UCHL1 provides diagnostic and antimetastatic strategies due to its deubiquitinating effect on HIF-1α

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

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High-Efficiency Transformation of Mammalian Cells by Plasmid DNA

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A Perspective on Cancer Cell Metastasis

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

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Breast cancer metastasis: markers and models

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Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics

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Hypoxia-inducible factors: mediators of cancer progression and targets for cancer therapy

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FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity

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PrognoScan: a new database for meta-analysis of the prognostic value of genes

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Mechanism of regulation of the hypoxia‐inducible factor‐1α by the von Hippel‐Lindau tumor suppressor protein

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The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities that Affect α-Synuclein Degradation and Parkinson's Disease Susceptibility

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Correction: Corrigendum: Cancer cells that survive radiation therapy acquire HIF-1 activity and translocate toward tumour blood vessels

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Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases

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Differential prognostic impact of hypoxia induced and diffuse HIF-1α expression in invasive breast cancer

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HIF‐1α and CA IX staining in invasive breast carcinomas: Prognosis and treatment outcome

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Molecular mechanisms mediating metastasis of hypoxic breast cancer cells

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VHL protein‐interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF‐1α

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Cancer cells that survive radiation therapy acquire HIF-1 activity and translocate towards tumour blood vessels

Harada, H., Inoue, M., Itasaka, S., Hirota, K., Morinibu, A., Shinomiya, K., Zeng, L., Ou, G., Zhu, Y., Yoshimura, M., et al. (2012) · Nature Communications · doi:10.1038/ncomms1786 · Cited by 182 · see citing works

PGP9.5 As a Candidate Tumor Marker for Non-Small-Cell Lung Cancer

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The Akt/mTOR Pathway Assures the Synthesis of HIF-1α Protein in a Glucose- and Reoxygenation-dependent Manner in Irradiated Tumors

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The Tumor Suppressor UCHL1 Forms a Complex with p53/MDM2/ARF to Promote p53 Signaling and Is Frequently Silenced in Nasopharyngeal Carcinoma

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Ubiquitin C-terminal hydrolase-L1 is a key regulator of tumor cell invasion and metastasis

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PGP9.5 as a marker for invasive colorectal cancer.

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The de-ubiquitinase UCH-L1 is an oncogene that drives the development of lymphoma in vivo by deregulating PHLPP1 and Akt signaling

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HIF-1-mediated metabolic reprogramming reduces ROS levels and facilitates the metastatic colonization of cancers in lungs

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The potential role of ubiquitin c-terminal hydrolases in oncogenesis

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Optical Imaging of Tumor Hypoxia and Evaluation of Efficacy of a Hypoxia-Targeting Drug in Living Animals

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Enhancement of gene expression under hypoxic conditions using fragments of the human vascular endothelial growth factor and the erythropoietin genes

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Unique DNA Methylation Loci Distinguish Anatomic Site and HPV Status in Head and Neck Squamous Cell Carcinoma

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UCH-L1 promotes cancer metastasis in prostate cancer cells through EMT induction

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Stromal plasma cells expressing immunoglobulin G4 subclass in non–small cell lung cancer

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Ubiquitin C-Terminal Hydrolase-L1 Potentiates Cancer Chemosensitivity by Stabilizing NOXA

Brinkmann, K., Zigrino, P., Witt, A., Schell, M. J., Ackermann, L., Broxtermann, P. N., Schüll, S., Andree, M., Coutelle, O., Yazdanpanah, B., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.014 · Cited by 78 · see citing works

Hypomethylation of the protein gene product 9.5 promoter region in gallbladder cancer and its relationship with clinicopathological features

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Involvement of decreased hypoxia-inducible factor 1 activity and resultant G1–S cell cycle transition in radioresistance of perinecrotic tumor cells

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Non-terminal respiratory unit type lung adenocarcinoma has three distinct subtypes and is associated with poor prognosis

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The intravenous anesthetics barbiturates inhibit hypoxia-inducible factor 1 activation

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Prognostic relevance of ubiquitin C-terminal hydrolase L1 (UCH-L1) mRNA and protein expression in breast cancer patients

Schröder, C., Milde‐Langosch, K., Gebauer, F., Schmid, K., Müller, V., Wirtz, R. M., Meyer‐Schwesinger, C., Schlüter, H., Sauter, G., & Schumacher, U. (2013) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-013-1496-z · Cited by 24 · see citing works

