PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
23319881-2	2012	The archaeal exosome is functionally similar to bacterial polynucleotide phosphorylase (PNPase) and RNase PH enzymes as it uses inorganic phosphate (Pi) to processively cleave RNA substrates releasing nucleoside diphosphates.	Phosphates	128-147	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	58-86
23084291-9	2012	Finally, overexpression of the wild-type PNPT1 cDNA in fibroblasts of subject 1 induced an increase in 5S rRNA import in mitochondria and rescued the mitochondrial-translation deficiency.	CHEMBL3739852	103-105	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	41-46
22815474-0	2012	Nuclear EGFR suppresses ribonuclease activity of polynucleotide phosphorylase through DNAPK-mediated phosphorylation at serine 776.	Serine	120-126	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	49-77
22815474-8	2012	We also demonstrated that DNAPK phosphorylates PNPase at Ser-776, which is critical for its ribonuclease activity.	Serine	57-60	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	47-53
22815474-10	2012	Here, we uncovered a novel role of nEGFR in radioresistance, and that is, upon ionizing radiation, nEGFR inactivates the ribonuclease activity of PNPase toward c-MYC mRNA through DNAPK-mediated Ser-776 phosphorylation, leading to increase of c-MYC mRNA, which contributes to radioresistance of cancer cells.	Serine	194-197	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	146-152
23319881-2	2012	The archaeal exosome is functionally similar to bacterial polynucleotide phosphorylase (PNPase) and RNase PH enzymes as it uses inorganic phosphate (Pi) to processively cleave RNA substrates releasing nucleoside diphosphates.	Phosphates	128-147	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	88-94
23319881-2	2012	The archaeal exosome is functionally similar to bacterial polynucleotide phosphorylase (PNPase) and RNase PH enzymes as it uses inorganic phosphate (Pi) to processively cleave RNA substrates releasing nucleoside diphosphates.	nucleoside diphosphates	201-224	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	58-86
23319881-2	2012	The archaeal exosome is functionally similar to bacterial polynucleotide phosphorylase (PNPase) and RNase PH enzymes as it uses inorganic phosphate (Pi) to processively cleave RNA substrates releasing nucleoside diphosphates.	nucleoside diphosphates	201-224	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	88-94
23319881-7	2012	The high degree of structural conservation between the archaeal exosome and the PNPase including the requirement for divalent metal ions for catalysis is discussed.	Metals	126-131	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	80-86
15769737-5	2005	Here we show human mt PAP (hmtPAP) and human polynucleotide phosphorylase (hPNPase) control poly(A) synthesis in human mitochondria.	Poly A	92-99	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-82
20457661-0	2010	Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogues of ADP and ATP.	arsenic acid	81-89	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
20457661-0	2010	Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogues of ADP and ATP.	arsenite	108-116	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
20457661-0	2010	Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogues of ADP and ATP.	Adenosine Diphosphate	153-156	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	Poly A	130-144	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-103
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	Poly A	130-144	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	105-111
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	Poly A	146-152	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-103
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	Poly A	146-152	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	105-111
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	amp-asv	183-190	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-103
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	amp-asv	183-190	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	105-111
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	adp-asv	207-214	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-103
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	adp-asv	207-214	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	105-111
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	asunaprevir	187-190	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-103
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	asunaprevir	187-190	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	105-111
