Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589

Molecular cloning: A laboratory manual

Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684

Molecular classification of cancer: class discovery and class prediction by gene expression monitoring

Golub, T. R., Slonim, D. K., Tamayo, P., Huard, C., Gaasenbeek, M., Mesirov, J. P., Coller, H., Loh, M. L., Downing, J. R., Caligiuri, M. A., et al. (1999) · Science · doi:10.1126/science.286.5439.531 · Cited by 11,516

PGC-1α-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes

Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197

Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation

Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535

The Connectivity Map: Using Gene-Expression Signatures to Connect Small Molecules, Genes, and Disease

Lamb, J., Crawford, E. D., Peck, D., Modell, J. W., Blat, I. C., Wrobel, M. J., Lerner, J., Brunet, J.-P., Subramanian, A., Ross, K. N., et al. (2006) · Science · doi:10.1126/science.1132939 · Cited by 5,257

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180

HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing

Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735

A Third-Generation Lentivirus Vector with a Conditional Packaging System

Dull, T., Zufferey, R., Kelly, M., Mandel, R. J., Nguyen, M., Trono, D., & Naldini, L. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.8463-8471.1998 · Cited by 3,341

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333

Elevation of iron storage in humans attenuates the pulmonary vascular response to hypoxia

Bart, N., Curtis, M. K., Cheng, H., Hungerford, S. L., McLaren, R., Petousi, N., Dorrington, K. L., & Robbins, P. A. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00032.2016 · Cited by 30

Loss of vhl in the zebrafish pronephros recapitulates early stages of human clear cell renal cell carcinoma

Noonan, H. R., Metelo, A. M., Kamei, C. N., Peterson, R. T., Drummond, I. A. S., & Iliopoulos, O. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.024380 · Cited by 28

Basal expression of copper transporter 1 in intestinal epithelial cells is regulated by hypoxia‐inducible factor 2α

Pourvali, K., Matak, P., Latunde-Dada, G. O., Solomou, S., Mastrogiannaki, M., Peyssonnaux, C., & Sharp, P. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.05.058 · Cited by 29

Suppressive effects of iron chelation in clear cell renal cell carcinoma and their dependency on VHL inactivation

Greene, C., Sharma, N. J., Fiorica, P. N., Forrester, E. J., Smith, G. J., Gross, K. W., & KAUFFMAN, E. C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.013 · Cited by 28

Methods for identifying and characterizing interactions involving RNA

Blakeley, B. D., DePorter, S. M., Mohan, U., Burai, R., Tolbert, B. S., & McNaughton, B. R. (2012) · Tetrahedron · doi:10.1016/j.tet.2012.07.001 · Cited by 26

Friedreich Ataxia

Pandolfo, M. (2012) · Journal of Child Neurology · doi:10.1177/0883073812448534 · Cited by 26

Necdin Controls Proliferation and Apoptosis of Embryonic Neural Stem Cells in an Oxygen Tension-Dependent Manner

Huang, Z., Fujiwara, K., Minamide, R., Hasegawa, K., & Yoshikawa, K. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5682-12.2013 · Cited by 25

Human Folliculin Delays Cell Cycle Progression through Late S and G2/M-Phases: Effect of Phosphorylation and Tumor Associated Mutations

Laviolette, L. A., Wilson, J., Koller, J., Neil, C. R., Hulick, P. J., Rejtar, T., Karger, B. L., Teh, B. T., & Iliopoulos, O. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066775 · Cited by 24

AQP1 Is Up-Regulated by Hypoxia and Leads to Increased Cell Water Permeability, Motility, and Migration in Neuroblastoma

Huo, Z., Lomora, M., Kym, U., Palivan, C. G., Holland-Cunz, S. G., & Gros, S. J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.605272 · Cited by 23

Brain iron metabolism and its perturbation in neurological diseases

Crichton, R. R., Dexter, D. T., & Ward, R. J. (2011) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-011-0472-z · Cited by 23