Ubiquitin C‐terminal hydrolase‐L1 interacts with adhesion complexes and promotes cell migration, survival, and anchorage independent growth

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Frequent CpG methylation of ubiquitin carboxyl-terminal hydrolase 1 (UCHL1) in sporadic and hereditary Tunisian breast cancer patients: clinical significance

Trifa, F., Karray-Chouayekh, S., Jmaa, Z. B., Jmal, E., Khabir, A., Sellami‐Boudawara, T., Frikha, M., Daoud, J., & Mokdad‐Gargouri, R. (2013) · Medical Oncology · doi:10.1007/s12032-012-0418-2 · Cited by 11 · see citing works

Hypoxic control of metastasis

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Deubiquitylating enzymes and drug discovery: emerging opportunities

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HIF-1-Dependent Reprogramming of Glucose Metabolic Pathway of Cancer Cells and Its Therapeutic Significance

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Hypoxia: Signaling the Metastatic Cascade

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DUBs, Hypoxia, and Cancer

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Non-Canonical Mechanisms Regulating Hypoxia-Inducible Factor 1 Alpha in Cancer

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

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Hypoxia/pseudohypoxia‐mediated activation of hypoxia‐inducible factor‐1α in cancer

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USP22 promotes hypoxia-induced hepatocellular carcinoma stemness by a HIF1α/USP22 positive feedback loop upon TP53 inactivation

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The role of ubiquitination and deubiquitination in tumor invasion and metastasis

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Parkin targets HIF-1α for ubiquitination and degradation to inhibit breast tumor progression

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Tumor microenvironment and radioresistance

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The importance of regulatory ubiquitination in cancer and metastasis

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FOXC1-mediated LINC00301 facilitates tumor progression and triggers an immune-suppressing microenvironment in non-small cell lung cancer by regulating the HIF1α pathway

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Deubiquitinase Activity Profiling Identifies UCHL1 as a Candidate Oncoprotein That Promotes TGFβ-Induced Breast Cancer Metastasis

Liu, S., González‐Prieto, R., Zhang, M., Geurink, P. P., Kooij, R., Iyengar, P. V., van Dinther, M., Bos, E., Zhang, X., Dévédec, S. E. L., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-1373 · Cited by 159 · see citing works

Ubiquitin carboxyl-terminal hydrolases: involvement in cancer progression and clinical implications

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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

K63-polyubiquitinated HAUSP deubiquitinates HIF-1α and dictates H3K56 acetylation promoting hypoxia-induced tumour progression

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A compendium of proteins that interact with HIF-1α

Semenza, G. L. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.041 · Cited by 114 · see citing works

Hypoxia-inducible factor 1–mediated characteristic features of cancer cells for tumor radioresistance

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Role of UCHL1 in the pathogenesis of neurodegenerative diseases and brain injury

Mi, Z., & Graham, S. H. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101856 · Cited by 108 · see citing works

Correction to: FOXC1-mediated LINC00301 facilitates tumor progression and triggers an immune-suppressing microenvironment in non-small cell lung cancer by regulating the HIF1α pathway

Sun, C., Zhu, W., Li, S., Hu, W., Zhang, J., Zhuo, Y., Zhang, H., Wang, J., Zhang, Y., Huang, S.-X., et al. (2021) · Genome Medicine · doi:10.1186/s13073-021-00834-w · Cited by 107 · see citing works

Discovery of a Potent and Selective Covalent Inhibitor and Activity-Based Probe for the Deubiquitylating Enzyme UCHL1, with Antifibrotic Activity

Panyain, N., Godinat, A., Lanyon‐Hogg, T., Lachiondo‐Ortega, S., Will, E. J., Soudy, C., Mondal, M., Mason, K., Elkhalifa, S., Smith, L. M., et al. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c04527 · Cited by 106 · see citing works

Deubiquitylating Enzymes in Cancer and Immunity

Ren, J., Yu, P., Liu, S., Li, R., Niu, X., Chen, Y., Zhang, Z., Zhou, F., & Zhang, L. (2023) · Advanced Science · doi:10.1002/advs.202303807 · Cited by 107 · see citing works

The deubiquitinase UCHL1 regulates cardiac hypertrophy by stabilizing epidermal growth factor receptor