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	asiii	256-261	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-103
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	asiii	256-261	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	105-111
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	Sulfhydryl Compounds	277-283	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	75-103
20457661-4	2010	To test this hypothesis, we first examined whether the RNA-cleaving enzyme polynucleotide phosphorylase (PNPase), which can split poly-adenylate (poly-A) by arsenolysis into units of AMP-AsV (a homologue of ADP-AsV), could also promote reduction of AsV to AsIII in presence of thiols.	Sulfhydryl Compounds	277-283	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	105-111
20457661-5	2010	Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH.	asiii	59-64	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	18-24
20457661-5	2010	Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH.	Poly A	85-91	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	18-24
20457661-5	2010	Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH.	asunaprevir	93-96	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	18-24
20457661-5	2010	Indeed, bacterial PNPase markedly facilitated formation of AsIII when incubated with poly-A, AsV, and GSH.	Glutathione	102-105	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	18-24
20457661-6	2010	PNPase-mediated AsV reduction depended on arsenolysis of poly-A and presence of a thiol.	Poly A	57-63	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-6
20457661-6	2010	PNPase-mediated AsV reduction depended on arsenolysis of poly-A and presence of a thiol.	Sulfhydryl Compounds	82-87	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-6
20457661-7	2010	PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP).	amp-asv	21-28	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-6
20457661-7	2010	PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP).	Adenosine Diphosphate	34-37	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-6
20457661-7	2010	PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP).	asunaprevir	25-28	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-6
20457661-7	2010	PNPase can also form AMP-AsV from ADP and AsV (termed arsenolysis of ADP).	Adenosine Diphosphate	69-72	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-6
20457661-9	2010	Although various thiols did not influence the arsenolytic yield of AMP-AsV, they differentially promoted the PNPase-mediated reduction of AsV, with GSH being the most effective.	Sulfhydryl Compounds	17-23	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	109-115
20457661-9	2010	Although various thiols did not influence the arsenolytic yield of AMP-AsV, they differentially promoted the PNPase-mediated reduction of AsV, with GSH being the most effective.	Glutathione	148-151	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	109-115
20457661-10	2010	Circumstantial evidence indicated that AMP-AsV formed by PNPase is more reducible to AsIII by GSH than inorganic AsV.	amp-asv	39-46	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	57-63
20457661-10	2010	Circumstantial evidence indicated that AMP-AsV formed by PNPase is more reducible to AsIII by GSH than inorganic AsV.	Glutathione	94-97	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	57-63
20457661-13	2010	Thus, whereas PNPase promotes reduction of AsV by incorporating it into AMP-AsV, the mitochondrial ATP synthase facilitates AsV reduction by forming ADP-AsV; then GSH can easily reduce these arsenylated nucleotides to AsIII.	amp-asv	72-79	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	14-20
19509288-3	2009	In this communication, we demonstrated that purified human SUV3 (suppressor of Var1 3) dimer and polynucleotide phosphorylase (PNPase) trimer form a 330-kDa heteropentamer that is capable of efficiently degrading double-stranded RNA (dsRNA) substrates in the presence of ATP, a task the individual components cannot perform separately.	Adenosine Triphosphate	271-274	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	97-125
19509288-3	2009	In this communication, we demonstrated that purified human SUV3 (suppressor of Var1 3) dimer and polynucleotide phosphorylase (PNPase) trimer form a 330-kDa heteropentamer that is capable of efficiently degrading double-stranded RNA (dsRNA) substrates in the presence of ATP, a task the individual components cannot perform separately.	Adenosine Triphosphate	271-274	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	127-133