HuR and other turnover- and translation-regulatory RNA-binding proteins: implications for the kidney

Pullmann, R., & Rabb, H. (2014) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00270.2013 · Cited by 24

Molecular targets on the horizon for kidney and urothelial cancer

Joaquim Bellmunt, B., Teh, B. T., Tortora, G., & Rosenberg, J. E. (2013) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2013.155 · Cited by 24

Brain iron metabolism and its perturbation in neurological diseases

Crichton, R. R., Dexter, D. T., & Ward, R. J. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_1 · Cited by 22

Targeting HIF2α Translation with Tempol in VHL-Deficient Clear Cell Renal Cell Carcinoma

Sourbier, C., Srivastava, G. K., Ghosh, M. C., Ghosh, S., Yang, Y., Gupta, G. N., DeGraff, W., Krishna, M. C., Mitchell, J. B., Rouault, T. A., et al. (2012) · Oncotarget · doi:10.18632/oncotarget.561 · Cited by 23

Coalescing lessons from oxygen sensing, tumor metabolism, and epigenetics to target VHL loss in kidney cancer

Chakraborty, A. A. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.03.012 · Cited by 22

HIF2a inhibitors for the treatment of VHL disease

Metelo, A. M., Noonan, H. R., & Iliopoulos, O. (2015) · Oncotarget · doi:10.18632/oncotarget.4564 · Cited by 21

Updated perspective of EPAS1 and the role in pulmonary hypertension

Wang, N., Hua, J., Fu, Y., An, J., Chen, X., Wang, C., Zheng, Y., Wang, F., Ji, Y., & Li, Q. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1125723 · Cited by 20

A novel splicing site IRP1 somatic mutation in a patient with pheochromocytoma and JAK2V617F positive polycythemia vera: a case report

Pang, Y. K., Gupta, G., Yang, C., Wang, H., Huynh, T., Abdullaev, Z., Pack, S., Percy, M. J., Lappin, T. R. J., Zhuang, Z., et al. (2018) · BMC Cancer · doi:10.1186/s12885-018-4127-x · Cited by 20

Loss of Endothelial Hypoxia Inducible Factor‐Prolyl Hydroxylase 2 Induces Cardiac Hypertrophy and Fibrosis

Dai, Z., Cheng, J., Liu, B., Yi, D., Feng, A., Wang, T., An, L., Gao, C., Wang, Y., Zhu, M. M., et al. (2021) · Journal of the American Heart Association · doi:10.1161/jaha.121.022077 · Cited by 20

Iron Prevents Hypoxia-Associated Inflammation Through the Regulation of Nuclear Factor-κB in the Intestinal Epithelium

Simmen, S., Cosín‐Roger, J., Melhem, H., Maliachovas, N., Maane, M., Baebler, K., Weder, B., Maeyashiki, C., Spanaus, K. S., Scharl, M. M., et al. (2018) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2018.10.006 · Cited by 19

Prevalent RNA recognition motif duplication in the human genome

Tsai, Y., Gomez, S. M., & Wang, Z. (2014) · RNA · doi:10.1261/rna.044081.113 · Cited by 19

Host and microbiota derived extracellular vesicles: Crucial players in iron homeostasis

Daou, Y., Falabrègue, M., Pourzand, C., Peyssonnaux, C., & Edeas, M. A. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.985141 · Cited by 19

Discovery of a murine model of clinical PAH: Mission impossible?

