Hsp70 and CHIP Selectively Mediate Ubiquitination and Degradation of Hypoxia-inducible Factor (HIF)-1α but Not HIF-2α

Targeting HIF-1 for cancer therapy

Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717

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

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574

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

Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients

Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,836

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

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

Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway.

Kaelin, W. G., & Ratcliffe, P. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.009 · Cited by 3,251

Hsp70 chaperones: Cellular functions and molecular mechanism

Mayer, M. P., & Bukau, B. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4464-6 · Cited by 2,857

A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation

Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617

Diverse roles of C-terminal Hsp70-interacting protein (CHIP) in tumorigenesis

Sun, C., Li, H., Shi, M., Liu, Q.-H., Bai, J., & Zheng, J. (2013) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-013-1571-5 · Cited by 39

PRDX2 and PRDX4 are negative regulators of hypoxia-inducible factors under conditions of prolonged hypoxia

Luo, W., Chen, I., Chen, Y., Alkam, D., Wang, Y., & Semenza, G. L. (2016) · Oncotarget · doi:10.18632/oncotarget.7142 · Cited by 39

Docetaxel induced-JNK2/PHD1 signaling pathway increases degradation of HIF-1α and causes cancer cell death under hypoxia

Oh, E., Kim, C. W., Kim, S., Lee, J., Hong, S., & Park, H. J. (2016) · Scientific Reports · doi:10.1038/srep27382 · Cited by 39

Ubiquitination/de-ubiquitination: A promising therapeutic target for PTEN reactivation in cancer

Wang, K., Liu, J., Li, Y., Li, J., & Zhang, R. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188723 · Cited by 40

Differential redox proteomics allows identification of proteins reversibly oxidized at cysteine residues in endothelial cells in response to acute hypoxia

Izquierdo-Álvarez, A., Ramos, E. M., Villanueva, J., Hernansanz‐Agustín, P., Fernández‐Rodríguez, R., Tello, D., Carrascal, M., & Martı́nez-Ruiz, A. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.06.035 · Cited by 38

Reciprocal Regulation of ERα and ERβ Stability and Activity by Diptoindonesin G

Zhao, Z., Wang, L., James, T. T., Jung, Y., Kim, I., Tan, R. X., Hoffmann, F. M., & Xu, W. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.10.011 · Cited by 38

The E3 Ligase CHIP Mediates p21 Degradation to Maintain Radioresistance

Biswas, K., Sarkar, S., Du, K., Brautigan, D. L., Abbas, T., & Larner, J. M. (2017) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0466 · Cited by 38

Increased accumulation of hypoxia-inducible factor-1α with reduced transcriptional activity mediates the antitumor effect of triptolide

Zhou, Z.-L., Luo, Z.-G., Yu, B., Jiang, Y., Chen, Y., Feng, J.-M., Dai, M., Tong, L.-J., Li, Z., Li, Y.-C., et al. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-268 · Cited by 38

Unraveling the CHIP:Hsp70 complex as an information processor for protein quality control

VanPelt, J., & Page, R. C. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.11.005 · Cited by 38

Hypoxia signaling in the adipose tissue

Huynh, P. M., Wang, F., & An, Y. (2024) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjae039 · Cited by 42

Glucometabolic Reprogramming in the Hepatocellular Carcinoma Microenvironment: Cause and Effect

Tian, H., Zhu, X., Lv, Y., Jiao, Y., & Wang, G. (2020) · Cancer Management and Research · doi:10.2147/cmar.s258196 · Cited by 39

Feedback of hypoxia-inducible factor-1alpha (HIF-1alpha) transcriptional activity via redox factor-1 (Ref-1) induction by reactive oxygen species (ROS)

Kobayashi, Y., Oguro, A., & Imaoka, S. (2021) · Free Radical Research · doi:10.1080/10715762.2020.1870685 · Cited by 35

Monocyte Chemoattractant Protein‐Induced Protein 1 Targets Hypoxia‐Inducible Factor 1α to Protect Against Hepatic Ischemia/Reperfusion Injury

Sun, P., Lu, Y., Cheng, D., Zhang, K., Zheng, J., Liu, Y., Wang, X., Yuan, Y., & Tang, Y. (2018) · Hepatology · doi:10.1002/hep.30086 · Cited by 34

UBXN2A enhances CHIP‐mediated proteasomal degradation of oncoprotein mortalin‐2 in cancer cells

