PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
33932034-4	2021	Mechanistically, we found that BNIP3-deprived melanoma cells displayed increased intracellular iron levels caused by heightened NCOA4-mediated ferritinophagy, which fostered PHD2-mediated HIF-1alpha destabilization.	Iron	95-99	egl-9 family hypoxia inducible factor 1	Homo sapiens	174-178
33713969-0	2021	The DpdtbA induced EMT inhibition in gastric cancer cell lines was through ferritinophagy-mediated activation of p53 and PHD2/hif-1alpha pathway.	dpdtba	4-10	egl-9 family hypoxia inducible factor 1	Homo sapiens	121-125
33988258-2	2021	Recently, the reduction of prolyl hydroxylase domain-containing protein 2 (PHD2), a primary cellular oxygen sensor, has shown an incredible extensive effect on skeletal muscle tissue regeneration by improving cell resistance to reactive oxygen species, whereas its role in periodontal defect repair is unclear.	Oxygen	101-107	egl-9 family hypoxia inducible factor 1	Homo sapiens	27-73
33988258-2	2021	Recently, the reduction of prolyl hydroxylase domain-containing protein 2 (PHD2), a primary cellular oxygen sensor, has shown an incredible extensive effect on skeletal muscle tissue regeneration by improving cell resistance to reactive oxygen species, whereas its role in periodontal defect repair is unclear.	Oxygen	101-107	egl-9 family hypoxia inducible factor 1	Homo sapiens	75-79
33988258-2	2021	Recently, the reduction of prolyl hydroxylase domain-containing protein 2 (PHD2), a primary cellular oxygen sensor, has shown an incredible extensive effect on skeletal muscle tissue regeneration by improving cell resistance to reactive oxygen species, whereas its role in periodontal defect repair is unclear.	Oxygen	237-243	egl-9 family hypoxia inducible factor 1	Homo sapiens	27-73
33988258-2	2021	Recently, the reduction of prolyl hydroxylase domain-containing protein 2 (PHD2), a primary cellular oxygen sensor, has shown an incredible extensive effect on skeletal muscle tissue regeneration by improving cell resistance to reactive oxygen species, whereas its role in periodontal defect repair is unclear.	Oxygen	237-243	egl-9 family hypoxia inducible factor 1	Homo sapiens	75-79
33988258-6	2021	Under oxidative stress conditions, COL I and ALP expression levels, suppressed by 100 muM H2 O2 , were elevated by PHD2-gene-silencing in hPDLCs.	Hydrogen Peroxide	90-95	egl-9 family hypoxia inducible factor 1	Homo sapiens	115-119
33713969-4	2021	The data from immunofluorescent and Western blotting analysis revealed that DpdtbA treatment resulted in EMT inhibition along with downregulation of hypoxia-inducible factor (hif-1alpha), hinting that prolyl hydroxylase 2 (PHD2) was involved.	dpdtba	76-82	egl-9 family hypoxia inducible factor 1	Homo sapiens	201-221
33713969-4	2021	The data from immunofluorescent and Western blotting analysis revealed that DpdtbA treatment resulted in EMT inhibition along with downregulation of hypoxia-inducible factor (hif-1alpha), hinting that prolyl hydroxylase 2 (PHD2) was involved.	dpdtba	76-82	egl-9 family hypoxia inducible factor 1	Homo sapiens	223-227
33713969-9	2021	Taken together, All data supported that DpdtbA induced EMT inhibition was through activation of p53 and PHD2/hif-1alpha pathway.	dpdtba	40-46	egl-9 family hypoxia inducible factor 1	Homo sapiens	104-108
32754325-2	2020	Reverse transcription-quantitative PCR was used to quantify the mRNA expression levels of HIF-1alpha, HIF-2alpha, prolyl hydroxylase (PHD)1, PHD2 and PHD3 in formalin-fixed paraffin-embedded (FFPE) tumour tissue samples from 41 patients with RCC, including 33 cases of clear cell RCC (ccRCC).	Formaldehyde	158-166	egl-9 family hypoxia inducible factor 1	Homo sapiens	141-145
33871074-10	2021	Thus, the results obtained from pharmacophore, docking, and MD simulations depicted that linker length and metal binding in the scaffold could be effectively used as a potent inhibitor toward human PHD2 in AD therapeutics.	Metals	107-112	egl-9 family hypoxia inducible factor 1	Homo sapiens	198-202
33550096-2	2021	Oxygen-dependent hydroxylation of HIF-1alpha is tightly regulated by prolyl hydroxylase domain containing proteins (PHD1, PHD2, and PHD3).	Oxygen	0-6	egl-9 family hypoxia inducible factor 1	Homo sapiens	122-126
33410354-5	2021	In the present study, we demonstrated that prolonged hypoxia increased ROS, which induced prolyl hydroxylase domain-containing protein 2 (PHD2) and factor inhibiting HIF-1 (FIH-1), major regulators of HIF-1alpha.	Reactive Oxygen Species	71-74	egl-9 family hypoxia inducible factor 1	Homo sapiens	90-136
33410354-5	2021	In the present study, we demonstrated that prolonged hypoxia increased ROS, which induced prolyl hydroxylase domain-containing protein 2 (PHD2) and factor inhibiting HIF-1 (FIH-1), major regulators of HIF-1alpha.	Reactive Oxygen Species	71-74	egl-9 family hypoxia inducible factor 1	Homo sapiens	138-142
33410354-7	2021	PHD2 and FIH-1 were induced by external hydrogen peroxide (H2O2) but were suppressed by ROS-scavenging catalase.	Hydrogen Peroxide	40-57	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
33410354-7	2021	PHD2 and FIH-1 were induced by external hydrogen peroxide (H2O2) but were suppressed by ROS-scavenging catalase.	Hydrogen Peroxide	59-63	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
33410354-7	2021	PHD2 and FIH-1 were induced by external hydrogen peroxide (H2O2) but were suppressed by ROS-scavenging catalase.	Reactive Oxygen Species	88-91	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
33410354-8	2021	We investigated the mechanisms by which PHD2 and FIH-1 are regulated by ROS.	Reactive Oxygen Species	72-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	40-44
33410354-15	2021	Collectively, the present results showed that prolonged hypoxia or increased ROS levels induced Ref-1, leading to the activation of HIF-1alpha transcriptional activity, while the activation of HIF-1alpha via Ref-1 induced PHD2 and FIH-1, causing the feedback of HIF-1alpha.	Reactive Oxygen Species	77-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	222-226
33319810-4	2020	Following the observation that, despite weak inhibition/binding in solution, succinamic acid derivatives readily enable PHD2 crystallization, we explored methods to induce crystallization without active site binding.	SUCCINAMIC ACID	77-92	egl-9 family hypoxia inducible factor 1	Homo sapiens	120-124
31852247-1	2020	Background: Prolyl hydroxylase domain proteins (PHD2) is an oxygen sensor that is able to induce hypoxia-inducible factor-alpha (HIF-alpha) degradation under normoxic condition.	Peptide oostatic hormone	12-18	egl-9 family hypoxia inducible factor 1	Homo sapiens	48-52
31852247-1	2020	Background: Prolyl hydroxylase domain proteins (PHD2) is an oxygen sensor that is able to induce hypoxia-inducible factor-alpha (HIF-alpha) degradation under normoxic condition.	Oxygen	60-66	egl-9 family hypoxia inducible factor 1	Homo sapiens	48-52
31939292-5	2020	We employed a combined multiscale approach involving classical atomistic equilibrium and non-equilibrium MD simulations combined with QM/MM trajectories to investigate dioxygen diffusion to, and binding at, the active site in the PHD2.Fe(II).2OG.HIF substrate complex; PHD2 is the most important of the three human PHDs.	Oxygen	168-176	egl-9 family hypoxia inducible factor 1	Homo sapiens	230-234
32377332-2	2020	As a cellular oxygen sensor, prolyl hydroxylase domain containing protein 2 (PHD2, encoded by egl-9 family hypoxia inducible factor 1, EGLN1) modifies hypoxia-inducible factor alpha (HIF-alpha) protein for proteasomal destruction under normoxic condition.	Oxygen	14-20	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-75
32377332-2	2020	As a cellular oxygen sensor, prolyl hydroxylase domain containing protein 2 (PHD2, encoded by egl-9 family hypoxia inducible factor 1, EGLN1) modifies hypoxia-inducible factor alpha (HIF-alpha) protein for proteasomal destruction under normoxic condition.	Oxygen	14-20	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-81
32377332-2	2020	As a cellular oxygen sensor, prolyl hydroxylase domain containing protein 2 (PHD2, encoded by egl-9 family hypoxia inducible factor 1, EGLN1) modifies hypoxia-inducible factor alpha (HIF-alpha) protein for proteasomal destruction under normoxic condition.	Oxygen	14-20	egl-9 family hypoxia inducible factor 1	Homo sapiens	135-140
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Ketoglutaric Acids	13-27	egl-9 family hypoxia inducible factor 1	Homo sapiens	69-73
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Oxygen	47-53	egl-9 family hypoxia inducible factor 1	Homo sapiens	69-73
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Iron	104-108	egl-9 family hypoxia inducible factor 1	Homo sapiens	69-73
32142369-9	2020	The PHD2 (prolyl hydroxylase domain-containing protein 2) inhibitor FG-4592 significantly increased NAMPT promoter activity and protein expression in an HIF-2alpha-dependent manner.	roxadustat	68-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	4-8
32142369-9	2020	The PHD2 (prolyl hydroxylase domain-containing protein 2) inhibitor FG-4592 significantly increased NAMPT promoter activity and protein expression in an HIF-2alpha-dependent manner.	roxadustat	68-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	10-56
32023483-6	2020	SFMBT1 hydroxylation on Proline residue 651 by EglN1 mediated its ubiquitination and degradation governed by pVHL.	Proline	24-31	egl-9 family hypoxia inducible factor 1	Homo sapiens	47-52
31939292-5	2020	We employed a combined multiscale approach involving classical atomistic equilibrium and non-equilibrium MD simulations combined with QM/MM trajectories to investigate dioxygen diffusion to, and binding at, the active site in the PHD2.Fe(II).2OG.HIF substrate complex; PHD2 is the most important of the three human PHDs.	Iron	235-241	egl-9 family hypoxia inducible factor 1	Homo sapiens	230-234
31939292-6	2020	The transport of dioxygen to the active site is described; dioxygen transport follows a single well-defined hydrophobic tunnel, formed from both enzyme and substrate elements to reach the PHD2 active site.	Oxygen	17-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	188-192
31939292-6	2020	The transport of dioxygen to the active site is described; dioxygen transport follows a single well-defined hydrophobic tunnel, formed from both enzyme and substrate elements to reach the PHD2 active site.	Oxygen	59-67	egl-9 family hypoxia inducible factor 1	Homo sapiens	188-192
31939292-7	2020	The results provide estimates for rate constants that define a diffusion-reaction model for dioxygen:PHD2 interactions; in combination with reported biophysical analyses they provide chemical insight into the basis of the slow reaction of PHD2 with dioxygen.	Oxygen	92-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	101-105
31939292-7	2020	The results provide estimates for rate constants that define a diffusion-reaction model for dioxygen:PHD2 interactions; in combination with reported biophysical analyses they provide chemical insight into the basis of the slow reaction of PHD2 with dioxygen.	Oxygen	92-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	239-243
31939292-7	2020	The results provide estimates for rate constants that define a diffusion-reaction model for dioxygen:PHD2 interactions; in combination with reported biophysical analyses they provide chemical insight into the basis of the slow reaction of PHD2 with dioxygen.	Oxygen	249-257	egl-9 family hypoxia inducible factor 1	Homo sapiens	101-105
31939292-7	2020	The results provide estimates for rate constants that define a diffusion-reaction model for dioxygen:PHD2 interactions; in combination with reported biophysical analyses they provide chemical insight into the basis of the slow reaction of PHD2 with dioxygen.	Oxygen	249-257	egl-9 family hypoxia inducible factor 1	Homo sapiens	239-243
31939292-9	2020	The extent of HIF-alpha substrate prolyl hydroxylation, which signals for subsequent HIF-alpha degradation is thus a manifestation of the equilibrium between dioxygen in bulk solution and dioxygen bound to the PHD2.Fe.2OG.HIF-alpha substrate complex.	Peptide oostatic hormone	34-40	egl-9 family hypoxia inducible factor 1	Homo sapiens	210-214
31939292-9	2020	The extent of HIF-alpha substrate prolyl hydroxylation, which signals for subsequent HIF-alpha degradation is thus a manifestation of the equilibrium between dioxygen in bulk solution and dioxygen bound to the PHD2.Fe.2OG.HIF-alpha substrate complex.	Oxygen	188-196	egl-9 family hypoxia inducible factor 1	Homo sapiens	210-214
31285371-0	2019	ERK Regulates HIF1alpha-Mediated Platinum Resistance by Directly Targeting PHD2 in Ovarian Cancer.	Platinum	33-41	egl-9 family hypoxia inducible factor 1	Homo sapiens	75-79
31618435-2	2020	Hypoxia-inducible transcription factor prolyl hydroxylase-containing enzymes (PHD1, PHD2, and PHD3) are molecular oxygen sensors that control adaptive gene expression through hypoxia-inducible factor (HIF).	Oxygen	114-120	egl-9 family hypoxia inducible factor 1	Homo sapiens	84-88
31998438-10	2020	The above results indicated that direct peritoneal resuscitation with pyruvate showed effective protection to ischemia-reperfusion of the spinal cord through activating autophagy via acting on PHD2 and its downstream HIF-1alpha/BNIP3 pathway.	Pyruvic Acid	70-78	egl-9 family hypoxia inducible factor 1	Homo sapiens	193-197
31763849-1	2020	Prolyl Hydroxylase Domain-Containing Protein 2 (PHD2/EGLN1) is a key regulatory enzyme that plays a fundamental role in the cellular hypoxia response pathway, mediating proline hydroxylation-dependent protein degradation of selected target proteins.	isoleucyl-prolyl-proline	169-176	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-46
31763849-1	2020	Prolyl Hydroxylase Domain-Containing Protein 2 (PHD2/EGLN1) is a key regulatory enzyme that plays a fundamental role in the cellular hypoxia response pathway, mediating proline hydroxylation-dependent protein degradation of selected target proteins.	isoleucyl-prolyl-proline	169-176	egl-9 family hypoxia inducible factor 1	Homo sapiens	48-52
31763849-1	2020	Prolyl Hydroxylase Domain-Containing Protein 2 (PHD2/EGLN1) is a key regulatory enzyme that plays a fundamental role in the cellular hypoxia response pathway, mediating proline hydroxylation-dependent protein degradation of selected target proteins.	isoleucyl-prolyl-proline	169-176	egl-9 family hypoxia inducible factor 1	Homo sapiens	53-58
31853455-3	2019	PHD2 hydroxylates and downregulates hypoxia-inducible factor-2alpha (HIF-2alpha), a transcription factor that regulates erythropoiesis.	hydroxylates	5-17	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
31853455-9	2019	We also present results that indicate that PHD2 Arg-32 interacts with p23 Glu-160.	arginylarginine	48-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	43-47
31712437-4	2019	The encoded protein, EGLN1/PHD2, is an O2 sensor that controls levels of the Hypoxia Inducible Factor-alpha (HIF-alpha), which regulates the cellular response to hypoxia.	Superoxides	39-41	egl-9 family hypoxia inducible factor 1	Homo sapiens	21-26
31712437-4	2019	The encoded protein, EGLN1/PHD2, is an O2 sensor that controls levels of the Hypoxia Inducible Factor-alpha (HIF-alpha), which regulates the cellular response to hypoxia.	Superoxides	39-41	egl-9 family hypoxia inducible factor 1	Homo sapiens	27-31
31712437-10	2019	These findings contextualize previous reports of natural selection at EGLN1 in Andeans, and support the hypothesis that natural selection has increased the frequency of an EGLN1 causal variant that enhances O2 delivery or use during exercise at altitude in Peruvian Quechua.	Superoxides	207-209	egl-9 family hypoxia inducible factor 1	Homo sapiens	172-177
31285371-10	2019	Inhibition of TGFbeta1 by SB431542, ERK by selumetinib, or HIF1alpha by YC-1 efficiently overcame platinum resistance both in vitro and in vivo The results from clinical samples confirm activation of the ERK/PHD2/HIF1alpha axis in patients with PROC, correlating highly with poor prognoses for patients.Conclusions: HIF1alpha stabilization is regulated by TGFbeta1/ERK/PHD2 axis in PROC.	Platinum	98-106	egl-9 family hypoxia inducible factor 1	Homo sapiens	369-373
31285371-6	2019	Moreover, a novel TGFbeta1/ERK/PHD2-mediated pathway regulating HIF1alpha stability in PROC was discovered.Results: YC-1 and selumetinib resensitized PROC cells to cisplatin.	AZD 6244	125-136	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
31285371-6	2019	Moreover, a novel TGFbeta1/ERK/PHD2-mediated pathway regulating HIF1alpha stability in PROC was discovered.Results: YC-1 and selumetinib resensitized PROC cells to cisplatin.	Cisplatin	164-173	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
31285371-9	2019	Significantly, ERK/PHD2 signaling in PROC cells is dependent on TGFbeta1, promoting platinum resistance by stabilizing HIF1alpha.	Platinum	84-92	egl-9 family hypoxia inducible factor 1	Homo sapiens	19-23
31285371-10	2019	Inhibition of TGFbeta1 by SB431542, ERK by selumetinib, or HIF1alpha by YC-1 efficiently overcame platinum resistance both in vitro and in vivo The results from clinical samples confirm activation of the ERK/PHD2/HIF1alpha axis in patients with PROC, correlating highly with poor prognoses for patients.Conclusions: HIF1alpha stabilization is regulated by TGFbeta1/ERK/PHD2 axis in PROC.	Platinum	98-106	egl-9 family hypoxia inducible factor 1	Homo sapiens	208-212
30817904-3	2019	Prolyl-4-hydroxylase 2 (PHD2), one member of PHDs family, regulates the stability of the hypoxia-inducible factor-1 alpha (HIF-1alpha) in response to oxygen availability.	Oxygen	150-156	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-22
31239290-0	2019	Targeted and Interactome Proteomics Revealed the Role of PHD2 in Regulating BRD4 Proline Hydroxylation.	Proline	81-88	egl-9 family hypoxia inducible factor 1	Homo sapiens	57-61
31239290-6	2019	Our findings revealed that PHD2 is the key regulatory enzyme of BRD4 proline hydroxylation and the modification significantly affects BRD4 interactions with key transcription factors as well as BRD4-mediated transcriptional activation.	Proline	69-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	27-31
31413262-2	2019	Prolyl hydroxylase 2 (PHD2) dominantly hydroxylates two highly conserved proline residues of HIF-1alpha to promote its degradation.	Proline	73-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-20
31413262-2	2019	Prolyl hydroxylase 2 (PHD2) dominantly hydroxylates two highly conserved proline residues of HIF-1alpha to promote its degradation.	Proline	73-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	22-26
30849228-7	2019	Increased neutrophil apoptosis in hypoxia, also observed with IL-13, required active STAT signaling, and was dependent on expression of the oxygen-sensing prolyl hydroxylase PHD2.	Oxygen	140-146	egl-9 family hypoxia inducible factor 1	Homo sapiens	174-178
30898838-4	2019	EGLN1-dependent cells exhibited sensitivity to the pan-EGLN inhibitor FG-4592.	roxadustat	70-77	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-5
30719713-1	2019	EGLN1 encodes the hypoxia-inducible factor (HIF) pathway prolyl hydroxylase 2 (PHD2) that serves as an oxygen-sensitive regulator of HIF activity.	Oxygen	103-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-5
30719713-1	2019	EGLN1 encodes the hypoxia-inducible factor (HIF) pathway prolyl hydroxylase 2 (PHD2) that serves as an oxygen-sensitive regulator of HIF activity.	Oxygen	103-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	57-77
30719713-1	2019	EGLN1 encodes the hypoxia-inducible factor (HIF) pathway prolyl hydroxylase 2 (PHD2) that serves as an oxygen-sensitive regulator of HIF activity.	Oxygen	103-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	79-83
30817904-3	2019	Prolyl-4-hydroxylase 2 (PHD2), one member of PHDs family, regulates the stability of the hypoxia-inducible factor-1 alpha (HIF-1alpha) in response to oxygen availability.	Oxygen	150-156	egl-9 family hypoxia inducible factor 1	Homo sapiens	24-28
30817904-4	2019	During hypoxia, the inhibition of PHD2 permits the accumulation of HIF-1alpha, allowing the cellular adaptation to oxygen limitation, causing activation of numerous genes, which enhances the angiogenesis, metastasis and invasiveness.	Oxygen	115-121	egl-9 family hypoxia inducible factor 1	Homo sapiens	34-38
30817904-5	2019	Accurate regulation of oxygen homeostasis is essential, and which implies PHD2 may have a regulatory role in the pathogenesis of cancer.	Oxygen	23-29	egl-9 family hypoxia inducible factor 1	Homo sapiens	74-78
30817904-7	2019	Despite their original role as the oxygen sensors of the cell and many of the its functions are clearly conveyed through the HIF system, PHD2 is currently known to display HIF-independent and hydroxylase-independent functions in cancer cells and stroma in the control of different cellular pathways.	Oxygen	35-41	egl-9 family hypoxia inducible factor 1	Homo sapiens	137-141
30575721-1	2018	Prolyl hydroxylase domain protein 2 (PHD2) is a well-known master oxygen sensor.	Oxygen	66-72	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
30452037-2	2019	Reversible active site binding of electrophile bearing compounds enables susbsequent covalent reaction with a lysine residue (K408) in the flexible C-terminal region of PHD2 to give a modified protein that retains catalytic activity.	Lysine	110-116	egl-9 family hypoxia inducible factor 1	Homo sapiens	169-173
30452037-2	2019	Reversible active site binding of electrophile bearing compounds enables susbsequent covalent reaction with a lysine residue (K408) in the flexible C-terminal region of PHD2 to give a modified protein that retains catalytic activity.	DIMETHYLCARBAMOYL CHLORIDE	126-130	egl-9 family hypoxia inducible factor 1	Homo sapiens	169-173