Dai, Z., & Zhao, Y. (2016) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2016.12.003 · Cited by 19

Regulatory and Sensing Iron–Sulfur Clusters: New Insights and Unanswered Questions

SantaMaria, A. M., & Rouault, T. A. (2024) · Inorganics · doi:10.3390/inorganics12040101 · Cited by 17

Implications of Oxygen Homeostasis for Tumor Biology and Treatment

Garvalov, B. K., & Acker, T. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-7678-9_12 · Cited by 17

Mechanisms of Ferroptosis and Application to Head and Neck Squamous Cell Carcinoma Treatments

Li, S., Liu, Y., Li, J., Zhao, X. B., & Yu, D. (2021) · DNA and Cell Biology · doi:10.1089/dna.2021.0023 · Cited by 16

Radiation Therapy for Glioma Stem Cells

Rizzo, A. E., & Yu, J. S. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-16537-0_6 · Cited by 15

Combined Analyses of the VHL and Hypoxia Signaling Axes in an Isogenic Pairing of Renal Clear Cell Carcinoma Cells

Malec, V., Coulson, J. M., Urbé, S., & Clague, M. J. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00692 · Cited by 13

Iron–Sulfur Cluster Metabolism Impacts Iron Homeostasis, Ferroptosis Sensitivity, and Human Disease

Sviderskiy, V. O., Terzi, E. M., & Possemato, R. (2019) · Springer eBooks · doi:10.1007/978-3-030-26780-3_12 · Cited by 12

Therapeutic Strategies for Patients With Metastatic Renal Cell Carcinoma in Whom First-Line Vascular Endothelial Growth Factor Receptor–Directed Therapies Fail

Malouf, G. G., Flippot, R., & Khayat, D. (2016) · Journal of Oncology Practice · doi:10.1200/jop.2016.011809 · Cited by 12

Rethinking IRPs/IRE system in neurodegenerative disorders: Looking beyond iron metabolism

Yao, Z., Fu, L., Jia, F., Bi, M., Jiao, Q., Chen, X., Du, X., & Jiang, H. F. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101511 · Cited by 11

Evaluation of the iron regulatory protein-1 interactome

Connell, G. J., Danial, J. S., & Haastruthers, C. X. (2018) · BioMetals · doi:10.1007/s10534-018-0076-8 · Cited by 11

Development of small molecule inhibitors of hypoxia-inducible factors for cancer therapy

Semenza, G. L. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100075 · Cited by 10

Notch3 is involved in the proliferation of renal cancer cells via regulation of cell cycle progression and HIF‑2α

Han, Q., Han, F., Fan, Y., Lian, B., Xiao, J., Sun, W., Han, D., Kou, H., Li, C., & Wu, B. (2020) · Oncology Letters · doi:10.3892/ol.2020.12242 · Cited by 10

NADPH Oxidase 4: Crucial for Endothelial Function under Hypoxia—Complementing Prostacyclin

Brendel, H., Mittag, J., Hofmann, A., Hempel, H., Giebe, S., Diaba‐Nuhoho, P., Wolk, S., Reeps, C., Morawietz, H., & Brunßen, C. (2024) · Antioxidants · doi:10.3390/antiox13101178 · Cited by 9

Nucleolin Regulates Pulmonary Artery Smooth Muscle Cell Proliferation under Hypoxia by Modulating miRNA Expression

Lee, J., & Kang, H. (2023) · Cells · doi:10.3390/cells12050817 · Cited by 9

Zebrafish as a model for von Hippel Lindau and hypoxia-inducible factor signaling

Kim, H. R., Greenald, D., Vettori, A., Markham, E., Santhakumar, K., Argenton, F., & van Eeden, F. J. M. (2016) · Methods in cell biology · doi:10.1016/bs.mcb.2016.07.001 · Cited by 9

Macrophage Migration Inhibitory Factor Acts as the Potential Target of a Newly Synthesized Compound, 1-(9′-methyl-3′-carbazole)-3, 4-dihydro-β-carboline

Ko, P., Shen, Y., Murugan, K., Huang, C.-W., Sivakumar, G., Pal, P., Liao, C., Luo, K.-S., Chuang, E. Y.-Y., Tsai, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-38590-y · Cited by 9