18501193-6	2008	Overexpression of hPNPase reduces RNA oxidation and increases cell viability against H2O2 insult.	Hydrogen Peroxide	85-89	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	18-25
18501193-7	2008	Conversely, hPNPase knockdown decreases viability and increases 8-oxoG level in HeLa cell exposed to H2O2.	Hydrogen Peroxide	101-105	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	12-19
18083836-0	2008	Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.	Phosphates	111-120	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	22-50
18083836-0	2008	Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.	Phosphates	111-120	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	52-58
16525558-3	2006	Since the enantiomers of some pharmaceuticals have revealed surprising biological activities, the L-nucleoside analogues (+)-5 x HCl and (-)-6, respectively, of D-ImmH and D-DADMe-ImmH, were prepared and their PNPase binding properties were studied.	l-nucleoside	98-110	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	210-216
16525558-3	2006	Since the enantiomers of some pharmaceuticals have revealed surprising biological activities, the L-nucleoside analogues (+)-5 x HCl and (-)-6, respectively, of D-ImmH and D-DADMe-ImmH, were prepared and their PNPase binding properties were studied.	Deuterium	161-163	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	210-216
17084501-1	2007	Polynucleotide phosphorylase (PNPase) is a phosphate-dependent 3" to 5" exonuclease widely diffused among bacteria and eukaryotes.	Phosphates	43-52	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
17084501-1	2007	Polynucleotide phosphorylase (PNPase) is a phosphate-dependent 3" to 5" exonuclease widely diffused among bacteria and eukaryotes.	Phosphates	43-52	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	30-36
15978720-7	2006	hPNPase(old-35) promotes reactive oxygen species (ROS) production, activates the NF-kappaB pathway and initiates the production of pro-inflammatory cytokines, such as IL-6 and IL-8.	Reactive Oxygen Species	25-48	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-7
15978720-7	2006	hPNPase(old-35) promotes reactive oxygen species (ROS) production, activates the NF-kappaB pathway and initiates the production of pro-inflammatory cytokines, such as IL-6 and IL-8.	Reactive Oxygen Species	25-48	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	8-14
15978720-7	2006	hPNPase(old-35) promotes reactive oxygen species (ROS) production, activates the NF-kappaB pathway and initiates the production of pro-inflammatory cytokines, such as IL-6 and IL-8.	Reactive Oxygen Species	50-53	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-7
15978720-7	2006	hPNPase(old-35) promotes reactive oxygen species (ROS) production, activates the NF-kappaB pathway and initiates the production of pro-inflammatory cytokines, such as IL-6 and IL-8.	Reactive Oxygen Species	50-53	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	8-14
15492272-5	2004	We now document that overexpression of hPNPase(old-35) results in increased production of ROS, leading to activation of the nuclear factor (NF)-kappaB pathway.	Reactive Oxygen Species	90-93	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	39-53
15492272-7	2004	The generation of ROS and activation of NF-kappaB by hPNPase(old-35) are prevented by treatment with a cell-permeable antioxidant, N-acetyl-l-cysteine.	Reactive Oxygen Species	18-21	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	53-67
15492272-7	2004	The generation of ROS and activation of NF-kappaB by hPNPase(old-35) are prevented by treatment with a cell-permeable antioxidant, N-acetyl-l-cysteine.	Acetylcysteine	131-150	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	53-67
15492272-8	2004	Infection with Ad.hPNPase(old-35) enhances the production of interleukin (IL)-6 and IL-8, two classical NF-kappaB-responsive cytokines, and this induction is inhibited by N-acetyl-l-cysteine.	Acetylcysteine	171-190	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	18-32
15492272-10	2004	We hypothesize that hPNPase(old-35) might play a significant role in producing pathological changes associated with aging by generating proinflammatory cytokines via ROS and NF-kappaB.	Reactive Oxygen Species	166-169	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	20-34
8632418-1	1996	Phosphonate acyclic derivates of guanines, pyrazolo[3,4-d]pyrimidines, and triazolo[4,5-d]-pyrimidines (8-azaguanines) are inhibitors of the enzyme purine nucleoside phosphorylase (PNPase) with Ki" values ranging from 0.05 to 1.6 microM.	Organophosphonates	0-11	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	181-187
