Sumoylation increases HIF-1α stability and its transcriptional activity

Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.

Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

A conserved family of prolyl-4-hydroxylases that modify HIF

Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549 · see citing works

Regulation of angiogenesis by hypoxia: role of the HIF system

Pugh, C. W., & Ratcliffe, P. J. (2003) · Nature Medicine · doi:10.1038/nm0603-677 · Cited by 2,520 · see citing works

Regulation of hypoxia-inducible factor 1α is mediated by an O ₂ -dependent degradation domain via the ubiquitin-proteasome pathway

Huang, L. E., Gu, J., Schau, M., & Bunn, H. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.7987 · Cited by 2,113 · see citing works

Regulation of Mammalian O ₂ Homeostasis by Hypoxia-Inducible Factor 1

Semenza, G. L. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.551 · Cited by 1,914 · see citing works

Asparagine Hydroxylation of the HIF Transactivation Domain: A Hypoxic Switch

Lando, D., Peet, D. J., Whelan, D. A., Gorman, J. J., & Whitelaw, M. L. (2002) · Science · doi:10.1126/science.1068592 · Cited by 1,558 · see citing works

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550 · see citing works

A Small Ubiquitin-Related Polypeptide Involved in Targeting RanGAP1 to Nuclear Pore Complex Protein RanBP2

Mahajan, R. K., Delphin, C., Guan, T., Gerace, L., & Melchior, F. (1997) · Cell · doi:10.1016/s0092-8674(00)81862-0 · Cited by 1,258 · see citing works

SUMO-1 Modification of IκBα Inhibits NF-κB Activation

Desterro, J. M. P., Rodríguez, M. S., & Hay, R. T. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80133-1 · Cited by 1,048 · see citing works

Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation

Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W., & Ratcliffe, P. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5197 · Cited by 1,014 · see citing works

SUMO—Nonclassical Ubiquitin

Melchior, F. (2000) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.16.1.591 · Cited by 773 · see citing works

Sumo, ubiquitin's mysterious cousin

Müller, S. P., Hoege, C., Pyrowolakis, G., & Jentsch, S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056591 · Cited by 765 · see citing works

SUMO-1 Conjugation in Vivo Requires Both a Consensus Modification Motif and Nuclear Targeting

Rodríguez, M. S., Dargemont, C., & Hay, R. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009476200 · Cited by 753 · see citing works

Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

Hewitson, K. S., McNeill, L. A., Riordan, M. V., Tian, Y.-M., Bullock, A. N., Welford, R. W., Elkins, J. M., Oldham, N. J., Bhattacharya, S., Gleadle, J. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200273200 · Cited by 719 · see citing works

Regulation and Destabilization of HIF-1α by ARD1-Mediated Acetylation

Jeong, J.-W., Bae, M.-K., Ahn, M.-Y., Kim, S.-H., Sohn, T.-K., Bae, M.-H., Yoo, M.-A., Song, E. J., Lee, K.-J., & Kim, K.-W. (2002) · Cell · doi:10.1016/s0092-8674(02)01085-1 · Cited by 716 · see citing works

Conjugation with the ubiquitin‐related modifier SUMO‐1 regulates the partitioning of PML within the nucleus

Müller, S. P., Matunis, M. J., & Dejean, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.1.61 · Cited by 683 · see citing works

Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1

Gostissa, M., Hengstermann, A., Fogal, V., Sandy, P., Schwarz, S. E., Scheffner, M., & Sal, G. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6462 · Cited by 512 · see citing works

SUMO-1 Modification and Its Role in Targeting the Ran GTPase-activating Protein, RanGAP1, to the Nuclear Pore Complex

Matunis, M. J., Wu, J., & Blobel, G. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.3.499 · Cited by 471 · see citing works

Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)

Poukka, H., Karvonen, U., Jänne, O. A., & Palvimo, J. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.26.14145 · Cited by 459 · see citing works

Covalent Modification of PML by the Sentrin Family of Ubiquitin-like Proteins

Kamitani, T., Nguyen, H. P., Kito, K., Fukuda-Kamitani, T., & Yeh, E. T. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3117 · Cited by 207 · see citing works