Hypoxia and Reactive Oxygen Species

Görlach, A. (2013) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-1-4614-9167-5_4 · Cited by 8

Protective Effects of Hif2 Inhibitor PT-2385 on a Neurological Disorder Induced by Deficiency of Irp2

Shen, J., Xu, L., Li, Y., Dong, W., Cai, J., Liu, Y., Zhao, H., Xu, T., Meyron‐Holtz, E. G., Chang, Y., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.715222 · Cited by 8

Iron Metabolism in Humans: An Overview

Arora, S., & Kapoor, R. (2012) · BiblioBoard Library Catalog (Open Research Library) · doi:10.5772/39031 · Cited by 8

Mitochondrial Regulation of the Hypoxia-Inducible Factor in the Development of Pulmonary Hypertension

Zeidan, E. M., Hossain, M. A., El‐Daly, M., Abourehab, M. A. S., Khalifa, M. M. A., & Taye, A. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11175219 · Cited by 8

Synthesis of the HIF-2α translation inhibitor compound 76 via a Japp-Klingemann coupling

Wang, X., Ahn, J.-E., Fiejtek, D. K., Lin, L., Dinkelborg, K., Sundaram, R., Zheng, S., Iliopoulos, O., & Hodgetts, K. J. (2019) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.03.005 · Cited by 7

Identification of small-molecule ligand-binding sites on and in the ARNT PAS-B domain

Xu, X., Closson, J. D., Marcelino, L. P., Favaro, D. C., Silvestrini, M., Solazzo, R., Chong, L. T., & Gardner, K. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107606 · Cited by 7

Metabolism and Oxidative Stress Response Pathways in Kidney Cancer: A Tale of Chance and Necessity

Sourbier, C., Srinivasan, R., & Linehan, W. M. (2015) · American Society of Clinical Oncology Educational Book · doi:10.14694/edbook_am.2015.35.220 · Cited by 6

Cellular Iron Metabolism – The IRP/IRE Regulatory Network

Joshi, R. S., Moran, E. L., & Sánchez, M. (2012) · BiblioBoard Library Catalog (Open Research Library) · doi:10.5772/34987 · Cited by 6

The clinical landscape of HIF2α inhibitors in oncology

Saad, E., Machaalani, M., McDermott, D. F., & Choueiri, T. K. (2026) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-026-01145-y · Cited by 4

Iron Homeostasis and Metabolism During Pregnancy: Exploring Innovative Drug Delivery Approaches for Treating Iron Deficiency Anemia in Pregnant Women

Joshi, V. C., & Awasthi, R. (2025) · Archiv der Pharmazie · doi:10.1002/ardp.202400983 · Cited by 4

Severinia buxifolia-isolated acridones inhibit lung cancer invasion and decrease HIFα protein synthesis involving 5’UTR-mediated translation inhibition

Chen, P.-W., Huang, S., Chou, W., Chang, F., Cheng, Y., & Wang, H. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154570 · Cited by 4

The Genetic Basis of Kidney Cancer and Implications for Targeted Therapies

Schmidt, L. S., Srinivasan, R., & Linehan, W. M. (2012) · Springer eBooks · doi:10.1007/978-1-4614-2400-0_1 · Cited by 4

Hemangioblastomas of the central nervous system

Konstantakou, E. G., Metelo, A. M., & Iliopoulos, O. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813866-3.00015-1 · Cited by 4

Glucose deprivation impairs hypoxia-inducible factor-1α synthesis

Hubert, M., Stuart, S. E., & Ohh, M. (2024) · Discover Oncology · doi:10.1007/s12672-024-01484-1 · Cited by 3

Dysregulation of the sensory and regulatory pathways controlling cellular iron metabolism in unilateral obstructive nephropathy

Votava, J. A., Reese, S. R., Deck, K. M., Nizzi, C. P., Anderson, S. A., Djamali, A., & Eisenstein, R. S. (2021) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00537.2020 · Cited by 3