Sane, S., Hafner, A., Srinivasan, R., Masood, D., Slunecka, J. L., Noldner, C. J., Hanson, A., Kruisselbrink, T., Wang, X., Wang, Y., et al. (2018) · Molecular Oncology · doi:10.1002/1878-0261.12372 · Cited by 33

Involvement of E3 Ligases and Deubiquitinases in the Control of HIF-α Subunit Abundance

Kubaichuk, K. I., & Kietzmann, T. (2019) · Cells · doi:10.3390/cells8060598 · Cited by 34

Functional regulation of hypoxia inducible factor-1α by SET9 lysine methyltransferase

Liu, Q., Geng, H., Xue, C., Beer, T. M., & Qian, D. Z. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.011 · Cited by 32

Metastatic Lymph Node CHIP Expression is a Potential Prognostic Marker for Resected Esophageal Squamous Cell Carcinoma Patients

Wen, J., Luo, K., Hu, Y., Yang, H., & Fu, J. (2013) · Annals of Surgical Oncology · doi:10.1245/s10434-012-2733-4 · Cited by 32

Cerebral Oxygen Delivery and Consumption in Brain-Injured Patients

Siwicka-Gieroba, D., Robba, C., Gołacki, J., Badenes, R., & Dąbrowski, W. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12111763 · Cited by 32

Multidimensional Screening Platform for Simultaneously Targeting Oncogenic KRAS and Hypoxia-Inducible Factors Pathways in Colorectal Cancer

Bousquet, M. S., Ma, J., Ratnayake, R., Havre, P. A., Yao, J. G., Dang, N. H., Paul, V. J., Carney, T. J., Dang, L. H., & Luesch, H. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00860 · Cited by 31

Aurora Kinase A Promotes AR Degradation via the E3 Ligase CHIP

Sarkar, S., Brautigan, D. L., & Larner, J. M. (2017) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0062 · Cited by 30

CHIP Regulates AKT/FoxO/Bim Signaling in MCF7 and MCF10A Cells

Lv, Y., Song, S., Zhang, K., Gao, H., & Ma, R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083312 · Cited by 28

Hypoxia-Inducible Factors Regulate Osteoclasts in Health and Disease

Meng, X., Wielockx, B., Rauner, M., & Bözec, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.658893 · Cited by 28

VHL-recruiting PROTAC attenuates renal fibrosis and preserves renal function via simultaneous degradation of Smad3 and stabilization of HIF-2α

Yang, J., Ruan, Y., Wang, D., Fan, J., Luo, N., Chen, H., Li, X., Chen, W., & Wang, X. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00936-x · Cited by 28

Neuron‐generated thrombin induces a protective astrocyte response via protease activated receptors

Rajput, P. S., Lamb, J. A., Kothari, S., Pereira, B., Soetkamp, D., Wang, Y., Tang, J., Eyk, J. E. V., Mullins, E. S., & Lyden, P. D. (2019) · Glia · doi:10.1002/glia.23714 · Cited by 27

Bclaf1 is a direct target of HIF-1 and critically regulates the stability of HIF-1α under hypoxia

Shao, A., Lang, Y., Wang, M., Qin, C., Kuang, Y., Mei, Y., Lin, D., Zhang, S., & Tang, J. (2020) · Oncogene · doi:10.1038/s41388-020-1185-8 · Cited by 29

Expression of carboxyl terminus of Hsp70-interacting protein (CHIP) indicates poor prognosis in human gallbladder carcinoma

Liang, Z. L., KIM, M., Huang, S. M., Lee, H. J., & Kim, J. (2013) · Oncology Letters · doi:10.3892/ol.2013.1138 · Cited by 27

Transcriptomic responses of juvenile Pacific whiteleg shrimp,Litopenaeus vannamei, to hypoxia and hypercapnic hypoxia

Rathburn, C. K., Sharp, N. J., Ryan, J. C., Neely, M. G., Cook, M., Chapman, R. W., Burnett, L. E., & Burnett, K. G. (2013) · Physiological Genomics · doi:10.1152/physiolgenomics.00043.2013 · Cited by 28

Regulation of the HIF switch in human endothelial and cancer cells

Slawski, J., Jaśkiewicz, M., Barton, A., Kozioł, S., Collawn, J. F., & Bartoszewski, R. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151386 · Cited by 26