Increase of SUMO-1 expression in response to hypoxia: Direct interaction with HIF-1α in adult mouse brain and heart in vivo

Shao, R., Zhang, F.-P., Tian, F., Anders Friberg, P., Wang, X., Sjöland, H., & Billig, H. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.05.079 · Cited by 149 · see citing works

HIF‐1‐dependent transcriptional activity is required for oxygen‐mediated HIF‐1α degradation

Berra, E., Richard, D. E., Gothié, E., & Pouysségur, J. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02159-7 · Cited by 147 · see citing works

HIF1α and HIF2α: sibling rivalry in hypoxic tumour growth and progression

Keith, B., Johnson, R. S., & Simon, M. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3183 · Cited by 1,693 · see citing works

Hypoxia-Induced Angiogenesis: Good and Evil

Krock, B. L., Skuli, N., & Simon, M. C. (2011) · Genes & Cancer · doi:10.1177/1947601911423654 · Cited by 1,179 · see citing works

Transcriptional regulation by hypoxia inducible factors

Dengler, V. L., Galbraith, M. D., & Espinosa, J. M. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.838205 · Cited by 774 · see citing works

SUMO-Specific Protease 1 Is Essential for Stabilization of HIF1α during Hypoxia

Cheng, J., Kang, X., Zhang, S., & Yeh, E. T. H. (2007) · Cell · doi:10.1016/j.cell.2007.08.045 · Cited by 624 · see citing works

The use of cobalt chloride as a chemical hypoxia model

Muñoz‐Sánchez, J., & Chánez‐Cárdenas, M. E. (2018) · Journal of Applied Toxicology · doi:10.1002/jat.3749 · Cited by 535 · see citing works

The effect of HIF on metabolism and immunity

Taylor, C. T., & Scholz, C. C. (2022) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00587-8 · Cited by 517 · see citing works

HIF-1 and HIF-2 Transcription Factors - Similar but Not Identical

Loboda, A., Jozkowicz, A., & Dulak, J. (2010) · Molecules and Cells · doi:10.1007/s10059-010-0067-2 · Cited by 477 · see citing works

HIF-1 regulation: not so easy come, easy go

Koh, M. Y., Spivak-Kroizman, T. R., & Powis, G. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.08.002 · Cited by 339 · see citing works

Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation

Herrmann, J., Lerman, L. O., & Lerman, A. (2007) · Circulation Research · doi:10.1161/01.res.0000264500.11888.f0 · Cited by 332 · see citing works

RSUME, a Small RWD-Containing Protein, Enhances SUMO Conjugation and Stabilizes HIF-1α during Hypoxia

Carbia-Nagashima, A., Gerez, J., Perez-Castro, C., Paez-Pereda, M., Silberstein, S., Stalla, G. K., Holsboer, F., & Arzt, E. (2007) · Cell · doi:10.1016/j.cell.2007.07.044 · Cited by 318 · see citing works

Hypoxia-inducible factors and the regulation of lipid metabolism

Mylonis, I., Simos, G., & Paraskeva, E. (2019) · Cells · doi:10.3390/cells8030214 · Cited by 316 · see citing works

In Vivo Identification of Human Small Ubiquitin-like Modifier Polymerization Sites by High Accuracy Mass Spectrometry and an in Vitro to in Vivo Strategy

Matić, I., van Hagen, M., Schimmel, J., Maček, B., Ogg, S. C., Tatham, M. H., Hay, R. T., Lamond, A. I., Mann, M., & Vertegaal, A. C. O. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700173-mcp200 · Cited by 303 · see citing works

NRF2 Blockade Suppresses Colon Tumor Angiogenesis by Inhibiting Hypoxia-Induced Activation of HIF-1α

Kim, T., Hur, E.-G., Kang, S., Kim, J., Thapa, D., Lee, Y. M., Ku, S., Jung, Y., & Kwak, M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3007 · Cited by 292 · see citing works

Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing

Webb, J. D., Coleman, M. L., & Pugh, C. W. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0147-7 · Cited by 255 · see citing works

An additional role for SUMO in ubiquitin-mediated proteolysis

Geoffroy, M., & Hay, R. T. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2707 · Cited by 250 · see citing works

Sumoylation regulates diverse biological processes

Zhao, J. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7137-4 · Cited by 248 · see citing works

Cbx4 Governs HIF-1α to Potentiate Angiogenesis of Hepatocellular Carcinoma by Its SUMO E3 Ligase Activity

Li, J., Xu, Y., Long, X., Wang, W., Jiao, H., Mei, Z., Yin, Q., Ma, L., Zhou, A., Wang, L., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2013.12.008 · Cited by 243 · see citing works

Turn me on: regulating HIF transcriptional activity

Lisy, K., & Peet, D. J. (2008) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402315 · Cited by 235 · see citing works

Regulatory mechanisms of hypoxia‐inducible factor 1 activity: Two decades of knowledge

Koyasu, S., Kobayashi, M., Gotö, Y., Hiraoka, M., & Harada, H. (2017) · Cancer Science · doi:10.1111/cas.13483 · Cited by 226 · see citing works

The von Hippel–Lindau protein, HIF hydroxylation, and oxygen sensing

Kaelin, W. G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.165 · Cited by 213 · see citing works

Reactive oxygen species and HIF-1 signalling in cancer

Galanis, Α., Pappa, A., Giannakakis, A., Lanitis, E., Laniti, D. D., & Sandaltzopoulos, R. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.02.028 · Cited by 207 · see citing works

SENP3 is responsible for HIF‐1 transactivation under mild oxidative stress via p300 de‐SUMOylation

Huang, C., Han, Y. Y., Wang, Y., Sun, X., Yan, S., Yeh, E. T. H., Chen, Y., Cang, H., Li, H., Shi, G., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.210 · Cited by 206 · see citing works

Cancer Drug Discovery and Development

Humphrey, J. S., Price, K., Gupta, E., Baxter, A. R. W., Bird, J., Sonnichsen, D. S., & Naglich, J. G. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-325-5_21 · Cited by 195 · see citing works

Hypoxia Inducible Factor-1 as a Target for Neurodegenerative Diseases

Zhang, Z., Yan, J., Chang, Y. Z., Yan, S., & Shi, H. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711797200426 · Cited by 189 · see citing works

HIF in Kidney Disease and Development

Gunaratnam, L., & Bonventre, J. V. (2008) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008070804 · Cited by 171 · see citing works

SUMO under stress

Tempé, D., Piechaczyk, M., & Bossis, G. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360874 · Cited by 168 · see citing works

The Role of Hypoxia Inducible Factor-1 in Hepatocellular Carcinoma

Luo, D., Wang, Z., Wu, J., Jiang, C., & Wu, J. (2014) · BioMed Research International · doi:10.1155/2014/409272 · Cited by 157 · see citing works

Interactions between nitric oxide and hypoxia-inducible factor signaling pathways in inflammatory disease

Olson, N. C., & van der Vliet, A. (2011) · Nitric Oxide · doi:10.1016/j.niox.2010.12.010 · Cited by 158 · see citing works

Hypoxia-inducible factor prolyl hydroxylases as targets for neuroprotection by “antioxidant” metal chelators: From ferroptosis to stroke

Speer, R. E., Karuppagounder, S. S., Basso, M., Sleiman, S. F., Kumar, A., Brand, D., Smirnova, N., Gazaryan, I. G., Khim, S. J., & Ratan, R. R. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.026 · Cited by 155 · see citing works

Transient Global Cerebral Ischemia Induces a Massive Increase in Protein Sumoylation

Yang, W., Sheng, H., Warner, D. S., & Paschen, W. (2007) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600523 · Cited by 140 · see citing works

Common Molecular Mechanisms of Mammary Gland Development and Breast Cancer

Lundgren, K., Holm, C., & Landberg, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7390-6 · Cited by 140 · see citing works