Cell cultures in assessing radioresistance of glioblastomas

Belyashova, A. S., Галкин, М. В., Antipina, N., Pavlova, G. V., & Голанов, А. В. (2022) · Burdenko s Journal of Neurosurgery · doi:10.17116/neiro202286051126 · Cited by 3

Fe–S Clusters: Biogenesis and Redox, Catalytic, and Regulatory Properties

Nicolet, Y., & Fontecilla-Camps, J. C. (2014) · Wiley eBooks · doi:10.1002/9783527664160.ch2 · Cited by 3

FeS-cluster coordination of vertebrate thioredoxin regulates suppression of hypoxia-induced factor 2α through iron regulatory protein 1Preprint

Berndt, C., Hanschmann, E.-M., Jordt, L. M., Gellert, M., Thewes, L., Salas, C. O., Poschmann, G., Müller, C. S., Bodnar, Y., Schipper, S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.04.235721 · Cited by 3

Low Wall Shear Stress Promotes Atheroma via Arterial Iron Accumulation

Zheng, L., Zhang, Z., Liu, Y., Cheng, C., Zhao, B., Ji, R., Chen, Z., Yang, L., Cai, J., Li, K., et al. (2025) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.125.322495 · Cited by 1

Unraveling the Role of Hypoxia-Inducible Factor in Renal Cell Carcinoma: A Biological and Therapeutic Perspective

Pal, S. K., & Figlin, R. A. (2011) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0149 · Cited by 1

Анемии различного генеза у пациентов с ревматологической патологией. Роль системы HIF

Гулак, А. А., & Рукавицын, О. А. (2024) · Гематология Трансфузиология Восточная Европа · doi:10.34883/pi.2024.10.3.010 · Cited by 1

HIF Biology in RCC: Implications for Signaling, Disease Progression, and Treatment

Rathmell, W. K. (2012) · Springer eBooks · doi:10.1007/978-1-4614-2400-0_3 · Cited by 1

Familial Renal Cell Cancers and Pheochromocytomas

Chan–Smutko, G., & Iliopoulos, O. (2010) · Springer eBooks · doi:10.1007/978-0-387-93846-2_9 · Cited by 1

HIF‐1 Inhibitors for Cancer Therapy

Rapisarda, A., & Melillo, G. (2010) · Wiley eBooks · doi:10.1002/9780470669891.ch17 · Cited by 1

Cellular and Systemic Iron Homeostasis

Crichton, R. R. (2016) · Wiley eBooks · doi:10.1002/9781118925645.ch10 · Cited by 1

Hypoxia-induced pulmonary hypertension -- utilising experiments of naturePreprint

Zhao, L. (2020) · doi:10.22541/au.158212885.56141666 · Cited by 1

Mechanisms of Resistance to VEGF-Directed Therapy and Implications for Future Trial Design

Mier, J. W. (2012) · Springer eBooks · doi:10.1007/978-1-4614-2400-0_14

The regulation of protein synthesis by mTOR signaling : a potential target for cancer treatment?

Weppler, S. A. (2009) · Research Publications (Maastricht University) · doi:10.26481/dis.20091203sw

VHL and HIF in Clear Cell Renal Cell Carcinoma: Molecular Abnormalities and Potential Clinical Applications

Gossage, L. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1622-1_4

Biomarkers for Prognosis and Molecularly Targeted Therapy in Renal Cell Carcinoma

Schmidt, L. S. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-615-9_11

Regulation of hepcidin and hemojuvelin expression and their role in iron homeostasis

Salama, M. (2010) · UCL Discovery (University College London)

Development of Resistance to Targeted Therapy: Preclinical Findings and Clinical Relevance

Mier, J. W., Bhatt, R. S., Panka, D. J., & Atkins, M. B. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1622-1_16

Insulin Receptor Substrate-2 (IRS-2): A Novel Hypoxia-Responsive Gene in Breast Cancer: A Dissertation