9211914-1	1997	The exoribonuclease 100RNP/polynucleotide phosphorylase displays high binding affinity for poly(A) sequence.	Poly A	91-98	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	20-55
9211914-9	1997	100RNP/PNPase may therefore be involved in a mechanism in which post-transcriptional addition of poly(A)-rich sequence targets the chloroplast RNA for rapid exonucleolytic degradation.	Poly A	97-104	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	7-13
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	ribonucleoside-5"-diphosphate	208-237	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	111-139
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	ribonucleoside-5"-diphosphate	208-237	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	141-147
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	N,N-di-n-propylserotonin	239-242	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	43-71
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	N,N-di-n-propylserotonin	239-242	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	111-139
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	N,N-di-n-propylserotonin	239-242	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	141-147
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	Deoxyribonucleosides	283-302	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	43-71
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	Deoxyribonucleosides	283-302	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	111-139
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	Deoxyribonucleosides	283-302	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	141-147
8662001-1	1996	Our experiments show that when MgCl2 is replaced by FeCl3, PNPase becomes able to synthesize deoxyheteropolymers using deoxyribonucleoside-5"-diphosphates (dNDPs).	Magnesium Chloride	31-36	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	59-65
8662001-1	1996	Our experiments show that when MgCl2 is replaced by FeCl3, PNPase becomes able to synthesize deoxyheteropolymers using deoxyribonucleoside-5"-diphosphates (dNDPs).	ferric chloride	52-57	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	59-65
8662001-1	1996	Our experiments show that when MgCl2 is replaced by FeCl3, PNPase becomes able to synthesize deoxyheteropolymers using deoxyribonucleoside-5"-diphosphates (dNDPs).	deoxyheteropolymers	93-112	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	59-65
8662001-1	1996	Our experiments show that when MgCl2 is replaced by FeCl3, PNPase becomes able to synthesize deoxyheteropolymers using deoxyribonucleoside-5"-diphosphates (dNDPs).	deoxyribonucleoside-5"-diphosphates	119-154	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	59-65
8662001-1	1996	Our experiments show that when MgCl2 is replaced by FeCl3, PNPase becomes able to synthesize deoxyheteropolymers using deoxyribonucleoside-5"-diphosphates (dNDPs).	dndps	156-161	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	59-65
15210334-4	2004	The poly(A)-dependent pathway is catalyzed by polynucleotide phosphorylase (PNPase), which both adds and degrades destabilizing poly(A) tails, whereas RNase II and PNPase may both participate in the poly(A)-independent pathway.	Poly A	4-11	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	46-74
15210334-4	2004	The poly(A)-dependent pathway is catalyzed by polynucleotide phosphorylase (PNPase), which both adds and degrades destabilizing poly(A) tails, whereas RNase II and PNPase may both participate in the poly(A)-independent pathway.	Poly A	4-11	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	76-82
15210334-4	2004	The poly(A)-dependent pathway is catalyzed by polynucleotide phosphorylase (PNPase), which both adds and degrades destabilizing poly(A) tails, whereas RNase II and PNPase may both participate in the poly(A)-independent pathway.	Poly A	4-11	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	164-170
15210334-4	2004	The poly(A)-dependent pathway is catalyzed by polynucleotide phosphorylase (PNPase), which both adds and degrades destabilizing poly(A) tails, whereas RNase II and PNPase may both participate in the poly(A)-independent pathway.	Poly A	128-135	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	46-74
15210334-4	2004	The poly(A)-dependent pathway is catalyzed by polynucleotide phosphorylase (PNPase), which both adds and degrades destabilizing poly(A) tails, whereas RNase II and PNPase may both participate in the poly(A)-independent pathway.	Poly A	128-135	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	76-82
