate isomerase 1	Homo sapiens	62-87
23233058-6	2013	One of the most nitrotyrosinated proteins in AD is the enzyme triosephosphate isomerase (TPI) that isomerises trioses, regulating glucose consumption by both phosphate pentose and glycolytic pathways and thereby pyruvate production.	Glucose	130-137	triosephosphate isomerase 1	Homo sapiens	89-92
23233058-6	2013	One of the most nitrotyrosinated proteins in AD is the enzyme triosephosphate isomerase (TPI) that isomerises trioses, regulating glucose consumption by both phosphate pentose and glycolytic pathways and thereby pyruvate production.	phosphate pentose	158-175	triosephosphate isomerase 1	Homo sapiens	62-87
23233058-6	2013	One of the most nitrotyrosinated proteins in AD is the enzyme triosephosphate isomerase (TPI) that isomerises trioses, regulating glucose consumption by both phosphate pentose and glycolytic pathways and thereby pyruvate production.	phosphate pentose	158-175	triosephosphate isomerase 1	Homo sapiens	89-92
23233058-6	2013	One of the most nitrotyrosinated proteins in AD is the enzyme triosephosphate isomerase (TPI) that isomerises trioses, regulating glucose consumption by both phosphate pentose and glycolytic pathways and thereby pyruvate production.	Pyruvic Acid	212-220	triosephosphate isomerase 1	Homo sapiens	62-87
23233058-6	2013	One of the most nitrotyrosinated proteins in AD is the enzyme triosephosphate isomerase (TPI) that isomerises trioses, regulating glucose consumption by both phosphate pentose and glycolytic pathways and thereby pyruvate production.	Pyruvic Acid	212-220	triosephosphate isomerase 1	Homo sapiens	89-92
23233058-9	2013	Moreover, nitro-TPI aggregates interact with tau protein inducing the intraneuronal aggregation of tau.	nitro	10-15	triosephosphate isomerase 1	Homo sapiens	16-19
22622283-0	2012	TPI-287, a new taxane family member, reduces the brain metastatic colonization of breast cancer cells.	taxane	15-21	triosephosphate isomerase 1	Homo sapiens	0-3
22735906-1	2012	BACKGROUND: TAS-102 consists of alpha, alpha, alpha-trifluorothymidine (TFT) and an inhibitor of thymidine phosphorylase (TPI).	trifluridine tipiracil drug combination	12-19	triosephosphate isomerase 1	Homo sapiens	122-125
22411500-1	2012	The guanidine hydrochloride-induced conformational transitions of glycosomal triosephosphate isomerase (TIM) were monitored with functional, spectroscopic, and hydrodynamic measurements.	Guanidine	4-27	triosephosphate isomerase 1	Homo sapiens	77-102
22411500-1	2012	The guanidine hydrochloride-induced conformational transitions of glycosomal triosephosphate isomerase (TIM) were monitored with functional, spectroscopic, and hydrodynamic measurements.	Guanidine	4-27	triosephosphate isomerase 1	Homo sapiens	104-107
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	Dihydroxyacetone Phosphate	81-107	triosephosphate isomerase 1	Homo sapiens	0-25
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	Dihydroxyacetone Phosphate	81-107	triosephosphate isomerase 1	Homo sapiens	27-30
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	Dihydroxyacetone Phosphate	109-113	triosephosphate isomerase 1	Homo sapiens	0-25
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	Dihydroxyacetone Phosphate	109-113	triosephosphate isomerase 1	Homo sapiens	27-30
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	(r)-glyceraldehyde 3-phosphate	123-153	triosephosphate isomerase 1	Homo sapiens	0-25
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	(r)-glyceraldehyde 3-phosphate	123-153	triosephosphate isomerase 1	Homo sapiens	27-30
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	cis-enediolate phosphate	194-218	triosephosphate isomerase 1	Homo sapiens	0-25
22409228-1	2012	Triosephosphate isomerase (TIM) catalyzes the stereospecific 1,2-proton shift at dihydroxyacetone phosphate (DHAP) to give (R)-glyceraldehyde 3-phosphate through a pair of isomeric enzyme-bound cis-enediolate phosphate intermediates.	cis-enediolate phosphate	194-218	triosephosphate isomerase 1	Homo sapiens	27-30
22126412-0	2012	The structure of the thioredoxin-triosephosphate isomerase complex provides insights into the reversible glutathione-mediated regulation of triosephosphate isomerase.	Glutathione	105-116	triosephosphate isomerase 1	Homo sapiens	33-58
22126412-0	2012	The structure of the thioredoxin-triosephosphate isomerase complex provides insights into the reversible glutathione-mediated regulation of triosephosphate isomerase.	Glutathione	105-116	triosephosphate isomerase 1	Homo sapiens	140-165
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Cysteine	37-45	triosephosphate isomerase 1	Homo sapiens	98-123
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Cysteine	37-45	triosephosphate isomerase 1	Homo sapiens	202-227
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Cysteine	37-45	triosephosphate isomerase 1	Homo sapiens	202-227
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Sulfhydryl Compounds	82-87	triosephosphate isomerase 1	Homo sapiens	98-123
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Sulfhydryl Compounds	82-87	triosephosphate isomerase 1	Homo sapiens	202-227
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Cysteine	186-194	triosephosphate isomerase 1	Homo sapiens	98-123
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Cysteine	186-194	triosephosphate isomerase 1	Homo sapiens	202-227
22126412-7	2012	The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.	Cysteine	186-194	triosephosphate isomerase 1	Homo sapiens	202-227
22848767-6	2012	RESULTS: This study revealed that triterpenoid and steroid ligands were largely selective for sterol 14alpha-demethylase; anthraquinones, xanthones, and berberine alkaloids docked strongly to pteridine reductase 1 (TbPTR1); chromenes, pyrazole and pyridine alkaloids preferred docking to triose phosphate isomerase (TbTIM); and numerous indole alkaloids showed notable docking energies with UDP-galactose 4" epimerase (TbUDPGE).	triterpenoid TP-222	34-46	triosephosphate isomerase 1	Homo sapiens	288-314
21358682-9	2012	Wortmannin, but not PD98059, enhanced the downregulation of TPI in G-CSF-treated NK-92MI cells, indicating a correlation between PI3K and TPI.	Wortmannin	0-10	triosephosphate isomerase 1	Homo sapiens	60-63
21358682-9	2012	Wortmannin, but not PD98059, enhanced the downregulation of TPI in G-CSF-treated NK-92MI cells, indicating a correlation between PI3K and TPI.	Wortmannin	0-10	triosephosphate isomerase 1	Homo sapiens	138-141
22848767-6	2012	RESULTS: This study revealed that triterpenoid and steroid ligands were largely selective for sterol 14alpha-demethylase; anthraquinones, xanthones, and berberine alkaloids docked strongly to pteridine reductase 1 (TbPTR1); chromenes, pyrazole and pyridine alkaloids preferred docking to triose phosphate isomerase (TbTIM); and numerous indole alkaloids showed notable docking energies with UDP-galactose 4" epimerase (TbUDPGE).	Steroids	51-58	triosephosphate isomerase 1	Homo sapiens	288-314
22848767-6	2012	RESULTS: This study revealed that triterpenoid and steroid ligands were largely selective for sterol 14alpha-demethylase; anthraquinones, xanthones, and berberine alkaloids docked strongly to pteridine reductase 1 (TbPTR1); chromenes, pyrazole and pyridine alkaloids preferred docking to triose phosphate isomerase (TbTIM); and numerous indole alkaloids showed notable docking energies with UDP-galactose 4" epimerase (TbUDPGE).	Anthraquinones	122-136	triosephosphate isomerase 1	Homo sapiens	288-314