Bi, H.-L., Zhang, X.-L., Zhang, Y., Xie, X., Xia, Y., Du, J., & Li, H. (2020) · Science Advances · doi:10.1126/sciadv.aax4826 · Cited by 105 · see citing works

The ubiquitin–proteasome system in breast cancer

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Stromal Versican Regulates Tumor Growth by Promoting Angiogenesis

Asano, K., Nelson, C. M., Nandadasa, S., Aramaki‐Hattori, N., Lindner, D. J., Alban, T. J., Inagaki, J., Ohtsuki, T., Oohashi, T., Apte, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-17613-6 · Cited by 101 · see citing works

A molecular hypothesis to explain direct and inverse co-morbidities between Alzheimer’s Disease, Glioblastoma and Lung cancer

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Radiation Resistance: A Matter of Transcription Factors

Galeaz, C., Totis, C., & Bisio, A. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.662840 · Cited by 97 · see citing works

Ubiquitin-Specific Proteases: Players in Cancer Cellular Processes

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UCHL1-HIF-1 axis-mediated antioxidant property of cancer cells as a therapeutic target for radiosensitization

Nakashima, R., Gotö, Y., Koyasu, S., Kobayashi, M., Morinibu, A., Yoshimura, M., Hiraoka, M., Hammond, E. M., & Harada, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-06605-1 · Cited by 90 · see citing works

Hypoxia‐inducible factor 1 promotes chemoresistance of lung cancer by inducing carbonic anhydrase IX expression

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A circadian clock gene, PER 2, activates HIF ‐1 as an effector molecule for recruitment of HIF ‐1α to promoter regions of its downstream genes

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Epithelial-to-Mesenchymal Transition and MicroRNAs in Lung Cancer

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An Overview of the Recent Development of Anticancer Agents Targeting the HIF-1 Transcription Factor

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Natural products-prompted chemical biology: phenotypic screening and a new platform for target identification

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Functional analysis of deubiquitylating enzymes in tumorigenesis and development

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USP29-mediated HIF1α stabilization is associated with Sorafenib resistance of hepatocellular carcinoma cells by upregulating glycolysis

Gao, R., Buechel, D., Kalathur, R. K. R., Morini, M. F., Coto‐Llerena, M., Ercan, C., Piscuoglio, S., Chen, Q., Blumer, T., Wang, X., et al. (2021) · Oncogenesis · doi:10.1038/s41389-021-00338-7 · Cited by 61 · see citing works

UCH‐L1 promotes invasion of breast cancer cells through activating Akt signaling pathway

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Clinical significance of promoter methylation status of tumor suppressor genes in circulating DNA of pancreatic cancer patients

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The deubiquitinating enzyme UCHL1 promotes resistance to pemetrexed in non-small cell lung cancer by upregulating thymidylate synthase

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The de-ubiquitinase UCHL1 promotes gastric cancer metastasis via the Akt and Erk1/2 pathways

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LY6E: a conductor of malignant tumor growth through modulation of the PTEN/PI3K/Akt/HIF-1 axis

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The deubiquitinating enzyme UCHL1 negatively regulates the immunosuppressive capacity and survival of multipotent mesenchymal stromal cells

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Regulation of Cancer Metabolism by Deubiquitinating Enzymes: The Warburg Effect

Kim, S., & Baek, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126173 · Cited by 54 · see citing works

Deubiquitination of CD36 by UCHL1 promotes foam cell formation

Xia, X., Xu, Q., Liu, M., Chen, X., Liu, X., He, J., Hu, T., Yu, C., Huang, H., Liu, S., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02888-x · Cited by 51 · see citing works

The deubiquitinating enzyme UCHL1 is a favorable prognostic marker in neuroblastoma as it promotes neuronal differentiation

Gu, Y., Lv, F., Xue, M., Chen, K., Cheng, C., Ding, X., Jin, M., Xu, G., Zhang, Y., Wu, Z., et al. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0931-z · Cited by 51 · see citing works

USP33 deubiquitinates and stabilizes HIF‐2alpha to promote hypoxia response in glioma stem cells

Zhang, A., Huang, Z., Tao, W., Zhai, K., Wu, Q., Rich, J. N., Zhou, W., & Bao, S. (2022) · The EMBO Journal · doi:10.15252/embj.2021109187 · Cited by 49 · see citing works

Targeting the Ubiquitin Signaling Cascade in Tumor Microenvironment for Cancer Therapy