15210334-4	2004	The poly(A)-dependent pathway is catalyzed by polynucleotide phosphorylase (PNPase), which both adds and degrades destabilizing poly(A) tails, whereas RNase II and PNPase may both participate in the poly(A)-independent pathway.	Poly A	128-135	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	46-74
15210334-4	2004	The poly(A)-dependent pathway is catalyzed by polynucleotide phosphorylase (PNPase), which both adds and degrades destabilizing poly(A) tails, whereas RNase II and PNPase may both participate in the poly(A)-independent pathway.	Poly A	128-135	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	76-82
10222010-1	1999	Polynucleotide phosphorylase (PNPase) is a prokaryotic enzyme that catalyzes phosphorolysis of polynucleotides with release of NDPs.	Polynucleotides	95-110	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
10222010-1	1999	Polynucleotide phosphorylase (PNPase) is a prokaryotic enzyme that catalyzes phosphorolysis of polynucleotides with release of NDPs.	Polynucleotides	95-110	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	30-36
10222010-1	1999	Polynucleotide phosphorylase (PNPase) is a prokaryotic enzyme that catalyzes phosphorolysis of polynucleotides with release of NDPs.	N,N-di-n-propylserotonin	127-131	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
10222010-1	1999	Polynucleotide phosphorylase (PNPase) is a prokaryotic enzyme that catalyzes phosphorolysis of polynucleotides with release of NDPs.	N,N-di-n-propylserotonin	127-131	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	30-36
10222010-3	1999	At the moment, only radioisotopic methods are available for assaying PNPase in crude extracts; these involve incubating [32P]phosphate and poly(A) in the presence of the enzyme, separating [32P]phosphate from [32P]ADP, and quantifying ADP by scintillation counting.	Phosphorus-32	121-124	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	69-75
10222010-3	1999	At the moment, only radioisotopic methods are available for assaying PNPase in crude extracts; these involve incubating [32P]phosphate and poly(A) in the presence of the enzyme, separating [32P]phosphate from [32P]ADP, and quantifying ADP by scintillation counting.	Phosphates	125-134	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	69-75
10222010-3	1999	At the moment, only radioisotopic methods are available for assaying PNPase in crude extracts; these involve incubating [32P]phosphate and poly(A) in the presence of the enzyme, separating [32P]phosphate from [32P]ADP, and quantifying ADP by scintillation counting.	Poly A	139-146	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	69-75
8810258-8	1996	Conditions that remove the tryptophan-like fluorescence from preparations of GroEL also remove the PNPase activity.	Tryptophan	27-37	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	99-105
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	magnesium ion	100-104	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	43-71
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	magnesium ion	100-104	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	111-139
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	Polymers	193-201	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	43-71
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	Polymers	193-201	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	111-139
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	Polymers	193-201	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	141-147
8662001-0	1996	De Novo Synthesis of DNA-Like Molecules by Polynucleotide Phosphorylase In Vitro In the presence of Mg2+ ions, polynucleotide phosphorylase (PNPase, EC 2.7.7.8) is known to synthesize RNA-like polymers using ribonucleoside-5"-diphosphate (NDP) substrates but to be unable to utilize deoxyribonucleoside substrates.	ribonucleoside-5"-diphosphate	208-237	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	43-71
8632418-1	1996	Phosphonate acyclic derivates of guanines, pyrazolo[3,4-d]pyrimidines, and triazolo[4,5-d]-pyrimidines (8-azaguanines) are inhibitors of the enzyme purine nucleoside phosphorylase (PNPase) with Ki" values ranging from 0.05 to 1.6 microM.	pyrazolo(3,4-d)pyrimidine	43-69	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	181-187
8632418-1	1996	Phosphonate acyclic derivates of guanines, pyrazolo[3,4-d]pyrimidines, and triazolo[4,5-d]-pyrimidines (8-azaguanines) are inhibitors of the enzyme purine nucleoside phosphorylase (PNPase) with Ki" values ranging from 0.05 to 1.6 microM.	Azaguanine	104-117	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	181-187