The E3 ubiquitin ligase CHIP selectively regulates mutant epidermal growth factor receptor by ubiquitination and degradation

Chung, C., Yoo, G., Kim, T., Lee, D., Lee, C. S., Cha, H. R., Park, Y., Moon, J. Y., Jung, S. S., Kim, J. O., et al. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.111 · Cited by 26

Hypoxia and hypoxia-inducible factors in chronic kidney disease

Tanaka, S., Tanaka, T., & Nangaku, M. (2016) · Renal Replacement Therapy · doi:10.1186/s41100-016-0038-y · Cited by 28

Notch signaling promotes a HIF2α-driven hypoxic response in multiple tumor cell types

Mutvei, A. P., Landor, S. K.-J., Fox, R., Braune, E.-B., Tsoi, Y. L., Phoon, Y. P., Sahlgren, C., Hartman, J., Bergh, J. C. S., Jin, S., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0400-3 · Cited by 26

Identification of Factors Involved in the Anti-Tumor Activity of Carnosine on Glioblastomas Using a Proteomics Approach

Asperger, A., Renner, C., Menzel, M., Gebhardt, R., Meixensberger, J., & Gaunitz, F. (2011) · Cancer Investigation · doi:10.3109/07357907.2010.550666 · Cited by 26

Regulatory Molecules and Corresponding Processes of BCR-ABL Protein Degradation

Zhu, H., & Gao, F. (2019) · Journal of Cancer · doi:10.7150/jca.29528 · Cited by 23

Long-term HIF-1α stabilization reduces respiration, promotes mitophagy, and results in retinal cell death

Nsiah, N. Y., Morgan, A. B., Donkor, N., & Inman, D. M. (2023) · Scientific Reports · doi:10.1038/s41598-023-47942-8 · Cited by 27

Multiple functions of the E3 ubiquitin ligase CHIP in immunity

Zhan, S., Wang, T., & Ge, W. (2017) · International Reviews of Immunology · doi:10.1080/08830185.2017.1309528 · Cited by 23

MiR-1178 Promotes the Proliferation, G1/S Transition, Migration and Invasion of Pancreatic Cancer Cells by Targeting CHIP

Cao, Z., Xu, J., Huang, H., Shen, P. F., You, L., Zhou, L., Zheng, L., Zhang, T., & Zhao, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116934 · Cited by 23

Multifaceted C-terminus of HSP70-interacting protein regulates tumorigenesis via protein quality control

Seo, J., Han, S. Y., Seong, D., Han, H.-J., & Song, J. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-018-1101-8 · Cited by 24

CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome

Chakraborty, A., & Edkins, A. L. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-14740-1_12 · Cited by 24

DUBs, New Members in the Hypoxia Signaling clUb

Schober, A. S., & Berra, E. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00053 · Cited by 22

Decreased expression of the carboxyl terminus of heat shock cognate 70 interacting protein in human gastric cancer and its clinical significance

Gan, L., Liu, D., Lu, H., Long, G., Mei, Q., Hu, G., Qiu, H., & Hu, G. (2012) · Oncology Reports · doi:10.3892/or.2012.1957 · Cited by 22

Hypoxia-inducible factor-1α is involved in the response to heat stress in lactating dairy cows

Zhang, X., Wang, D., & Liu, J. (2023) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2023.103460 · Cited by 21

G protein pathway suppressor 2 suppresses aerobic glycolysis through RACK1-mediated HIF-1α degradation in breast cancer

Si, Y., Ou, H., Jin, X., Gu, M., Sheng, S., Peng, W., Yang, D., Zhan, X., Zhang, L., Yu, Q., et al. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.06.021 · Cited by 20

Heat Shock Proteins Regulate Activation-induced Proteasomal Degradation of the Mature Phosphorylated Form of Protein Kinase C

Lum, M. A., Balaburski, G. M., Murphy, M. E., Black, A. R., & Black, J. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437095 · Cited by 20

Decreased expression of CHIP leads to increased angiogenesis via VEGF-VEGFR2 pathway and poor prognosis in human renal cell carcinoma

Sun, C., Li, H., Chen, H., Shi, M., Liu, Q., Pan, Z., Bai, J., & Zheng, J. (2015) · Scientific Reports · doi:10.1038/srep09774 · Cited by 20

Heat Shock Protein 70 and CHIP Promote Nox4 Ubiquitination and Degradation within the Losartan Antioxidative Effect in Proximal Tubule Cells