22848767-6	2012	RESULTS: This study revealed that triterpenoid and steroid ligands were largely selective for sterol 14alpha-demethylase; anthraquinones, xanthones, and berberine alkaloids docked strongly to pteridine reductase 1 (TbPTR1); chromenes, pyrazole and pyridine alkaloids preferred docking to triose phosphate isomerase (TbTIM); and numerous indole alkaloids showed notable docking energies with UDP-galactose 4" epimerase (TbUDPGE).	Xanthones	138-147	triosephosphate isomerase 1	Homo sapiens	288-314
22848767-6	2012	RESULTS: This study revealed that triterpenoid and steroid ligands were largely selective for sterol 14alpha-demethylase; anthraquinones, xanthones, and berberine alkaloids docked strongly to pteridine reductase 1 (TbPTR1); chromenes, pyrazole and pyridine alkaloids preferred docking to triose phosphate isomerase (TbTIM); and numerous indole alkaloids showed notable docking energies with UDP-galactose 4" epimerase (TbUDPGE).	Berberine Alkaloids	153-172	triosephosphate isomerase 1	Homo sapiens	288-314
21873653-8	2011	RESULTS: Senofilcon A lenses were beneficial for protecting HLE B-3 cells against UVB radiation-induced changes in caldesmon 1 isoform, lamin A/C transcript variant 1, DEAD (Asp-Glu-Ala-Asp) box polypeptide, beta-actin, glyceraldehyde 3-phosphate dehydrogenase (G3PDH), annexin A2, triose phosphate isomerase, and ubiquitin B precursor.	senofilcon A	9-21	triosephosphate isomerase 1	Homo sapiens	282-308
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	Ketoses	80-86	triosephosphate isomerase 1	Homo sapiens	0-53
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	Ketoses	80-86	triosephosphate isomerase 1	Homo sapiens	55-58
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	Xylose	114-122	triosephosphate isomerase 1	Homo sapiens	0-53
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	Xylose	114-122	triosephosphate isomerase 1	Homo sapiens	55-58
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	d-glyceraldehyde 3-phosphate	127-155	triosephosphate isomerase 1	Homo sapiens	0-53
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	d-glyceraldehyde 3-phosphate	127-155	triosephosphate isomerase 1	Homo sapiens	55-58
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	DGAP	157-161	triosephosphate isomerase 1	Homo sapiens	0-53
21995300-1	2011	D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively.	DGAP	157-161	triosephosphate isomerase 1	Homo sapiens	55-58
21995300-2	2011	D-Glyceraldehyde (DGA) is the triose fragment common to the substrates for XI and TIM.	Glyceraldehyde	0-16	triosephosphate isomerase 1	Homo sapiens	82-85
21995300-2	2011	D-Glyceraldehyde (DGA) is the triose fragment common to the substrates for XI and TIM.	Glyceraldehyde	18-21	triosephosphate isomerase 1	Homo sapiens	82-85
21633986-0	2011	High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: the conformational flexibility of the catalytic glutamate in its closed, liganded active site.	Glutamic Acid	151-160	triosephosphate isomerase 1	Homo sapiens	38-63
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Dihydroxyacetone Phosphate	165-191	triosephosphate isomerase 1	Homo sapiens	117-142
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Dihydroxyacetone Phosphate	165-191	triosephosphate isomerase 1	Homo sapiens	144-147
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Dihydroxyacetone Phosphate	193-197	triosephosphate isomerase 1	Homo sapiens	117-142
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Dihydroxyacetone Phosphate	193-197	triosephosphate isomerase 1	Homo sapiens	144-147
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Glyceraldehyde 3-Phosphate	202-228	triosephosphate isomerase 1	Homo sapiens	117-142
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Glyceraldehyde 3-Phosphate	202-228	triosephosphate isomerase 1	Homo sapiens	144-147
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Glyceraldehyde 3-Phosphate	230-233	triosephosphate isomerase 1	Homo sapiens	117-142
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Glyceraldehyde 3-Phosphate	230-233	triosephosphate isomerase 1	Homo sapiens	144-147
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Asparagine	339-349	triosephosphate isomerase 1	Homo sapiens	117-142
21651995-1	2011	Research carried out up to 3 decades ago by Gracy and co-workers revealed that the activity of the glycolytic enzyme triosephosphate isomerase (TPI), which converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), gradually declines whilst carrying out its catalytic function, primarily due to deamidation of certain asparagine residues.	Asparagine	339-349	triosephosphate isomerase 1	Homo sapiens	144-147
21651995-2	2011	It is suggested here that excessive or continuous glycolysis increases TPI deamidation and thereby lowers TPI activity and causes accumulation of its substrate, DHAP, which in turn decomposes into methylglyoxal (MG), a well-recognised reactive bicarbonyl whose actions in cells and tissues, as well as at the whole organism level, mimic much age-relate dysfunction.	Pyruvaldehyde	212-214	triosephosphate isomerase 1	Homo sapiens	71-74
21786322-4	2011	We previously demonstrated that the glycolytic enzyme triosephosphate isomerase from G. lamblia (GlTIM), could be completely inactivated by low micromolar concentrations of thiol-reactive compounds, whereas, in the same conditions, the activity of human TIM (HuTIM) was almost unaltered.	Sulfhydryl Compounds	173-178	triosephosphate isomerase 1	Homo sapiens	54-79
21786322-4	2011	We previously demonstrated that the glycolytic enzyme triosephosphate isomerase from G. lamblia (GlTIM), could be completely inactivated by low micromolar concentrations of thiol-reactive compounds, whereas, in the same conditions, the activity of human TIM (HuTIM) was almost unaltered.	Sulfhydryl Compounds	173-178	triosephosphate isomerase 1	Homo sapiens	99-102
21633986-1	2011	The key residue of the active site of triosephosphate isomerase (TIM) is the catalytic glutamate, which is proposed to be important (i) as a catalytic base, for initiating the reaction, as well as (ii) for the subsequent proton shuttling steps.	Glutamic Acid	87-96	triosephosphate isomerase 1	Homo sapiens	38-63
21633986-1	2011	The key residue of the active site of triosephosphate isomerase (TIM) is the catalytic glutamate, which is proposed to be important (i) as a catalytic base, for initiating the reaction, as well as (ii) for the subsequent proton shuttling steps.	Glutamic Acid	87-96	triosephosphate isomerase 1	Homo sapiens	65-68
21633986-2	2011	The structural properties of this glutamate in the liganded complex have been investigated by studying the high resolution crystal structures of typanosomal TIM, complexed with three suicide inhibitors: (S)-glycidol phosphate ((S)-GOP, at 0.99 A resolution), (R)-glycidol phosphate, ((R)-GOP, at 1.08 A resolution), and bromohydroxyacetone phosphate (BHAP, at 1.97 A resolution).	Glutamic Acid	34-43	triosephosphate isomerase 1	Homo sapiens	157-160
21633986-2	2011	The structural properties of this glutamate in the liganded complex have been investigated by studying the high resolution crystal structures of typanosomal TIM, complexed with three suicide inhibitors: (S)-glycidol phosphate ((S)-GOP, at 0.99 A resolution), (R)-glycidol phosphate, ((R)-GOP, at 1.08 A resolution), and bromohydroxyacetone phosphate (BHAP, at 1.97 A resolution).	glycidol phosphate	203-225	triosephosphate isomerase 1	Homo sapiens	157-160
21633986-8	2011	The importance of this conformational flexibility for the proton shuttling steps in the TIM catalytic cycle, which is apparently achieved by a sliding motion of the side chain carboxylate group above the enediolate plane, is also discussed.	carboxylate	176-187	triosephosphate isomerase 1	Homo sapiens	88-91