8632418-2	1996	These compounds are enzymatically stable congeners of the potent PNPase inhibitor acyclovir diphosphate (53).	Acyclovir Diphosphate	82-103	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	65-71
34074335-6	2021	The binding interaction between miR-889-3p and circ-PNPT1 or PAK1 was verified using dual-luciferase reporter, RNA immunoprecipitation (RIP) and RNA pull-down assays.	mir-889	32-39	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	52-57
1908235-1	1991	CI-972 (2,6-diamino-3,5-dihydro-7-(3-thienylmethyl)-4H-pyrrolo[3,2- d]pyrimidin-4-one monohydrochloride, monohydrate) is a competitive inhibitor of PNPase (E.C.	CI 972	0-6	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	148-154
1908235-1	1991	CI-972 (2,6-diamino-3,5-dihydro-7-(3-thienylmethyl)-4H-pyrrolo[3,2- d]pyrimidin-4-one monohydrochloride, monohydrate) is a competitive inhibitor of PNPase (E.C.	2,6-diamino-3,5-dihydro-7-(3-thienylmethyl)-4h-pyrrolo	8-62	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	148-154
1908235-1	1991	CI-972 (2,6-diamino-3,5-dihydro-7-(3-thienylmethyl)-4H-pyrrolo[3,2- d]pyrimidin-4-one monohydrochloride, monohydrate) is a competitive inhibitor of PNPase (E.C.	- d]pyrimidin-4-one monohydrochloride	66-103	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	148-154
2114620-1	1990	Formycin B [9-deazainosine] was reacted with epoxy-activated Sepharose 6B to form an affinity resin for purine nucleoside phosphorylase (PNPase).	formycin B	0-10	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	137-143
2114620-1	1990	Formycin B [9-deazainosine] was reacted with epoxy-activated Sepharose 6B to form an affinity resin for purine nucleoside phosphorylase (PNPase).	9-deazainosine	12-26	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	137-143
2114620-1	1990	Formycin B [9-deazainosine] was reacted with epoxy-activated Sepharose 6B to form an affinity resin for purine nucleoside phosphorylase (PNPase).	sepharose 6b	61-73	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	137-143
1909177-4	1991	The amine-phosphate interaction also served to confirm that a quinazolin-4(3H)-one binds in the PNPase active sites like a purine substrate.	amine-phosphate	4-19	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	96-102
1909177-4	1991	The amine-phosphate interaction also served to confirm that a quinazolin-4(3H)-one binds in the PNPase active sites like a purine substrate.	4-hydroxyquinazoline	62-82	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	96-102
1909177-4	1991	The amine-phosphate interaction also served to confirm that a quinazolin-4(3H)-one binds in the PNPase active sites like a purine substrate.	purine	123-129	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	96-102
1909177-5	1991	From models of the PNPase active site it was possible to design quinazoline-based quinones that undergo a reductive-addition reaction with an active-site glutamate residue.	quinazoline-based quinones	64-90	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	19-25
1909177-5	1991	From models of the PNPase active site it was possible to design quinazoline-based quinones that undergo a reductive-addition reaction with an active-site glutamate residue.	Glutamic Acid	154-163	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	19-25
1909177-6	1991	The best inhibitor studied, 2-(chloromethyl)quinazoline-4,5,8(3H)-trione, rapidly inactivates PNPase by a first-order process with an inhibitor to enzyme stoichiometry of 150.	2-(chloromethyl)quinazoline-4,5,8(3h)-trione	28-72	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	94-100
1909177-8	1991	Thus, this inhibitor is designed to cross-link the PNPase active site by reductive addition followed by the generation of an alkylating quinone methide species.	quinone	136-143	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	51-57
34074335-8	2021	RESULTS: Circ-PNPT1 was highly expressed in the placental tissues of GDM and high glucose (HG)-induced trophoblast cells.	Glucose	82-89	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	14-19
108675-3	1979	Of the four substrates of PNPase, only deoxyguanosine at low concentrations is toxic to the PNPase-deficient (NSU-1) cells.	Deoxyguanosine	39-53	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	26-32
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	poly 8-bromoadenylic acid	0-29	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	204-232
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	poly 8-bromoadenylic acid	0-29	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	234-240
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	adenosine-5"-monophosphate	68-94	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	204-232