Mardilovich, K. (2011) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/3w9g-7v51

Oxygen-Dependent Regulation of Erythropoiesis

Haase, V. H. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-857-7_23

Hemangioblastomas of the Central Nervous System

Metelo, A. M., & Iliopoulos, O. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-410529-4.00082-6

THE IMPORTANCE OF IRP AS REGULATORS OF IRON METABOLISM IN β THALASSEMIA PATIENTS

Kartal, Y., Kaya-Akyüzlü, D., & Kayaaltı, Z. (2016) · MARMARA PHARMACEUTCAL JOURNAL · doi:10.12991/mpj.20162098496

Ο ρόλος του επαγόμενου από την υποξία μεταγραφικού παράγοντα HIF-2α στην κυτταρική λειτουργία

Pangou, E. (2016) · doi:10.12681/eadd/39127

In silico strategies to study polypharmacology of G-protein-coupled receptors

Hajjo, R. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/xtc7-2969

Hypoxia-inducible factor 2α but not hypoxia-inducible factor-1α increases iron traffic in astrocytesPreprint

Xu, M., Chen, Z., Ma, X., Xu, H., Fan, C., Wang, J., & Xie, J. (2020) · doi:10.21203/rs.3.rs-24083/v1

Pathology of Pancreatic Neuroendocrine Tumors

Borri, F., Bonfiglio, R., & Mandarano, M. (2021) · Springer eBooks · doi:10.1007/978-3-030-37482-2_37-1

Faculty Opinions recommendation of Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia.

Bassingthwaighte, J. B. (2012) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.716647808.792052808

Evolutionary Adaptation of Human Lens to Ultraviolet Radiation and Hypoxia

(2017) · Journal of Ophthalmology & Clinical Research · doi:10.33140/jocr/01/02/00001

Hypoxia-inducible factor-2α but not hypoxia-inducible factor-1α increases iron traffic in astrocytesPreprint

Xu, M., Chen, Z., Ma, X., Xu, H., Fan, C., Xie, J., & Wang, J. (2020) · doi:10.21203/rs.3.rs-25260/v1

Pathology of Pancreatic Neuroendocrine Tumors

Borri, F., Bonfiglio, R., & Mandarano, M. (2022) · Springer eBooks · doi:10.1007/978-3-030-41683-6_37

Tumor Hypoxia: An Introduction

Ray, S. K., & Mukherjee, S. (2025) · Springer eBooks · doi:10.1007/978-981-96-1016-7_1

Influencing iron homeostasis by a transition metal complex interacting with a messenger-RNA stem loop in the iron regulating element

Hognon, C., Froux, A., Grandemange, S., & Monari, A. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp02185e

The Disadvantageous Interrelationship between Lenticular Mitoprotection and Epithelial-Mesenchymal transition via Nuclear Beta catenin

Neelam, S. (2014) · Digital Commons @ UNT Health Science Center

Rôle des facteurs de transcription HIF (Hypoxia Inducible Factor) dans le maintien à long terme des cellules souches hématopoïétiques humaines chez la souris immunodéficiente

Rouault-Pierre, K. (2010) · theses.fr (ABES) · doi:10.70675/d19021d9z37c5z4948zb727z5f042b13da9d

Impact du ciblage du domaine de liaison de HIF-1α avec HIF-1β sur le paysage immunitaire du mélanome

Lequeux, A. (2020) · theses.fr (ABES) · doi:10.70675/a29d12dbz79c1z4d37za978z2e2319131c82

Modulating the Tumor Microenvironment: Small-Molecule Strategies in Combination Regimens

Daripa, S., & Hira, S. K. (2026) · Springer eBooks · doi:10.1007/978-981-95-9777-2_12

aip Mutant Zebrafish Display Morphological and Transcriptional Changes Associated with Stress-Induced Hematopoiesis

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