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	d-glyceraldehyde 3-phosphate	61-89	triosephosphate isomerase 1	Homo sapiens	0-25
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	d-glyceraldehyde 3-phosphate	61-89	triosephosphate isomerase 1	Homo sapiens	27-30
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	Dihydroxyacetone Phosphate	94-120	triosephosphate isomerase 1	Homo sapiens	0-25
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	Dihydroxyacetone Phosphate	94-120	triosephosphate isomerase 1	Homo sapiens	27-30
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	orotidine monophosphate decarboxylase	195-232	triosephosphate isomerase 1	Homo sapiens	0-25
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	orotidine monophosphate decarboxylase	195-232	triosephosphate isomerase 1	Homo sapiens	27-30
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	ompdc	234-239	triosephosphate isomerase 1	Homo sapiens	0-25
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	ompdc	234-239	triosephosphate isomerase 1	Homo sapiens	27-30
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	orotidylic acid	270-296	triosephosphate isomerase 1	Homo sapiens	0-25
23505326-3	2011	Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation.	orotidylic acid	270-296	triosephosphate isomerase 1	Homo sapiens	27-30
22977515-1	2011	TAS-102 is an oral anticancer drug composed of trifluorothymidine (TFT) and TPI (an inhibitor of thymidine phosphorylase that strongly inhibits the biodegradation of TFT).	trifluridine tipiracil drug combination	0-7	triosephosphate isomerase 1	Homo sapiens	76-79
21173383-8	2011	Second, photoreceptors contain very little triosephosphate isomerase, an enzyme converting dihydroxyacetone phosphate into glyceraldehyde-3-phosphate.	Dihydroxyacetone Phosphate	91-117	triosephosphate isomerase 1	Homo sapiens	43-68
21173383-8	2011	Second, photoreceptors contain very little triosephosphate isomerase, an enzyme converting dihydroxyacetone phosphate into glyceraldehyde-3-phosphate.	Glyceraldehyde 3-Phosphate	123-149	triosephosphate isomerase 1	Homo sapiens	43-68
20349518-8	2010	Cobalt is a hypoxia mimicking agent and N-myc downstream regulated gene 1 protein, Triose phosphate isomerase, Pyruvate kinase, and Annexin II are important hypoxia regulated gene products that are found to be over expressed in cellular oxidative stress response.	Cobalt	0-6	triosephosphate isomerase 1	Homo sapiens	83-109
20730777-7	2011	A similar result is obtained for TIM in the unliganded and dihydroxyacetone phosphate bound states.	Dihydroxyacetone Phosphate	59-85	triosephosphate isomerase 1	Homo sapiens	33-36
20149834-0	2010	Functional inactivation of triosephosphate isomerase through phosphorylation during etoposide-induced apoptosis in HeLa cells: potential role of Cdk2.	Etoposide	84-93	triosephosphate isomerase 1	Homo sapiens	27-52
20149834-6	2010	Among the six candidate phosphoproteins, human triosephosphate isomerase (TPI), a glycolytic enzyme, was found to be a direct substrate of Cdk2 during etoposide-induced apoptosis.	Etoposide	151-160	triosephosphate isomerase 1	Homo sapiens	47-72
20149834-6	2010	Among the six candidate phosphoproteins, human triosephosphate isomerase (TPI), a glycolytic enzyme, was found to be a direct substrate of Cdk2 during etoposide-induced apoptosis.	Etoposide	151-160	triosephosphate isomerase 1	Homo sapiens	74-77
20149834-9	2010	Such phosphorylation of TPI and a subsequent decrease in its enzyme activity were prevented by treatment with olomoucine, a specific inhibitor of Cdk2.	olomoucine	110-120	triosephosphate isomerase 1	Homo sapiens	24-27
20149834-11	2010	Loss of catalytic activity of TPI as a consequence of phosphorylation of this glycolytic enzyme may disrupt energy production in etoposide-treated HeLa cells, rendering these cells prone to undergo apoptosis.	Etoposide	129-138	triosephosphate isomerase 1	Homo sapiens	30-33
20951028-1	2010	Triosephosphate isomerase (TIM), glycerol 3-phosphate dehydrogenase, and orotidine 5"-monophosphate decarboxylase each use the binding energy from the interaction of phosphite dianion with a flexible phosphate gripper loop to activate a second, phosphodianion-truncated, substrate towards enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation, respectively.	phosphite dianion	166-183	triosephosphate isomerase 1	Homo sapiens	0-25
20951028-1	2010	Triosephosphate isomerase (TIM), glycerol 3-phosphate dehydrogenase, and orotidine 5"-monophosphate decarboxylase each use the binding energy from the interaction of phosphite dianion with a flexible phosphate gripper loop to activate a second, phosphodianion-truncated, substrate towards enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation, respectively.	phosphite dianion	166-183	triosephosphate isomerase 1	Homo sapiens	27-30
20951028-1	2010	Triosephosphate isomerase (TIM), glycerol 3-phosphate dehydrogenase, and orotidine 5"-monophosphate decarboxylase each use the binding energy from the interaction of phosphite dianion with a flexible phosphate gripper loop to activate a second, phosphodianion-truncated, substrate towards enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation, respectively.	Phosphates	6-15	triosephosphate isomerase 1	Homo sapiens	27-30
20951028-1	2010	Triosephosphate isomerase (TIM), glycerol 3-phosphate dehydrogenase, and orotidine 5"-monophosphate decarboxylase each use the binding energy from the interaction of phosphite dianion with a flexible phosphate gripper loop to activate a second, phosphodianion-truncated, substrate towards enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation, respectively.	phosphodianion	245-259	triosephosphate isomerase 1	Homo sapiens	0-25
20951028-1	2010	Triosephosphate isomerase (TIM), glycerol 3-phosphate dehydrogenase, and orotidine 5"-monophosphate decarboxylase each use the binding energy from the interaction of phosphite dianion with a flexible phosphate gripper loop to activate a second, phosphodianion-truncated, substrate towards enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation, respectively.	phosphodianion	245-259	triosephosphate isomerase 1	Homo sapiens	27-30
20951028-2	2010	Studies on TIM suggest that the most important general effect of loop closure over the substrate phosphodianion, and the associated conformational changes, is to extrude water from the enzyme active site.	Water	170-175	triosephosphate isomerase 1	Homo sapiens	11-14
21738601-0	2011	A ribosomal misincorporation of Lys for Arg in human triosephosphate isomerase expressed in Escherichia coli gives rise to two protein populations.	Lysine	32-35	triosephosphate isomerase 1	Homo sapiens	53-78
21738601-0	2011	A ribosomal misincorporation of Lys for Arg in human triosephosphate isomerase expressed in Escherichia coli gives rise to two protein populations.	Arginine	40-43	triosephosphate isomerase 1	Homo sapiens	53-78
21738601-6	2011	They were catalytically active, but differed in molecular mass, thermostability, susceptibility to urea and proteinase K. An analysis of the nucleotides in the human TIM gene revealed the presence of six codons that are not commonly used in E. coli.	Urea	99-103	triosephosphate isomerase 1	Homo sapiens	166-169
20866109-3	2010	The combined equilibrium constant for glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and triose phosphate isomerase for the three reactions (K(GG-TPI)") was corrected using new binding constants for dihydroxyacetone-phosphate and 3-phosphoglycerate.	Dihydroxyacetone Phosphate	219-245	triosephosphate isomerase 1	Homo sapiens	109-135