The role of hypoxia-inducible factor post-translational modifications in regulating its localisation, stability, and activity

Albanese, A., Daly, L. A., Mennerich, D., Kietzmann, T., & Sée, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010268 · Cited by 136 · see citing works

Systematic and comprehensive insights into HIF-1 stabilization under normoxic conditions: implications for cellular adaptation and therapeutic strategies in cancer

Zhang, J., Yao, M., Xia, S., Zeng, F., & Liu, Q. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00682-7 · Cited by 139 · see citing works

SUMOylation of hypoxia-inducible factor-1α reduces its transcriptional activity

Berta, M., Mazure, N. M., Hattab, M., Pouysségur, J., & Brahimi-Horn, M. C. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.103 · Cited by 125 · see citing works

The Ubiquitin Ligase Siah2 and the Hypoxia Response

Nakayama, K., Qi, J., & Ronai, Z. A. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0458 · Cited by 122 · see citing works

Ubiquitin-like Protein FAT10 Promotes the Invasion and Metastasis of Hepatocellular Carcinoma by Modifying β-Catenin Degradation

Yuan, R., Wang, K., Hu, J., Chen, Y., Li, M., Yu, X., Liu, X., Lei, J., Guo, W.-H., Wu, L., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0284 · Cited by 119 · see citing works

Emerging roles of desumoylating enzymes

Kim, J. H., & Baek, S. H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.12.008 · Cited by 119 · see citing works

mRNA-to-protein translation in hypoxia

Chee, N. T., Lohse, I., & Brothers, S. P. (2019) · Molecular Cancer · doi:10.1186/s12943-019-0968-4 · Cited by 113 · see citing works

Repression of hypoxia-inducible factor α signaling by Set7-mediated methylation

Liu, X., Chen, Z., Xu, C., Leng, X., Cao, H., Ouyang, G., & Xiao, W. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv379 · Cited by 107 · see citing works

Hypoxia and the Malignant Glioma Microenvironment: Regulation and Implications for Therapy

Oliver, L., Olivier, C., Marhuenda, F., Campone, M., & Vallette, F. M. (2009) · Current Molecular Pharmacology · doi:10.2174/1874467210902030263 · Cited by 102 · see citing works

HIF-1α: a Valid Therapeutic Target for Tumor Therapy

Hong, S., Lee, H., & Kim, K. (2004) · Cancer Research and Treatment · doi:10.4143/crt.2004.36.6.343 · Cited by 105 · see citing works

Mutation of SENP1/SuPr-2 Reveals an Essential Role for Desumoylation in Mouse Development

Yamaguchi, T., Sharma, P., Athanasiou, M., Kumar, A., Yamada, S., & Kuehn, M. R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.12.5171-5182.2005 · Cited by 100 · see citing works

Therapeutic Potential of Targeting the SUMO Pathway in Cancer

Kukkula, A., Ojala, V. K., Mendez, L., Sistonen, L., Elenius, K., & Sundvall, M. (2021) · Cancers · doi:10.3390/cancers13174402 · Cited by 92 · see citing works

RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2α

van Hagen, M., Overmeer, R., Abolvardi, S. S., & Vertegaal, A. C. O. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1157 · Cited by 92 · see citing works

Advances in the development of SUMO specific protease (SENP) inhibitors

Kumar, A., & Zhang, K. Y. J. (2015) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2015.03.001 · Cited by 91 · see citing works

Negative regulation of HIF-1α by an FBW7-mediated degradation pathway during hypoxia

Cassavaugh, J. M., Hale, S. A., Wellman, T. L., Howe, A. K., Wong, C., & Lounsbury, K. M. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23321 · Cited by 88 · see citing works

Ubiquitin–proteasome system as a modulator of cell fate

Thompson, S. J., Loftus, L. T., Ashley, M. D., & Meller, R. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2007.09.010 · Cited by 87 · see citing works

A computational model of intracellular oxygen sensing by hypoxia-inducible factor HIF1α

Qutub, A. A., & Popel, A. S. (2006) · Journal of Cell Science · doi:10.1242/jcs.03087 · Cited by 87 · see citing works