30339780-0	2019	A redox ruthenium compound directly targets PHD2 and inhibits the HIF1 pathway to reduce tumor angiogenesis independently of p53.	Ruthenium Compounds	8-26	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-48
30339780-7	2019	The rapid downregulation of HIF1A protein levels involved a direct interaction of the ruthenium compound with the redox enzyme PHD2, a HIF1A master regulator.	Ruthenium	86-95	egl-9 family hypoxia inducible factor 1	Homo sapiens	127-131
30575721-1	2018	Prolyl hydroxylase domain protein 2 (PHD2) is a well-known master oxygen sensor.	Oxygen	66-72	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
30179610-4	2018	TP0463518 competitively inhibited human PHD2 with a Ki value of 5.3 nM.	TP0463518	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	40-44
30575913-7	2018	The methylation status of two CpG sites (cg07040244 and cg21875980) in PHD2 was at least moderately and negatively correlated with PHD2 expression.	cg07040244	41-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	71-75
30575913-7	2018	The methylation status of two CpG sites (cg07040244 and cg21875980) in PHD2 was at least moderately and negatively correlated with PHD2 expression.	cg07040244	41-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	131-135
30575913-10	2018	Cg07040244 and cg21875980 might be two CpG sites modulating PHD2 expression in LUAD.	cg21875980	15-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	60-64
30179610-5	2018	TP0463518 also inhibited human PHD1/3 with IC50 values of 18 and 63 nM as well as monkey PHD2 with an IC50 value of 22 nM.	TP0463518	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	89-93
29599405-4	2018	Depletion of TKT or addition of alpha-ketoglutarate (alphaKG) enhanced the levels of tumor suppressors succinate dehydrogenase and fumarate hydratase (FH), decreasing oncometabolites succinate and fumarate, and further stabilizing HIF prolyl hydroxylase 2 (PHD2) and decreasing HIF1alpha, ultimately suppressing breast cancer metastasis.	Ketoglutaric Acids	32-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	235-255
29930174-4	2018	LIMD1 complexes with PHD2 and VHL in physiological oxygen levels (normoxia) to facilitate proteasomal degradation of the HIF-alpha subunit.	Oxygen	51-57	egl-9 family hypoxia inducible factor 1	Homo sapiens	21-25
29772209-5	2018	Prolyl hydroxylase 2 (PHD2) is a negative regulator of HIF-1alpha and causes degradation of HIF-1alpha in the presence of oxygen.	Oxygen	122-128	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-20
29772209-5	2018	Prolyl hydroxylase 2 (PHD2) is a negative regulator of HIF-1alpha and causes degradation of HIF-1alpha in the presence of oxygen.	Oxygen	122-128	egl-9 family hypoxia inducible factor 1	Homo sapiens	22-26
30255776-5	2018	In addition, fenofibrate therapy modified the methylation levels on the following 4 CpG sites: cg20015535 (gene EGLN1, chromosome 1); cg24870738 (gene RNF220, chromosome 1); cg06891775 (gene LOC283050, chromosome 10); and cg00607630 (gene USP7, chromosome 16).	Fenofibrate	13-24	egl-9 family hypoxia inducible factor 1	Homo sapiens	112-117
29967369-7	2018	Thus, oxygen sensing by PHD2 in osteocytes negatively regulates bone mass through epigenetic regulation of sclerostin and targeting PHD2 elicits an osteo-anabolic response in osteoporotic models.	Oxygen	6-12	egl-9 family hypoxia inducible factor 1	Homo sapiens	24-28
29967369-7	2018	Thus, oxygen sensing by PHD2 in osteocytes negatively regulates bone mass through epigenetic regulation of sclerostin and targeting PHD2 elicits an osteo-anabolic response in osteoporotic models.	Oxygen	6-12	egl-9 family hypoxia inducible factor 1	Homo sapiens	132-136
29917232-7	2018	Taken together, these findings demonstrate a key role for the PHD2-HIF-2alpha couple in Type I cells with respect to the oxygen sensing functions of the carotid body.	Oxygen	121-127	egl-9 family hypoxia inducible factor 1	Homo sapiens	62-66
29917232-16	2018	These findings implicate specific components of the HIF hydroxylase pathway (PHD2 and HIF-2alpha) within Type I cells of the carotid body with respect to the oxygen sensing and adaptive functions of that organ.	Oxygen	158-164	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-81
29599405-4	2018	Depletion of TKT or addition of alpha-ketoglutarate (alphaKG) enhanced the levels of tumor suppressors succinate dehydrogenase and fumarate hydratase (FH), decreasing oncometabolites succinate and fumarate, and further stabilizing HIF prolyl hydroxylase 2 (PHD2) and decreasing HIF1alpha, ultimately suppressing breast cancer metastasis.	Ketoglutaric Acids	32-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	257-261
28816009-6	2018	Proliferation of HLF-1 was reduced after atazanavir treatment, meanwhile the expression of hypoxia-inducible factor-1alpha (HIF-1alpha), prolyl hydroxylase domain protein 2 (PHD-2), HMGB1, TLR-9, p-NF-kappaB, collagen I and collagen III was decreased.	Atazanavir Sulfate	41-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	137-172
29355756-0	2018	GLA supplementation regulates PHD2 mediated hypoxia and mitochondrial apoptosis in DMBA induced mammary gland carcinoma.	gamma-Linolenic Acid	0-3	egl-9 family hypoxia inducible factor 1	Homo sapiens	30-34
29530922-5	2018	Physiologically, the hypoxia response is tempered through HIF-1alpha hydroxylation by the oxygen-sensing prolyl hydroxylase-domain protein 2 (PHD2) and subsequent ubiquitination and degradation.	Oxygen	90-96	egl-9 family hypoxia inducible factor 1	Homo sapiens	105-140
29530922-5	2018	Physiologically, the hypoxia response is tempered through HIF-1alpha hydroxylation by the oxygen-sensing prolyl hydroxylase-domain protein 2 (PHD2) and subsequent ubiquitination and degradation.	Oxygen	90-96	egl-9 family hypoxia inducible factor 1	Homo sapiens	142-146
29741264-6	2018	Secondary CE can also result from defects in the components of the oxygen-sensing pathway (PHD2, HIF2alpha and VHL).	Oxygen	67-73	egl-9 family hypoxia inducible factor 1	Homo sapiens	91-95
29625625-0	2018	Association of EGLN1 genetic polymorphisms with SpO2 responses to acute hypobaric hypoxia in a Japanese cohort.	spo2	48-52	egl-9 family hypoxia inducible factor 1	Homo sapiens	15-20
29471019-5	2018	We discovered an increased interaction between PHD2 and the p23:Hsp90 chaperone complex in response to mitochondrial stress elicited by the mitochondrial neurotoxin 1-methyl-4-phenylpyridine (MPP+) within cultured DAergic cells.	1-Methyl-4-phenylpyridinium	165-190	egl-9 family hypoxia inducible factor 1	Homo sapiens	47-51
29471019-5	2018	We discovered an increased interaction between PHD2 and the p23:Hsp90 chaperone complex in response to mitochondrial stress elicited by the mitochondrial neurotoxin 1-methyl-4-phenylpyridine (MPP+) within cultured DAergic cells.	mangion-purified polysaccharide (Candida albicans)	192-196	egl-9 family hypoxia inducible factor 1	Homo sapiens	47-51
28816009-6	2018	Proliferation of HLF-1 was reduced after atazanavir treatment, meanwhile the expression of hypoxia-inducible factor-1alpha (HIF-1alpha), prolyl hydroxylase domain protein 2 (PHD-2), HMGB1, TLR-9, p-NF-kappaB, collagen I and collagen III was decreased.	Atazanavir Sulfate	41-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	174-179
29962348-6	2018	ROS inhibit the enzyme PHD2, which leads to the stabilization of HIF-alpha and the formation of the active transcription factor HIF.	Reactive Oxygen Species	0-3	egl-9 family hypoxia inducible factor 1	Homo sapiens	23-27
29158549-9	2017	Overexpression of prolyl-hydroxylase 2 (PHD2) transgene, a predominant isoform of PHDs in renal tubules, to reduce HIF-1alpha level significantly attenuated albumin-induced increases in TIMP-1 and collagen-I levels.	Thromboxane B2	82-86	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-38
28699703-14	2017	The mechanism may function through miR-210-mediated repression of RUNX3, which further decreases the hydroxylation activity of PHD2, enhances the stability of HIF-1alpha, and promotes PQ-induced EMT, aggravating the progression of pulmonary fibrosis.	Paraquat	184-186	egl-9 family hypoxia inducible factor 1	Homo sapiens	127-131
30411685-5	2018	In normoxia condition HIF is inactivated by prolyl hydroxylase enzymes (EGLN 1-3, also known as PHD 1-3) using oxygen as a substrate.	Oxygen	111-117	egl-9 family hypoxia inducible factor 1	Homo sapiens	72-80
29295567-4	2017	The inhibitory effect of minoxidil on hypoxia-inducible factor (HIF) prolyl hydroxylase-2 (PHD-2) was tested by an in vitro von Hippel-Lindau protein (VHL) binding assay.	Minoxidil	25-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	38-89
29295567-4	2017	The inhibitory effect of minoxidil on hypoxia-inducible factor (HIF) prolyl hydroxylase-2 (PHD-2) was tested by an in vitro von Hippel-Lindau protein (VHL) binding assay.	Minoxidil	25-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	91-96
29295567-9	2017	In an in vitro VHL binding assay, minoxidil directly inhibited PHD-2, thus preventing the hydroxylation of cellular HIF-1alpha and VHL-dependent proteasome degradation and resulting in the stabilization of HIF-1alpha protein.	Minoxidil	34-43	egl-9 family hypoxia inducible factor 1	Homo sapiens	63-68
29295567-10	2017	Minoxidil inhibition of PHD-2 was reversed by ascorbate, a cofactor of PHD-2, and the minoxidil induction of cellular HIF-1alpha was abrogated by the cofactor.	Minoxidil	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	24-29
29295567-10	2017	Minoxidil inhibition of PHD-2 was reversed by ascorbate, a cofactor of PHD-2, and the minoxidil induction of cellular HIF-1alpha was abrogated by the cofactor.	Minoxidil	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	71-76
29295567-10	2017	Minoxidil inhibition of PHD-2 was reversed by ascorbate, a cofactor of PHD-2, and the minoxidil induction of cellular HIF-1alpha was abrogated by the cofactor.	Ascorbic Acid	46-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	24-29
29295567-10	2017	Minoxidil inhibition of PHD-2 was reversed by ascorbate, a cofactor of PHD-2, and the minoxidil induction of cellular HIF-1alpha was abrogated by the cofactor.	Ascorbic Acid	46-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	71-76
29158549-9	2017	Overexpression of prolyl-hydroxylase 2 (PHD2) transgene, a predominant isoform of PHDs in renal tubules, to reduce HIF-1alpha level significantly attenuated albumin-induced increases in TIMP-1 and collagen-I levels.	Thromboxane B2	82-86	egl-9 family hypoxia inducible factor 1	Homo sapiens	40-44
28805660-6	2017	Together, these data identify Phd2 as the dominant HIF-hydroxylase in neutrophils under normoxic conditions and link intrinsic regulation of glycolysis and glycogen stores to the resolution of neutrophil-mediated inflammatory responses.	Glycogen	156-164	egl-9 family hypoxia inducible factor 1	Homo sapiens	30-34
29163216-8	2017	By contrast, a lower concentration of oxaliplatin (100 muM) did not increase the intracellular Ca2+ concentration but did confer cold sensitivity on hTRPA1-expressing cells, and this was inhibited by PHD2 co-overexpression.	Oxaliplatin	38-49	egl-9 family hypoxia inducible factor 1	Homo sapiens	200-204
28883660-9	2017	Arg starvation induces p300 dissociation, allowing histone HDAC2 and cofactor Sin3A to deacetylate these histones at the ASS1 promoter, thereby facilitating HIF-1alpha-proteasomal complex, driven by PHD2, to degrade HIF-1alpha in situ.	Arginine	0-3	egl-9 family hypoxia inducible factor 1	Homo sapiens	199-203
28883660-10	2017	Arg starvation induces PHD2 and HDAC2 interaction which is sensitive to antioxidants.	Arginine	0-3	egl-9 family hypoxia inducible factor 1	Homo sapiens	23-27
28625716-3	2017	Hypoxia inducible transcription factor prolyl hydroxylase 2 (HIF-PHD2), as the key regulator of hypoxia response, is function of hydroxylating specify proline residues of HIF-alpha, which may lead to the degradation of HIF-alpha and eventually cause disenabling the expression of erythropoietin.	Proline	151-158	egl-9 family hypoxia inducible factor 1	Homo sapiens	65-69
27297870-12	2017	Taken together, these results suggest that andrographolide suppresses hypoxia-induced pro-inflammatory ET-1 expression by activating Nrf2/HO-1, inhibiting p38 MAPK signaling, and promoting PHD2/3 expression.	andrographolide	43-58	egl-9 family hypoxia inducible factor 1	Homo sapiens	189-193
28329677-3	2017	Here, we show that, in turn, PHD2 triggers degradation of B55alpha by hydroxylating it at proline 319.	Proline	90-97	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
28329677-6	2017	Treatment of MDA-MB231-derived xenografts with the glucose competitor 2-deoxy-glucose leads to tumor regression in the presence of PHD2.	Glucose	51-58	egl-9 family hypoxia inducible factor 1	Homo sapiens	131-135
28329677-6	2017	Treatment of MDA-MB231-derived xenografts with the glucose competitor 2-deoxy-glucose leads to tumor regression in the presence of PHD2.	Deoxyglucose	70-85	egl-9 family hypoxia inducible factor 1	Homo sapiens	131-135
27297870-10	2017	Moreover, andrographolide increased the expression of prolyl hydroxylases (PHD) 2/3, which hydroxylate HIF-1alpha and promotes HIF-1alpha proteasome degradation, with an increase in HIF-1alpha hydroxylation was noted under hypoxia.	andrographolide	10-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	54-83
28051298-2	2017	These enzymes require molecular oxygen for catalytic activity and, as 2-oxoglutarate (2OG)-dependent oxygenases, are related to the cellular oxygen sensing HIF hydroxylases PHD2 and FIH.	Oxygen	32-38	egl-9 family hypoxia inducible factor 1	Homo sapiens	173-177
28051298-2	2017	These enzymes require molecular oxygen for catalytic activity and, as 2-oxoglutarate (2OG)-dependent oxygenases, are related to the cellular oxygen sensing HIF hydroxylases PHD2 and FIH.	Oxygen	101-107	egl-9 family hypoxia inducible factor 1	Homo sapiens	173-177
28038470-3	2017	Since the oxygen sensor hypoxia-inducible factor prolyl hydroxylase 2 (PHD2) is considered to be the main HIF-1alpha regulator, we hypothesized that PHD2 and EGFR may be interconnected at the molecular level.	Oxygen	10-16	egl-9 family hypoxia inducible factor 1	Homo sapiens	149-153
28199842-1	2017	Oxygen-dependent HIF1alpha hydroxylation and degradation are strictly controlled by PHD2.	Oxygen	0-6	egl-9 family hypoxia inducible factor 1	Homo sapiens	84-88
28199842-3	2017	Here, we show that PHD2 is phosphorylated on serine 125 (S125) by the mechanistic target of rapamycin (mTOR) downstream kinase P70S6K and that this phosphorylation increases its ability to degrade HIF1alpha.	Serine	45-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	19-23
28038470-3	2017	Since the oxygen sensor hypoxia-inducible factor prolyl hydroxylase 2 (PHD2) is considered to be the main HIF-1alpha regulator, we hypothesized that PHD2 and EGFR may be interconnected at the molecular level.	Oxygen	10-16	egl-9 family hypoxia inducible factor 1	Homo sapiens	24-69
28038470-6	2017	Overall, we introduce for the first time the direct crosstalk between the oxygen sensor PHD2 and EGFR-mediated tumorigenesis in breast cancer.	Oxygen	74-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	88-92
28038470-3	2017	Since the oxygen sensor hypoxia-inducible factor prolyl hydroxylase 2 (PHD2) is considered to be the main HIF-1alpha regulator, we hypothesized that PHD2 and EGFR may be interconnected at the molecular level.	Oxygen	10-16	egl-9 family hypoxia inducible factor 1	Homo sapiens	71-75
27902963-1	2017	BACKGROUND: Hypoxia-inducible factor 2 alpha (HIF2alpha), prolyl hydroxylase domain protein 2 (PHD2), and the von Hippel Lindau tumor suppressor protein (pVHL) are three principal proteins in the oxygen-sensing pathway.	Oxygen	196-202	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-93
27902963-2	2017	Under normoxic conditions, a conserved proline in HIF2alpha is hydroxylated by PHD2 in an oxygen-dependent manner, and then pVHL binds and promotes the degradation of HIF2alpha.	Proline	39-46	egl-9 family hypoxia inducible factor 1	Homo sapiens	79-83
27902963-2	2017	Under normoxic conditions, a conserved proline in HIF2alpha is hydroxylated by PHD2 in an oxygen-dependent manner, and then pVHL binds and promotes the degradation of HIF2alpha.	Oxygen	90-96	egl-9 family hypoxia inducible factor 1	Homo sapiens	79-83
28163901-4	2016	Recently, innovative experimental observations have suggested that remote ischaemic preconditioning (RIPC) may be largely mediated through hypoxic inhibition of the oxygen-sensing enzyme PHD2, leading to enhanced levels of alpha-ketoglutarate and subsequent increases in circulating kynurenic acid (KYNA).	Oxygen	165-171	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
28163901-4	2016	Recently, innovative experimental observations have suggested that remote ischaemic preconditioning (RIPC) may be largely mediated through hypoxic inhibition of the oxygen-sensing enzyme PHD2, leading to enhanced levels of alpha-ketoglutarate and subsequent increases in circulating kynurenic acid (KYNA).	Ketoglutaric Acids	223-242	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
28163901-4	2016	Recently, innovative experimental observations have suggested that remote ischaemic preconditioning (RIPC) may be largely mediated through hypoxic inhibition of the oxygen-sensing enzyme PHD2, leading to enhanced levels of alpha-ketoglutarate and subsequent increases in circulating kynurenic acid (KYNA).	Kynurenic Acid	299-303	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
28163901-4	2016	Recently, innovative experimental observations have suggested that remote ischaemic preconditioning (RIPC) may be largely mediated through hypoxic inhibition of the oxygen-sensing enzyme PHD2, leading to enhanced levels of alpha-ketoglutarate and subsequent increases in circulating kynurenic acid (KYNA).	Kynurenic Acid	283-297	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
27393459-0	2016	beta-N-oxalyl-L-alpha, beta- diaminopropionic acid induces HRE expression by inhibiting HIF-prolyl hydroxylase-2 in normoxic conditions.	beta-n-oxalyl-l-alpha, beta- diaminopropionic acid	0-50	egl-9 family hypoxia inducible factor 1	Homo sapiens	88-112
27393459-6	2016	In silico approach was used to understand the mechanism of stabilization of HIF-1alpha which revealed beta-ODAP interacts with key amino acid residues and Fe2+ at the catalytic site of PHD-2.	ammonium ferrous sulfate	155-159	egl-9 family hypoxia inducible factor 1	Homo sapiens	185-190
26951539-5	2016	Phd-2 is a group of enzymes that acts as an oxygen sensor.	Oxygen	44-50	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-5
27598034-8	2016	Alternatively, 15d-PGJ2 was found to covalently bind to HIF-1alpha prolyl-4-hydroxylase 2 (PHD2) in MCF-7 cells, which hampers the proline hydroxylation of HIF-1alpha, thereby disrupting ubiquitin-dependent proteasomal degradation of this transcription factor.	15-deoxy-delta(12,14)-prostaglandin J2	15-23	egl-9 family hypoxia inducible factor 1	Homo sapiens	91-95
27598034-8	2016	Alternatively, 15d-PGJ2 was found to covalently bind to HIF-1alpha prolyl-4-hydroxylase 2 (PHD2) in MCF-7 cells, which hampers the proline hydroxylation of HIF-1alpha, thereby disrupting ubiquitin-dependent proteasomal degradation of this transcription factor.	Proline	131-138	egl-9 family hypoxia inducible factor 1	Homo sapiens	91-95
27598034-10	2016	Molecular docking analysis suggests that 15d-PGJ2 preferentially binds to PHD2 in the vicinity of the Cys201 residue based on binding energies and carbon-sulfur distances.	15-deoxy-delta(12,14)-prostaglandin J2	41-49	egl-9 family hypoxia inducible factor 1	Homo sapiens	74-78
27598034-10	2016	Molecular docking analysis suggests that 15d-PGJ2 preferentially binds to PHD2 in the vicinity of the Cys201 residue based on binding energies and carbon-sulfur distances.	Carbon	147-153	egl-9 family hypoxia inducible factor 1	Homo sapiens	74-78
27598034-10	2016	Molecular docking analysis suggests that 15d-PGJ2 preferentially binds to PHD2 in the vicinity of the Cys201 residue based on binding energies and carbon-sulfur distances.	Sulfur	154-160	egl-9 family hypoxia inducible factor 1	Homo sapiens	74-78
27325674-1	2016	Prolyl hydroxylase domain protein 2 (PHD2) (also known as EGLN1) is a key oxygen sensor in mammals that posttranslationally modifies hypoxia-inducible factor alpha (HIF-alpha) and targets it for degradation.	Oxygen	74-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
27325674-1	2016	Prolyl hydroxylase domain protein 2 (PHD2) (also known as EGLN1) is a key oxygen sensor in mammals that posttranslationally modifies hypoxia-inducible factor alpha (HIF-alpha) and targets it for degradation.	Oxygen	74-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
27325674-1	2016	Prolyl hydroxylase domain protein 2 (PHD2) (also known as EGLN1) is a key oxygen sensor in mammals that posttranslationally modifies hypoxia-inducible factor alpha (HIF-alpha) and targets it for degradation.	Oxygen	74-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-63
27563096-4	2016	We found that Akt was prolyl-hydroxylated by the oxygen-dependent hydroxylase EglN1.	Oxygen	49-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	78-83
26676934-0	2016	Tetramethylpyrazine protects CoCl2-induced apoptosis in human umbilical vein endothelial cells by regulating the PHD2/HIF/1alpha-VEGF pathway.	tetramethylpyrazine	0-19	egl-9 family hypoxia inducible factor 1	Homo sapiens	113-117
26972007-0	2016	The Oxygen Sensor PHD2 Controls Dendritic Spines and Synapses via Modification of Filamin A.	Oxygen	4-10	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-22
26972007-4	2016	In normoxia, PHD2 hydroxylates the proline residues P2309 and P2316 in FLNA, leading to von Hippel-Lindau (VHL)-mediated ubiquitination and proteasomal degradation.	Proline	35-42	egl-9 family hypoxia inducible factor 1	Homo sapiens	13-17