Lorenzo, A. F. G., Costantino, V. V., Appiolaza, M. L., Cacciamani, V. E., Benardón, M. E., Bocanegra, V., & Vallés, P. G. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000430184 · Cited by 20

Macrophage infiltration in 3D cancer spheroids to recapitulate the TME and unveil interactions within cancer cells and macrophages to modulate chemotherapeutic drug efficacy

Singh, K., & Gautam, P. K. (2023) · BMC Cancer · doi:10.1186/s12885-023-11674-9 · Cited by 21

NDRG3 lowers the metastatic potential in prostate cancer as a feedback controller of hypoxia-inducible factors

Lee, G. Y., Shin, S. H., Shin, H., Chun, Y. S., & Park, J.-W. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0089-y · Cited by 20

β‐TrCP upregulates HIF‐1 in prostate cancer cells

Cohen, M., Amir, S., Golan, M., Ben‐Neriah, Y., & Mabjeesh, N. J. (2018) · The Prostate · doi:10.1002/pros.23746 · Cited by 18

Pyrithione-zinc Prevents UVB-induced Epidermal Hyperplasia by Inducing HIF-1α

Cho, Y., Lee, K.-H., & Park, J. (2010) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2010.14.2.91 · Cited by 18

Comparative Analysis of Metabolic Differences of Jersey Cattle in Different High-Altitude Areas

Kong, Z., Li, B., Zhou, C., He, Q., Zheng, Y., & Tan, Z. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.713913 · Cited by 17

Full-Length Transcriptome of Red Swamp Crayfish Hepatopancreas Reveals Candidate Genes in Hif-1 and Antioxidant Pathways in Response to Hypoxia-Reoxygenation

Xu, Y., Lin, H., Yan, W., Li, J., Sun, M., Chen, J., & Xu, Z. (2022) · Marine Biotechnology · doi:10.1007/s10126-021-10086-9 · Cited by 17

VBP1 negatively regulates CHIP and selectively inhibits the activity of hypoxia-inducible factor (HIF)-1α but not HIF-2α

Yue, Y., Tang, Y., Huang, H., Zheng, D., Liu, C., Zhang, H., Liu, Y., Li, Y., Sun, X., & Lu, L. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104829 · Cited by 17

Hypertonicity contributes to seawater aspiration-induced lung injury: Role of hypoxia-inducible factor 1α

Liu, Z., Zhang, B., Wang, X., Li, Y., Xi, R., Han, F., Li, W., Fu, L., Li, Z., & Jin, F. (2015) · Experimental Lung Research · doi:10.3109/01902148.2015.1030803 · Cited by 17

The Kaposi's Sarcoma-Associated Herpesvirus ORF34 Protein Binds to HIF-1α and Causes Its Degradation via the Proteasome Pathway

Haque, M., & Kousoulas, K. G. (2012) · Journal of Virology · doi:10.1128/jvi.02460-12 · Cited by 17

Requirement of Hsp105 in CoCl 2 -induced HIF-1α accumulation and transcriptional activation

Mikami, H., Saito, Y., Okamoto, N., Kakihana, A., Kuga, T., & Nakayama, Y. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.02.004 · Cited by 17

Novel Interaction between the Major Bacterial Heat Shock Chaperone (GroESL) and an RNA Chaperone (CspC)

Lenz, G., & Ron, E. Z. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.10.018 · Cited by 17

The insights into molecular pathways of hypoxia‐inducible factor in the brain

Ostrowski, R. P., & Zhang, J. H. (2018) · Journal of Neuroscience Research · doi:10.1002/jnr.24366 · Cited by 17

Increased expression of PHD3 represses the HIF-1 signaling pathway and contributes to poor neovascularization in pancreatic ductal adenocarcinoma

Tanaka, T., Li, T., Urata, Y., Goto, S., Ono, Y., Kawakatsu, M., Matsushima, H., Hirabaru, M., Adachi, T., Kitasato, A., et al. (2014) · Journal of Gastroenterology · doi:10.1007/s00535-014-1030-3 · Cited by 17

Hypoxia-inducible transcription factors: architects of tumorigenesis and targets for anticancer drug discovery

McDermott, A., & Tavassoli, A. (2024) · Transcription · doi:10.1080/21541264.2024.2417475 · Cited by 18