20866109-3	2010	The combined equilibrium constant for glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and triose phosphate isomerase for the three reactions (K(GG-TPI)") was corrected using new binding constants for dihydroxyacetone-phosphate and 3-phosphoglycerate.	Dihydroxyacetone Phosphate	219-245	triosephosphate isomerase 1	Homo sapiens	166-169
20866109-3	2010	The combined equilibrium constant for glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and triose phosphate isomerase for the three reactions (K(GG-TPI)") was corrected using new binding constants for dihydroxyacetone-phosphate and 3-phosphoglycerate.	3-phosphoglycerate	250-268	triosephosphate isomerase 1	Homo sapiens	109-135
20866109-3	2010	The combined equilibrium constant for glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and triose phosphate isomerase for the three reactions (K(GG-TPI)") was corrected using new binding constants for dihydroxyacetone-phosphate and 3-phosphoglycerate.	3-phosphoglycerate	250-268	triosephosphate isomerase 1	Homo sapiens	166-169
20694739-1	2010	Triosephosphate isomerase (TIM) is a perfectly evolved enzyme which very fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate.	Dihydroxyacetone Phosphate	92-118	triosephosphate isomerase 1	Homo sapiens	0-25
20694739-1	2010	Triosephosphate isomerase (TIM) is a perfectly evolved enzyme which very fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate.	Dihydroxyacetone Phosphate	92-118	triosephosphate isomerase 1	Homo sapiens	27-30
20694739-1	2010	Triosephosphate isomerase (TIM) is a perfectly evolved enzyme which very fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate.	d: -glyceraldehyde-3-phosphate	123-153	triosephosphate isomerase 1	Homo sapiens	0-25
20694739-1	2010	Triosephosphate isomerase (TIM) is a perfectly evolved enzyme which very fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate.	d: -glyceraldehyde-3-phosphate	123-153	triosephosphate isomerase 1	Homo sapiens	27-30
20541591-8	2010	CONCLUSION: Protein arginine dimethylations of hnRNPR, CstF-64, and TPI were regulated during HeLa cell cycle by respective PRMTs.	Arginine	20-28	triosephosphate isomerase 1	Homo sapiens	68-71
20541591-9	2010	GENERAL SIGNIFICANCE: These results suggest that regulation of arginine dimethylation of hnRNPR, CstF-64, and TPI at G0/G1 to G1 are most likely to modulate the cellular growth and proliferation in HeLa cell cycle.	Arginine	63-71	triosephosphate isomerase 1	Homo sapiens	110-113
20235230-3	2010	Here, we have investigated the reaction mechanism of triosephosphate isomerase (TIM) using atomic resolution crystallographic studies at 0.82-A resolution of leishmanial TIM complexed with the well-studied reaction-intermediate analog phosphoglycolohydroxamate (PGH).	phosphoglycolohydroxamate	235-260	triosephosphate isomerase 1	Homo sapiens	53-78
20105085-6	2010	Adriamycin decreased the expression of the metabolism-related proteins, ATP synthase, Sdha protein, Triose phosphate isomerase 1 (TPI-1), pyruvate dehydrogenase E1 alpha1, 6-phosphofructokinase, and fructose-1,6-bisphosphatase, as did cytoskeletal proteins, such as actin.	Doxorubicin	0-10	triosephosphate isomerase 1	Homo sapiens	100-128
20105085-6	2010	Adriamycin decreased the expression of the metabolism-related proteins, ATP synthase, Sdha protein, Triose phosphate isomerase 1 (TPI-1), pyruvate dehydrogenase E1 alpha1, 6-phosphofructokinase, and fructose-1,6-bisphosphatase, as did cytoskeletal proteins, such as actin.	Doxorubicin	0-10	triosephosphate isomerase 1	Homo sapiens	130-135
20621659-5	2010	The ethanol-treated NCCIT cells demonstrate significant up regulation of SMAP1, dual specificity phosphatase 1 and pro isomerase domain-containing 1, cytokeratin 18, triosephosphate isomerase and beta-tubulin.	Ethanol	4-11	triosephosphate isomerase 1	Homo sapiens	166-191
20693693-4	2010	The A-TIM crystals were grown in the presence of citrate, which is bound in the active site of each of the two molecules in the asymmetric unit.	Citric Acid	49-56	triosephosphate isomerase 1	Homo sapiens	6-9
20693693-6	2010	Extensive crystal-soaking protocols have been developed to flush the bound citrate out of the active-site pocket of both molecules and the crystal structure shows that the unliganded open conformation of the A-TIM active site is the same as in unliganded wild-type TIM.	Citric Acid	75-82	triosephosphate isomerase 1	Homo sapiens	210-213
20693693-6	2010	Extensive crystal-soaking protocols have been developed to flush the bound citrate out of the active-site pocket of both molecules and the crystal structure shows that the unliganded open conformation of the A-TIM active site is the same as in unliganded wild-type TIM.	Citric Acid	75-82	triosephosphate isomerase 1	Homo sapiens	265-268
20693693-8	2010	It is also shown that the new binding pocket of A-TIM can bind 3-phosphoglycerate (3PGA; an analogue of a C4-sugar phosphate) and 4-phospho-D-erythronohydroxamic acid (4PEH; an analogue of a C5-sugar phosphate).	3-phosphoglycerate	63-81	triosephosphate isomerase 1	Homo sapiens	50-53
20693693-8	2010	It is also shown that the new binding pocket of A-TIM can bind 3-phosphoglycerate (3PGA; an analogue of a C4-sugar phosphate) and 4-phospho-D-erythronohydroxamic acid (4PEH; an analogue of a C5-sugar phosphate).	c4-sugar phosphate	106-124	triosephosphate isomerase 1	Homo sapiens	50-53
20693693-8	2010	It is also shown that the new binding pocket of A-TIM can bind 3-phosphoglycerate (3PGA; an analogue of a C4-sugar phosphate) and 4-phospho-D-erythronohydroxamic acid (4PEH; an analogue of a C5-sugar phosphate).	4-phosphoerythronohydroxamic acid	130-166	triosephosphate isomerase 1	Homo sapiens	50-53
20693693-8	2010	It is also shown that the new binding pocket of A-TIM can bind 3-phosphoglycerate (3PGA; an analogue of a C4-sugar phosphate) and 4-phospho-D-erythronohydroxamic acid (4PEH; an analogue of a C5-sugar phosphate).	c5-sugar phosphate	191-209	triosephosphate isomerase 1	Homo sapiens	50-53
20639142-0	2010	TPI 1020, a novel anti-inflammatory, nitric oxide donating compound, potentiates the bronchodilator effects of salbutamol in conscious guinea-pigs.	Nitric Oxide	37-49	triosephosphate isomerase 1	Homo sapiens	0-3
20639142-0	2010	TPI 1020, a novel anti-inflammatory, nitric oxide donating compound, potentiates the bronchodilator effects of salbutamol in conscious guinea-pigs.	Albuterol	111-121	triosephosphate isomerase 1	Homo sapiens	0-3
20639142-2	2010	This study evaluates in conscious guinea-pigs the bronchodilator effect, alone or combined with salbutamol, of TPI 1020, a novel anti-inflammatory corticosteroid and nitric oxide (NO) donor derived from budesonide.	Nitric Oxide	166-178	triosephosphate isomerase 1	Homo sapiens	111-114
20639142-2	2010	This study evaluates in conscious guinea-pigs the bronchodilator effect, alone or combined with salbutamol, of TPI 1020, a novel anti-inflammatory corticosteroid and nitric oxide (NO) donor derived from budesonide.	Budesonide	203-213	triosephosphate isomerase 1	Homo sapiens	111-114
20639142-5	2010	Salbutamol and TPI 1020 caused concentration-dependent bronchodilatation measured as inhibition of histamine-induced bronchoconstriction.	Histamine	99-108	triosephosphate isomerase 1	Homo sapiens	15-18
20639142-6	2010	TPI 1020-induced bronchodilatation was blocked by the guanylyl cyclise inhibitor, ODQ, indicating cGMP-dependence through released NO.	1H-(1,2,3)oxadiazolo(4,4-a)quinoxalin-1-one	82-85	triosephosphate isomerase 1	Homo sapiens	0-3