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	adenosine-5"-monophosphate	68-94	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	234-240
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	8-bromoadenosine-5"-monophosphate	104-137	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	204-232
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	8-bromoadenosine-5"-monophosphate	104-137	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	234-240
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	5"-diphosphate	165-179	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	204-232
6097591-1	1984	Poly-8-bromoriboadenylic acid was synthesized by the bromination of adenosine-5"-monophosphate to yield 8-bromoadenosine-5"-monophosphate which on conversion to the 5"-diphosphate form was polymerized by polynucleotide phosphorylase (PNPase).	5"-diphosphate	165-179	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	234-240
3157330-3	1985	The product diphosphates, without purification, can be polymerized by polynucleotide phosphorylase (PNPase) in 1 h with an average yield of 60%.	Diphosphates	12-24	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	70-98
3157330-3	1985	The product diphosphates, without purification, can be polymerized by polynucleotide phosphorylase (PNPase) in 1 h with an average yield of 60%.	Diphosphates	12-24	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	100-106
3157330-5	1985	Since myosin ATPase and PNPase both have little base specificity, the method can be used to synthesize a radiolabeled polymer of any desired base composition.	Polymers	118-125	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	24-30
6090133-6	1984	Polynucleotide phosphorylase (PNPase) was found both in thylakoid and CF1 preparations and catalyzed the formation of [beta-32P]ADP via its Pi----ADP exchange activity.	[beta-32p]adp	118-131	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
6090133-6	1984	Polynucleotide phosphorylase (PNPase) was found both in thylakoid and CF1 preparations and catalyzed the formation of [beta-32P]ADP via its Pi----ADP exchange activity.	[beta-32p]adp	118-131	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	30-36
6090133-6	1984	Polynucleotide phosphorylase (PNPase) was found both in thylakoid and CF1 preparations and catalyzed the formation of [beta-32P]ADP via its Pi----ADP exchange activity.	Adenosine Diphosphate	128-131	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28
6090133-6	1984	Polynucleotide phosphorylase (PNPase) was found both in thylakoid and CF1 preparations and catalyzed the formation of [beta-32P]ADP via its Pi----ADP exchange activity.	Adenosine Diphosphate	128-131	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	30-36
6090133-8	1984	In addition, PNPase also degraded RNA present in thylakoid preparations yielding all four [32P]nucleoside diphosphates.	[32p]nucleoside diphosphates	90-118	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	13-19
6090133-9	1984	PNPase was also shown to catalyze a Pi----ATP exchange that is dependent on RNA primers and other cofactors.	Adenosine Triphosphate	42-45	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-6
108675-3	1979	Of the four substrates of PNPase, only deoxyguanosine at low concentrations is toxic to the PNPase-deficient (NSU-1) cells.	Deoxyguanosine	39-53	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	92-98
824697-4	1976	Kinetic studies carried out with homogenates and purified preparations of pigeon liver PNPase seem to suggest that inosine and deoxynosine react on the same catalytic site of the enzyme molecule.	Inosine	115-122	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	87-93
824697-4	1976	Kinetic studies carried out with homogenates and purified preparations of pigeon liver PNPase seem to suggest that inosine and deoxynosine react on the same catalytic site of the enzyme molecule.	deoxynosine	127-138	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	87-93
31988703-5	2020	In the present study, we have examined the interaction of PNPase with 8-oxoG in atomic detail to provide insights into the mechanism of 8-oxoG discrimination.	8-hydroxyguanosine	70-76	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	58-64
1109594-4	1975	Treatment of human erythrocytic PNPase with dithiobisnitrobenzoate changed the enzyme to a more acidic form (pI = 5.05).	dithiobisnitrobenzoate	44-66	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	32-38