27019453-11	2016	We also observe a significant enr ichment of the highly connected hub genes which could explain differences in prakriti, focussing on EGLN1, a key oxygen sensor that differs between prakriti types and is linked to high altitude adaptation.	Oxygen	147-153	egl-9 family hypoxia inducible factor 1	Homo sapiens	134-139
27368101-0	2016	Paracrine Induction of HIF by Glutamate in Breast Cancer: EglN1 Senses Cysteine.	Glutamic Acid	30-39	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-63
27368101-0	2016	Paracrine Induction of HIF by Glutamate in Breast Cancer: EglN1 Senses Cysteine.	Cysteine	71-79	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-63
27368101-6	2016	Therefore, EglN1 senses both oxygen and cysteine.	Oxygen	29-35	egl-9 family hypoxia inducible factor 1	Homo sapiens	11-16
27368101-6	2016	Therefore, EglN1 senses both oxygen and cysteine.	Cysteine	40-48	egl-9 family hypoxia inducible factor 1	Homo sapiens	11-16
26765925-3	2016	TSA-mediated HIF-1alpha degradation was rescued by concomitant inhibition of not only the 26S proteasome but also PHD2 function.	trichostatin A	0-3	egl-9 family hypoxia inducible factor 1	Homo sapiens	114-118
26082309-0	2016	Impairment of hypoxia-induced HIF-1alpha signaling in keratinocytes and fibroblasts by sulfur mustard is counteracted by a selective PHD-2 inhibitor.	Mustard Gas	87-101	egl-9 family hypoxia inducible factor 1	Homo sapiens	133-138
26082309-6	2016	Addition of a selective inhibitor of the oxygen-sensitive prolyl hydroxylase domain-containing protein 2 (PHD-2), IOX2, fully recovered HIF-1alpha stability, nuclear translocation, and target gene expression in NHEK and NHDF.	Oxygen	41-47	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-104
26082309-6	2016	Addition of a selective inhibitor of the oxygen-sensitive prolyl hydroxylase domain-containing protein 2 (PHD-2), IOX2, fully recovered HIF-1alpha stability, nuclear translocation, and target gene expression in NHEK and NHDF.	Oxygen	41-47	egl-9 family hypoxia inducible factor 1	Homo sapiens	106-111
26863487-7	2016	Pharmacological inhibition of PHD2 recapitulated the adaptations in glutamine and glycogen metabolism and, consequently, the beneficial effects on cell survival.	Glutamine	68-77	egl-9 family hypoxia inducible factor 1	Homo sapiens	30-34
26863487-7	2016	Pharmacological inhibition of PHD2 recapitulated the adaptations in glutamine and glycogen metabolism and, consequently, the beneficial effects on cell survival.	Glycogen	82-90	egl-9 family hypoxia inducible factor 1	Homo sapiens	30-34
26676934-0	2016	Tetramethylpyrazine protects CoCl2-induced apoptosis in human umbilical vein endothelial cells by regulating the PHD2/HIF/1alpha-VEGF pathway.	cobaltous chloride	29-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	113-117
26676934-4	2016	Following pre-incubation with CoCl2 (150 microM/ml) for 4 h, the HUVECs were treated with TMP at different concentrations (50, 100 and 200 microM/ml) for 8 h. TMP upregulated the expression of prolyl hydroxylase (PHD)2, reduced the protein and mRNA expression levels of vascular endothelial growth factor (VEGF), and reduced the expression of HIF-1alpha only at the protein level, not at the mRNA level in HUVECs, in a concentration-dependent manner.	tetramethylpyrazine	159-162	egl-9 family hypoxia inducible factor 1	Homo sapiens	193-218
26676934-5	2016	Furthermore, silencing of the PHD2 gene with small interfering (si)RNAs abolished the reduction in the expression of hypoxia-inducible factor (HIF)-1alpha and VEGF by TMP.	tetramethylpyrazine	167-170	egl-9 family hypoxia inducible factor 1	Homo sapiens	30-34
26676934-8	2016	The present study demonstrated that the antiapoptotic effect of TMP in CoCl2-induced HUVECs was, at least in part, via the regulation of the PHD2/HIF-1alpha signaling pathway.	tetramethylpyrazine	64-67	egl-9 family hypoxia inducible factor 1	Homo sapiens	141-145
26676934-8	2016	The present study demonstrated that the antiapoptotic effect of TMP in CoCl2-induced HUVECs was, at least in part, via the regulation of the PHD2/HIF-1alpha signaling pathway.	cobaltous chloride	71-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	141-145
26610437-3	2015	In this review, we first describe the structure of PHD2 as a molecular basis for structure-based drug design (SBDD) and various experimental methods developed for measuring PHD activity.	sbdd	110-114	egl-9 family hypoxia inducible factor 1	Homo sapiens	51-55
26754054-1	2016	Idiopathic erythrocytosis is a rare disease characterized by an increase in red blood cell mass due to mutations in proteins of the oxygen-sensing pathway, such as prolyl hydroxylase 2 (PHD2).	Oxygen	132-138	egl-9 family hypoxia inducible factor 1	Homo sapiens	164-184
26754054-1	2016	Idiopathic erythrocytosis is a rare disease characterized by an increase in red blood cell mass due to mutations in proteins of the oxygen-sensing pathway, such as prolyl hydroxylase 2 (PHD2).	Oxygen	132-138	egl-9 family hypoxia inducible factor 1	Homo sapiens	186-190
26740011-7	2016	Moreover, oncogenic H-ras(V12) does not trigger aerobic glycolysis in antioxidant-treated or PHD2 knocked-down cells, suggesting the participation of the ROS-mediated PHD2 inactivation in the oncogenic H-ras(V12)-mediated metabolic reprogramming.	ros	154-157	egl-9 family hypoxia inducible factor 1	Homo sapiens	167-171
26740011-8	2016	We provide here a better understanding of the mechanism by which disulfide bond-mediated PHD2 dimerization and inactivation result in the activation of HIF-1alpha and aerobic glycolysis in response to oxidative stress.	Disulfides	65-74	egl-9 family hypoxia inducible factor 1	Homo sapiens	89-93
26818499-0	2016	Regulation of ATP13A2 via PHD2-HIF1alpha Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson"s Disease.	Iron	76-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	26-30
26818499-8	2016	These data suggest that regulation of ATP13A2 by the PHD2-HIF1alpha signaling pathway affects cellular iron homeostasis and DAergic neuronal survival.	Iron	103-107	egl-9 family hypoxia inducible factor 1	Homo sapiens	53-57
26740011-1	2016	Prolyl hydroxylase domain protein 2 (PHD2) belongs to an evolutionarily conserved superfamily of 2-oxoglutarate and Fe(II)-dependent dioxygenases that mediates homeostatic responses to oxygen deprivation by mediating hypoxia-inducible factor-1alpha (HIF-1alpha) hydroxylation and degradation.	Ketoglutaric Acids	97-111	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
26740011-1	2016	Prolyl hydroxylase domain protein 2 (PHD2) belongs to an evolutionarily conserved superfamily of 2-oxoglutarate and Fe(II)-dependent dioxygenases that mediates homeostatic responses to oxygen deprivation by mediating hypoxia-inducible factor-1alpha (HIF-1alpha) hydroxylation and degradation.	Ketoglutaric Acids	97-111	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
26740011-1	2016	Prolyl hydroxylase domain protein 2 (PHD2) belongs to an evolutionarily conserved superfamily of 2-oxoglutarate and Fe(II)-dependent dioxygenases that mediates homeostatic responses to oxygen deprivation by mediating hypoxia-inducible factor-1alpha (HIF-1alpha) hydroxylation and degradation.	Oxygen	135-141	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
26740011-1	2016	Prolyl hydroxylase domain protein 2 (PHD2) belongs to an evolutionarily conserved superfamily of 2-oxoglutarate and Fe(II)-dependent dioxygenases that mediates homeostatic responses to oxygen deprivation by mediating hypoxia-inducible factor-1alpha (HIF-1alpha) hydroxylation and degradation.	Oxygen	135-141	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
26740011-3	2016	Here, we identified disulfide bond-mediated PHD2 homo-dimer formation in response to oxidative stress caused by oxidizing agents and oncogenic H-ras(V12) signalling.	Disulfides	20-29	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-48
26740011-5	2016	Furthermore, we demonstrated that disulfide bond-mediated PHD2 dimerization is associated with the stabilization and activation of HIF-1alpha under oxidative stress.	Disulfides	34-43	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-62
26498856-0	2015	The PHD2 oxygen sensor paves the way to metastasis.	Oxygen	9-15	egl-9 family hypoxia inducible factor 1	Homo sapiens	4-8
26713111-1	2015	Prolyl hydroxylase domain 2 (PHD2) enzyme, a Fe(II) and 2-oxoglutarate (2-OG) dependent oxygenase, mediates key physiological responses to hypoxia by modulating the levels of hypoxia inducible factor 1-alpha (HIF1alpha).	ammonium ferrous sulfate	45-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-27
26713111-1	2015	Prolyl hydroxylase domain 2 (PHD2) enzyme, a Fe(II) and 2-oxoglutarate (2-OG) dependent oxygenase, mediates key physiological responses to hypoxia by modulating the levels of hypoxia inducible factor 1-alpha (HIF1alpha).	ammonium ferrous sulfate	45-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
26713111-1	2015	Prolyl hydroxylase domain 2 (PHD2) enzyme, a Fe(II) and 2-oxoglutarate (2-OG) dependent oxygenase, mediates key physiological responses to hypoxia by modulating the levels of hypoxia inducible factor 1-alpha (HIF1alpha).	Ketoglutaric Acids	56-70	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-27
26713111-1	2015	Prolyl hydroxylase domain 2 (PHD2) enzyme, a Fe(II) and 2-oxoglutarate (2-OG) dependent oxygenase, mediates key physiological responses to hypoxia by modulating the levels of hypoxia inducible factor 1-alpha (HIF1alpha).	Ketoglutaric Acids	56-70	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
26713111-4	2015	Here we report an affinity-based fluorescence polarization method using FITC-labeled HIF1alpha (556-574) peptide as a probe for quantitative and site-specific screening of small molecule PHD2 inhibitors.	Fluorescein-5-isothiocyanate	72-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
26112411-5	2015	PHD2, the most important human PHD isoform, is proposed to be biochemically/kinetically suited as a hypoxia sensor due to its relatively high sensitivity to changes in O2 concentration and slow reaction with O2.	Oxygen	168-170	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
26324945-4	2015	Consistent with this hypothesis, blood lactate levels measured after a treadmill or lactate tolerance test were significantly lower in Phd2-liver-specific knockout (Phd2-LKO) mice than in control mice.	Lactic Acid	39-46	egl-9 family hypoxia inducible factor 1	Homo sapiens	165-169
26324945-4	2015	Consistent with this hypothesis, blood lactate levels measured after a treadmill or lactate tolerance test were significantly lower in Phd2-liver-specific knockout (Phd2-LKO) mice than in control mice.	Lactic Acid	84-91	egl-9 family hypoxia inducible factor 1	Homo sapiens	165-169
26235614-0	2015	The Cancer Cell Oxygen Sensor PHD2 Promotes Metastasis via Activation of Cancer-Associated Fibroblasts.	Oxygen	16-22	egl-9 family hypoxia inducible factor 1	Homo sapiens	30-34
26235614-1	2015	Several questions about the role of the oxygen sensor prolyl-hydroxylase 2 (PHD2) in cancer have not been addressed.	Oxygen	40-46	egl-9 family hypoxia inducible factor 1	Homo sapiens	54-74
26235614-1	2015	Several questions about the role of the oxygen sensor prolyl-hydroxylase 2 (PHD2) in cancer have not been addressed.	Oxygen	40-46	egl-9 family hypoxia inducible factor 1	Homo sapiens	76-80
26112411-5	2015	PHD2, the most important human PHD isoform, is proposed to be biochemically/kinetically suited as a hypoxia sensor due to its relatively high sensitivity to changes in O2 concentration and slow reaction with O2.	Oxygen	208-210	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
26112411-6	2015	To ascertain whether these parameters are conserved among the HIF hydroxylases, we compared the reactions of FIH and PHD2 with O2.	Oxygen	127-129	egl-9 family hypoxia inducible factor 1	Homo sapiens	117-121
25936780-3	2015	Oxygen negatively regulates NDRG3 expression at the protein level via the PHD2/VHL system, whereas lactate, produced in excess under prolonged hypoxia, blocks its proteasomal degradation by binding to NDRG3.	Oxygen	0-6	egl-9 family hypoxia inducible factor 1	Homo sapiens	74-78
26051901-1	2015	We report herein that Zn(II) selectively inhibits the hypoxia-inducible factor prolyl hydroxylase PHD3 over PHD2, and does not compete with Fe(II).	Zinc	22-28	egl-9 family hypoxia inducible factor 1	Homo sapiens	108-112
25797536-4	2015	Esculetin directly inhibited HIF prolyl hydroxylase-2 (HPH-2), an enzyme playing a major role in negatively regulating HIF-1alpha protein stability.	esculetin	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-53
25797536-4	2015	Esculetin directly inhibited HIF prolyl hydroxylase-2 (HPH-2), an enzyme playing a major role in negatively regulating HIF-1alpha protein stability.	esculetin	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	55-60
25809665-5	2015	In the presence of O2, the alpha subunits are hydroxylated by specific prolyl-4-hydroxylase domain proteins (PHD1, PHD2, and PHD3) and an asparaginyl hydroxylase (factor inhibiting HIF-1, FIH-1).	Oxygen	19-21	egl-9 family hypoxia inducible factor 1	Homo sapiens	115-119
25732824-6	2015	Downregulation of IDH3alpha decreases the effective level of alpha-ketoglutarate (alpha-KG) by reducing the ratio of alpha-KG to fumarate and succinate, resulting in PHD2 inhibition and HIF-1alpha protein stabilization.	Ketoglutaric Acids	61-80	egl-9 family hypoxia inducible factor 1	Homo sapiens	166-170
25857330-0	2015	Increased Turnover at Limiting O2 Concentrations by the Thr(387)   Ala Variant of HIF-Prolyl Hydroxylase PHD2.	Oxygen	31-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	105-109
25857330-0	2015	Increased Turnover at Limiting O2 Concentrations by the Thr(387)   Ala Variant of HIF-Prolyl Hydroxylase PHD2.	Threonine	56-59	egl-9 family hypoxia inducible factor 1	Homo sapiens	105-109
25857330-0	2015	Increased Turnover at Limiting O2 Concentrations by the Thr(387)   Ala Variant of HIF-Prolyl Hydroxylase PHD2.	Alanine	67-70	egl-9 family hypoxia inducible factor 1	Homo sapiens	105-109
25857330-1	2015	PHD2 is a 2-oxoglutarate, non-heme Fe(2+)-dependent oxygenase that senses O2 levels in human cells by hydroxylating two prolyl residues in the oxygen-dependent degradation domain (ODD) of HIF1alpha.	Ketoglutaric Acids	10-24	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25857330-1	2015	PHD2 is a 2-oxoglutarate, non-heme Fe(2+)-dependent oxygenase that senses O2 levels in human cells by hydroxylating two prolyl residues in the oxygen-dependent degradation domain (ODD) of HIF1alpha.	Oxygen	74-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25857330-1	2015	PHD2 is a 2-oxoglutarate, non-heme Fe(2+)-dependent oxygenase that senses O2 levels in human cells by hydroxylating two prolyl residues in the oxygen-dependent degradation domain (ODD) of HIF1alpha.	Peptide oostatic hormone	120-126	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25857330-1	2015	PHD2 is a 2-oxoglutarate, non-heme Fe(2+)-dependent oxygenase that senses O2 levels in human cells by hydroxylating two prolyl residues in the oxygen-dependent degradation domain (ODD) of HIF1alpha.	Oxygen	52-58	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25857330-4	2015	Here we tested the impact of the side chain of Thr(387) on the reactivity of PHD2 toward O2 through a combination of point mutagenesis, steady state kinetic experiments and {FeNO}(7) EPR spectroscopy.	Threonine	47-50	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-81
25857330-4	2015	Here we tested the impact of the side chain of Thr(387) on the reactivity of PHD2 toward O2 through a combination of point mutagenesis, steady state kinetic experiments and {FeNO}(7) EPR spectroscopy.	Oxygen	89-91	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-81
25857330-6	2015	X-Band electron paramagnetic resonance spectroscopy of the {FeNO}(7) centers of the (Fe+NO+2OG) enzyme forms showed the presence of a more rhombic line shape in Thr(387)   Ala than in WT PHD2, indicating an altered conformation for bound gas in this variant.	Iron	60-62	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
25857330-6	2015	X-Band electron paramagnetic resonance spectroscopy of the {FeNO}(7) centers of the (Fe+NO+2OG) enzyme forms showed the presence of a more rhombic line shape in Thr(387)   Ala than in WT PHD2, indicating an altered conformation for bound gas in this variant.	Threonine	161-164	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
25857330-6	2015	X-Band electron paramagnetic resonance spectroscopy of the {FeNO}(7) centers of the (Fe+NO+2OG) enzyme forms showed the presence of a more rhombic line shape in Thr(387)   Ala than in WT PHD2, indicating an altered conformation for bound gas in this variant.	Alanine	172-175	egl-9 family hypoxia inducible factor 1	Homo sapiens	187-191
25857330-7	2015	Here we show that the side chain of residue Thr(387) plays a significant role in determining the rate of turnover by PHD2 at low O2 concentrations.	Threonine	44-47	egl-9 family hypoxia inducible factor 1	Homo sapiens	117-121
25857330-7	2015	Here we show that the side chain of residue Thr(387) plays a significant role in determining the rate of turnover by PHD2 at low O2 concentrations.	Oxygen	129-131	egl-9 family hypoxia inducible factor 1	Homo sapiens	117-121
25732824-6	2015	Downregulation of IDH3alpha decreases the effective level of alpha-ketoglutarate (alpha-KG) by reducing the ratio of alpha-KG to fumarate and succinate, resulting in PHD2 inhibition and HIF-1alpha protein stabilization.	Ketoglutaric Acids	82-90	egl-9 family hypoxia inducible factor 1	Homo sapiens	166-170
25773848-5	2015	Moreover, chloroquine stabilized the protein level of prolyl hydroxylase domain proteins (PHD-2) but reduced the levels of hypoxic responsive proteins such as hypoxia-inducible factor (HIF-1alpha) and vascular endothelial growth factor (VEGF).	Chloroquine	10-21	egl-9 family hypoxia inducible factor 1	Homo sapiens	90-95
25483211-2	2015	Rosmarinic acid (RA), an ester of caffeic acid and 3,4-dihydroxyphenyllactic acid is a naturally occurring polyphenolic compound with two catechols, a or inhibition of HPH.	rosmarinic acid	0-15	egl-9 family hypoxia inducible factor 1	Homo sapiens	168-171
25483211-2	2015	Rosmarinic acid (RA), an ester of caffeic acid and 3,4-dihydroxyphenyllactic acid is a naturally occurring polyphenolic compound with two catechols, a or inhibition of HPH.	rosmarinic acid	17-19	egl-9 family hypoxia inducible factor 1	Homo sapiens	168-171
25483211-2	2015	Rosmarinic acid (RA), an ester of caffeic acid and 3,4-dihydroxyphenyllactic acid is a naturally occurring polyphenolic compound with two catechols, a or inhibition of HPH.	3,4-dihydroxyphenyllactic acid	51-81	egl-9 family hypoxia inducible factor 1	Homo sapiens	168-171
25483211-3	2015	To improve accessibility of highly hydrophilic RA to HPH, an intracellular target, RA was chemically modified to decrease hydrophilicity.	rosmarinic acid	47-49	egl-9 family hypoxia inducible factor 1	Homo sapiens	53-56
25483211-3	2015	To improve accessibility of highly hydrophilic RA to HPH, an intracellular target, RA was chemically modified to decrease hydrophilicity.	rosmarinic acid	83-85	egl-9 family hypoxia inducible factor 1	Homo sapiens	53-56
25483211-4	2015	Of the less-hydrophilic derivatives, rosmarinic acid methyl ester (RAME) most potently inhibited HPH.	Rosmarinic Acid Methyl Ester	37-65	egl-9 family hypoxia inducible factor 1	Homo sapiens	97-100
25483211-4	2015	Of the less-hydrophilic derivatives, rosmarinic acid methyl ester (RAME) most potently inhibited HPH.	Copper	67-71	egl-9 family hypoxia inducible factor 1	Homo sapiens	97-100
25483211-6	2015	RAME inhibition of HPH and induction of HIF-1alpha were diminished by elevated doses of the required factors of HPH, 2-ketoglutarate and ascorbate.	Ketoglutaric Acids	117-132	egl-9 family hypoxia inducible factor 1	Homo sapiens	19-22
25483211-6	2015	RAME inhibition of HPH and induction of HIF-1alpha were diminished by elevated doses of the required factors of HPH, 2-ketoglutarate and ascorbate.	Ascorbic Acid	137-146	egl-9 family hypoxia inducible factor 1	Homo sapiens	19-22
25483211-10	2015	Thus, lipophilic modification of RA improves its ability to inhibit HPH, leading to activation of the HIF-1-VEGF pathway.	rosmarinic acid	33-35	egl-9 family hypoxia inducible factor 1	Homo sapiens	68-71
26624507-4	2015	The best-known function of PHD2 is to mediate the oxygen-dependent degradation of the labile alpha-subunit of hypoxia-inducible factor (HIF).	Oxygen	50-56	egl-9 family hypoxia inducible factor 1	Homo sapiens	27-31
25431923-0	2014	Variants of the low oxygen sensors EGLN1 and HIF-1AN associated with acute mountain sickness.	Oxygen	20-26	egl-9 family hypoxia inducible factor 1	Homo sapiens	35-40
25431923-1	2014	Two low oxygen sensors, Egl nine homolog 1 (EGLN1) and hypoxia-inducible factor 1-alpha inhibitor (HIF-1AN), play pivotal roles in the regulation of HIF-1alpha, and high altitude adaption may be involved in the pathology of acute mountain sickness (AMS).	Oxygen	8-14	egl-9 family hypoxia inducible factor 1	Homo sapiens	24-42
25431923-1	2014	Two low oxygen sensors, Egl nine homolog 1 (EGLN1) and hypoxia-inducible factor 1-alpha inhibitor (HIF-1AN), play pivotal roles in the regulation of HIF-1alpha, and high altitude adaption may be involved in the pathology of acute mountain sickness (AMS).	Oxygen	8-14	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-49
25429216-5	2014	Herein, we developed a novel PHD2 silencing system based on arginine-terminated generation 4 poly(amidoamine) (Arg-G4) nanoparticles.	Arginine	60-68	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
25420025-0	2014	Intermediary metabolite precursor dimethyl-2-ketoglutarate stabilizes hypoxia-inducible factor-1alpha by inhibiting prolyl-4-hydroxylase PHD2.	dimethyl-2-ketoglutarate	34-58	egl-9 family hypoxia inducible factor 1	Homo sapiens	137-141