Enhanceosomes as integrators of hypoxia inducible factor (HIF) and other transcription factors in the hypoxic transcriptional response

Pawlus, M. R., & Hu, C. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.05.018 · Cited by 83 · see citing works

Induction of SENP1 in Endothelial Cells Contributes to Hypoxia-driven VEGF Expression and Angiogenesis

Xu, Y., Zuo, Y., Zhang, H., Kang, X., Fei, Y., Yi, Z., Liu, M., Yeh, E. T. H., Chen, G., & Cheng, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.164236 · Cited by 81 · see citing works

Hypoxia Inactivates the VHL Tumor Suppressor through PIASy-Mediated SUMO Modification

Cai, Q., Verma, S. C., Kumar, P., Ma, M., & Robertson, E. S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009720 · Cited by 76 · see citing works

SUMO1 promotes Aβ production via the modulation of autophagy

Cho, S., Yun, S., Jo, C., Lee, D., Choi, K. J., Song, J. C., Park, S. I., Kim, Y.-J., & Koh, Y. H. (2014) · Autophagy · doi:10.4161/15548627.2014.984283 · Cited by 76 · see citing works

Hypoxia causes trophoblast cell ferroptosis to induce miscarriage through lnc-HZ06/HIF1α-SUMO/NCOA4 axis

Tian, P., Xu, Z., Guo, J., Zhao, J., Chen, W., Huang, W., Wang, M., Mi, C., Zhang, Y., Yang, Y., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103073 · Cited by 71 · see citing works

PIASy stimulates HIF1α SUMOylation and negatively regulates HIF1α activity in response to hypoxia

Kang, X., Li, J., Zou, Y., Yi, J., Zhang, H., Cao, M., Yeh, E. T. H., & Cheng, J. (2010) · Oncogene · doi:10.1038/onc.2010.297 · Cited by 71 · see citing works

Sumoylation as a Signal for Polyubiquitylation and Proteasomal Degradation

Miteva, M., Keusekotten, K., Hofmann, K., Praefcke, G. J. K., & Dohmen, R. J. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4419-6676-6_16 · Cited by 70 · see citing works

Mesenchymal Stem Cell Migration and Proliferation Are Mediated by Hypoxia-Inducible Factor-1α Upstream of Notch and SUMO Pathways

Ciria, M., García, N. A., Ontoria‐Oviedo, I., González‐King, H., Carrero, R., de la Pompa, J. L., Montero, J., & Sepúlveda, P. (2017) · Stem Cells and Development · doi:10.1089/scd.2016.0331 · Cited by 69 · see citing works

Small Ubiquitin-related Modifier (SUMO)-1 Promotes Glycolysis in Hypoxia

Agbor, T. A., Cheong, A., Comerford, K. M., Scholz, C. C., Bruning, U., Clarke, A., Cummins, E. P., Cagney, G., & Taylor, C. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.115931 · Cited by 68 · see citing works

2‐Methoxyestradiol confers neuroprotection and inhibits a maladaptive HIF ‐1α response after traumatic brain injury in mice

Schaible, E., Windschügl, J., Bobkiewicz, W., Kaburov, Y., Dangel, L., Krämer, T. J., Huang, C., Sebastiani, A., Luh, C., Werner, C. D., et al. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12708 · Cited by 67 · see citing works

Global SUMO ylation facilitates the multimodal neuroprotection afforded by quercetin against the deleterious effects of oxygen/glucose deprivation and the restoration of oxygen/glucose

Lee, Y., Bernstock, J. D., Nagaraja, N., Ko, B., & Hallenbeck, J. M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13643 · Cited by 68 · see citing works

HIF-1 and HIF-2 in cancer: structure, regulation, and therapeutic prospects

Shi, Y., & Gilkes, D. M. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05537-0 · Cited by 70 · see citing works

Sumoylation: Implications for Neurodegenerative Diseases

Anderson, D. B., Zanella, C. A., Henley, J. M., & Cimarosti, H. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50044-7_16 · Cited by 61 · see citing works

Intracellular energy production and distribution in hypoxia

Flood, D., Lee, E. S., & Taylor, C. T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105103 · Cited by 59 · see citing works

The Role of Sumoylation in the Response to Hypoxia: An Overview

Filippopoulou, C., Simos, G., & Chachami, G. (2020) · Cells · doi:10.3390/cells9112359 · Cited by 56 · see citing works

Cerebral ischemia/stroke and small ubiquitin‐like modifier (SUMO) conjugation – a new target for therapeutic intervention?