DAB2IP inhibits glucose uptake by modulating HIF-1α ubiquitination under hypoxia in breast cancer

Dong, H., Jia, W., Meng, W., Zhang, R., Qi, Z., Chen, Z., Xie, S., Min, J., Liu, L., & Shen, J. (2024) · Oncogenesis · doi:10.1038/s41389-024-00523-4 · Cited by 15

The evolutionarily conserved arginyltransferase 1 mediates a pVHL-independent oxygen-sensing pathway in mammalian cells

Moorthy, B. T., Jiang, C., Patel, D. M., Ban, Y. J., O’Shea, C. R., Kumar, A., Yuan, T., Birnbaum, M. D., Gomes, A. V., Chen, X., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.02.010 · Cited by 14

Heat Shock Protein 70 Negatively Regulates TGF-β-Stimulated VEGF Synthesis via p38 MAP Kinase in Osteoblasts

Sakai, G., Tokuda, H., Fujita, K., Kainuma, S., Kawabata, T., Matsushima‐Nishiwaki, R., Kozawa, O., & Otsuka, T. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485418 · Cited by 14

Chaperone-Mediated Regulation of Choline Acetyltransferase Protein Stability and Activity by HSC/HSP70, HSP90, and p97/VCP

Morey, T. M., Winick‐Ng, W., Seah, C., & Rylett, R. J. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00415 · Cited by 14

Bicalutamide Elicits Renal Damage by Causing Mitochondrial Dysfunction via ROS Damage and Upregulation of HIF-1

Chen, K., Chen, C.-R., Chen, C.-Y., Tzou, K.-Y., Peng, C.-C., & Peng, R. Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093400 · Cited by 13

Nkx3.2 induces oxygen concentration-independent and lysosome-dependent degradation of HIF-1α to modulate hypoxic responses in chondrocytes

Im, S., & Kim, D. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.05.001 · Cited by 14

The Pro-Oncogenic Adaptor CIN85 Acts as an Inhibitory Binding Partner of Hypoxia-Inducible Factor Prolyl Hydroxylase 2

Kozlova, N., Mennerich, D., Samoylenko, A., Dimova, E. Y., Koivunen, P., Biterova, E. I., Richter, K., Hassinen, A., Kellokumpu, S., Manninen, A., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3852 · Cited by 15

Kelch-like 20 up-regulates the expression of hypoxia-inducible factor-2α through hypoxia- and von Hippel–Lindau tumor suppressor protein-independent regulatory mechanisms

Higashimura, Y., Terai, T., Yamaji, R., Mitani, T., Ogawa, M., Harada, N., Inui, H., & Nakano, Y. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.08.058 · Cited by 13

CHIP involves in non-small cell lung cancer prognosis through VEGF pathway

Tingting, Q., Jiao, W., Qingfeng, W., Yancheng, L., Yu, S.-J., Zhaoqi, W., Dongmei, S., & ShiLong, W. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.06.015 · Cited by 12

Mutant versions of von Hippel-Lindau (VHL) can protect HIF1α from SART1-mediated degradation in clear-cell renal cell carcinoma

Ordóñez-Navadijo, Á., Fuertes-Yebra, E., Acosta‐Iborra, B., Balsa, E., Elorza, A., Aragonés, J., & Landázuri, M. O. (2015) · Oncogene · doi:10.1038/onc.2015.113 · Cited by 12

Aurora B Kinase Promotes CHIP-Dependent Degradation of HIF1α in Prostate Cancer Cells

Biswas, K., Sarkar, S., Said, N. A., Brautigan, D. L., & Larner, J. M. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0777 · Cited by 13

LUBAC promotes angiogenesis and lung tumorigenesis by ubiquitinating and antagonizing autophagic degradation of HIF1α

Jin, Y. H., Peng, Y., Xu, J., Yuan, Y., Yang, N., Zhang, Z., Xu, L., Li, L., Xiong, Y., Sun, D., et al. (2024) · Oncogenesis · doi:10.1038/s41389-024-00508-3 · Cited by 12

Fine tuning of the transcription juggernaut: A sweet and sour saga of acetylation and ubiquitination

Ghosh, A., Chakraborty, P., & Biswas, D. (2023) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2023.194944 · Cited by 11

Histone deacetylase inhibitor induced pVHL-independent degradation of HIF-1α and hierarchical quality control of pVHL via chaperone system