25420025-4	2014	Here, we show that dimethyl-2-ketoglutarate (DKG), a cell membrane-permeable precursor of a key metabolic intermediate, alpha-ketoglutarate (alpha-KG), known for its ability to rescue glutamine deficiency, transiently stabilized HIF-1alpha by inhibiting activity of the HIF prolyl hydroxylase domain-containing protein, PHD2.	dimethyl-2-ketoglutarate	19-43	egl-9 family hypoxia inducible factor 1	Homo sapiens	320-324
25420025-4	2014	Here, we show that dimethyl-2-ketoglutarate (DKG), a cell membrane-permeable precursor of a key metabolic intermediate, alpha-ketoglutarate (alpha-KG), known for its ability to rescue glutamine deficiency, transiently stabilized HIF-1alpha by inhibiting activity of the HIF prolyl hydroxylase domain-containing protein, PHD2.	Ketoglutaric Acids	120-139	egl-9 family hypoxia inducible factor 1	Homo sapiens	320-324
25429216-5	2014	Herein, we developed a novel PHD2 silencing system based on arginine-terminated generation 4 poly(amidoamine) (Arg-G4) nanoparticles.	Poly(amidoamine)	93-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
25429216-5	2014	Herein, we developed a novel PHD2 silencing system based on arginine-terminated generation 4 poly(amidoamine) (Arg-G4) nanoparticles.	Arginine	111-114	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
25429216-5	2014	Herein, we developed a novel PHD2 silencing system based on arginine-terminated generation 4 poly(amidoamine) (Arg-G4) nanoparticles.	g4	115-117	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
25429216-9	2014	This work demonstrated that an Arg-G4 nanovector-based PHD2 silencing system could enhance the efficiency of MSC transplantation for infarcted myocardium repair.	Arginine	31-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	55-59
24201705-4	2014	Two of these loci, EGLN1 and EPAS1, encode major components of the hypoxia-inducible factor transcriptional system, which has a central role in oxygen sensing and coordinating an organism"s response to hypoxia, as evidenced by studies in humans and mice.	Oxygen	144-150	egl-9 family hypoxia inducible factor 1	Homo sapiens	19-24
25120187-3	2014	Transient kinetic studies have shown that purified PHD2 reacts slowly with O2 compared with some other studied 2OG oxygenases, a property which may be related to its hypoxia-sensing role.	Oxygen	75-77	egl-9 family hypoxia inducible factor 1	Homo sapiens	51-55
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	ammonium ferrous sulfate	33-39	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	ammonium ferrous sulfate	33-39	egl-9 family hypoxia inducible factor 1	Homo sapiens	226-230
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	ammonium ferrous sulfate	104-110	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	ammonium ferrous sulfate	104-110	egl-9 family hypoxia inducible factor 1	Homo sapiens	226-230
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	Water	124-129	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	Water	124-129	egl-9 family hypoxia inducible factor 1	Homo sapiens	226-230
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	Oxygen	171-173	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
25120187-4	2014	PHD2 forms a stable complex with Fe(II) and 2OG; crystallographic and kinetic analyses indicate that an Fe(II)-co-ordinated water molecule, which must be displaced before O2 binding, is relatively stable in the active site of PHD2.	Oxygen	171-173	egl-9 family hypoxia inducible factor 1	Homo sapiens	226-230
25120187-5	2014	We used active site substitutions to investigate whether these properties are related to the slow reaction of PHD2 with O2.	Oxygen	120-122	egl-9 family hypoxia inducible factor 1	Homo sapiens	110-114
25129147-5	2014	The PHD2 p.[Asp4Glu; Cys127Ser] variant exhibits a lower K(m) value for oxygen, suggesting that it promotes increased HIF degradation under hypoxic conditions.	Oxygen	72-78	egl-9 family hypoxia inducible factor 1	Homo sapiens	4-8
27774468-11	2014	Some are close to the hypoxia-inducible transcription factor alpha/2-oxoglutarate or the iron binding sites for PHD2.	Ketoglutaric Acids	67-81	egl-9 family hypoxia inducible factor 1	Homo sapiens	112-116
27774468-11	2014	Some are close to the hypoxia-inducible transcription factor alpha/2-oxoglutarate or the iron binding sites for PHD2.	Iron	89-93	egl-9 family hypoxia inducible factor 1	Homo sapiens	112-116
24711448-0	2014	Defective Tibetan PHD2 binding to p23 links high altitude adaption to altered oxygen sensing.	Oxygen	78-84	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-22
24711448-2	2014	Tibetans bear a genetic signature in the prolyl hydroxylase domain protein 2 (PHD2/EGLN1) gene, which encodes for the central oxygen sensor of the hypoxia-inducible factor (HIF) pathway.	Oxygen	126-132	egl-9 family hypoxia inducible factor 1	Homo sapiens	78-82
24711448-2	2014	Tibetans bear a genetic signature in the prolyl hydroxylase domain protein 2 (PHD2/EGLN1) gene, which encodes for the central oxygen sensor of the hypoxia-inducible factor (HIF) pathway.	Oxygen	126-132	egl-9 family hypoxia inducible factor 1	Homo sapiens	83-88
24711448-4	2014	These amino acids reside in a region of PHD2 that harbors a zinc finger, which we have previously discovered binds to a Pro-Xaa-Leu-Glu (PXLE) motif in the HSP90 cochaperone p23, thereby recruiting PHD2 to the HSP90 pathway to facilitate HIF-alpha hydroxylation.	pro-xaa-leu-glu	120-135	egl-9 family hypoxia inducible factor 1	Homo sapiens	40-44
24711448-4	2014	These amino acids reside in a region of PHD2 that harbors a zinc finger, which we have previously discovered binds to a Pro-Xaa-Leu-Glu (PXLE) motif in the HSP90 cochaperone p23, thereby recruiting PHD2 to the HSP90 pathway to facilitate HIF-alpha hydroxylation.	pro-xaa-leu-glu	120-135	egl-9 family hypoxia inducible factor 1	Homo sapiens	198-202
24581673-6	2014	Moreover, PHD2 inhibitors may increase the endogenous circulating iron availability via suppression of hepcidin, a master regulator of iron homeostasis which further reduces the need for exogenous intravenous iron administration for effective erythropoiesis in renal anemia patients.	Iron	66-70	egl-9 family hypoxia inducible factor 1	Homo sapiens	10-14
24581673-6	2014	Moreover, PHD2 inhibitors may increase the endogenous circulating iron availability via suppression of hepcidin, a master regulator of iron homeostasis which further reduces the need for exogenous intravenous iron administration for effective erythropoiesis in renal anemia patients.	Iron	135-139	egl-9 family hypoxia inducible factor 1	Homo sapiens	10-14
24581673-6	2014	Moreover, PHD2 inhibitors may increase the endogenous circulating iron availability via suppression of hepcidin, a master regulator of iron homeostasis which further reduces the need for exogenous intravenous iron administration for effective erythropoiesis in renal anemia patients.	Iron	135-139	egl-9 family hypoxia inducible factor 1	Homo sapiens	10-14
25010988-4	2014	Prolyl-4-hydroxylase 2 (PHD2) is known as an important mediator of the oxygen-dependent degradation of HIF-alpha subunits.	Oxygen	71-77	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-22
25010988-4	2014	Prolyl-4-hydroxylase 2 (PHD2) is known as an important mediator of the oxygen-dependent degradation of HIF-alpha subunits.	Oxygen	71-77	egl-9 family hypoxia inducible factor 1	Homo sapiens	24-28
24468676-4	2014	In contrast, chronic hypoxia evokes cellular responses that lead to transcriptional changes mediated by the hypoxia inducible factor (HIF), which is directly controlled by post-translational hydroxylation of HIF by the non-heme Fe(II)/alphaKG-dependent enzymes FIH and PHD2.	Heme	223-227	egl-9 family hypoxia inducible factor 1	Homo sapiens	269-273
24468676-4	2014	In contrast, chronic hypoxia evokes cellular responses that lead to transcriptional changes mediated by the hypoxia inducible factor (HIF), which is directly controlled by post-translational hydroxylation of HIF by the non-heme Fe(II)/alphaKG-dependent enzymes FIH and PHD2.	ammonium ferrous sulfate	228-234	egl-9 family hypoxia inducible factor 1	Homo sapiens	269-273
24468676-5	2014	Research on PHD2 and FIH is focused on developing inhibitors and understanding the links between HIF binding and the O2 reaction in these enzymes.	Oxygen	117-119	egl-9 family hypoxia inducible factor 1	Homo sapiens	12-16
23378141-7	2014	Specifically, EtOH treatment let to a reduction in ALDOC, ENO2 and CDH1 expression, whereas EtOH treatment induced the expression of PTCH1, EGLN1, VEGFA and DEC2 in treated EBs.	Ethanol	92-96	egl-9 family hypoxia inducible factor 1	Homo sapiens	140-145
23542169-7	2014	In addition, RUNX3 directly interacted with the C-terminal activation domain of HIF-1alpha and prolyl hydroxylase (PHD) 2 and enhanced the interaction between HIF-1alpha and PHD2, which potentiated proline hydroxylation and promoted the degradation of HIF-1alpha.	Proline	198-205	egl-9 family hypoxia inducible factor 1	Homo sapiens	174-178
23542169-9	2014	Taken together, these results suggest that RUNX3 destabilizes HIF-1alpha protein by promoting the proline hydroxylation of HIF-1alpha through binding to HIF-1alpha/PHD2.	Proline	98-105	egl-9 family hypoxia inducible factor 1	Homo sapiens	164-168
24761603-2	2014	PHD2 plays a critical role in cells and tissues adaptation to the low oxygen environment.	Oxygen	70-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
24761603-4	2014	Subsequently, PHD2 acts as an important factor in oxygen homeostasis.	Oxygen	50-56	egl-9 family hypoxia inducible factor 1	Homo sapiens	14-18
23836663-3	2013	HIF-1alpha stabilization is mediated by VACV protein C16 that binds the human oxygen sensing enzyme prolyl-hydroxylase domain containing protein (PHD)2 and thereby inhibits PHD2-dependent hydroxylation of HIF-1alpha.	Oxygen	78-84	egl-9 family hypoxia inducible factor 1	Homo sapiens	146-151
24010824-0	2014	DMOG ameliorates IFN-gamma-induced intestinal barrier dysfunction by suppressing PHD2-dependent HIF-1alpha degradation.	dimethyloxallyl glycine	0-4	egl-9 family hypoxia inducible factor 1	Homo sapiens	81-85
23787140-1	2013	HIF prolyl-4-hydroxylase 2 (PHD2) is a non-heme Fe, 2-oxoglutarate (2OG) dependent dioxygenase that regulates the hypoxia inducible transcription factor (HIF) by hydroxylating two conserved prolyl residues in N-terminal oxygen degradation domain (NODD) and C-terminal oxygen degradation domain (CODD) of HIF-1alpha.	Heme	43-47	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
23787140-1	2013	HIF prolyl-4-hydroxylase 2 (PHD2) is a non-heme Fe, 2-oxoglutarate (2OG) dependent dioxygenase that regulates the hypoxia inducible transcription factor (HIF) by hydroxylating two conserved prolyl residues in N-terminal oxygen degradation domain (NODD) and C-terminal oxygen degradation domain (CODD) of HIF-1alpha.	Iron	48-50	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
23787140-1	2013	HIF prolyl-4-hydroxylase 2 (PHD2) is a non-heme Fe, 2-oxoglutarate (2OG) dependent dioxygenase that regulates the hypoxia inducible transcription factor (HIF) by hydroxylating two conserved prolyl residues in N-terminal oxygen degradation domain (NODD) and C-terminal oxygen degradation domain (CODD) of HIF-1alpha.	Ketoglutaric Acids	52-66	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
23787140-1	2013	HIF prolyl-4-hydroxylase 2 (PHD2) is a non-heme Fe, 2-oxoglutarate (2OG) dependent dioxygenase that regulates the hypoxia inducible transcription factor (HIF) by hydroxylating two conserved prolyl residues in N-terminal oxygen degradation domain (NODD) and C-terminal oxygen degradation domain (CODD) of HIF-1alpha.	Peptide oostatic hormone	4-10	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
23787140-1	2013	HIF prolyl-4-hydroxylase 2 (PHD2) is a non-heme Fe, 2-oxoglutarate (2OG) dependent dioxygenase that regulates the hypoxia inducible transcription factor (HIF) by hydroxylating two conserved prolyl residues in N-terminal oxygen degradation domain (NODD) and C-terminal oxygen degradation domain (CODD) of HIF-1alpha.	Oxygen	85-91	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
24042008-2	2013	Using a lead generation process, a series of [(4-Hydroxyl-benzo[4,5]thieno[3,2-c]pyridine-3-carbonyl)-amino]-acetic acid derivatives was developed as potent PHD2 inhibitors.	[(4-hydroxyl-benzo[4,5]thieno[3,2-c]pyridine-3-carbonyl)-amino]-acetic acid	45-120	egl-9 family hypoxia inducible factor 1	Homo sapiens	157-161
23787140-1	2013	HIF prolyl-4-hydroxylase 2 (PHD2) is a non-heme Fe, 2-oxoglutarate (2OG) dependent dioxygenase that regulates the hypoxia inducible transcription factor (HIF) by hydroxylating two conserved prolyl residues in N-terminal oxygen degradation domain (NODD) and C-terminal oxygen degradation domain (CODD) of HIF-1alpha.	Oxygen	220-226	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
23787140-3	2013	In this study we tested the substrate selectivity of PHD2 by kinetic competition assays, varied ionic strength, and global protein flexibility using amide H/D exchange (HDX).	Amides	149-154	egl-9 family hypoxia inducible factor 1	Homo sapiens	53-57
23466866-8	2013	Finally, Smad2/3 inhibitor SB431542 prevented TGF-beta1-induced PHD2 decrease, suggesting that Smad2/3 may mediate TGF-beta1-induced EMT through PHD2/HIF-1alpha pathway.	4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide	27-35	egl-9 family hypoxia inducible factor 1	Homo sapiens	64-68
23694817-3	2013	Prolyl hydroxylase domain protein 2 (PHD2) is a cellular oxygen sensor that regulates 2 key transcription factors involved in cell survival and inflammation: hypoxia-inducible factor and nuclear factor-kappaB.	Oxygen	57-63	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
23694817-3	2013	Prolyl hydroxylase domain protein 2 (PHD2) is a cellular oxygen sensor that regulates 2 key transcription factors involved in cell survival and inflammation: hypoxia-inducible factor and nuclear factor-kappaB.	Oxygen	57-63	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
23466866-8	2013	Finally, Smad2/3 inhibitor SB431542 prevented TGF-beta1-induced PHD2 decrease, suggesting that Smad2/3 may mediate TGF-beta1-induced EMT through PHD2/HIF-1alpha pathway.	4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide	27-35	egl-9 family hypoxia inducible factor 1	Homo sapiens	145-149
23130672-0	2013	EGLN1 variants influence expression and SaO2 levels to associate with high-altitude pulmonary oedema and adaptation.	sao2	40-44	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-5
23413029-3	2013	In this report we show that the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif (where Xaa = any amino acid) in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2.	Glutamic Acid	128-131	egl-9 family hypoxia inducible factor 1	Homo sapiens	257-261
23413029-0	2013	Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway.	pro-xaa-leu	51-62	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
23413029-0	2013	Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway.	pro-xaa-leu	51-62	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
23413029-0	2013	Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway.	Glutamic Acid	63-66	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
23413029-0	2013	Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway.	Glutamic Acid	63-66	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
23413029-1	2013	Prolyl hydroxylase domain protein 2 (PHD2, also known as Egg Laying Defective Nine homolog 1) is a key oxygen-sensing protein in metazoans.	Oxygen	103-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
23413029-1	2013	Prolyl hydroxylase domain protein 2 (PHD2, also known as Egg Laying Defective Nine homolog 1) is a key oxygen-sensing protein in metazoans.	Oxygen	103-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
23413029-2	2013	In an oxygen-dependent manner, PHD2 site-specifically prolyl hydroxylates the master transcription factor of the hypoxic response, hypoxia-inducible factor-alpha (HIF-alpha), thereby targeting HIF-alpha for degradation.	Oxygen	6-12	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
23413029-3	2013	In this report we show that the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif (where Xaa = any amino acid) in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2.	Leucine	124-127	egl-9 family hypoxia inducible factor 1	Homo sapiens	257-261
23380539-2	2013	Together with the two closest paralogues, PHD1 and PHD2, these enzymes have been identified as cellular oxygen sensors that can mark the hypoxia-inducible factor alpha (HIF-alpha) for von Hippel-Lindau protein-mediated proteasomal destruction.	Oxygen	104-110	egl-9 family hypoxia inducible factor 1	Homo sapiens	51-55
23130672-2	2013	EGLN1, being an actual oxygen sensor, appears to have a potential role in the functional adaptation to the hypobaric hypoxic environment.	Oxygen	23-29	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-5
23130672-11	2013	The significant inverse correlation of SaO2 levels with PASP (pulmonary artery systolic pressure) and EGLN1 expression and the association of these polymorphisms with SaO2 levels and EGLN1 expression contributed to uncovering the molecular mechanism underlying hypobaric hypoxic adaptation and maladaptation.	sao2	39-43	egl-9 family hypoxia inducible factor 1	Homo sapiens	102-107
23151668-5	2013	Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2 iron inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion.	Iron	37-41	egl-9 family hypoxia inducible factor 1	Homo sapiens	202-206
23348729-4	2013	One gene previously known to be important in cellular oxygen sensing, egl nine homolog 1 (EGLN1), shows evidence of positive selection in both Tibetans and Andeans.	Oxygen	54-60	egl-9 family hypoxia inducible factor 1	Homo sapiens	70-88
23348729-4	2013	One gene previously known to be important in cellular oxygen sensing, egl nine homolog 1 (EGLN1), shows evidence of positive selection in both Tibetans and Andeans.	Oxygen	54-60	egl-9 family hypoxia inducible factor 1	Homo sapiens	90-95
23487784-3	2013	We report that ERbeta regulates the ligand (3beta-adiol)-dependent transcription of prolyl hydroxylase 2 (PHD2) also known as Egl nine homolog 1 (EGLN1), a 2-oxoglutarate-dependent dioxygenase that hydroxylates HIF-1alpha and targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degradation.	3beta-adiol	44-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	84-104
23487784-3	2013	We report that ERbeta regulates the ligand (3beta-adiol)-dependent transcription of prolyl hydroxylase 2 (PHD2) also known as Egl nine homolog 1 (EGLN1), a 2-oxoglutarate-dependent dioxygenase that hydroxylates HIF-1alpha and targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degradation.	3beta-adiol	44-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	106-110
23487784-3	2013	We report that ERbeta regulates the ligand (3beta-adiol)-dependent transcription of prolyl hydroxylase 2 (PHD2) also known as Egl nine homolog 1 (EGLN1), a 2-oxoglutarate-dependent dioxygenase that hydroxylates HIF-1alpha and targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degradation.	3beta-adiol	44-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	126-144
23487784-3	2013	We report that ERbeta regulates the ligand (3beta-adiol)-dependent transcription of prolyl hydroxylase 2 (PHD2) also known as Egl nine homolog 1 (EGLN1), a 2-oxoglutarate-dependent dioxygenase that hydroxylates HIF-1alpha and targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degradation.	3beta-adiol	44-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	146-151
23487784-7	2013	Moreover, expression of HIF-1alpha in cells that express PHD2 does not induce dedifferentiation but expression of HIF-1alpha containing mutations in the proline residues that are hydroxylated by PHD2 induces dedifferentiation.	Proline	153-160	egl-9 family hypoxia inducible factor 1	Homo sapiens	195-199
23151668-5	2013	Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2 iron inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion.	Iron	127-131	egl-9 family hypoxia inducible factor 1	Homo sapiens	122-126
23151668-5	2013	Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2 iron inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion.	Iron	127-131	egl-9 family hypoxia inducible factor 1	Homo sapiens	202-206
23151668-5	2013	Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2 iron inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion.	diacylhydrazines	166-182	egl-9 family hypoxia inducible factor 1	Homo sapiens	122-126
23151668-5	2013	Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2 iron inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion.	diacylhydrazines	166-182	egl-9 family hypoxia inducible factor 1	Homo sapiens	202-206
23151668-5	2013	Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2 iron inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion.	Iron	127-131	egl-9 family hypoxia inducible factor 1	Homo sapiens	122-126
23151668-5	2013	Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2 iron inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion.	Iron	127-131	egl-9 family hypoxia inducible factor 1	Homo sapiens	202-206
22628534-9	2012	Furthermore, the identification of the EGLN1 gene from the HIF pathway suggests a common adaptive mechanism for Eurasian human populations residing at different altitudes with different oxygen pressures.	Oxygen	186-192	egl-9 family hypoxia inducible factor 1	Homo sapiens	39-44
22946054-0	2012	Oxygen sensing by the prolyl-4-hydroxylase PHD2 within the nuclear compartment and the influence of compartmentalisation on HIF-1 signalling.	Oxygen	0-6	egl-9 family hypoxia inducible factor 1	Homo sapiens	43-47
23261967-4	2013	PCT inhibition of HPH-2 was reversed by addition of ascorbate, a cofactor of HPH-2, but not the cosubstrate, 2-ketoglutarate, to the reaction mixture of an in vitro von Hippel-Lindau (VHL) capture assay, and pretreatment with ascorbate abrogated PCT induction of cellular HIF-1alpha.	Ascorbic Acid	52-61	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-23