20639142-6	2010	TPI 1020-induced bronchodilatation was blocked by the guanylyl cyclise inhibitor, ODQ, indicating cGMP-dependence through released NO.	Cyclic GMP	98-102	triosephosphate isomerase 1	Homo sapiens	0-3
20639142-11	2010	This study has shown that TPI 1020 potentiates the bronchodilator activity of salbutamol, and their combination lasted longer than either drug administered individually.	Albuterol	78-88	triosephosphate isomerase 1	Homo sapiens	26-29
20639142-12	2010	Both the corticosteroid and NO-releasing activities of TPI 1020 appear to be required for the potentiation of salbutamol.	Albuterol	110-120	triosephosphate isomerase 1	Homo sapiens	55-58
20235230-3	2010	Here, we have investigated the reaction mechanism of triosephosphate isomerase (TIM) using atomic resolution crystallographic studies at 0.82-A resolution of leishmanial TIM complexed with the well-studied reaction-intermediate analog phosphoglycolohydroxamate (PGH).	phosphoglycolohydroxamate	235-260	triosephosphate isomerase 1	Homo sapiens	80-83
20235230-3	2010	Here, we have investigated the reaction mechanism of triosephosphate isomerase (TIM) using atomic resolution crystallographic studies at 0.82-A resolution of leishmanial TIM complexed with the well-studied reaction-intermediate analog phosphoglycolohydroxamate (PGH).	phosphoglycolohydroxamate	235-260	triosephosphate isomerase 1	Homo sapiens	170-173
20235230-3	2010	Here, we have investigated the reaction mechanism of triosephosphate isomerase (TIM) using atomic resolution crystallographic studies at 0.82-A resolution of leishmanial TIM complexed with the well-studied reaction-intermediate analog phosphoglycolohydroxamate (PGH).	phosphoglycolohydroxamate	262-265	triosephosphate isomerase 1	Homo sapiens	53-78
20235230-3	2010	Here, we have investigated the reaction mechanism of triosephosphate isomerase (TIM) using atomic resolution crystallographic studies at 0.82-A resolution of leishmanial TIM complexed with the well-studied reaction-intermediate analog phosphoglycolohydroxamate (PGH).	phosphoglycolohydroxamate	262-265	triosephosphate isomerase 1	Homo sapiens	80-83
20235230-4	2010	Remaining unresolved aspects of the reaction mechanism of TIM such as the protonation state of the first reaction intermediate and the properties of the hydrogen-bonding interactions in the active site are being addressed.	Hydrogen	153-161	triosephosphate isomerase 1	Homo sapiens	58-61
19951750-8	2010	We focused on four glycoproteins (tumor rejection antigen (gp96) 1, triose phosphate isomerase, palmitoyl-protein thioesterase 1 precursor and ER-associated DNAJ) which were remarkably upregulated in A2780TC1 compared to A2780 cell line and which may represent biomarkers for paclitaxel resistance in ovarian cancer.	Paclitaxel	276-286	triosephosphate isomerase 1	Homo sapiens	34-94
20372793-5	2010	TPI, a newly synthesized inhibitor for TP (Ki=2.36 x 10(-9) M), decreased the sensitivity to 5-FU of the TP expressing cells but not of the parental cells.	Fluorouracil	93-97	triosephosphate isomerase 1	Homo sapiens	0-3
20391192-1	2010	An investigation was conducted to determine if the 5-fluoro analog of TPI (5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]uracil), a potent inhibitor of human thymidine phosphorylase (TP), has an IC(50) in a range that might allow to use it labeled for imaging of TP expression in vivo.	5-chloro-6-[(2-iminopyrrolidin-1-yl)methyl]uracil	75-124	triosephosphate isomerase 1	Homo sapiens	70-73
20018339-6	2010	(S)-Methyl-[16O,17O,18O]-phosphate (MePi*), 7 and enantiomeric [16O,17O,18O]-thiophosphate (TPi*), 10, were previously reported to exhibit weak electronic circular dichroism (ECD), although with 10 the result was considered to be uncertain.	16o,17o,18o]-thiophosphate	64-90	triosephosphate isomerase 1	Homo sapiens	92-96
19891501-5	2009	Glycolytic enzymes, namely, phosphoglycerate mutase (PGM) and triosephosphate isomerase (TPI), were overexpressed in capsaicin-treated Caco-2 cells.	Capsaicin	117-126	triosephosphate isomerase 1	Homo sapiens	62-87
20499682-4	2010	A novel inhibitor of thymidine phosphorylase (TP), 5-chloro-6-[1-(2-iminopyrrolidinyl) methyl] uracil hydrochloride (TPI) is about 1000-fold more active than 6-amino-5-chlorouracil, one of the most potent TP inhibitors to 1999 year.	5-chloro-6-(1-(2-iminopyrrolidinyl) methyl)uracil hydrochloride	51-115	triosephosphate isomerase 1	Homo sapiens	117-120
20499682-4	2010	A novel inhibitor of thymidine phosphorylase (TP), 5-chloro-6-[1-(2-iminopyrrolidinyl) methyl] uracil hydrochloride (TPI) is about 1000-fold more active than 6-amino-5-chlorouracil, one of the most potent TP inhibitors to 1999 year.	6-Amino-5-chloropyrimidine-2,4(1H,3H)-dione	158-180	triosephosphate isomerase 1	Homo sapiens	117-120
19891501-5	2009	Glycolytic enzymes, namely, phosphoglycerate mutase (PGM) and triosephosphate isomerase (TPI), were overexpressed in capsaicin-treated Caco-2 cells.	Capsaicin	117-126	triosephosphate isomerase 1	Homo sapiens	89-92
19891501-6	2009	mRNA expression levels of TPI and PGM were also increased in capsaicin-treated Caco-2 cells.	Capsaicin	61-70	triosephosphate isomerase 1	Homo sapiens	26-29
20161396-6	2009	Similar electrochemical-EPR experiments for Tp(i) (Pr)MoO(2)(SPh) indicated that the pK(a) for its Mo(V)(OH) unit was ~1.7 units smaller than that for Tp*Mo(V)O(OH)(SPh).	Sphingosine	61-64	triosephosphate isomerase 1	Homo sapiens	44-49
19482002-4	2009	The proteomic screen revealed triosephosphate isomerase oligomer as a dextran-binding, high M(R) complex.	Dextrans	70-77	triosephosphate isomerase 1	Homo sapiens	30-55
18420726-1	2008	OBJECTIVE: The goal of this study was to evaluate the utility of the stroke thrombolytic predictive instrument (s-TPI) in predicting clinical outcome in patients with acute ischaemic stroke treated with intravenous tissue plasminogen activator (t-PA).	Sulfur	26-27	triosephosphate isomerase 1	Homo sapiens	114-117
19286361-2	2009	TPI 1020 exerts its effects by a dual mechanism of action involving corticosteroid activity and controlled donation of nitric oxide.	Nitric Oxide	119-131	triosephosphate isomerase 1	Homo sapiens	0-3
19286361-8	2009	Sputum neutrophils (%) tended to decrease more with TPI 1020 (32.6% decrease versus 3.7% increase for budesonide); the decrease occurring only in patients with high neutrophils at baseline.	Budesonide	102-112	triosephosphate isomerase 1	Homo sapiens	52-55
19286361-10	2009	Budesonide caused a statistically significant decrease in 24h urinary free cortisol over 22days (median of 4.4-2.8mcg/ml, p=0.01) whereas TPI 1020 had no such effect (4.4-5.8mcg/ml), suggesting lower systemic corticosteroid exposure following TPI 1020 treatment.	Budesonide	0-10	triosephosphate isomerase 1	Homo sapiens	243-246
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	glycolaldehyde	42-56	triosephosphate isomerase 1	Homo sapiens	131-156
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	glycolaldehyde	42-56	triosephosphate isomerase 1	Homo sapiens	158-161
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	Carbon-13	70-79	triosephosphate isomerase 1	Homo sapiens	131-156
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	Carbon-13	70-79	triosephosphate isomerase 1	Homo sapiens	158-161
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	Carbon	70-76	triosephosphate isomerase 1	Homo sapiens	131-156
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	Carbon	70-76	triosephosphate isomerase 1	Homo sapiens	158-161