Ni, J., & Anping, N. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248019 · Cited by 11

Myeloid Translocation Gene-16 Co-Repressor Promotes Degradation of Hypoxia-Inducible Factor 1

Kumar, P., Gullberg, U., Olsson, I., & Ajore, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123725 · Cited by 10

Coordination of Timers and Sensors in Cell Signaling

Qian, J., Gelens, L., & Bollen, M. (2019) · BioEssays · doi:10.1002/bies.201800217 · Cited by 10

The human testis-enriched HSPA2 interacts with HIF-1α in epidermal keratinocytes, yet HIF-1α stability and HIF-1-dependent gene expression rely on the HSPA (HSP70) activity

Sojka, D. R., Gogler‐Pigłowska, A., Kania, D., Vydra, N., Wiecha, K., Adamiec‐Organiściok, M., Wilk, A., Chumak, V., Matysniak, D. P., & Ścieglińska, D. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119735 · Cited by 9

The Inhibition of Heat Shock Protein 90 Facilitates the Degradation of Poly-Alanine Expanded Poly (A) Binding Protein Nuclear 1 via the Carboxyl Terminus of Heat Shock Protein 70-Interacting Protein

Shi, C., Huang, X., Zhang, B., Zhu, D., Luo, H., Lu, Q., Xiong, W., Mei, L., & Luo, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138936 · Cited by 8

Daily Light–Dark Cycles Influence Hypoxia‐Inducible Factor 1 and Heat Shock Protein Levels in the Pacemakers of Crayfish

Velázquez-Amado, R. M., Escamilla‐Chimal, E. G., & Fanjul‐Moles, M. L. (2011) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2011.01012.x · Cited by 8

Dynamics of heat shock protein 70 kDa in heat-shocked and hypoxic human endothelial cells

Coimbra, L. B. C. T., Pinto-Martínez, A., Pavan, I. C. B., Melo, E. G., & Araujo, T. L. S. (2025) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2025.100085 · Cited by 7

The Functions of HSP70 in Normal Cells

Malyshev, I. Y. (2013) · SpringerBriefs in biochemistry and molecular biology · doi:10.1007/978-94-007-5943-5_2 · Cited by 7

CHIP suppresses the proliferation and migration of A549 cells by mediating the ubiquitination of eIF2α and upregulation of tumor suppressor RBM5

Jin, B., Wang, M., Sun, Y., Lee, P. A. H., Zhang, X., Lu, Y., & Zhao, B. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105673 · Cited by 5

Molecular architecture and regulatory dynamics of Hypoxia-Inducible Factors in livestock: A narrative review

Parsad, R., Bagiyal, M., Malhotra, S., Arora, R., & Ahlawat, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149673 · Cited by 5

Inhibition of apoptosis via CHIP‐mediated proteasomal degradation of TAp73α

Tanwar, K., & Pati, U. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28386 · Cited by 5

STUB1/CHIP promotes ubiquitination and degradation of HIV-1 Vif to restore the cellular level of APOBEC3G protein

Ali, A., Kumar, V., & Banerjea, A. C. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.08.031 · Cited by 5

A novel micropeptide, Slitharin, exerts cardioprotective effects in myocardial infarction

Ibrahim, A. G.-E., Ciullo, A., Yamaguchi, S., Li, C., Antes, T. J., Jones, X. M., Li, L., Murali, R., Maslennikov, I., Sundararaman, N., et al. (2024) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.202300128 · Cited by 4

Ubiquitous points of control over regulatory T cells

Pan, F., & Barbi, J. J. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1156-z · Cited by 4

HIF repressors under chronic hypoxia

Luo, W., & Wang, Y. (2016) · Aging · doi:10.18632/aging.100922 · Cited by 4

Brain-Derived Neurotrophic Factor and Heat Shock Protein-32: Potential Targets for Microglial Response to Glucose and Oxygen Manipulation

Mussa, B. M., Srivastava, A., Bajbouj, K., Shafarin, J., Rajan, R., & Hisham, A. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05378-3 · Cited by 3

Endothelin-1 level in the tear fluid of children with primary congenital glaucoma

Катаргина, Л. А., Chesnokova, N. B., Arestova, N. N., Sorokin, A. A., Pavlenko, T. A., Валерьевна, Б. О., & Lisovskaya, O. A. (2023) · Russian Ophthalmological Journal · doi:10.21516/2072-0076-2023-16-1-36-40 · Cited by 3