Yang, W., Sheng, H., Homi, H. M., Warner, D. S., & Paschen, W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05404.x · Cited by 55 · see citing works

Regulation of matrixmetalloproteinase-3 and matrixmetalloproteinase-13 by SUMO-2/3 through the transcription factor NF-κB

Frank, S., Peters, M. A., Wehmeyer, C., Strietholt, S., Wunrau, C., Bertrand, J., Heitzmann, M., Hillmann, A., Sherwood, J., Seyfert, C., et al. (2013) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2012-202080 · Cited by 55 · see citing works

The Role of the Ubiquitin Proteasome System in Ischemia and Ischemic Tolerance

Meller, R. (2009) · The Neuroscientist · doi:10.1177/1073858408327809 · Cited by 52 · see citing works

Inhibitor of DNA Binding 1 Activates Vascular Endothelial Growth Factor through Enhancing the Stability and Activity of Hypoxia-Inducible Factor-1α

Kim, H., Chung, H., Yoo, Y., Kim, I. H., Lee, J., Lee, M., & Kong, G. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0218 · Cited by 52 · see citing works

SENP1/HIF‐1α feedback loop modulates hypoxia‐induced cell proliferation, invasion, and EMT in human osteosarcoma cells

Wang, X., Liang, X., Liang, H., & Wang, B. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26342 · Cited by 51 · see citing works

Hypoxia-inducible factor–1 and associated upstream and downstream proteins in the pathophysiology and management of glioblastoma

Womeldorff, M. R., Gillespie, D. L., & Jensen, R. L. (2014) · Neurosurgical FOCUS · doi:10.3171/2014.9.focus14496 · Cited by 50 · see citing works

SENP1 desensitizes hypoxic ovarian cancer cells to cisplatin by up-regulating HIF-1α

Ao, Q., Su, W., Guo, S., Cai, L., & Huang, L. (2015) · Scientific Reports · doi:10.1038/srep16396 · Cited by 49 · see citing works

Hypoxia‐inducible factors in metabolic reprogramming during sepsis

Vanderhaeghen, T., Vandewalle, J., & Libert, C. (2020) · FEBS Journal · doi:10.1111/febs.15222 · Cited by 47 · see citing works

The Potential Role of Hypoxia-Inducible Factor-1 in the Progression and Therapy of Central Nervous System Diseases

Chen, H., Ma, D., Yue, F., Qi, Y., Dou, M., Cui, L., & Xing, Y. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210729123137 · Cited by 49 · see citing works

The emerging roles of SUMOylation in the tumor microenvironment and therapeutic implications

Gu, Y., Fang, Y., Wu, X., Xu, T., Hu, T., Xu, Y., Ma, P., Wang, Q., & Shu, Y. (2023) · Experimental Hematology and Oncology · doi:10.1186/s40164-023-00420-3 · Cited by 49 · see citing works

Basic Biology of Hypoxic Responses Mediated by the Transcription Factor HIFs and Its Implication for Medicine

Hirota, K. (2020) · Biomedicines · doi:10.3390/biomedicines8020032 · Cited by 48 · see citing works

Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity

Oh, S.-M., Liu, Z., Okada, M., Jang, S.-W., Liu, X., Chan, C.-B., Luo, H., & Ye, K.-N. (2009) · Oncogene · doi:10.1038/onc.2009.411 · Cited by 47 · see citing works

Topotecan is a potent inhibitor of SUMOylation in glioblastoma multiforme and alters both cellular replication and metabolic programming