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	phosphite dianion	201-218	triosephosphate isomerase 1	Homo sapiens	131-156
19425580-2	2009	Product distributions for the reaction of glycolaldehyde labeled with carbon-13 at the carbonyl carbon ([1-(13)C]-GA) catalyzed by triosephosphate isomerase (TIM) in D(2)O at pD 7.0 in the presence of phosphite dianion and in its absence were determined by (1)H NMR spectroscopy.	phosphite dianion	201-218	triosephosphate isomerase 1	Homo sapiens	158-161
19425580-7	2009	The data provide evidence that phosphite dianion affects the rate, but not the product distribution, of the TIM-catalyzed reaction of [1-(13)C]-GA at the enzyme active site.	phosphite dianion	31-48	triosephosphate isomerase 1	Homo sapiens	108-111
19425580-8	2009	They are consistent with the conclusion that both reactions occur at an unstable loop-closed form of TIM and that activation of the isomerization reaction by phosphite dianion results from utilization of the intrinsic binding energy of phosphite dianion to stabilize the active loop-closed enzyme.	phosphite dianion	158-175	triosephosphate isomerase 1	Homo sapiens	101-104
19425580-8	2009	They are consistent with the conclusion that both reactions occur at an unstable loop-closed form of TIM and that activation of the isomerization reaction by phosphite dianion results from utilization of the intrinsic binding energy of phosphite dianion to stabilize the active loop-closed enzyme.	phosphite dianion	236-253	triosephosphate isomerase 1	Homo sapiens	101-104
19251756-13	2009	Our results link oxidative stress, the main etiopathogenic mechanism in sporadic Alzheimer"s disease, via the production of peroxynitrite and nitrotyrosination of triosephosphate isomerase, to amyloid beta-peptide-induced toxicity and tau pathology.	nitrotyrosination	142-159	triosephosphate isomerase 1	Homo sapiens	163-188
19251756-13	2009	Our results link oxidative stress, the main etiopathogenic mechanism in sporadic Alzheimer"s disease, via the production of peroxynitrite and nitrotyrosination of triosephosphate isomerase, to amyloid beta-peptide-induced toxicity and tau pathology.	beta-Peptide	201-213	triosephosphate isomerase 1	Homo sapiens	163-188
18761414-1	2008	TPI ASM8 and TPI 1100 are two products containing modified phosphorothioate antisense oligonucleotides (AONs), which are undergoing development for the treatment of asthma and chronic obstructive pulmonary disease (COPD), respectively.	Parathion	59-75	triosephosphate isomerase 1	Homo sapiens	0-3
18761414-1	2008	TPI ASM8 and TPI 1100 are two products containing modified phosphorothioate antisense oligonucleotides (AONs), which are undergoing development for the treatment of asthma and chronic obstructive pulmonary disease (COPD), respectively.	Parathion	59-75	triosephosphate isomerase 1	Homo sapiens	13-16
18761414-1	2008	TPI ASM8 and TPI 1100 are two products containing modified phosphorothioate antisense oligonucleotides (AONs), which are undergoing development for the treatment of asthma and chronic obstructive pulmonary disease (COPD), respectively.	Oligonucleotides	86-102	triosephosphate isomerase 1	Homo sapiens	0-3
18761414-1	2008	TPI ASM8 and TPI 1100 are two products containing modified phosphorothioate antisense oligonucleotides (AONs), which are undergoing development for the treatment of asthma and chronic obstructive pulmonary disease (COPD), respectively.	Oligonucleotides	86-102	triosephosphate isomerase 1	Homo sapiens	13-16
18761414-1	2008	TPI ASM8 and TPI 1100 are two products containing modified phosphorothioate antisense oligonucleotides (AONs), which are undergoing development for the treatment of asthma and chronic obstructive pulmonary disease (COPD), respectively.	Oligonucleotides, Antisense	104-108	triosephosphate isomerase 1	Homo sapiens	0-3
18761414-1	2008	TPI ASM8 and TPI 1100 are two products containing modified phosphorothioate antisense oligonucleotides (AONs), which are undergoing development for the treatment of asthma and chronic obstructive pulmonary disease (COPD), respectively.	Oligonucleotides, Antisense	104-108	triosephosphate isomerase 1	Homo sapiens	13-16
18553501-1	2008	In this article we report on the characterization of the enzymatic synthesis of D-xylulose 5-phosphate using triosephosphate isomerase and transketolase.	xylulose-5-phosphate	80-102	triosephosphate isomerase 1	Homo sapiens	109-134
18309519-7	2008	The sensitivity of TPI-SGC7901/VCR cells to adriamycin (ADR), VCR, 5-fluorouracil and cis-dichlorodiamine platinum, as well as the accumulation and retention to ADR, were significantly increased when compared to their control cell lines.	Doxorubicin	44-54	triosephosphate isomerase 1	Homo sapiens	19-22
18309519-7	2008	The sensitivity of TPI-SGC7901/VCR cells to adriamycin (ADR), VCR, 5-fluorouracil and cis-dichlorodiamine platinum, as well as the accumulation and retention to ADR, were significantly increased when compared to their control cell lines.	cis-Diaminedichloroplatinum	86-114	triosephosphate isomerase 1	Homo sapiens	19-22
18458110-3	2008	TPI has a well-characterized role in glycolysis, catalyzing the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P); however, little is known mechanistically about the pathogenesis associated with specific recessive mutations that cause progressive neurodegeneration.	Dihydroxyacetone Phosphate	81-107	triosephosphate isomerase 1	Homo sapiens	0-3
18991142-5	2008	A molecular 3-D model provides the first structural information of human GDE4 and suggests a triose-phosphate-isomerase barrel core as typically found in bacterial GDPDs.	gdpds	164-169	triosephosphate isomerase 1	Homo sapiens	93-119
18562316-6	2008	An analysis of the available high resolution structures of TIM dimers revealed that this cluster forms a cavity that possesses an elaborate conserved network of buried water molecules that bridge the two subunits.	Water	168-173	triosephosphate isomerase 1	Homo sapiens	59-62
18555978-5	2008	The reduction in cytostatic activity could be fully restored in the presence of TPI (5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracil hydrochloride), a known inhibitor of human TP.	5-chloro-6-(1-(2-iminopyrrolidinyl) methyl)uracil hydrochloride	85-147	triosephosphate isomerase 1	Homo sapiens	80-83
18458110-3	2008	TPI has a well-characterized role in glycolysis, catalyzing the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P); however, little is known mechanistically about the pathogenesis associated with specific recessive mutations that cause progressive neurodegeneration.	Dihydroxyacetone Phosphate	109-113	triosephosphate isomerase 1	Homo sapiens	0-3
18458110-3	2008	TPI has a well-characterized role in glycolysis, catalyzing the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P); however, little is known mechanistically about the pathogenesis associated with specific recessive mutations that cause progressive neurodegeneration.	Glyceraldehyde 3-Phosphate	118-144	triosephosphate isomerase 1	Homo sapiens	0-3
18458110-3	2008	TPI has a well-characterized role in glycolysis, catalyzing the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P); however, little is known mechanistically about the pathogenesis associated with specific recessive mutations that cause progressive neurodegeneration.	Glyceraldehyde 3-Phosphate	146-149	triosephosphate isomerase 1	Homo sapiens	0-3
21122290-6	2007	CONCLUSIONS: The down-regulation of HSP90 and triosephosphate isomerase may be related to the synergistic effects of NS-398 and cisplatin on human lung adenocarcinoma cells.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	117-123	triosephosphate isomerase 1	Homo sapiens	46-71