STUB1 promotes the degradation of HSPB1 and induces ferroptosis in lung cancer cells

Tieliwaerdi, A., Aini, A., Amuti, M., Aierken, Y., Nijiati, M., & Luo, B. (2024) · Environmental Toxicology · doi:10.1002/tox.24296 · Cited by 3

HSP70 promotes amino acid‐dependent mTORC1 signaling by mediating CHIP‐induced NPRL2 ubiquitination and degradation

Gao, J., Lin, M., Qing, J.-N., Li, H., Zeng, X., Yuan, W., Li, T., & He, S. (2024) · The FASEB Journal · doi:10.1096/fj.202401352r · Cited by 2

[Protective effects of heat shock protein 70 against hypoxic pulmonary hypertension in neonatal rats].

Wang, L., Wu, H.-Y., & Li, M. (2017) · PubMed Central · doi:10.7499/j.issn.1008-8830.2017.01.015 · Cited by 3

Regulation of Gene Transcription by Hypoxia-Inducible Factor 1

Semenza, G. L. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00054-2 · Cited by 3

Transcription | Regulation of Gene Transcription by Hypoxia-Inducible Factor 1α

Child, F., Frost, J., Shakir, D., Wilson, J. W., & Rocha, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00033-5 · Cited by 4

The E3 ubiquitin ligase STUB1 inhibits Senecavirus A replication by mediating VP1 ubiquitination and proteasomal degradation

Zeng, P., Mao, J., Guo, J., Yang, X., Shi, Y., Wang, X., Song, J., Zhou, J., Hou, L., & Liu, J. (2025) · Journal of Virology · doi:10.1128/jvi.01152-25 · Cited by 2

Deciphering the interplay between hypoxia, angiogenesis, and endoplasmic reticulum stress in carcinogenesis: A narrative review

Bhardwaj, S., Pandey, S., Ghosh, D. K., Sharma, T., & Jain, B. P. (2026) · World Journal of Experimental Medicine · doi:10.5493/wjem.v16.i1.115478 · Cited by 2

Hypoxia-inducible Factors—Their Regulation and Function in Neural Tissue

Baranich, T. I., Voronkova, A. S., Ануфриев, П. Л., Brydun, A. V., Анатольевна, Т. С., Glinkina, V. V., & Sukhorukov, V. S. (2020) · Human Physiology · doi:10.1134/s0362119720080022 · Cited by 2

Next-Cell Hypothesis: Mechanism of Obesity-Associated Carcinogenesis

Engin, A. B., & Engin, A. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-63657-8_25 · Cited by 2

New insights into the integrative effects of resistance training at moderate altitude on systemic inflammation

Pérez-Regalado, S., León, J., Padial, P., Benavente, C., Almeida, F., Bonitch‐Góngora, J., & Feriche, B. (2025) · European Journal of Applied Physiology · doi:10.1007/s00421-025-05842-x · Cited by 2

5,2′,4′-trihydroxy-6,7,5′-trimethoxyflavone-nanoparticle regulation mechanism of basic transcription factor 3 through hypoxia inducible factor-1α ubiquitination mediation to inhibit human hepatoma cell proliferation

Chen, J., Wang, Y., Wang, S., Cheng, H., Wang, D., Fu, J., Hao, J., Zhang, J., & Zhang, X. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157236 · Cited by 2

Ubiquitination is absolutely required for the degradation of hypoxia-inducible factor - 1 alpha protein in hypoxic conditions

Wang, R., Zhang, P., Li, J., Guan, H., & Shi, G. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.01.005 · Cited by 11

Constitutive/Hypoxic Degradation of HIF-α Proteins by the Proteasome Is Independent of von Hippel Lindau Protein Ubiquitylation and the Transactivation Activity of the Protein

Kong, X., Alvarez‐Castelao, B., Lin, Z., Castaño, J. G., & Caro, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700704200 · Cited by 72

Analysis of HIF-1alpha degradation and function

André, H. (2005) · Figshare

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

Spermidine/Spermine N1-Acetyltransferase-1 Binds to Hypoxia-inducible Factor-1α (HIF-1α) and RACK1 and Promotes Ubiquitination and Degradation of HIF-1α

Baek, J. H., Liu, Y. V., McDonald, K. R., Wesley, J. B., Zhang, H., & Semenza, G. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705627200 · Cited by 71