23261967-4	2013	PCT inhibition of HPH-2 was reversed by addition of ascorbate, a cofactor of HPH-2, but not the cosubstrate, 2-ketoglutarate, to the reaction mixture of an in vitro von Hippel-Lindau (VHL) capture assay, and pretreatment with ascorbate abrogated PCT induction of cellular HIF-1alpha.	Ascorbic Acid	52-61	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-82
23261967-4	2013	PCT inhibition of HPH-2 was reversed by addition of ascorbate, a cofactor of HPH-2, but not the cosubstrate, 2-ketoglutarate, to the reaction mixture of an in vitro von Hippel-Lindau (VHL) capture assay, and pretreatment with ascorbate abrogated PCT induction of cellular HIF-1alpha.	Ascorbic Acid	226-235	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-23
22747465-1	2012	Prolyl hydroxylase domain 2 (PHD2) is deemed a primary oxygen sensor in humans, yet many details of its underlying mechanism are still not fully understood.	Oxygen	55-61	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-27
22971010-10	2012	This suggested that ROS- and NO-mediated HIF-1alpha stabilization involved S-nitrosation, which was confirmed by demonstrating increased S-nitrosation of PHD2 during hypoxia.	Reactive Oxygen Species	20-23	egl-9 family hypoxia inducible factor 1	Homo sapiens	154-158
22971010-11	2012	Our results support a regulatory mechanism of HIF-1alpha during hypoxia in which endogenously generated NO and ROS promote inhibition of PHD2 activity, probably by its S-nitrosation.	Reactive Oxygen Species	111-114	egl-9 family hypoxia inducible factor 1	Homo sapiens	137-141
22747465-1	2012	Prolyl hydroxylase domain 2 (PHD2) is deemed a primary oxygen sensor in humans, yet many details of its underlying mechanism are still not fully understood.	Oxygen	55-61	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
22747465-2	2012	(Fe(2+) + alphaKG)PHD2 is 6-coordinate, with a 2His/1Asp facial triad occupying three coordination sites, a bidentate alpha-ketoglutarate occupying two sites, and an aquo ligand in the final site.	Iron	1-3	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-22
22747465-2	2012	(Fe(2+) + alphaKG)PHD2 is 6-coordinate, with a 2His/1Asp facial triad occupying three coordination sites, a bidentate alpha-ketoglutarate occupying two sites, and an aquo ligand in the final site.	2his	47-51	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-22
22747465-2	2012	(Fe(2+) + alphaKG)PHD2 is 6-coordinate, with a 2His/1Asp facial triad occupying three coordination sites, a bidentate alpha-ketoglutarate occupying two sites, and an aquo ligand in the final site.	Ketoglutaric Acids	118-137	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-22
22747465-5	2012	A variety of spectroscopic probes were employed to identify the active-site acid, through comparison of (Fe(2+) + alphaKG)PHD2 at pH 6.50 with pH 8.50.	ammonium ferrous sulfate	105-111	egl-9 family hypoxia inducible factor 1	Homo sapiens	122-126
22747465-10	2012	The unusual kinetic pK(a) further suggested that PHD2 might function physiologically to sense both intracellular pO(2) as well as pH, which could provide for feedback between anaerobic metabolism and hypoxia sensing.	PO-2	113-118	egl-9 family hypoxia inducible factor 1	Homo sapiens	49-53
22360728-5	2012	In order to shed light on the redox-regulation of HIF-1 by ROS, we studied the impact of exogenous ROS treatment (H(2)O(2)) on HIF-1alpha and HIF-1 regulatory protein prolyl hydroxylase 2 (PHD2) in the human osteosarcoma cell line U2OS.	Reactive Oxygen Species	99-102	egl-9 family hypoxia inducible factor 1	Homo sapiens	167-187
22897855-2	2012	Prolyl hydroxylase domain protein 2 (PHD2) is an oxygen/redox-sensitive enzyme that induces cellular adaptations to stress conditions.	Oxygen	49-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-35
22897855-2	2012	Prolyl hydroxylase domain protein 2 (PHD2) is an oxygen/redox-sensitive enzyme that induces cellular adaptations to stress conditions.	Oxygen	49-55	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
22687491-2	2012	These enzymes are factor inhibiting HIF (FIH) and prolyl hydroxylase-2 (PHD2), each an alpha-ketoglutarate (alphaKG) dependent, non-heme Fe(II) dioxygenase.	Ketoglutaric Acids	87-106	egl-9 family hypoxia inducible factor 1	Homo sapiens	50-70
22687491-2	2012	These enzymes are factor inhibiting HIF (FIH) and prolyl hydroxylase-2 (PHD2), each an alpha-ketoglutarate (alphaKG) dependent, non-heme Fe(II) dioxygenase.	Ketoglutaric Acids	87-106	egl-9 family hypoxia inducible factor 1	Homo sapiens	72-76
22687491-3	2012	Although the two enzymes have similar active sites, FIH hydroxylates Asn(803) of HIF-1alpha while PHD2 hydroxylates Pro(402) and/or Pro(564) of HIF-1alpha.	Asparagine	69-72	egl-9 family hypoxia inducible factor 1	Homo sapiens	98-102
22687491-7	2012	Dose response curves at moderate [alphaKG] ([alphaKG]~K(M)) showed that the hydroxypyrones/hydroxypyridinones were selective inhibitors, with IC(50) in the muM range, and that the catechols were generally strong inhibitors of both FIH and PHD2, with IC(50) in the low muM range.	hydroxypyrones	76-90	egl-9 family hypoxia inducible factor 1	Homo sapiens	239-243
22687491-7	2012	Dose response curves at moderate [alphaKG] ([alphaKG]~K(M)) showed that the hydroxypyrones/hydroxypyridinones were selective inhibitors, with IC(50) in the muM range, and that the catechols were generally strong inhibitors of both FIH and PHD2, with IC(50) in the low muM range.	1-hydroxy-2(1H)-pyridinone	91-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	239-243
22687491-9	2012	This work shows some selective inhibition between FIH and PHD2, primarily through the use of simple aromatic or pseudo-aromatic chelators, and suggests that hydroxypyrones and hydroxypyridones may be promising chelates for FIH or PHD2 inhibition.	hydroxypyrones	157-171	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-62
22687491-9	2012	This work shows some selective inhibition between FIH and PHD2, primarily through the use of simple aromatic or pseudo-aromatic chelators, and suggests that hydroxypyrones and hydroxypyridones may be promising chelates for FIH or PHD2 inhibition.	hydroxypyrones	157-171	egl-9 family hypoxia inducible factor 1	Homo sapiens	230-234
22687491-9	2012	This work shows some selective inhibition between FIH and PHD2, primarily through the use of simple aromatic or pseudo-aromatic chelators, and suggests that hydroxypyrones and hydroxypyridones may be promising chelates for FIH or PHD2 inhibition.	hydroxypyridones	176-192	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-62
22687491-9	2012	This work shows some selective inhibition between FIH and PHD2, primarily through the use of simple aromatic or pseudo-aromatic chelators, and suggests that hydroxypyrones and hydroxypyridones may be promising chelates for FIH or PHD2 inhibition.	hydroxypyridones	176-192	egl-9 family hypoxia inducible factor 1	Homo sapiens	230-234
22360728-0	2012	Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia.	Reactive Oxygen Species	8-31	egl-9 family hypoxia inducible factor 1	Homo sapiens	62-82
22364528-2	2012	The initial hit class, spirooxindoles, was identified through affinity selection mass spectrometry (AS-MS) and optimized for PHD2 inhibition and optimal PK/PD profile (short-acting PHDi inhibitors).	spirooxindoles	23-37	egl-9 family hypoxia inducible factor 1	Homo sapiens	125-129
22451659-8	2012	Finally, loss of function studies using lentiviral transduction of ShPHDs clearly shows that even at 1% O(2), PHD2 selectively degrades HIF-1alpha.	Oxygen	104-108	egl-9 family hypoxia inducible factor 1	Homo sapiens	110-114
22245592-6	2012	We also found that myricetin, quercetin, piceatannol and resveratrol up-regulated HIF-1alpha and down-regulated c-Myc, PHD2 and beta-catenin expressions via SIRT1 activation, in a manner that mimics hypoxic preconditioning.	myricetin	19-28	egl-9 family hypoxia inducible factor 1	Homo sapiens	119-123
22395314-3	2012	Three HIF prolyl hydroxylase enzymes (PHD1, PHD2 and PHD3) function as oxygen sensing enzymes, which regulate the activity of HIFs in normoxic and hypoxic conditions.	Oxygen	71-77	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-48
21904933-9	2012	In Laks, a non-synonymous variant within HIF1A already known to be associated with improvement in oxygen metabolism was rediscovered, and in Kubachians a cluster of 13 SNPs located in a conserved intronic region within EGLN1 showing high population differentiation was found.	Oxygen	98-104	egl-9 family hypoxia inducible factor 1	Homo sapiens	219-224
22245592-6	2012	We also found that myricetin, quercetin, piceatannol and resveratrol up-regulated HIF-1alpha and down-regulated c-Myc, PHD2 and beta-catenin expressions via SIRT1 activation, in a manner that mimics hypoxic preconditioning.	Quercetin	30-39	egl-9 family hypoxia inducible factor 1	Homo sapiens	119-123
22245592-6	2012	We also found that myricetin, quercetin, piceatannol and resveratrol up-regulated HIF-1alpha and down-regulated c-Myc, PHD2 and beta-catenin expressions via SIRT1 activation, in a manner that mimics hypoxic preconditioning.	3,3',4,5'-tetrahydroxystilbene	41-52	egl-9 family hypoxia inducible factor 1	Homo sapiens	119-123
22245592-6	2012	We also found that myricetin, quercetin, piceatannol and resveratrol up-regulated HIF-1alpha and down-regulated c-Myc, PHD2 and beta-catenin expressions via SIRT1 activation, in a manner that mimics hypoxic preconditioning.	Resveratrol	57-68	egl-9 family hypoxia inducible factor 1	Homo sapiens	119-123
21792862-3	2012	PHD2 is considered the key oxygen sensor-regulating hypoxia-inducible factor (HIF).	Oxygen	27-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
21951999-3	2011	The alpha-subunits of HIFs are hydroxylated by members of the prolyl-4-hydroxylase domain (PHD) family, PHD1, PHD2, and PHD3, in an oxygen-dependent manner.	Oxygen	132-138	egl-9 family hypoxia inducible factor 1	Homo sapiens	110-114
22236543-3	2012	METHODS: In a total of 121 patients, PHD2 expression was investigated by immunohistochemistry in paraffin-embedded tissue and correlated with clinicopathological parameters and patient survival.	Paraffin	97-105	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
21665470-1	2011	Oxygen dependent degradation of hypoxia-inducible factor (HIF)-1alpha is triggered with hydroxylation by proline hydroxylase domain 2 (PHD2) under normoxic conditions.	Oxygen	0-6	egl-9 family hypoxia inducible factor 1	Homo sapiens	105-133
21255264-5	2011	PHD2 hydroxylates beta-arrestin 2 at the proline (Pro)(176), Pro(179) and Pro(181) sites, which retards the recruitment of beta-arrestin 2 to the plasma membrane and inhibits subsequent co-internalization with beta(2) -AR into the cytosol.	Proline	41-48	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
21255264-5	2011	PHD2 hydroxylates beta-arrestin 2 at the proline (Pro)(176), Pro(179) and Pro(181) sites, which retards the recruitment of beta-arrestin 2 to the plasma membrane and inhibits subsequent co-internalization with beta(2) -AR into the cytosol.	Proline	50-53	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
21255264-5	2011	PHD2 hydroxylates beta-arrestin 2 at the proline (Pro)(176), Pro(179) and Pro(181) sites, which retards the recruitment of beta-arrestin 2 to the plasma membrane and inhibits subsequent co-internalization with beta(2) -AR into the cytosol.	Proline	61-64	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
21255264-5	2011	PHD2 hydroxylates beta-arrestin 2 at the proline (Pro)(176), Pro(179) and Pro(181) sites, which retards the recruitment of beta-arrestin 2 to the plasma membrane and inhibits subsequent co-internalization with beta(2) -AR into the cytosol.	Proline	61-64	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
21785823-6	2011	PHD2 accumulation, which occurred concomitant with HIF1 stabilization, may have compensated for the lack of oxygen under hypoxic conditions to regulate the HIF levels.	Oxygen	108-114	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
21723853-4	2011	In an in vitro VHL capture assay, hydroxylation of the 19mer HIF peptide (corresponding to HIF-1alpha residues 556-574) by HPH-2 was effectively prevented by nitric oxide (NO) donors, (+-)-S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione.	Nitric Oxide	158-170	egl-9 family hypoxia inducible factor 1	Homo sapiens	123-128
21723853-4	2011	In an in vitro VHL capture assay, hydroxylation of the 19mer HIF peptide (corresponding to HIF-1alpha residues 556-574) by HPH-2 was effectively prevented by nitric oxide (NO) donors, (+-)-S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione.	S-Nitroso-N-Acetylpenicillamine	184-220	egl-9 family hypoxia inducible factor 1	Homo sapiens	123-128
21723853-4	2011	In an in vitro VHL capture assay, hydroxylation of the 19mer HIF peptide (corresponding to HIF-1alpha residues 556-574) by HPH-2 was effectively prevented by nitric oxide (NO) donors, (+-)-S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione.	S-Nitrosoglutathione	232-252	egl-9 family hypoxia inducible factor 1	Homo sapiens	123-128
21723853-9	2011	Our data suggest that NO inhibits HPH-2 via competing with dioxygen and that the discriminative effect of NO on CPHs and HPH-2 is attributable to the difference in the affinity of the two enzymes toward dioxygen.	Oxygen	203-211	egl-9 family hypoxia inducible factor 1	Homo sapiens	34-39
21723853-9	2011	Our data suggest that NO inhibits HPH-2 via competing with dioxygen and that the discriminative effect of NO on CPHs and HPH-2 is attributable to the difference in the affinity of the two enzymes toward dioxygen.	Oxygen	203-211	egl-9 family hypoxia inducible factor 1	Homo sapiens	121-126
21504793-7	2011	For the most potent compound, a hydroxyl thiazole derivative, the potency against HPH2 and HPH3 was 7nM and 0.49nM, respectively corresponding to a 14-fold difference.	hydroxyl thiazole	32-49	egl-9 family hypoxia inducible factor 1	Homo sapiens	82-86
21665470-1	2011	Oxygen dependent degradation of hypoxia-inducible factor (HIF)-1alpha is triggered with hydroxylation by proline hydroxylase domain 2 (PHD2) under normoxic conditions.	Oxygen	0-6	egl-9 family hypoxia inducible factor 1	Homo sapiens	135-139
21335603-12	2011	Src-induced ROS reduces cellular vitamin C, which is required for the activity of PHD2, thus Src can block VHL recruitment of HIF-1alpha, leading to stabilization of HIF-1alpha.	ros	12-15	egl-9 family hypoxia inducible factor 1	Homo sapiens	82-86
21742796-15	2011	More recently, genetic and pharmacological approaches have begun to unravel some other key regulators of vascular normalization such as proteins that regulate tissue oxygen sensing (PHD2) and vessel maturation (PDGFRbeta, RGS5, Ang1/2, TGF-beta).	Oxygen	166-172	egl-9 family hypoxia inducible factor 1	Homo sapiens	182-186
21410436-2	2011	HIF proteins are regulated by three Fe(II)- and alpha-KG (alpha-ketoglutarate)-dependent prolyl hydroxylase enzymes [PHD (prolyl hydroxylase domain) isoenzymes 1-3 or PHD1, PHD2 and PHD3] and one asparaginyl hydroxylase [FIH (factor inhibiting HIF)].	ammonium ferrous sulfate	36-42	egl-9 family hypoxia inducible factor 1	Homo sapiens	173-177
21410436-2	2011	HIF proteins are regulated by three Fe(II)- and alpha-KG (alpha-ketoglutarate)-dependent prolyl hydroxylase enzymes [PHD (prolyl hydroxylase domain) isoenzymes 1-3 or PHD1, PHD2 and PHD3] and one asparaginyl hydroxylase [FIH (factor inhibiting HIF)].	Ketoglutaric Acids	58-77	egl-9 family hypoxia inducible factor 1	Homo sapiens	173-177
21601578-0	2011	Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).	Nitric Oxide	27-39	egl-9 family hypoxia inducible factor 1	Homo sapiens	103-108
21601578-4	2011	We describe biochemical and biophysical studies on the reaction of prolyl hydroxylase domain-containing enzyme (PHD) isoform 2 (EGLN1) with nitric oxide and a nitric oxide transfer reagent.	Nitric Oxide	140-152	egl-9 family hypoxia inducible factor 1	Homo sapiens	128-133
21601578-4	2011	We describe biochemical and biophysical studies on the reaction of prolyl hydroxylase domain-containing enzyme (PHD) isoform 2 (EGLN1) with nitric oxide and a nitric oxide transfer reagent.	Nitric Oxide	159-171	egl-9 family hypoxia inducible factor 1	Homo sapiens	128-133
21601578-5	2011	The combined results reveal the potential for the catalytic domain of PHD2 to react with nitric oxide both at its Fe(II) and at cysteine residues.	Nitric Oxide	89-101	egl-9 family hypoxia inducible factor 1	Homo sapiens	70-74
21601578-5	2011	The combined results reveal the potential for the catalytic domain of PHD2 to react with nitric oxide both at its Fe(II) and at cysteine residues.	ammonium ferrous sulfate	114-120	egl-9 family hypoxia inducible factor 1	Homo sapiens	70-74
21601578-5	2011	The combined results reveal the potential for the catalytic domain of PHD2 to react with nitric oxide both at its Fe(II) and at cysteine residues.	Cysteine	128-136	egl-9 family hypoxia inducible factor 1	Homo sapiens	70-74
21601578-6	2011	Although the biological significance is unclear, the results suggest that the reaction of PHD2 with nitric oxide has the potential to be complex and are consistent with proposals based on cellular studies that nitric oxide may regulate the hypoxic response by direct reaction with the HIF hydroxylases.	Nitric Oxide	100-112	egl-9 family hypoxia inducible factor 1	Homo sapiens	90-94
21601578-6	2011	Although the biological significance is unclear, the results suggest that the reaction of PHD2 with nitric oxide has the potential to be complex and are consistent with proposals based on cellular studies that nitric oxide may regulate the hypoxic response by direct reaction with the HIF hydroxylases.	Nitric Oxide	210-222	egl-9 family hypoxia inducible factor 1	Homo sapiens	90-94
21335603-11	2011	HIF-1alpha-hydroxylation-dependent VHL pull-down assay showed that Src inhibits cellular PHD2 activity by inducing ROS production in a mechanism involving Rac1-dependent NADPH oxidase.	ros	115-118	egl-9 family hypoxia inducible factor 1	Homo sapiens	89-93
21335603-12	2011	Src-induced ROS reduces cellular vitamin C, which is required for the activity of PHD2, thus Src can block VHL recruitment of HIF-1alpha, leading to stabilization of HIF-1alpha.	Ascorbic Acid	33-42	egl-9 family hypoxia inducible factor 1	Homo sapiens	82-86
21300765-6	2011	PHD2 silencing in endothelial cells recapitulated the proangiogenic effects of lactate, whereas a blocking IL-8 antibody or IL-8-targeting siRNA prevented them.	Lactic Acid	79-86	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
20801873-3	2010	Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells resulted in increased F-actin formation as detected by phalloidin staining.	Tetracycline	33-45	egl-9 family hypoxia inducible factor 1	Homo sapiens	15-19
21076780-3	2011	The subsequently prepared di-acids were tested for in vitro inhibition of the histone demethylase JMJD2E and another human 2OG oxygenase, prolyl-hydroxylase domain isoform 2 (PHD2, EGLN1).	di-acids	26-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	138-173
21076780-3	2011	The subsequently prepared di-acids were tested for in vitro inhibition of the histone demethylase JMJD2E and another human 2OG oxygenase, prolyl-hydroxylase domain isoform 2 (PHD2, EGLN1).	di-acids	26-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	175-179
21076780-3	2011	The subsequently prepared di-acids were tested for in vitro inhibition of the histone demethylase JMJD2E and another human 2OG oxygenase, prolyl-hydroxylase domain isoform 2 (PHD2, EGLN1).	di-acids	26-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	181-186
21887331-8	2011	In the multivariate analyses we found high tumor cell expression of PHD2 (HR = 2.03, CI 95% 1.20-3.42, P = 0.008) and PHD1 (HR = 1.45, CI 95% 1.01-2.10, P = 0.047) to be significant independent prognosticators for DSS.	dss	214-217	egl-9 family hypoxia inducible factor 1	Homo sapiens	68-72
21278251-5	2011	Here, we determine the solution structure of PHD2 in complex with H3K9me3, revealing the molecular basis of histone recognition, including a cation-pi recognition mechanism for methylated Lys(9).	Lysine	188-191	egl-9 family hypoxia inducible factor 1	Homo sapiens	45-49
21143197-8	2011	However, the hPCL3L-specific PHD2 domain, which is better conserved than PHD1 in the PCL family, is also involved in this interaction and implicated in the self-association of hPCL3L.	hpcl3l	13-19	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-33
21287578-0	2011	An activator of PHD2, KRH102140, decreases angiogenesis via inhibition of HIF-1alpha.	(2-fluorobenzyl)-(2-methyl-2-phenyl-2H-chromen-6-yl-amine)	22-31	egl-9 family hypoxia inducible factor 1	Homo sapiens	16-20
21287578-5	2011	We previously reported that KRH102053, an activator of PHD2, rapidly decreased HIF-1alpha and eventually inhibited angiogenesis.	2-amino-4-methylsulfanylbutyric acid 4-methoxy-6-(4-methoxybenzylamino)-2,2-dimethylchroman-3-yl ester	28-37	egl-9 family hypoxia inducible factor 1	Homo sapiens	55-59
21287578-6	2011	Here, we report a potent activator of PHD2, KRH102140, which has a structure similar to KRH102053.	(2-fluorobenzyl)-(2-methyl-2-phenyl-2H-chromen-6-yl-amine)	44-53	egl-9 family hypoxia inducible factor 1	Homo sapiens	38-42
21287578-6	2011	Here, we report a potent activator of PHD2, KRH102140, which has a structure similar to KRH102053.	2-amino-4-methylsulfanylbutyric acid 4-methoxy-6-(4-methoxybenzylamino)-2,2-dimethylchroman-3-yl ester	88-97	egl-9 family hypoxia inducible factor 1	Homo sapiens	38-42
21291529-7	2011	PHD1, PHD2 and PHD3 expression was significantly increased after epirubicin therapy (all P < 0.000) with no significant difference in PHD changes between the treatment arms.	Epirubicin	65-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	6-10