17593366-8	2008	Together, at both the mRNA and protein levels, SAHA suppressed the expression of reticulocalbin 1 precursor (RCN1), annexin A3 (ANXA3) and heat shock 27 kDa protein 1 (HSP27), while increasing the expression of aldose reductase (AR), triosephosphate isomerase 1 (TPI) and manganese superoxide dismutase (SOD2).	Vorinostat	47-51	triosephosphate isomerase 1	Homo sapiens	234-261
17593366-8	2008	Together, at both the mRNA and protein levels, SAHA suppressed the expression of reticulocalbin 1 precursor (RCN1), annexin A3 (ANXA3) and heat shock 27 kDa protein 1 (HSP27), while increasing the expression of aldose reductase (AR), triosephosphate isomerase 1 (TPI) and manganese superoxide dismutase (SOD2).	Vorinostat	47-51	triosephosphate isomerase 1	Homo sapiens	263-266
18239072-3	2008	Here, it is reported that in the V233A variant of ml8bTIM (A-TIM), three important properties of the wild-type TIM active site have been restored: (i) the structural properties of loop-7, (ii) the binding site of a conserved water molecule between loop-7 and loop-8 and (iii) the binding site of the phosphate moiety.	Water	225-230	triosephosphate isomerase 1	Homo sapiens	54-57
18239072-3	2008	Here, it is reported that in the V233A variant of ml8bTIM (A-TIM), three important properties of the wild-type TIM active site have been restored: (i) the structural properties of loop-7, (ii) the binding site of a conserved water molecule between loop-7 and loop-8 and (iii) the binding site of the phosphate moiety.	Water	225-230	triosephosphate isomerase 1	Homo sapiens	61-64
18239072-3	2008	Here, it is reported that in the V233A variant of ml8bTIM (A-TIM), three important properties of the wild-type TIM active site have been restored: (i) the structural properties of loop-7, (ii) the binding site of a conserved water molecule between loop-7 and loop-8 and (iii) the binding site of the phosphate moiety.	Phosphates	300-309	triosephosphate isomerase 1	Homo sapiens	54-57
18239072-3	2008	Here, it is reported that in the V233A variant of ml8bTIM (A-TIM), three important properties of the wild-type TIM active site have been restored: (i) the structural properties of loop-7, (ii) the binding site of a conserved water molecule between loop-7 and loop-8 and (iii) the binding site of the phosphate moiety.	Phosphates	300-309	triosephosphate isomerase 1	Homo sapiens	61-64
18239072-7	2008	It is also shown that the A-TIM active site can bind compounds which do not bind to wild-type TIM and which are completely different from the normal TIM substrate, like a citrate molecule.	Citric Acid	171-178	triosephosphate isomerase 1	Homo sapiens	28-31
18175010-1	2008	The catalytic base at the active site of triosephosphate isomerase (TIM) was labelled with -H by abstraction of a proton from substrate d-glyceraldehyde 3-phosphate to form an enzyme-bound enediol(ate) in D2O solvent.	Deuterium Oxide	205-208	triosephosphate isomerase 1	Homo sapiens	68-71
18175010-3	2008	The yield of hydrogen-labelled product DHAP remains constant as the concentration of the basic form of imidazole buffer is increased from 0.014 to 0.56 M. This shows that the active site of free TIM, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O.	Hydrogen	13-21	triosephosphate isomerase 1	Homo sapiens	195-198
18175010-3	2008	The yield of hydrogen-labelled product DHAP remains constant as the concentration of the basic form of imidazole buffer is increased from 0.014 to 0.56 M. This shows that the active site of free TIM, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O.	Dihydroxyacetone Phosphate	39-43	triosephosphate isomerase 1	Homo sapiens	195-198
18175010-3	2008	The yield of hydrogen-labelled product DHAP remains constant as the concentration of the basic form of imidazole buffer is increased from 0.014 to 0.56 M. This shows that the active site of free TIM, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O.	imidazole	103-112	triosephosphate isomerase 1	Homo sapiens	195-198
18175010-3	2008	The yield of hydrogen-labelled product DHAP remains constant as the concentration of the basic form of imidazole buffer is increased from 0.014 to 0.56 M. This shows that the active site of free TIM, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O.	imidazole	402-411	triosephosphate isomerase 1	Homo sapiens	195-198
18175010-3	2008	The yield of hydrogen-labelled product DHAP remains constant as the concentration of the basic form of imidazole buffer is increased from 0.014 to 0.56 M. This shows that the active site of free TIM, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O.	Deuterium Oxide	425-428	triosephosphate isomerase 1	Homo sapiens	195-198
18575103-8	2008	HPO-A, HPO-N, TPI-A, and TPI-N contained 3.02%-3.52% of nitrogen.	Nitrogen	56-64	triosephosphate isomerase 1	Homo sapiens	25-28
18575103-12	2008	The ratio of aliphatic to aromatic protons increased in the order of HPO-A < HPO-N < TPI-A < TPI-N. FT-IR analysis of the four fractions showed that HPO-A had greater aromatic C[double bond]C content whereas HPO-N, TPI-A, and TPI-N had greater aliphatic C--H content.	hpo-n	80-85	triosephosphate isomerase 1	Homo sapiens	91-94
18575103-12	2008	The ratio of aliphatic to aromatic protons increased in the order of HPO-A < HPO-N < TPI-A < TPI-N. FT-IR analysis of the four fractions showed that HPO-A had greater aromatic C[double bond]C content whereas HPO-N, TPI-A, and TPI-N had greater aliphatic C--H content.	hpo-n	80-85	triosephosphate isomerase 1	Homo sapiens	102-105
18575103-12	2008	The ratio of aliphatic to aromatic protons increased in the order of HPO-A < HPO-N < TPI-A < TPI-N. FT-IR analysis of the four fractions showed that HPO-A had greater aromatic C[double bond]C content whereas HPO-N, TPI-A, and TPI-N had greater aliphatic C--H content.	hpo-n	80-85	triosephosphate isomerase 1	Homo sapiens	102-105
18575103-12	2008	The ratio of aliphatic to aromatic protons increased in the order of HPO-A < HPO-N < TPI-A < TPI-N. FT-IR analysis of the four fractions showed that HPO-A had greater aromatic C[double bond]C content whereas HPO-N, TPI-A, and TPI-N had greater aliphatic C--H content.	hpo-n	80-85	triosephosphate isomerase 1	Homo sapiens	102-105
18575103-13	2008	TPI-N contained more oxygen-containing functional groups than the other fractions.	Oxygen	21-27	triosephosphate isomerase 1	Homo sapiens	0-3
18776537-7	2008	L-deoxyribose and a specific TP inhibitor, TPI, can reverse these effects, supporting the role of the enzymatic reaction and that of the sugar.	l-deoxyribose	0-13	triosephosphate isomerase 1	Homo sapiens	43-46
18776537-7	2008	L-deoxyribose and a specific TP inhibitor, TPI, can reverse these effects, supporting the role of the enzymatic reaction and that of the sugar.	Sugars	137-142	triosephosphate isomerase 1	Homo sapiens	43-46
18776537-21	2008	The association between rapamycin and TP was shown by the protection by thymidine of rapamycin induced cytotoxicity, while TPI inhibited the effect of thymidine addition.	Thymidine	151-160	triosephosphate isomerase 1	Homo sapiens	123-126
18189421-3	2008	Both dimeric and monomeric (isolated from dimer) forms of TIM are simulated in explicit water at 300 K and 1 bar to inspect any differences between the structures in terms of fluctuation dynamics and functionally important loop 6 dynamics/closure.	Water	88-93	triosephosphate isomerase 1	Homo sapiens	58-61
18183605-7	2008	Transaldolase and triose phosphate isomerase exchange activities were estimated by applying the (13)C-isotopomer data to a model of hepatic sugar phosphate metabolism.	Sugar Phosphates	140-155	triosephosphate isomerase 1	Homo sapiens	18-44