Bernstock, J. D., Ye, D., Gessler, F. A., Lee, Y.-J., Peruzzotti-Jametti, L., Baumgarten, P., Johnson, K. R., Maric, D., Yang, W., Kögel, D., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-07631-9 · Cited by 46 · see citing works

Lactylation modification of HIF-1α enhances its stability by blocking VHL recognition

Li, C., Fu, C., Zhou, W., Li, H., Liu, Z., Wu, G., He, T., Shen, M., & Liu, H. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02366-x · Cited by 45 · see citing works

Oxygen-dependent changes in binding partners and post-translational modifications regulate the abundance and activity of HIF-1α/2α

Daly, L. A., Brownridge, P., Batie, M., Rocha, S., Sée, V., & Eyers, C. E. (2021) · Science Signaling · doi:10.1126/scisignal.abf6685 · Cited by 44 · see citing works

Inflammation and Its Correlates in Regenerative Wound Healing: An Alternate Perspective

Gourevitch, D., Kossenkov, A. V., Zhang, Y., Clark, L. D., Chang, C., Showe, L. C., & Heber‐Katz, E. (2014) · Advances in Wound Care · doi:10.1089/wound.2014.0528 · Cited by 44 · see citing works

Natural compounds and the hypoxia-inducible factor (HIF) signalling pathway

Manolescu, B. N., Oprea, E., Buşu, C., & Cercasov, C. (2009) · Biochimie · doi:10.1016/j.biochi.2009.08.005 · Cited by 45 · see citing works

Molecular targets underlying SUMO‐mediated neuroprotection in brain ischemia

Silveirinha, V., Stephens, G., & Cimarosti, H. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12347 · Cited by 43 · see citing works

Increased SUMO-1 expression in response to hypoxia: Interaction with HIF-1α in hypoxic pulmonary hypertension

Jiang, Y., Wang, J., TIAN, H., Li, G., Zhu, H., Liu, L., Hu, R., & Dai, A. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2209 · Cited by 41 · see citing works

Clinical significance of hypoxia-inducible factor 1 and VEGF-A in osteosarcoma

Zhao, H., Wu, Y., Yang, C., & Liu, H. (2015) · International Journal of Clinical Oncology · doi:10.1007/s10147-015-0848-x · Cited by 40 · see citing works

Sumoylation enhances the activity of the TGF-β/SMAD and HIF-1 signaling pathways in keloids

Lin, X., Wang, Y., Jiang, Y., Xu, M., Pang, Q., Sun, J., Yu, Y., Shen, Z., Lei, R., & Xu, J. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117859 · Cited by 39 · see citing works

Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF‐1α fragments in vitro

Murray-Rust, T. A., Oldham, N. J., Hewitson, K. S., & Schofield, C. J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.02.012 · Cited by 40 · see citing works

T Helper Cell Activation and Expansion Is Sensitive to Glutaminase Inhibition under Both Hypoxic and Normoxic Conditions

Sener, Z., Cederkvist, F. H., Volchenkov, R., Holen, H. L., & Skålhegg, B. S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160291 · Cited by 38 · see citing works

Nuclear FGFR2 negatively regulates hypoxia-induced cell invasion in prostate cancer by interacting with HIF-1 and HIF-2

Lee, J. E., Shin, S.-H., Shin, H., Chun, Y., & Park, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-39843-6 · Cited by 39 · see citing works

Adenosine Signaling Mediates SUMO-1 Modification of IκBα during Hypoxia and Reoxygenation

Liu, Q., Li, J., Khoury, J., Colgan, S. P., & Ibla, J. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809275200 · Cited by 38 · see citing works

HIF signaling: A new propellant in bone regeneration

Bai, H., Wang, Y., Zhao, Y. D., Chen, X., Xiao, Y. M., & Bao, C. (2022) · Biomaterials Advances · doi:10.1016/j.bioadv.2022.212874 · Cited by 37 · see citing works

Hypoxia-Inducible Factor-1 Facilitates Cervical Cancer Progression in Human Papillomavirus Type 16 Transgenic Mice