21134392-7	2011	Molecular data showed that all these effects of Andro might be mediated via TGFbeta1/PHD2/HIF-1alpha pathway, as demonstrated by the transfection of TGFbeta1 overexpression vector and PHD2 siRNA, and the usage of a pharmacological MG132 inhibitor.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	231-236	egl-9 family hypoxia inducible factor 1	Homo sapiens	85-89
20801873-3	2010	Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells resulted in increased F-actin formation as detected by phalloidin staining.	Tetracycline	33-45	egl-9 family hypoxia inducible factor 1	Homo sapiens	61-65
20801873-3	2010	Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells resulted in increased F-actin formation as detected by phalloidin staining.	Phalloidine	137-147	egl-9 family hypoxia inducible factor 1	Homo sapiens	15-19
20801873-3	2010	Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells resulted in increased F-actin formation as detected by phalloidin staining.	Phalloidine	137-147	egl-9 family hypoxia inducible factor 1	Homo sapiens	61-65
24900242-2	2010	Certain benzimidazole-2-pyrazole carboxylates were discovered to be PHD2 inhibitors using ligand- and structure-based methods and found to be potent, orally efficacious stimulators of erythropoietin secretion in vivo.	benzimidazole-2-pyrazole carboxylates	8-45	egl-9 family hypoxia inducible factor 1	Homo sapiens	68-72
20404338-8	2010	Depletion of PHD2 resulted in greater HIF-2alpha levels and therefore enhanced SOX9-induced cartilage matrix production compared with the levels normally found in hypoxia (1% oxygen) implying that PHD2 inhibition offers a novel means to enhance cartilage repair in vivo.	Oxygen	175-181	egl-9 family hypoxia inducible factor 1	Homo sapiens	13-17
20973793-3	2010	In the presence of oxygen, HIF1alpha is prolyl hydroxylated by EglN1 (also called PHD2); this modification recruits pVHL, which then targets HIF1alpha for proteasomal degradation.	Oxygen	19-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	63-68
20973793-3	2010	In the presence of oxygen, HIF1alpha is prolyl hydroxylated by EglN1 (also called PHD2); this modification recruits pVHL, which then targets HIF1alpha for proteasomal degradation.	Oxygen	19-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	82-86
20840591-0	2010	Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen.	Oxygen	85-91	egl-9 family hypoxia inducible factor 1	Homo sapiens	34-79
20838600-10	2010	Interestingly, one gene previously known to be important in cellular oxygen sensing, EGLN1 (also known as PHD2), shows evidence of positive selection in both Tibetans and Andeans.	Oxygen	69-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	85-90
20838600-10	2010	Interestingly, one gene previously known to be important in cellular oxygen sensing, EGLN1 (also known as PHD2), shows evidence of positive selection in both Tibetans and Andeans.	Oxygen	69-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	106-110
20613843-3	2010	Recently, a tandem plant homeodomain (PHD) finger (PHD1-PHD2, or PHD12) of human DPF3b, which functions in association with the BAF chromatin remodelling complex to initiate gene transcription during heart and muscle development, was reported to bind histones H3 and H4 in an acetylation-sensitive manner, making it the first alternative to bromodomains for acetyl-lysine binding.	N(alpha)-acetyllysine	358-371	egl-9 family hypoxia inducible factor 1	Homo sapiens	56-60
20416277-4	2010	In vitro PHD2 and FIH activity assays based on fluorescence polarization reveal that such HIF-1alpha stabilization is likely medicated by inhibitory effects of hinokitiol on prolyl and asparaginyl hydroxylation of HIF-1alpha.	beta-thujaplicin	160-170	egl-9 family hypoxia inducible factor 1	Homo sapiens	9-13
20527723-0	2010	Apicidin upregulates PHD2 prolyl hydroxylase gene expression in cervical cancer cells.	apicidin	0-8	egl-9 family hypoxia inducible factor 1	Homo sapiens	21-25
20527723-2	2010	We used HeLa, CaSki, C33A, and SiHa cervical cancer cells to show the effect of apicidin on cellular levels of PHD2 enzyme.	apicidin	80-88	egl-9 family hypoxia inducible factor 1	Homo sapiens	111-115
20527723-3	2010	Using reverse transcription, real-time quantitative PCR, and western blot analysis, we established that apicidin upregulates PHD2 transcript and protein levels in HeLa, CaSki, and C33A, but not in SiHa cervical cancer cells.	apicidin	104-112	egl-9 family hypoxia inducible factor 1	Homo sapiens	125-129
20527723-4	2010	Bisulfite sequencing showed that the increase in PHD2 expression was accompanied by demethylation ofCpG islands located in the first exon of the PHD2 gene.As decreased PHD2 expression supports tumor progression, our findings may validate the usefulness of apicidin as an anticancer drug.	hydrogen sulfite	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	49-53
20527723-4	2010	Bisulfite sequencing showed that the increase in PHD2 expression was accompanied by demethylation ofCpG islands located in the first exon of the PHD2 gene.As decreased PHD2 expression supports tumor progression, our findings may validate the usefulness of apicidin as an anticancer drug.	hydrogen sulfite	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	145-149
20527723-4	2010	Bisulfite sequencing showed that the increase in PHD2 expression was accompanied by demethylation ofCpG islands located in the first exon of the PHD2 gene.As decreased PHD2 expression supports tumor progression, our findings may validate the usefulness of apicidin as an anticancer drug.	hydrogen sulfite	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	145-149
20527723-4	2010	Bisulfite sequencing showed that the increase in PHD2 expression was accompanied by demethylation ofCpG islands located in the first exon of the PHD2 gene.As decreased PHD2 expression supports tumor progression, our findings may validate the usefulness of apicidin as an anticancer drug.	apicidin	256-264	egl-9 family hypoxia inducible factor 1	Homo sapiens	49-53
20527723-4	2010	Bisulfite sequencing showed that the increase in PHD2 expression was accompanied by demethylation ofCpG islands located in the first exon of the PHD2 gene.As decreased PHD2 expression supports tumor progression, our findings may validate the usefulness of apicidin as an anticancer drug.	apicidin	256-264	egl-9 family hypoxia inducible factor 1	Homo sapiens	145-149
20527723-4	2010	Bisulfite sequencing showed that the increase in PHD2 expression was accompanied by demethylation ofCpG islands located in the first exon of the PHD2 gene.As decreased PHD2 expression supports tumor progression, our findings may validate the usefulness of apicidin as an anticancer drug.	apicidin	256-264	egl-9 family hypoxia inducible factor 1	Homo sapiens	145-149
20461086-2	2010	Of the four identified PHD enzymes, PHD2 is considered to be the key oxygen sensor, as knockdown of PHD2 results in elevated HIF protein.	Oxygen	69-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-40
20461086-2	2010	Of the four identified PHD enzymes, PHD2 is considered to be the key oxygen sensor, as knockdown of PHD2 results in elevated HIF protein.	Oxygen	69-75	egl-9 family hypoxia inducible factor 1	Homo sapiens	100-104
20216402-0	2010	Double immunohistochemical staining method for HIF-1alpha and its regulators PHD2 and PHD3 in formalin-fixed paraffin-embedded tissues.	Formaldehyde	94-102	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-81
20416277-5	2010	In addition, the inhibition of PHD2 by hinokitiol is reversed by the addition of 2-OG and iron(II), suggesting that the underlying inhibitory mechanism involves displacement of 2-OG and a chelate formation with iron(II) at the enzyme active site by hinokitiol.	beta-thujaplicin	39-49	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
20416277-5	2010	In addition, the inhibition of PHD2 by hinokitiol is reversed by the addition of 2-OG and iron(II), suggesting that the underlying inhibitory mechanism involves displacement of 2-OG and a chelate formation with iron(II) at the enzyme active site by hinokitiol.	Ketoglutaric Acids	81-85	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
20416277-5	2010	In addition, the inhibition of PHD2 by hinokitiol is reversed by the addition of 2-OG and iron(II), suggesting that the underlying inhibitory mechanism involves displacement of 2-OG and a chelate formation with iron(II) at the enzyme active site by hinokitiol.	ammonium ferrous sulfate	90-98	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
20416277-5	2010	In addition, the inhibition of PHD2 by hinokitiol is reversed by the addition of 2-OG and iron(II), suggesting that the underlying inhibitory mechanism involves displacement of 2-OG and a chelate formation with iron(II) at the enzyme active site by hinokitiol.	Ketoglutaric Acids	177-181	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
20416277-5	2010	In addition, the inhibition of PHD2 by hinokitiol is reversed by the addition of 2-OG and iron(II), suggesting that the underlying inhibitory mechanism involves displacement of 2-OG and a chelate formation with iron(II) at the enzyme active site by hinokitiol.	ammonium ferrous sulfate	211-219	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
20416277-5	2010	In addition, the inhibition of PHD2 by hinokitiol is reversed by the addition of 2-OG and iron(II), suggesting that the underlying inhibitory mechanism involves displacement of 2-OG and a chelate formation with iron(II) at the enzyme active site by hinokitiol.	beta-thujaplicin	249-259	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-35
20055761-3	2010	We have investigated the ascorbate dependence of PHD2-catalysed hydroxylation of two prolyl hydroxylation sites in human HIF-1alpha, and of FIH-catalysed hydroxylation of asparaginyl hydroxylation sites in HIF-1alpha and in a consensus ankyrin repeat domain peptide.	Ascorbic Acid	25-34	egl-9 family hypoxia inducible factor 1	Homo sapiens	49-53
20007141-2	2010	In this pathway, Prolyl Hydroxylase Domain protein 2 (PHD2) hydroxylates two prolyl residues in HIF-alpha, which in turn promotes HIF-alpha degradation by the von Hippel Lindau (VHL) protein.	Peptide oostatic hormone	77-83	egl-9 family hypoxia inducible factor 1	Homo sapiens	17-52
20007141-2	2010	In this pathway, Prolyl Hydroxylase Domain protein 2 (PHD2) hydroxylates two prolyl residues in HIF-alpha, which in turn promotes HIF-alpha degradation by the von Hippel Lindau (VHL) protein.	Peptide oostatic hormone	77-83	egl-9 family hypoxia inducible factor 1	Homo sapiens	54-58
20302516-5	2010	Here, the effects of NANT in inhibiting recombinant PHD2 and up-regulating of HIF-1 and HIF-1-mediated carboanhydrase-9 (CA9) mRNA expression were compared in living cells with the NO donors N-nitrosomelatonin (NOMela) and S-nitrosoglutathione (GSNO) under normoxic and hypoxic conditions.	N-acetyl-N-nitrosotryptophan	21-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	52-56
20302516-6	2010	In contrast to GSNO, NANT was similar to NOMela being highly effective in inhibiting recombinant PHD2.	N-acetyl-N-nitrosotryptophan	21-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	97-101
20302516-8	2010	In contrast, under hypoxia NANT was able to boost hypoxic cellular HIF-1 levels by further reducing the activity of cellular PHD2.	N-acetyl-N-nitrosotryptophan	27-31	egl-9 family hypoxia inducible factor 1	Homo sapiens	125-129
20025281-2	2010	The method was exemplified using prolyl hydroxylase domain containing enzyme 2 (PHD2), a human enzyme involved in hypoxic sensing, with Mn(II) substituting for Fe(II) at the active site.	Manganese(2+)	136-142	egl-9 family hypoxia inducible factor 1	Homo sapiens	80-84
20025281-2	2010	The method was exemplified using prolyl hydroxylase domain containing enzyme 2 (PHD2), a human enzyme involved in hypoxic sensing, with Mn(II) substituting for Fe(II) at the active site.	ammonium ferrous sulfate	160-166	egl-9 family hypoxia inducible factor 1	Homo sapiens	80-84
19817749-5	2010	Evidence for an etoposide-specific resistance, which develops as a consequence of inhibiting the PHD activity, was further supported in a tetracycline-inducible PHD2 knockdown HeLa cell model.	Etoposide	16-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	161-165
19817749-5	2010	Evidence for an etoposide-specific resistance, which develops as a consequence of inhibiting the PHD activity, was further supported in a tetracycline-inducible PHD2 knockdown HeLa cell model.	Tetracycline	138-150	egl-9 family hypoxia inducible factor 1	Homo sapiens	161-165
20028863-6	2010	Gain and loss of function experiments defined PHD2 and PHD3 as HIF target genes that remained operative even at low oxygen concentrations.	Oxygen	116-122	egl-9 family hypoxia inducible factor 1	Homo sapiens	46-50
19563769-2	2009	Here we report studies on the reactivity of cysteinyl residues of the catalytic domain of PHD2 using an approach in which nondenaturing electrospray ionization-mass spectrometry (ESI-MS) analyses were combined with the use of a thiol library and residue substitution.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	44-53	egl-9 family hypoxia inducible factor 1	Homo sapiens	90-94
19775891-0	2009	2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2.	Ketoglutaric Acids	0-14	egl-9 family hypoxia inducible factor 1	Homo sapiens	38-65
19775891-1	2009	Analogues of the 2-oxoglutarate cosubstrate of the human oxygen sensing enzyme prolyl hydroxylase domain 2 (PHD2) with variations in the potential iron-chelating group were screened as inhibitors and for binding (using non-denaturing electrospray ionization mass spectrometry) to PHD2.	Ketoglutaric Acids	17-31	egl-9 family hypoxia inducible factor 1	Homo sapiens	79-106
19775891-1	2009	Analogues of the 2-oxoglutarate cosubstrate of the human oxygen sensing enzyme prolyl hydroxylase domain 2 (PHD2) with variations in the potential iron-chelating group were screened as inhibitors and for binding (using non-denaturing electrospray ionization mass spectrometry) to PHD2.	Ketoglutaric Acids	17-31	egl-9 family hypoxia inducible factor 1	Homo sapiens	108-112
19775891-1	2009	Analogues of the 2-oxoglutarate cosubstrate of the human oxygen sensing enzyme prolyl hydroxylase domain 2 (PHD2) with variations in the potential iron-chelating group were screened as inhibitors and for binding (using non-denaturing electrospray ionization mass spectrometry) to PHD2.	Ketoglutaric Acids	17-31	egl-9 family hypoxia inducible factor 1	Homo sapiens	280-284
19775891-1	2009	Analogues of the 2-oxoglutarate cosubstrate of the human oxygen sensing enzyme prolyl hydroxylase domain 2 (PHD2) with variations in the potential iron-chelating group were screened as inhibitors and for binding (using non-denaturing electrospray ionization mass spectrometry) to PHD2.	Oxygen	57-63	egl-9 family hypoxia inducible factor 1	Homo sapiens	79-106
19775891-1	2009	Analogues of the 2-oxoglutarate cosubstrate of the human oxygen sensing enzyme prolyl hydroxylase domain 2 (PHD2) with variations in the potential iron-chelating group were screened as inhibitors and for binding (using non-denaturing electrospray ionization mass spectrometry) to PHD2.	Oxygen	57-63	egl-9 family hypoxia inducible factor 1	Homo sapiens	108-112
19775891-1	2009	Analogues of the 2-oxoglutarate cosubstrate of the human oxygen sensing enzyme prolyl hydroxylase domain 2 (PHD2) with variations in the potential iron-chelating group were screened as inhibitors and for binding (using non-denaturing electrospray ionization mass spectrometry) to PHD2.	Iron	147-151	egl-9 family hypoxia inducible factor 1	Homo sapiens	79-106
19775891-1	2009	Analogues of the 2-oxoglutarate cosubstrate of the human oxygen sensing enzyme prolyl hydroxylase domain 2 (PHD2) with variations in the potential iron-chelating group were screened as inhibitors and for binding (using non-denaturing electrospray ionization mass spectrometry) to PHD2.	Iron	147-151	egl-9 family hypoxia inducible factor 1	Homo sapiens	108-112
19563769-2	2009	Here we report studies on the reactivity of cysteinyl residues of the catalytic domain of PHD2 using an approach in which nondenaturing electrospray ionization-mass spectrometry (ESI-MS) analyses were combined with the use of a thiol library and residue substitution.	Sulfhydryl Compounds	228-233	egl-9 family hypoxia inducible factor 1	Homo sapiens	90-94
19563769-3	2009	Among the seven cysteinyl residues of the PHD2 catalytic domain, Cys201 was found to be predominantly modified by thiols or N-ethylmaleimide.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	16-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	42-46
19563769-3	2009	Among the seven cysteinyl residues of the PHD2 catalytic domain, Cys201 was found to be predominantly modified by thiols or N-ethylmaleimide.	Sulfhydryl Compounds	114-120	egl-9 family hypoxia inducible factor 1	Homo sapiens	42-46
19563769-3	2009	Among the seven cysteinyl residues of the PHD2 catalytic domain, Cys201 was found to be predominantly modified by thiols or N-ethylmaleimide.	Ethylmaleimide	124-140	egl-9 family hypoxia inducible factor 1	Homo sapiens	42-46
19604478-4	2009	We report crystal structures of the catalytic domain of PHD2, the most important of the human PHDs, in complex with the C-terminal oxygen-dependent degradation domain of HIF-1alpha.	Oxygen	131-137	egl-9 family hypoxia inducible factor 1	Homo sapiens	56-60
19546213-2	2009	Whereas PHD1 and PHD3 proteolysis has been shown to be regulated by Siah2 ubiquitin E3 ligase-mediated polyubiquitylation and proteasomal destruction, protein regulation of the main oxygen sensor responsible for hypoxia-inducible factor alpha regulation, PHD2, remained unknown.	Oxygen	182-188	egl-9 family hypoxia inducible factor 1	Homo sapiens	255-259
19546213-4	2009	Using peptide array binding assays, fluorescence spectroscopy, and fluorescence resonance energy transfer analysis, we defined a minimal linear glutamate-rich PHD2 binding domain in the N-terminal part of FKBP38 and showed that this domain forms a high affinity complex with PHD2.	Glutamic Acid	144-153	egl-9 family hypoxia inducible factor 1	Homo sapiens	159-163
19546213-4	2009	Using peptide array binding assays, fluorescence spectroscopy, and fluorescence resonance energy transfer analysis, we defined a minimal linear glutamate-rich PHD2 binding domain in the N-terminal part of FKBP38 and showed that this domain forms a high affinity complex with PHD2.	Glutamic Acid	144-153	egl-9 family hypoxia inducible factor 1	Homo sapiens	275-279
19631610-0	2009	Cellular oxygen sensing: Importins and exportins are mediators of intracellular localisation of prolyl-4-hydroxylases PHD1 and PHD2.	Oxygen	9-15	egl-9 family hypoxia inducible factor 1	Homo sapiens	127-131
19604478-5	2009	Together with biochemical analyses, the results reveal that PHD catalysis involves a mobile region that isolates the hydroxylation site and stabilizes the PHD2.Fe(II).2OG complex.	ammonium ferrous sulfate	160-166	egl-9 family hypoxia inducible factor 1	Homo sapiens	155-159
19304911-2	2009	Here, we tested the hypothesis that PHD2, a prolyl hydroxylase domain (PHD)-containing O(2) sensor, modulates growth factor-induced proliferative responses of human pulmonary artery SMC (HPASMC).	Oxygen	87-91	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-40
19498081-3	2009	Because PHD2 hydroxylates HIF-1alpha, with succinic acid produced as an end product, radiolabeled [5-(14)C]-2-oxoglutaric acid was used and formation of [14C]-succinic acid was measured to quantify PHD2(181-417) enzymatic activity.	Succinic Acid	43-56	egl-9 family hypoxia inducible factor 1	Homo sapiens	8-12
19498081-3	2009	Because PHD2 hydroxylates HIF-1alpha, with succinic acid produced as an end product, radiolabeled [5-(14)C]-2-oxoglutaric acid was used and formation of [14C]-succinic acid was measured to quantify PHD2(181-417) enzymatic activity.	14c]-succinic acid	154-172	egl-9 family hypoxia inducible factor 1	Homo sapiens	8-12
19498081-10	2009	The authors conclude that a by-product enzyme assay measuring the conversion of 2-oxoglutaric acid to succinic acid using the catalytic domain of the human PHD2 provides a convenient method for the biochemical evaluation of inhibitors of the 2-oxoglutaric acid-dependent hydroxylases.	Ketoglutaric Acids	80-98	egl-9 family hypoxia inducible factor 1	Homo sapiens	156-160
19498081-10	2009	The authors conclude that a by-product enzyme assay measuring the conversion of 2-oxoglutaric acid to succinic acid using the catalytic domain of the human PHD2 provides a convenient method for the biochemical evaluation of inhibitors of the 2-oxoglutaric acid-dependent hydroxylases.	Succinic Acid	102-115	egl-9 family hypoxia inducible factor 1	Homo sapiens	156-160
19304911-8	2009	Given the role of PHD2 as an oxygen sensor in mammalian cells, these results raise the possibility that PHD2 links VSMC proliferation to O(2) availability.	vsmc	115-119	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-22
19304911-3	2009	We found that both PHD1 and PHD2 were robustly expressed by HPASMC, and inhibiting prolyl hydroxylase activity pharmacologically by using the nonselective dioxygenase inhibitor dimethyloxalylglycine (DMOG) inhibited proliferation and cyclin A expression induced by PDGF-AB or FGF-2.	oxalylglycine	177-198	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
19304911-8	2009	Given the role of PHD2 as an oxygen sensor in mammalian cells, these results raise the possibility that PHD2 links VSMC proliferation to O(2) availability.	vsmc	115-119	egl-9 family hypoxia inducible factor 1	Homo sapiens	104-108
19304911-8	2009	Given the role of PHD2 as an oxygen sensor in mammalian cells, these results raise the possibility that PHD2 links VSMC proliferation to O(2) availability.	Oxygen	137-141	egl-9 family hypoxia inducible factor 1	Homo sapiens	104-108
19304911-3	2009	We found that both PHD1 and PHD2 were robustly expressed by HPASMC, and inhibiting prolyl hydroxylase activity pharmacologically by using the nonselective dioxygenase inhibitor dimethyloxalylglycine (DMOG) inhibited proliferation and cyclin A expression induced by PDGF-AB or FGF-2.	oxalylglycine	200-204	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