18175010-0	2008	Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.	Hydrogen	30-38	triosephosphate isomerase 1	Homo sapiens	88-113
18175010-0	2008	Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.	Carboxylic Acids	48-63	triosephosphate isomerase 1	Homo sapiens	88-113
18175010-0	2008	Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.	Glutamic Acid	76-79	triosephosphate isomerase 1	Homo sapiens	88-113
18175010-0	2008	Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.	imidazole	117-126	triosephosphate isomerase 1	Homo sapiens	88-113
18175010-0	2008	Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.	Deuterium Oxide	137-140	triosephosphate isomerase 1	Homo sapiens	88-113
18175010-1	2008	The catalytic base at the active site of triosephosphate isomerase (TIM) was labelled with -H by abstraction of a proton from substrate d-glyceraldehyde 3-phosphate to form an enzyme-bound enediol(ate) in D2O solvent.	d-glyceraldehyde 3-phosphate	136-164	triosephosphate isomerase 1	Homo sapiens	41-66
18175010-1	2008	The catalytic base at the active site of triosephosphate isomerase (TIM) was labelled with -H by abstraction of a proton from substrate d-glyceraldehyde 3-phosphate to form an enzyme-bound enediol(ate) in D2O solvent.	d-glyceraldehyde 3-phosphate	136-164	triosephosphate isomerase 1	Homo sapiens	68-71
18175010-1	2008	The catalytic base at the active site of triosephosphate isomerase (TIM) was labelled with -H by abstraction of a proton from substrate d-glyceraldehyde 3-phosphate to form an enzyme-bound enediol(ate) in D2O solvent.	Deuterium Oxide	205-208	triosephosphate isomerase 1	Homo sapiens	41-66
21122290-6	2007	CONCLUSIONS: The down-regulation of HSP90 and triosephosphate isomerase may be related to the synergistic effects of NS-398 and cisplatin on human lung adenocarcinoma cells.	Cisplatin	128-137	triosephosphate isomerase 1	Homo sapiens	46-71
17444661-0	2007	Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.	Carbon	42-48	triosephosphate isomerase 1	Homo sapiens	64-89
17444661-8	2007	TIM catalyzes proton transfer from glycolaldehyde in D2O, resulting in deuterium incorporation that can be monitored by 1H NMR spectroscopy, with kcat/Km = 0.26 M-1 s-1.	Deuterium Oxide	53-56	triosephosphate isomerase 1	Homo sapiens	0-3
17444661-8	2007	TIM catalyzes proton transfer from glycolaldehyde in D2O, resulting in deuterium incorporation that can be monitored by 1H NMR spectroscopy, with kcat/Km = 0.26 M-1 s-1.	glycolaldehyde	35-49	triosephosphate isomerase 1	Homo sapiens	0-3
17444661-8	2007	TIM catalyzes proton transfer from glycolaldehyde in D2O, resulting in deuterium incorporation that can be monitored by 1H NMR spectroscopy, with kcat/Km = 0.26 M-1 s-1.	Deuterium	71-80	triosephosphate isomerase 1	Homo sapiens	0-3
17444661-8	2007	TIM catalyzes proton transfer from glycolaldehyde in D2O, resulting in deuterium incorporation that can be monitored by 1H NMR spectroscopy, with kcat/Km = 0.26 M-1 s-1.	Hydrogen	120-122	triosephosphate isomerase 1	Homo sapiens	0-3
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	glycolaldehyde	52-66	triosephosphate isomerase 1	Homo sapiens	70-73
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	glycolaldehyde	52-66	triosephosphate isomerase 1	Homo sapiens	168-171
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	phosphite dianion	97-114	triosephosphate isomerase 1	Homo sapiens	70-73
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	phosphite dianion	97-114	triosephosphate isomerase 1	Homo sapiens	168-171
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	phosphite dianion	147-164	triosephosphate isomerase 1	Homo sapiens	70-73
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	phosphite dianion	147-164	triosephosphate isomerase 1	Homo sapiens	168-171
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	Carbon	231-237	triosephosphate isomerase 1	Homo sapiens	70-73
17444661-10	2007	The data give kcat/Km = 185 M-1 s-1 for turnover of glycolaldehyde by TIM that is saturated with phosphite dianion so that the separate binding of phosphite dianion to TIM results in a 700-fold acceleration of proton transfer from carbon.	Carbon	231-237	triosephosphate isomerase 1	Homo sapiens	168-171
17444661-11	2007	The binding of phosphite dianion to the free enzyme (Kd = 38 mM) is 700-fold weaker than its binding to the fleeting complex of TIM with the altered substrate in the transition state (Kd = 53 muM); the total intrinsic binding energy of phosphite dianion in the transition state is 5.8 kcal/mol.	phosphite dianion	15-32	triosephosphate isomerase 1	Homo sapiens	128-131
17444661-11	2007	The binding of phosphite dianion to the free enzyme (Kd = 38 mM) is 700-fold weaker than its binding to the fleeting complex of TIM with the altered substrate in the transition state (Kd = 53 muM); the total intrinsic binding energy of phosphite dianion in the transition state is 5.8 kcal/mol.	phosphite dianion	236-253	triosephosphate isomerase 1	Homo sapiens	128-131
17444661-12	2007	We propose a physical model for catalysis by TIM in which the intrinsic binding energy of the substrate phosphodianion group is utilized to drive closing of the "mobile loop" and a protein conformational change that leads to formation of an active site environment that is optimally organized for stabilization of the transition state for proton transfer from alpha-carbonyl carbon.	Carbon	366-372	triosephosphate isomerase 1	Homo sapiens	45-48
17336327-12	2007	In addition, as indicated by 1H, 15N and 13CO chemical-shifts, the glycine substitutions diminished the enzyme"s response to ligand, and induced structural perturbations in apo and 2-PGA-bound forms of TIM that are atypical of WT.	Glycine	67-74	triosephosphate isomerase 1	Homo sapiens	202-205
17336327-12	2007	In addition, as indicated by 1H, 15N and 13CO chemical-shifts, the glycine substitutions diminished the enzyme"s response to ligand, and induced structural perturbations in apo and 2-PGA-bound forms of TIM that are atypical of WT.	2-Propylglutaric acid	181-186	triosephosphate isomerase 1	Homo sapiens	202-205
17287353-1	2007	The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol(ate).	Ketones	145-151	triosephosphate isomerase 1	Homo sapiens	40-65
17287353-1	2007	The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol(ate).	Aldehydes	153-161	triosephosphate isomerase 1	Homo sapiens	40-65
17219461-2	2007	The aliphatic primary alcohol-leaving group released the fluorescent product umbelliferone by an enolization/beta-elimination reaction similar to the triose phosphate isomerase (TIM) reaction.	Alcohols	22-29	triosephosphate isomerase 1	Homo sapiens	150-176
17219461-2	2007	The aliphatic primary alcohol-leaving group released the fluorescent product umbelliferone by an enolization/beta-elimination reaction similar to the triose phosphate isomerase (TIM) reaction.	Alcohols	22-29	triosephosphate isomerase 1	Homo sapiens	178-181
17219461-2	2007	The aliphatic primary alcohol-leaving group released the fluorescent product umbelliferone by an enolization/beta-elimination reaction similar to the triose phosphate isomerase (TIM) reaction.	7-hydroxycoumarin	77-90	triosephosphate isomerase 1	Homo sapiens	150-176
17219461-2	2007	The aliphatic primary alcohol-leaving group released the fluorescent product umbelliferone by an enolization/beta-elimination reaction similar to the triose phosphate isomerase (TIM) reaction.	7-hydroxycoumarin	77-90	triosephosphate isomerase 1	Homo sapiens	178-181