1109594-6	1975	All six variants of the human erythrocytic PNPase and the two variants of rat erythrocytic PNPase displayed substrate activation at high concentrations of inosine and deoxyinosine.	Inosine	155-162	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	43-49
1109594-6	1975	All six variants of the human erythrocytic PNPase and the two variants of rat erythrocytic PNPase displayed substrate activation at high concentrations of inosine and deoxyinosine.	Inosine	155-162	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	91-97
1109594-6	1975	All six variants of the human erythrocytic PNPase and the two variants of rat erythrocytic PNPase displayed substrate activation at high concentrations of inosine and deoxyinosine.	deoxyinosine	167-179	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	43-49
1109594-6	1975	All six variants of the human erythrocytic PNPase and the two variants of rat erythrocytic PNPase displayed substrate activation at high concentrations of inosine and deoxyinosine.	deoxyinosine	167-179	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	91-97
33158637-5	2021	Via whole-exome sequencing, we identified a novel homozygous missense variant (c.1399C > T, p.Pro467Ser) in PNPT1 (NM_033109).	pro467ser	94-103	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	108-113
32809827-6	2020	Importantly, QD394 decreases the expression of LRPPRC and PNPT1, two proteins involved in mitochondrial RNA catabolic processes and both negatively correlated with the overall survival of pancreatic cancer patients.	qd394	13-18	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	58-63
31995710-7	2020	Furthermore, we show that PNPase localizes predominantly into the coacervate phase and that its depolymerization activity in high-phosphate buffer causes coacervate degradation.	Phosphates	130-139	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	26-32
32540202-0	2020	Novel PNPT1-ALK fusion variant exerted significant benefit to crizotinib in NSCLC.	Crizotinib	62-72	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	6-11
31988703-5	2020	In the present study, we have examined the interaction of PNPase with 8-oxoG in atomic detail to provide insights into the mechanism of 8-oxoG discrimination.	8-hydroxyguanosine	136-142	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	58-64
31752325-0	2019	Clinical Spectrum and Functional Consequences Associated with Bi-Allelic Pathogenic PNPT1 Variants.	Bismuth	62-64	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	84-89
31752325-2	2019	Bi-allelic pathogenic PNPT1 variants cause heterogeneous clinical phenotypes affecting multiple organs without any established genotype-phenotype correlations.	Bismuth	0-2	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	22-27
28594066-7	2018	Exogenous expression of wild-type PNPT1, but not mutants, rescued ATP production in patient skin fibroblasts, suggesting the pathogenicity of the identified mutations.	Adenosine Triphosphate	66-69	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	34-39
24770417-4	2014	Here, we demonstrated that a fraction of the SUV3 PNPase complex interacts with mitochondrial polyadenylation polymerase (mtPAP) under low mitochondrial matrix inorganic phosphate (Pi) conditions.	Phosphates	160-179	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	50-56
24770417-9	2014	Furthermore, purified SUV3 PNPase mtPAP complex is capable of lengthening or shortening the RNA poly(A) tail lengths in low or high Pi/ATP ratios, respectively.	Adenosine Triphosphate	135-138	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	27-33
24729470-6	2014	Further analysis comparing the gene expression changes between Ad.hPNPase(old-35) infected HO-1 melanoma cells and HeLa cells overexpressing hPNPase(old-35) under the control of a doxycycline-inducible promoter, revealed global changes in genes involved in cell cycle and mitosis.	Doxycycline	180-191	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	66-80
24729470-6	2014	Further analysis comparing the gene expression changes between Ad.hPNPase(old-35) infected HO-1 melanoma cells and HeLa cells overexpressing hPNPase(old-35) under the control of a doxycycline-inducible promoter, revealed global changes in genes involved in cell cycle and mitosis.	Doxycycline	180-191	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	141-155
24143183-4	2013	Ingenuity Pathway Analysis indicated that knockdown of hPNPase(old-35) resulted in significant gene expression changes associated with mitochondrial dysfunction and cholesterol biosynthesis; whereas overexpression of hPNPase(old-35) caused global changes in cell-cycle related functions.	Cholesterol	165-176	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	55-69