19304911-5	2009	The inhibitory effects of DMOG and PHD2 knockdown on proliferation and cyclin A expression were seen under both normoxic (20% O(2)) and moderately hypoxic (5% O(2)) conditions, and PHD2 expression was not affected by O(2) level nor by stimulation with PDGF or FGF-2, indicating that the proproliferative influence of PHD2 does not involve alterations of its expression.	oxalylglycine	26-30	egl-9 family hypoxia inducible factor 1	Homo sapiens	181-185
19304911-5	2009	The inhibitory effects of DMOG and PHD2 knockdown on proliferation and cyclin A expression were seen under both normoxic (20% O(2)) and moderately hypoxic (5% O(2)) conditions, and PHD2 expression was not affected by O(2) level nor by stimulation with PDGF or FGF-2, indicating that the proproliferative influence of PHD2 does not involve alterations of its expression.	oxalylglycine	26-30	egl-9 family hypoxia inducible factor 1	Homo sapiens	181-185
19304911-8	2009	Given the role of PHD2 as an oxygen sensor in mammalian cells, these results raise the possibility that PHD2 links VSMC proliferation to O(2) availability.	Oxygen	29-35	egl-9 family hypoxia inducible factor 1	Homo sapiens	18-22
19284310-7	2009	We identified two aptamers, WT-15 and SM-20, that disrupt the interactions between PAI-1 and heparin, as well as PAI-1 and vitronectin, without affecting the antiprotease activity of PAI-1.	Heparin	93-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	38-43
19455291-6	2009	Recent genetic data indicate that ECs sense an imbalance in oxygen levels, by using the oxygen-sensing prolyl hydroxylase PHD2.	Oxygen	60-66	egl-9 family hypoxia inducible factor 1	Homo sapiens	122-126
19455291-6	2009	Recent genetic data indicate that ECs sense an imbalance in oxygen levels, by using the oxygen-sensing prolyl hydroxylase PHD2.	Oxygen	88-94	egl-9 family hypoxia inducible factor 1	Homo sapiens	122-126
19277991-6	2009	HIF-1alpha stabilization was induced in cells cultured in 21% oxygen by treatment with dimethyloxaloglycine (DMOG) or siRNA targeted against PHD2.	Oxygen	62-68	egl-9 family hypoxia inducible factor 1	Homo sapiens	141-145
18776187-6	2008	Maximal PHD2 activity was found between 120 and 210 microm O2.	Oxygen	59-61	egl-9 family hypoxia inducible factor 1	Homo sapiens	8-12
19028544-3	2009	The nuclear localization of HIF-1alpha appeared to be triggered by the Al-induced perturbation of prolyl hydroxylase 2 (PHD2).	Aluminum	71-73	egl-9 family hypoxia inducible factor 1	Homo sapiens	98-118
19028544-3	2009	The nuclear localization of HIF-1alpha appeared to be triggered by the Al-induced perturbation of prolyl hydroxylase 2 (PHD2).	Aluminum	71-73	egl-9 family hypoxia inducible factor 1	Homo sapiens	120-124
19028544-5	2009	The fate of PHD2 and HIF-1alpha was intricately linked to the mitochondrial dysfunction observed during Al stress.	Aluminum	104-106	egl-9 family hypoxia inducible factor 1	Homo sapiens	12-16
19028544-7	2009	However, the treatment of the Al-stressed cells with KG recovered the activity and expression of KGDH, SDH, and PHD2 with a concomitant decrease in the levels of HIF-1alpha in the nucleus.	Aluminum	30-32	egl-9 family hypoxia inducible factor 1	Homo sapiens	112-116
18952043-5	2009	We demonstrated submicromolar affinities for 2-OG and ferrous iron and HIF-PHD2 Km values for oxygen that are greater than atmospheric oxygen levels, suggesting that molecular oxygen is indeed the key regulator of this pathway.	Oxygen	94-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	75-79
18952043-5	2009	We demonstrated submicromolar affinities for 2-OG and ferrous iron and HIF-PHD2 Km values for oxygen that are greater than atmospheric oxygen levels, suggesting that molecular oxygen is indeed the key regulator of this pathway.	Oxygen	135-141	egl-9 family hypoxia inducible factor 1	Homo sapiens	75-79
18952043-5	2009	We demonstrated submicromolar affinities for 2-OG and ferrous iron and HIF-PHD2 Km values for oxygen that are greater than atmospheric oxygen levels, suggesting that molecular oxygen is indeed the key regulator of this pathway.	Oxygen	135-141	egl-9 family hypoxia inducible factor 1	Homo sapiens	75-79
18952043-6	2009	In addition, we observed enhancement of HIF-PHD2 catalytic activity in the presence of ascorbic acid with only minor modifications of HIF-PHD2 requirements for 2-OG, and a detailed pH study demonstrated optimal HIF-PHD2 catalytic activity at pH 6.0.	Ascorbic Acid	87-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-48
20008248-4	2009	Congenital causes include mutations of the erythropoietin receptor and defects of the oxygen-sensing pathway including VHL, PHD2 and HIF2A mutations.	Oxygen	86-92	egl-9 family hypoxia inducible factor 1	Homo sapiens	124-128
19639506-0	2009	Expression of the cellular oxygen sensor PHD2 (EGLN-1) predicts radiation sensitivity in squamous cell cancer of the head and neck.	Oxygen	27-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	41-45
19639506-0	2009	Expression of the cellular oxygen sensor PHD2 (EGLN-1) predicts radiation sensitivity in squamous cell cancer of the head and neck.	Oxygen	27-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	47-53
19339211-5	2009	Treatment of cells with leptomycin B revealed that PHD2 was able to shuttle between the cytoplasm and the nucleus.	leptomycin B	24-36	egl-9 family hypoxia inducible factor 1	Homo sapiens	51-55
18776187-7	2008	PHD2 activity was strongly decreased below 100 microm O2 with a half-maximum activity at 53 +/- 13 microm O2 for the cytosolic and 54 +/- 10 microm O2 for nuclear PHD2 matching the physiological O2 concentration within most cells.	Oxygen	54-56	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
18776187-7	2008	PHD2 activity was strongly decreased below 100 microm O2 with a half-maximum activity at 53 +/- 13 microm O2 for the cytosolic and 54 +/- 10 microm O2 for nuclear PHD2 matching the physiological O2 concentration within most cells.	Oxygen	54-56	egl-9 family hypoxia inducible factor 1	Homo sapiens	163-167
18776187-7	2008	PHD2 activity was strongly decreased below 100 microm O2 with a half-maximum activity at 53 +/- 13 microm O2 for the cytosolic and 54 +/- 10 microm O2 for nuclear PHD2 matching the physiological O2 concentration within most cells.	Oxygen	106-108	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
18776187-7	2008	PHD2 activity was strongly decreased below 100 microm O2 with a half-maximum activity at 53 +/- 13 microm O2 for the cytosolic and 54 +/- 10 microm O2 for nuclear PHD2 matching the physiological O2 concentration within most cells.	Oxygen	106-108	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
18776187-7	2008	PHD2 activity was strongly decreased below 100 microm O2 with a half-maximum activity at 53 +/- 13 microm O2 for the cytosolic and 54 +/- 10 microm O2 for nuclear PHD2 matching the physiological O2 concentration within most cells.	Oxygen	106-108	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
18776187-8	2008	Our data suggest a role for PHD2 as a decisive oxygen sensor of the hypoxia-inducible factor degradation pathway within the cell nucleus.	Oxygen	47-53	egl-9 family hypoxia inducible factor 1	Homo sapiens	28-32
18927305-0	2008	Overexpression of the oxygen sensors PHD-1, PHD-2, PHD-3, and FIH Is associated with tumor aggressiveness in pancreatic endocrine tumors.	Oxygen	22-28	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-49
18710826-3	2008	Mammalian PHDs comprise three isozymes, PHD1, PHD2 and PHD3, and belong to the iron(II)-2-oxoglutarate-dependent dioxygenase family.	ammonium ferrous sulfate	79-87	egl-9 family hypoxia inducible factor 1	Homo sapiens	46-50
18834144-3	2008	Herein, we examine the biochemical characterization of PHD2 variants, Arg371His and Pro317Arg, identified from patients with familial erythrocytosis.	pro317arg	84-93	egl-9 family hypoxia inducible factor 1	Homo sapiens	55-59
18927305-2	2008	Our aim was to assess the expression of proteins that act as cellular oxygen sensors, directly regulating the hypoxia inducible factor (HIF) pathway, i.e., prolyl hydroxylase domain proteins (PHD)-1, PHD-2, PHD-3, and FIH in pancreatic endocrine tumors (PET).	Oxygen	70-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	200-205
18755588-1	2008	We report the structure-based design and synthesis of a novel series of aza-benzimidazoles as PHD2 inhibitors.	1H-imidazo(4,5-b)pyridine	72-90	egl-9 family hypoxia inducible factor 1	Homo sapiens	94-98
18579373-2	2008	From a screening hit, a series of novel hydroxyl-thiazoles were developed as potent PHD2 inhibitors.	hydroxyl-thiazoles	40-58	egl-9 family hypoxia inducible factor 1	Homo sapiens	84-88
18332861-6	2008	KEY RESULTS: We found a potent activator of PHD2, KRH102053 (2-amino-4-methylsulphanyl-butylic acid-4-methoxy-6-(4-methoxy-benzylamino)-2,2-dimethyl-chroman-3-yl ester).	2-amino-4-methylsulfanylbutyric acid 4-methoxy-6-(4-methoxybenzylamino)-2,2-dimethylchroman-3-yl ester	50-59	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-48
17725546-2	2007	The activity of these transcription factors is mainly determined by the stability of the HIFalpha subunit, which is regulated, in an oxygen-dependent manner, by a family of three prolyl 4-hydroxylases [EGLN1-EGLN3 (EGL nine homologues 1-3)].	Oxygen	133-139	egl-9 family hypoxia inducible factor 1	Homo sapiens	202-207
18332861-5	2008	EXPERIMENTAL APPROACH: By using the overproduced PHD2 as a target, a molecular library consisting of more than 600 small molecules with a benzopyran structure was screened with an HPLC assay method.	Benzopyrans	138-148	egl-9 family hypoxia inducible factor 1	Homo sapiens	49-53
17933562-7	2008	The genetic defects herein described are the first frameshift and nonsense mutations reported in the PHD2 gene and, as the previous missense mutation described, suggest that a decreased prolyl hydroxylase activity disturbing the oxygen-sensing pathway might be the cause of erythrocytosis.	Oxygen	229-235	egl-9 family hypoxia inducible factor 1	Homo sapiens	101-105
18072750-8	2008	Under exposure to TCDD or hypoxia, the main regulator of HIF-1 alpha stability, the prolyl hydroxylase domain containing protein 2 (PHD2) showed an increase in promoter activity, transcript numbers, and protein amount.	Polychlorinated Dibenzodioxins	18-22	egl-9 family hypoxia inducible factor 1	Homo sapiens	84-130
18072750-8	2008	Under exposure to TCDD or hypoxia, the main regulator of HIF-1 alpha stability, the prolyl hydroxylase domain containing protein 2 (PHD2) showed an increase in promoter activity, transcript numbers, and protein amount.	Polychlorinated Dibenzodioxins	18-22	egl-9 family hypoxia inducible factor 1	Homo sapiens	132-136
18072750-10	2008	The AhR-dependent regulation of PHD2 under normoxia, however, is overwritten by the TCDD-mediated destabilization of HIF-1 alpha.	Polychlorinated Dibenzodioxins	84-88	egl-9 family hypoxia inducible factor 1	Homo sapiens	32-36
18072750-11	2008	The destabilization of HIF-1 alpha is the dominant effect causing the reduced PHD2 expression after simultaneous exposure to TCDD and hypoxia.	Polychlorinated Dibenzodioxins	125-129	egl-9 family hypoxia inducible factor 1	Homo sapiens	78-82
17135241-4	2007	Under the assay conditions, no significant FIH inhibition was observed by the TCAIs or pyruvate, but fumarate, succinate, and isocitrate inhibited PHD2.	Fumarates	101-109	egl-9 family hypoxia inducible factor 1	Homo sapiens	147-151
17135241-4	2007	Under the assay conditions, no significant FIH inhibition was observed by the TCAIs or pyruvate, but fumarate, succinate, and isocitrate inhibited PHD2.	Succinic Acid	111-120	egl-9 family hypoxia inducible factor 1	Homo sapiens	147-151
17135241-4	2007	Under the assay conditions, no significant FIH inhibition was observed by the TCAIs or pyruvate, but fumarate, succinate, and isocitrate inhibited PHD2.	isocitric acid	126-136	egl-9 family hypoxia inducible factor 1	Homo sapiens	147-151
17135241-7	2007	The in vitro results suggest that the cellular inhibition of PHD2, but probably not FIH, by fumarate and succinate may play a role in the Warburg effect providing that appropriate relative concentrations of the components are achieved under physiological conditions.	Fumarates	92-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	61-65
17135241-7	2007	The in vitro results suggest that the cellular inhibition of PHD2, but probably not FIH, by fumarate and succinate may play a role in the Warburg effect providing that appropriate relative concentrations of the components are achieved under physiological conditions.	Succinic Acid	105-114	egl-9 family hypoxia inducible factor 1	Homo sapiens	61-65
16931007-1	2006	A new series of potent 8-hydroxyquinolines was designed based on the newly resolved X-ray crystal structure of EGLN-1.	Oxyquinoline	23-42	egl-9 family hypoxia inducible factor 1	Homo sapiens	111-117
16962772-1	2006	Utilizing modeling information from a recently resolved structure of human HIF-1alpha prolyl hydroxylase (EGLN1) and structure-based design, a novel series of imidazo[1,2-a]pyridine derivatives was prepared.	imidazo(1,2-a)pyridine	159-181	egl-9 family hypoxia inducible factor 1	Homo sapiens	106-111
16952279-2	2007	An oxygen consumption assay was developed and used to study the relationship between HIF hydroxylase activity and oxygen concentration for recombinant forms of two human HIF hydroxylases, PHD2 (prolyl hydroxylase domain-containing protein 2) and FIH (factor inhibiting HIF), and compared with two other 2OG-dependent dioxygenases.	Oxygen	3-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	188-192
16952279-2	2007	An oxygen consumption assay was developed and used to study the relationship between HIF hydroxylase activity and oxygen concentration for recombinant forms of two human HIF hydroxylases, PHD2 (prolyl hydroxylase domain-containing protein 2) and FIH (factor inhibiting HIF), and compared with two other 2OG-dependent dioxygenases.	Oxygen	3-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	194-240
16952279-2	2007	An oxygen consumption assay was developed and used to study the relationship between HIF hydroxylase activity and oxygen concentration for recombinant forms of two human HIF hydroxylases, PHD2 (prolyl hydroxylase domain-containing protein 2) and FIH (factor inhibiting HIF), and compared with two other 2OG-dependent dioxygenases.	Oxygen	114-120	egl-9 family hypoxia inducible factor 1	Homo sapiens	188-192
16952279-2	2007	An oxygen consumption assay was developed and used to study the relationship between HIF hydroxylase activity and oxygen concentration for recombinant forms of two human HIF hydroxylases, PHD2 (prolyl hydroxylase domain-containing protein 2) and FIH (factor inhibiting HIF), and compared with two other 2OG-dependent dioxygenases.	Oxygen	114-120	egl-9 family hypoxia inducible factor 1	Homo sapiens	194-240
16952279-3	2007	Although there are caveats on the absolute values, the apparent K(m) (oxygen) values for PHD2 and FIH were within the range observed for other 2OG oxygenases.	Oxygen	70-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	89-93
16952279-5	2007	The analyses also suggest that human PHD2 is selective for fragments of the C-terminal over the N-terminal oxygen-dependent degradation domain of HIF-1alpha.	Oxygen	107-113	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
17101841-1	2007	Prolyl hydroxylase domain 2 protein (PHD2) signals the degradation of hypoxia-inducible factor (HIF)-1alpha by hydroxylating specific prolyl residues located within oxygen-dependent degradation domains.	Peptide oostatic hormone	134-140	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
17101841-1	2007	Prolyl hydroxylase domain 2 protein (PHD2) signals the degradation of hypoxia-inducible factor (HIF)-1alpha by hydroxylating specific prolyl residues located within oxygen-dependent degradation domains.	Oxygen	165-171	egl-9 family hypoxia inducible factor 1	Homo sapiens	37-41
17056012-7	2006	Model building studies on the human HIF prolyl hydroxylase 2 showed that the two phenolate oxygen atoms of gallate form a chelate with the active site Fe(2+), while the carboxyl group of gallate forms a strong ionic/hydrogen bonding interaction with Arg383, explaining why nPG, which has an esterified carboxyl group, is unable to inhibit the hydroxylase.	Oxygen	91-97	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-60
17056012-7	2006	Model building studies on the human HIF prolyl hydroxylase 2 showed that the two phenolate oxygen atoms of gallate form a chelate with the active site Fe(2+), while the carboxyl group of gallate forms a strong ionic/hydrogen bonding interaction with Arg383, explaining why nPG, which has an esterified carboxyl group, is unable to inhibit the hydroxylase.	Gallic acid	107-114	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-60
17056012-7	2006	Model building studies on the human HIF prolyl hydroxylase 2 showed that the two phenolate oxygen atoms of gallate form a chelate with the active site Fe(2+), while the carboxyl group of gallate forms a strong ionic/hydrogen bonding interaction with Arg383, explaining why nPG, which has an esterified carboxyl group, is unable to inhibit the hydroxylase.	Iron	151-153	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-60
17056012-7	2006	Model building studies on the human HIF prolyl hydroxylase 2 showed that the two phenolate oxygen atoms of gallate form a chelate with the active site Fe(2+), while the carboxyl group of gallate forms a strong ionic/hydrogen bonding interaction with Arg383, explaining why nPG, which has an esterified carboxyl group, is unable to inhibit the hydroxylase.	Gallic acid	187-194	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-60
17056012-7	2006	Model building studies on the human HIF prolyl hydroxylase 2 showed that the two phenolate oxygen atoms of gallate form a chelate with the active site Fe(2+), while the carboxyl group of gallate forms a strong ionic/hydrogen bonding interaction with Arg383, explaining why nPG, which has an esterified carboxyl group, is unable to inhibit the hydroxylase.	Hydrogen	216-224	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-60
17056012-7	2006	Model building studies on the human HIF prolyl hydroxylase 2 showed that the two phenolate oxygen atoms of gallate form a chelate with the active site Fe(2+), while the carboxyl group of gallate forms a strong ionic/hydrogen bonding interaction with Arg383, explaining why nPG, which has an esterified carboxyl group, is unable to inhibit the hydroxylase.	Propyl Gallate	273-276	egl-9 family hypoxia inducible factor 1	Homo sapiens	36-60
16908149-2	2006	Pyridine carboxyamide derivatives bearing a substituted aryl group at the 5-position of the pyridine ring show appreciable activity, while constraining the side chain by placing a pyrazole carboxylic acid generated a potent lead series with consistent activity against EGLN-1.	pyridine carboxyamide	0-21	egl-9 family hypoxia inducible factor 1	Homo sapiens	269-275
16908149-2	2006	Pyridine carboxyamide derivatives bearing a substituted aryl group at the 5-position of the pyridine ring show appreciable activity, while constraining the side chain by placing a pyrazole carboxylic acid generated a potent lead series with consistent activity against EGLN-1.	pyridine	92-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	269-275
16908149-2	2006	Pyridine carboxyamide derivatives bearing a substituted aryl group at the 5-position of the pyridine ring show appreciable activity, while constraining the side chain by placing a pyrazole carboxylic acid generated a potent lead series with consistent activity against EGLN-1.	pyrazole carboxylic acid	180-204	egl-9 family hypoxia inducible factor 1	Homo sapiens	269-275
16509823-2	2006	Three oxygen-dependent prolyl hydroxylase enzymes [PHD1 (prolyl hydroxylase domain 1), PHD2 and PHD3] control the abundance of HIF.	Oxygen	6-12	egl-9 family hypoxia inducible factor 1	Homo sapiens	87-91
16893883-8	2006	Furthermore, this polybasic region binds specifically to PI(3)P when fused to maltose-binding protein, PHD2, or as an isolated peptide, demonstrating that it is sufficient for specific PI binding.	1,2-dipalmitoyl-sn-glycero-3-phospho-(1'D-myo-inositol-3'-phosphate)	57-63	egl-9 family hypoxia inducible factor 1	Homo sapiens	103-107
16565084-2	2006	These oxygen-sensitive modifications are catalyzed by members of the 2-oxoglutarate (2-OG) dioxygenase family (PHD1, PHD2, PHD3, and FIH-1), raising an important question regarding the extent of involvement of these and other enzymes of the same family in directing the global changes in gene expression that are induced by hypoxia.	Oxygen	6-12	egl-9 family hypoxia inducible factor 1	Homo sapiens	117-121
16611863-10	2006	EGLN1, EGLN2, and EGLN3 were also temporally expressed in an oxygen-dependent fashion, with greatest mRNA expression at 10-12 wk of gestation.	Oxygen	61-67	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-5
16782814-0	2006	Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).	Oxygen	9-15	egl-9 family hypoxia inducible factor 1	Homo sapiens	91-95
16782814-4	2006	We describe crystal structures of the catalytic domain of human PHD2, an important prolyl-4-hydroxylase in the human hypoxic response in normal cells, in complex with Fe(II) and an inhibitor to 1.7 A resolution.	ammonium ferrous sulfate	167-173	egl-9 family hypoxia inducible factor 1	Homo sapiens	64-68
16782814-5	2006	PHD2 crystallizes as a homotrimer and contains a double-stranded beta-helix core fold common to the Fe(II) and 2-oxoglutarate-dependant dioxygenase family, the residues of which are well conserved in the three human PHD enzymes (PHD 1-3).	ammonium ferrous sulfate	100-106	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