Lu, Z. H., Wright, J. D., Belt, B. A., Cardiff, R. D., & Arbeit, J. M. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.061138 · Cited by 37 · see citing works

Cytotoxic necrotizing factor 1 promotes bladder cancer angiogenesis through activating RhoC

Guo, Y., Wang, J., Zhou, K., Lv, J., Wang, L., Gao, S., Keller, E. T., Zhang, Z., Wang, Q., & Yao, Z. (2020) · The FASEB Journal · doi:10.1096/fj.201903266rr · Cited by 36 · see citing works

Cardiac function and disease: emerging role of small ubiquitin‐related modifier

Wang, J. (2010) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.130 · Cited by 35 · see citing works

Hypoxia-Inducible Factors: Post-translational Crosstalk of Signaling Pathways

Dimova, E. Y., & Kietzmann, T. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-738-9_13 · Cited by 35 · see citing works

POU6F1 cooperates with RORA to suppress the proliferation of lung adenocarcinoma by downregulating HIF1A signaling pathway

Xiao, W., Geng, W., Zhou, M. L., Xu, J., Wang, S., Huang, Q., Sun, Y., Li, Y., Yang, G., & Jin, Y. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04857-y · Cited by 33 · see citing works

OTUB1 augments hypoxia signaling via its non-canonical ubiquitination inhibition of HIF-1α during hypoxia adaptation

Liu, X., Deng, H., Tang, J., Wang, Z., Zhu, C., Cai, X., Rong, F., Chen, X., Sun, X., Jia, S., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05008-z · Cited by 34 · see citing works

Regulation of the nucleocytoplasmic trafficking of viral and cellular proteins by ubiquitin and small ubiquitin‐related modifiers

Wang, Y. E., Pernet, O., & Lee, B. (2011) · Biology of the Cell · doi:10.1111/boc.201100105 · Cited by 32 · see citing works

Hypoxia activates SUMO-1-HIF-1α signaling pathway to upregulate pro-inflammatory cytokines and permeability in human tonsil epithelial cells

Lin, Y., Wang, M.-J., Xiao, Z., & Jiang, Z. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119432 · Cited by 33 · see citing works

Relationship between RSUME and HIF-1α/VEGF-A with invasion of pituitary adenoma

He, W., Huang, L., Shen, X., Yang, Y., Wang, D., Yang, Y. W., & Zhu, X. (2016) · Gene · doi:10.1016/j.gene.2016.12.012 · Cited by 33 · see citing works

SUMOylation as a Therapeutic Target for Myocardial Infarction

Zhao, W., Zhang, X., & Rong, J. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.701583 · Cited by 32 · see citing works

SUMO downregulates GLP-1-stimulated cAMP generation and insulin secretion

Rajan, S., Torres, J., Thompson, M. S., & Philipson, L. H. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00486.2011 · Cited by 32 · see citing works

SUMOylation of hypoxia-inducible factor-1α reduces its transcriptional activity

Berta, M., Mazure, N. M., Hattab, M., Pouysségur, J., & Brahimi-Horn, M. C. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.103 · Cited by 125 · see citing works

SUMOylation indirectly suppresses activity of the HIF-1α pathway in intestinal epithelial cells

Malkov, M. I., Flood, D., & Taylor, C. T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105280 · Cited by 11 · see citing works

Hypoxia-inducible factor-1α and small ubiquitin-related modifier

Li, Z., Qu, Y., & Mu, D. (2010) · International journal of pediatrics · doi:10.3760/cma.j.issn.1673-4408.2010.02.003

Ubiquitinational and SUMOylational Modification of Alpha Subunit of HIF-1

Dai, F. (2008) · Zhongguo shengwu huaxue yu fenzi shengwu xuebao

Sumoylation of hypoxia inducible factor-1α and its significance in cancer

Li, J., Xu, Y., Jiao, H., Wang, W., Mei, Z., & Chen, G. (2014) · Science China Life Sciences · doi:10.1007/s11427-014-4685-3 · Cited by 24 · see citing works