16565084-2	2006	These oxygen-sensitive modifications are catalyzed by members of the 2-oxoglutarate (2-OG) dioxygenase family (PHD1, PHD2, PHD3, and FIH-1), raising an important question regarding the extent of involvement of these and other enzymes of the same family in directing the global changes in gene expression that are induced by hypoxia.	Ketoglutaric Acids	69-83	egl-9 family hypoxia inducible factor 1	Homo sapiens	117-121
16585195-4	2006	Hydroxylation of two proline residues by prolyl hydroxylase domain (PHD) 2 protein earmarks the protein for degradation, whereas hydroxylation of an asparagine residue by factor-inhibiting HIF-1 (FIH-1 or FIH) reduces its transcriptional activity.	Proline	21-28	egl-9 family hypoxia inducible factor 1	Homo sapiens	68-74
16179542-7	2005	The upregulated genes are clustered in cell adhesion/cytoskeleton, extracellular matrix components, cell cycle, protein modification/phosphorylation, protein metabolism and transcription, and inflammation/hypoxia (e.g., key iron and oxygen sensor EGLN1) classes.	Iron	224-228	egl-9 family hypoxia inducible factor 1	Homo sapiens	247-252
16489060-6	2006	EXPERIMENTAL DESIGN: The expression of PHD2 was studied from paraffin-embedded normal tissue (n = 21) and head and neck squamous cell carcinoma (HNSCC; n = 44) by immunohistochemistry.	Paraffin	61-69	egl-9 family hypoxia inducible factor 1	Homo sapiens	39-43
16489060-14	2006	CONCLUSIONS: Our results show that increased levels and nuclear translocation of the cellular oxygen sensor, PHD2, are associated with less differentiated and strongly proliferating tumors.	Oxygen	94-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	109-113
16185289-6	2005	HIF-1 is composed of two subunits, HIF-1alpha and HIF-1beta, and HIF-1 activity depends mainly on the intracellular level of HIF-1alpha protein, which is regulated to be in inverse relation to the oxygen concentration by an oxygen-dependent enzyme, prolyl hydroxylase 2 (PHD2).	Oxygen	197-203	egl-9 family hypoxia inducible factor 1	Homo sapiens	249-269
16185289-6	2005	HIF-1 is composed of two subunits, HIF-1alpha and HIF-1beta, and HIF-1 activity depends mainly on the intracellular level of HIF-1alpha protein, which is regulated to be in inverse relation to the oxygen concentration by an oxygen-dependent enzyme, prolyl hydroxylase 2 (PHD2).	Oxygen	197-203	egl-9 family hypoxia inducible factor 1	Homo sapiens	271-275
16185289-7	2005	Thus, cells respond to tissue hypoxia by sensing the oxygen concentration as the enzyme activity of PHD2, regulating the HIF-1 activity and consequently changing the expression of various hypoxia-responsive molecules.	Oxygen	53-59	egl-9 family hypoxia inducible factor 1	Homo sapiens	100-104
16880998-0	2005	Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate.	Iron	70-82	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-45
16880998-0	2005	Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate.	Ketoglutaric Acids	87-101	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-45
16880998-1	2005	Regulation of the hypoxic response in humans is regulated by the post-translational hydroxylation of hypoxia inducible transcription factor; a recombinant form of a human prolyl-4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity for, and to copurify with endogenous levels of, its Fe(ii) cofactor and 2-oxoglutarate cosubstrate.	ammonium ferrous sulfate	317-323	egl-9 family hypoxia inducible factor 1	Homo sapiens	193-197
16880998-1	2005	Regulation of the hypoxic response in humans is regulated by the post-translational hydroxylation of hypoxia inducible transcription factor; a recombinant form of a human prolyl-4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity for, and to copurify with endogenous levels of, its Fe(ii) cofactor and 2-oxoglutarate cosubstrate.	Ketoglutaric Acids	337-351	egl-9 family hypoxia inducible factor 1	Homo sapiens	193-197
15563275-4	2005	Therefore PHD2 is regarded as the main cellular oxygen sensor.	Oxygen	48-54	egl-9 family hypoxia inducible factor 1	Homo sapiens	10-14
16024780-8	2005	In these domain-swapping experiments, prolyl hydroxylase domain 1 (PHD1) and PHD2 preferentially hydroxylated the proline located in the site of the original 564 ODD, while PHD3 preferred the proline 564 sequence, regardless of its location.	Proline	114-121	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-81
16024780-8	2005	In these domain-swapping experiments, prolyl hydroxylase domain 1 (PHD1) and PHD2 preferentially hydroxylated the proline located in the site of the original 564 ODD, while PHD3 preferred the proline 564 sequence, regardless of its location.	Proline	192-199	egl-9 family hypoxia inducible factor 1	Homo sapiens	77-81
14984367-10	2004	Pyruvate and oxaloacetate treatment of cells also up-regulates HPH-1 and HPH-2, but not HPH-3 or the HIF asparaginyl hydroxylase FIH-1 (factor inhibiting HIF).	Pyruvic Acid	0-8	egl-9 family hypoxia inducible factor 1	Homo sapiens	73-78
15474027-3	2004	We show that all three are capable of high rates of catalysis, in the order PHD2=PHD3>PHD1, using substrate peptides derived from the C-terminal degradation domain of HIF-alpha subunits, and that each demonstrates similar and remarkable sensitivity to oxygen, commensurate with a common role in signaling hypoxia.	Oxygen	255-261	egl-9 family hypoxia inducible factor 1	Homo sapiens	76-80
15455214-4	2004	Up-regulated genes, clustered mainly in biological processes involving cell adhesion/cytoskeleton, extracellular matrix components, cell cycle, protein modification/phosphorylation, protein metabolism, transcription and inflammation/stress (e.g. key iron and oxygen sensor EGLN1).	Iron	250-254	egl-9 family hypoxia inducible factor 1	Homo sapiens	273-278
15455214-4	2004	Up-regulated genes, clustered mainly in biological processes involving cell adhesion/cytoskeleton, extracellular matrix components, cell cycle, protein modification/phosphorylation, protein metabolism, transcription and inflammation/stress (e.g. key iron and oxygen sensor EGLN1).	Oxygen	259-265	egl-9 family hypoxia inducible factor 1	Homo sapiens	273-278
15302861-7	2004	Evidence for FIH activity in severely hypoxic cells contrasted with results for the prolyl hydroxylase PHD2, suggesting that these enzymes display different oxygen dependence in vivo, with PHD2 requiring higher levels of oxygen for biological activity.	Oxygen	221-227	egl-9 family hypoxia inducible factor 1	Homo sapiens	189-193
14984367-10	2004	Pyruvate and oxaloacetate treatment of cells also up-regulates HPH-1 and HPH-2, but not HPH-3 or the HIF asparaginyl hydroxylase FIH-1 (factor inhibiting HIF).	Oxaloacetic Acid	13-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	73-78
15084514-6	2004	We show here that the role of Leu-574 is to recruit PHD2/HPH2 for Pro-564 hydroxylation.	Leucine	30-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	52-56
15084514-6	2004	We show here that the role of Leu-574 is to recruit PHD2/HPH2 for Pro-564 hydroxylation.	Leucine	30-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	57-61
15084514-6	2004	We show here that the role of Leu-574 is to recruit PHD2/HPH2 for Pro-564 hydroxylation.	Proline	66-69	egl-9 family hypoxia inducible factor 1	Homo sapiens	52-56
15084514-6	2004	We show here that the role of Leu-574 is to recruit PHD2/HPH2 for Pro-564 hydroxylation.	Proline	66-69	egl-9 family hypoxia inducible factor 1	Homo sapiens	57-61
15084514-9	2004	Furthermore, mutation of Leu-574 disrupts the binding of PHD2/HPH2, a key prolyl hydroxylase for oxygen-dependent proteolysis of HIF-1alpha.	Leucine	25-28	egl-9 family hypoxia inducible factor 1	Homo sapiens	57-61
15084514-9	2004	Furthermore, mutation of Leu-574 disrupts the binding of PHD2/HPH2, a key prolyl hydroxylase for oxygen-dependent proteolysis of HIF-1alpha.	Leucine	25-28	egl-9 family hypoxia inducible factor 1	Homo sapiens	62-66
15084514-9	2004	Furthermore, mutation of Leu-574 disrupts the binding of PHD2/HPH2, a key prolyl hydroxylase for oxygen-dependent proteolysis of HIF-1alpha.	Oxygen	97-103	egl-9 family hypoxia inducible factor 1	Homo sapiens	57-61
15084514-9	2004	Furthermore, mutation of Leu-574 disrupts the binding of PHD2/HPH2, a key prolyl hydroxylase for oxygen-dependent proteolysis of HIF-1alpha.	Oxygen	97-103	egl-9 family hypoxia inducible factor 1	Homo sapiens	62-66
15084514-10	2004	Hence, our findings indicate that Leu-574 is essential for recruiting PHD2/HPH2, thereby providing a molecular basis for modulating HIF-1alpha activity.	Leucine	34-37	egl-9 family hypoxia inducible factor 1	Homo sapiens	70-74
15084514-10	2004	Hence, our findings indicate that Leu-574 is essential for recruiting PHD2/HPH2, thereby providing a molecular basis for modulating HIF-1alpha activity.	Leucine	34-37	egl-9 family hypoxia inducible factor 1	Homo sapiens	75-79
12839937-8	2003	In addition, we found a number of other hypoxia-inducible genes up-regulated by nickel in a HIF-dependent manner including BCL-2-binding protein Nip3, EGLN1, hypoxia-inducible gene 1 (HIG1), and prolyl 4-hydroxylase.	Nickel	80-86	egl-9 family hypoxia inducible factor 1	Homo sapiens	151-156
12912907-0	2003	HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia.	Oxygen	36-42	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-24
12912907-6	2003	We therefore conclude that, in vivo, PHDs have distinct assigned functions, PHD2 being the critical oxygen sensor setting the low steady-state levels of HIF-1alpha in normoxia.	Oxygen	100-106	egl-9 family hypoxia inducible factor 1	Homo sapiens	76-80
12912907-7	2003	Interestingly, PHD2 is upregulated by hypoxia, providing an HIF-1-dependent auto-regulatory mechanism driven by the oxygen tension.	Oxygen	116-122	egl-9 family hypoxia inducible factor 1	Homo sapiens	15-19
12670503-1	2003	Three HIF-alpha prolyl-4-hydroxylases (PHDs) (named PHD1, PHD2, and PHD3) effect the proteasome-mediated degradation of HIF by catalyzing the hydroxylation of key proline residues in the HIF-1 alpha subunit under normoxic conditions.	Proline	163-170	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-62
12670503-4	2003	Treatment of human cardiac myocytes, smooth muscle cells, and endothelial cells with hypoxia or CoCl(2), a hypoxia mimic, resulted in a significant time-dependent increase in PHD3, but not PHD1 or PHD2, mRNA levels, which correlated with an increase in HIF-1 alpha protein expression.	cobaltous chloride	96-103	egl-9 family hypoxia inducible factor 1	Homo sapiens	197-201
12163023-3	2002	Under normoxia, two highly conserved proline residues within the oxygen-dependent degradation domain (ODDD) are hydroxylated by oxoglutarate-dependent proline 4-hydroxylases EGLN1-3.	Proline	37-44	egl-9 family hypoxia inducible factor 1	Homo sapiens	174-179
12615973-3	2003	Three human oxygen-dependent HIF-1 alpha prolyl hydroxylases (PHD1, PHD2, and PHD3) function as oxygen sensors in vivo.	Oxygen	12-18	egl-9 family hypoxia inducible factor 1	Homo sapiens	68-72
12615973-3	2003	Three human oxygen-dependent HIF-1 alpha prolyl hydroxylases (PHD1, PHD2, and PHD3) function as oxygen sensors in vivo.	Oxygen	96-102	egl-9 family hypoxia inducible factor 1	Homo sapiens	68-72
12570801-5	2003	Finally, we will present recent advances into oxygen-sensing, in particular the HIF-hydroxylases that govern HIF-1alpha instability (PHD2) or inactivation (FIH-1).	Oxygen	46-52	egl-9 family hypoxia inducible factor 1	Homo sapiens	133-137
12163023-3	2002	Under normoxia, two highly conserved proline residues within the oxygen-dependent degradation domain (ODDD) are hydroxylated by oxoglutarate-dependent proline 4-hydroxylases EGLN1-3.	Oxygen	65-71	egl-9 family hypoxia inducible factor 1	Homo sapiens	174-179
34265075-10	2021	Lastly, targeted metabolomic studies revealed that intracellular lactate and succinate correlated with PHD2 activity.	Lactic Acid	65-72	egl-9 family hypoxia inducible factor 1	Homo sapiens	103-107
12234095-1	2002	The mammalian EGLN family contains three paralagous genes (EGLN1, EGLN2, and EGLN3) encoding prolyl hydroxylase isoforms that mediate the oxygen-dependent targeting of the transcription factor hypoxia inducible factor alpha to the proteosome.	Oxygen	138-144	egl-9 family hypoxia inducible factor 1	Homo sapiens	59-64
10386996-4	1999	Expression of SM-20 also increases during neuronal death caused by cytosine arabinoside or the phosphatidylinositol 3-kinase inhibitor LY294002.	Cytarabine	67-87	egl-9 family hypoxia inducible factor 1	Homo sapiens	14-19
10386996-4	1999	Expression of SM-20 also increases during neuronal death caused by cytosine arabinoside or the phosphatidylinositol 3-kinase inhibitor LY294002.	Phosphatidylinositols	95-115	egl-9 family hypoxia inducible factor 1	Homo sapiens	14-19
10386996-4	1999	Expression of SM-20 also increases during neuronal death caused by cytosine arabinoside or the phosphatidylinositol 3-kinase inhibitor LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	135-143	egl-9 family hypoxia inducible factor 1	Homo sapiens	14-19
26053282-7	2015	Consistent with the phenotype, EGLN1 in Tibetans has a gain-of-function mutation that confers a higher affinity for oxygen, hence less sensitivity to hypoxia.	Oxygen	116-122	egl-9 family hypoxia inducible factor 1	Homo sapiens	31-36
26053282-12	2015	It should also be considered in future work in the field that because iron is a cofactor for EGLN1, there may be significant associations of phenotypes with the significant degrees of variation seen in tissue iron among human populations.	Iron	70-74	egl-9 family hypoxia inducible factor 1	Homo sapiens	93-98
26053282-12	2015	It should also be considered in future work in the field that because iron is a cofactor for EGLN1, there may be significant associations of phenotypes with the significant degrees of variation seen in tissue iron among human populations.	Iron	209-213	egl-9 family hypoxia inducible factor 1	Homo sapiens	93-98
34773469-0	2022	PHD2 attenuates high-glucose-induced blood retinal barrier breakdown in human retinal microvascular endothelial cells by regulating the Hif-1alpha/VEGF pathway.	Glucose	21-28	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-4
34773469-11	2022	The PHD2 activator R59949 (diacylglycerol kinase inhibitor II), altered these pathological changes, and the PHD2 inhibitor dimethyloxalylglycine (DMOG) resulted in the opposite effects.	R 59949	19-25	egl-9 family hypoxia inducible factor 1	Homo sapiens	4-8
34773469-11	2022	The PHD2 activator R59949 (diacylglycerol kinase inhibitor II), altered these pathological changes, and the PHD2 inhibitor dimethyloxalylglycine (DMOG) resulted in the opposite effects.	oxalylglycine	123-144	egl-9 family hypoxia inducible factor 1	Homo sapiens	108-112
34773469-11	2022	The PHD2 activator R59949 (diacylglycerol kinase inhibitor II), altered these pathological changes, and the PHD2 inhibitor dimethyloxalylglycine (DMOG) resulted in the opposite effects.	oxalylglycine	146-150	egl-9 family hypoxia inducible factor 1	Homo sapiens	108-112
34773469-13	2022	Therefore, it is reasonable to propose that PHD2 could be a potential novel target for the treatment of DME or other diseases with a similar pathogenesis.	dme	104-107	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-48
34265075-10	2021	Lastly, targeted metabolomic studies revealed that intracellular lactate and succinate correlated with PHD2 activity.	Succinic Acid	77-86	egl-9 family hypoxia inducible factor 1	Homo sapiens	103-107
34587217-7	2021	The percentage of time spent above the criterion HR was also significantly lower in SM-20:10 compared to all other protocols (Ergo-60:60 13.9+-4.9min, BW-60:60 13.5+-3.5min, SM-40:20 12.1+-2.4min, SM-20:10 7.7+-3.1, P<0.05).	Samarium	174-176	egl-9 family hypoxia inducible factor 1	Homo sapiens	84-89
34502144-8	2021	AuNP@PLA in combination with desloratadine was proven to induce PHD-2 silencing in fibroblasts, allowing upregulation of pro-angiogenic pathways.	desloratadine	29-42	egl-9 family hypoxia inducible factor 1	Homo sapiens	64-69
34137488-0	2021	Carbon monoxide is an inhibitor of HIF prolyl hydroxylase domain 2.	Carbon Monoxide	0-15	egl-9 family hypoxia inducible factor 1	Homo sapiens	39-66
34137488-1	2021	Hypoxia-inducible factor prolyl hydroxylase domain 2 (PHD2) is an important oxygen sensor in animals.	Oxygen	76-82	egl-9 family hypoxia inducible factor 1	Homo sapiens	54-58
35415275-10	2022	In this review, we will summarize the state of current knowledge on the role and mechanism of action of PHD2 as oxygen sensor in regulating bone metabolism.	Oxygen	112-118	egl-9 family hypoxia inducible factor 1	Homo sapiens	104-108
35192944-6	2022	Myricetin was identified as a novel potent PHD2 inhibitor by high-throughput screening of a natural compound library.	myricetin	0-9	egl-9 family hypoxia inducible factor 1	Homo sapiens	43-47
35517429-8	2022	This effect could be weakened in the presence of dimethyloxalylglycine (DMOG), suggesting that EGLN1 down-regulated p53 based on its hydroxylase activity.	oxalylglycine	49-70	egl-9 family hypoxia inducible factor 1	Homo sapiens	95-100
35517429-8	2022	This effect could be weakened in the presence of dimethyloxalylglycine (DMOG), suggesting that EGLN1 down-regulated p53 based on its hydroxylase activity.	oxalylglycine	72-76	egl-9 family hypoxia inducible factor 1	Homo sapiens	95-100
34102396-10	2021	Hereafter, we also attempted to resolve hypoxia-triggered inflammation in vitro as well as in vivo by augmenting the function of PHD2 using alpha-ketoglutarate (alphaKG), a co-factor of PHD2.	Ketoglutaric Acids	140-159	egl-9 family hypoxia inducible factor 1	Homo sapiens	129-133
34102396-10	2021	Hereafter, we also attempted to resolve hypoxia-triggered inflammation in vitro as well as in vivo by augmenting the function of PHD2 using alpha-ketoglutarate (alphaKG), a co-factor of PHD2.	Ketoglutaric Acids	140-159	egl-9 family hypoxia inducible factor 1	Homo sapiens	186-190
35112795-8	2022	Meanwhile, TSL administration facilitated the interaction of the Hif-1alpha/PHD2 complex and restored the Hif-1alpha protein level increased by PM2.5.	tussilagone	11-14	egl-9 family hypoxia inducible factor 1	Homo sapiens	76-80
35452683-0	2022	EGLN1 prolyl hydroxylation of hypoxia-induced transcription factor HIF1alpha is repressed by SET7-catalyzed lysine methylation.	Lysine	108-114	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-5
35452683-1	2022	Egg laying defective nine 1 (EGLN1) functions as an oxygen sensor to catalyze prolyl hydroxylation of the transcription factor hypoxia-inducible factor-1 alpha (HIF1alpha) under normoxia conditions, leading to its proteasomal degradation.	Oxygen	52-58	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-27
35452683-1	2022	Egg laying defective nine 1 (EGLN1) functions as an oxygen sensor to catalyze prolyl hydroxylation of the transcription factor hypoxia-inducible factor-1 alpha (HIF1alpha) under normoxia conditions, leading to its proteasomal degradation.	Oxygen	52-58	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-34
35452683-1	2022	Egg laying defective nine 1 (EGLN1) functions as an oxygen sensor to catalyze prolyl hydroxylation of the transcription factor hypoxia-inducible factor-1 alpha (HIF1alpha) under normoxia conditions, leading to its proteasomal degradation.	Peptide oostatic hormone	78-84	egl-9 family hypoxia inducible factor 1	Homo sapiens	0-27
35452683-1	2022	Egg laying defective nine 1 (EGLN1) functions as an oxygen sensor to catalyze prolyl hydroxylation of the transcription factor hypoxia-inducible factor-1 alpha (HIF1alpha) under normoxia conditions, leading to its proteasomal degradation.	Peptide oostatic hormone	78-84	egl-9 family hypoxia inducible factor 1	Homo sapiens	29-34
35452683-3	2022	Here, we identified that a lysine monomethylase, SET7, catalyzes EGLN1 methylation on lysine 297, resulting in the repression of EGLN1 activity in catalyzing prolyl hydroxylation of HIF1alpha.	Lysine	27-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	65-70
35452683-3	2022	Here, we identified that a lysine monomethylase, SET7, catalyzes EGLN1 methylation on lysine 297, resulting in the repression of EGLN1 activity in catalyzing prolyl hydroxylation of HIF1alpha.	Lysine	27-33	egl-9 family hypoxia inducible factor 1	Homo sapiens	129-134
35452683-3	2022	Here, we identified that a lysine monomethylase, SET7, catalyzes EGLN1 methylation on lysine 297, resulting in the repression of EGLN1 activity in catalyzing prolyl hydroxylation of HIF1alpha.	Lysine	86-92	egl-9 family hypoxia inducible factor 1	Homo sapiens	65-70
35452683-3	2022	Here, we identified that a lysine monomethylase, SET7, catalyzes EGLN1 methylation on lysine 297, resulting in the repression of EGLN1 activity in catalyzing prolyl hydroxylation of HIF1alpha.	Lysine	86-92	egl-9 family hypoxia inducible factor 1	Homo sapiens	129-134
35452683-4	2022	Notably, we demonstrate that the methylation mimic mutant of EGLN1 loses the capability to suppress the hypoxia signaling pathway, leading to the enhancement of cell proliferation and the oxygen consumption rate.	Oxygen	188-194	egl-9 family hypoxia inducible factor 1	Homo sapiens	61-66
35010112-8	2022	This method also enabled two clinically used inhibitors-vadadustat and roxadustat-to be loaded into liposomes with a high encapsulation efficiency, indicating its generality to load other heterocyclic glycinamide PHD2 inhibitors.	vadadustat	56-66	egl-9 family hypoxia inducible factor 1	Homo sapiens	213-217
35010112-8	2022	This method also enabled two clinically used inhibitors-vadadustat and roxadustat-to be loaded into liposomes with a high encapsulation efficiency, indicating its generality to load other heterocyclic glycinamide PHD2 inhibitors.	roxadustat	71-81	egl-9 family hypoxia inducible factor 1	Homo sapiens	213-217
35010112-8	2022	This method also enabled two clinically used inhibitors-vadadustat and roxadustat-to be loaded into liposomes with a high encapsulation efficiency, indicating its generality to load other heterocyclic glycinamide PHD2 inhibitors.	glycine amide	201-212	egl-9 family hypoxia inducible factor 1	Homo sapiens	213-217