Liu, Q., Aminu, B., Roscow, O., & Zhang, W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020791 · Cited by 51 · see citing works

LncRNA DRAIC inhibits proliferation and metastasis of gastric cancer cells through interfering with NFRKB deubiquitination mediated by UCHL5

Zhang, Z., Hu, X., Kuang, J. C., Liao, J., & Yuan, Q. (2020) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00221-0 · Cited by 50 · see citing works

Epithelial to Mesenchymal Transition History: From Embryonic Development to Cancers

Lachat, C., Peixoto, P., & Hervouet, É. (2021) · Biomolecules · doi:10.3390/biom11060782 · Cited by 49 · see citing works

The roles of ubiquitin modifying enzymes in neoplastic disease

Kumari, N., Jaynes, P. W., Saei, A., Iyengar, P. V., Richard, J. L. C., & Eichhorn, P. J. A. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.09.002 · Cited by 49 · see citing works

UCHL1 protects against ischemic heart injury via activating HIF-1α signal pathway

Geng, B., Wang, X., Park, K. H., Lee, K. E., Kim, J., Chen, P., Zhou, X., Tan, T., Yang, C., Zou, X., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102295 · Cited by 48 · see citing works

Ubiquitin carboxy‐terminal hydrolase L1 – physiology and pathology

Matuszczak, E., Tylicka, M., Komarowska, M., Dębek, W., & Hermanowicz, A. (2020) · Cell Biochemistry and Function · doi:10.1002/cbf.3527 · Cited by 48 · see citing works

HIV-1 Tat-mediated astrocytic amyloidosis involves the HIF-1α/lncRNA BACE1-AS axis

Sil, S., Hu, G., Liao, K., Niu, F., Callen, S. E., Periyasamy, P., Fox, H. S., & Buch, S. J. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000660 · Cited by 45 · see citing works

Structural basis for specific inhibition of the deubiquitinase UCHL1

Grethe, C., Schmidt, M., Kipka, G., O’Dea, R., Gallant, K., Janning, P., & Gersch, M. (2022) · Nature Communications · doi:10.1038/s41467-022-33559-4 · Cited by 44 · see citing works

The intricate interplay between HIFs, ROS, and the ubiquitin system in the tumor hypoxic microenvironment

Wang, Y., Liu, X., Huang, W., Liang, J., & Chen, Y. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108303 · Cited by 44 · see citing works

Ubiquitin C‐Terminal Hydrolase L1: Biochemical and Cellular Characterization of a Covalent Cyanopyrrolidine‐Based Inhibitor

Krabill, A. D., Chen, H., Hussain, S., Feng, C., Abdullah, A., Das, C., Aryal, U. K., Post, C. B., Wendt, M. K., Galardy, P. J., et al. (2019) · ChemBioChem · doi:10.1002/cbic.201900434 · Cited by 44 · see citing works

A Proteomic Analysis of the Malignant Mesothelioma Secretome Using iTRAQ

Creaney, J., Dick, I. M., Leon, J. S., & Robinson, B. W. S. (2017) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20023 · Cited by 42 · see citing works

Transcriptome analysis and prognosis of ALDH isoforms in human cancer

Chang, P. M., Chen, C., Yeh, C.-C., Lu, H., Liu, T.-T., Chen, M., Liu, C., Wu, A. T. H., Yang, M., Tai, S., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-21123-4 · Cited by 43 · see citing works

Familial Mutations and Post-translational Modifications of UCH-L1 in Parkinson's Disease and Neurodegenerative Disorders

Lee, Y.-T. C., & Hsu, S. D. (2016) · Current Protein and Peptide Science · doi:10.2174/1389203717666160217143721 · Cited by 41 · see citing works

Revisiting the role of mitochondria in spinal muscular atrophy

James, R., Chaytow, H., Ledahawsky, L. M., & Gillingwater, T. H. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03819-5 · Cited by 43 · see citing works

Understanding and modeling nerve–cancer interactions

Le, T. T., & Oudin, M. J. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.049729 · Cited by 41 · see citing works

UCHL1is a biomarker of aggressive multiple myeloma required for disease progression

Hussain, S., Bedekovics, T., Chesi, M., Bergsagel, P. L., & Galardy, P. J. (2015) · Oncotarget · doi:10.18632/oncotarget.5727 · Cited by 40 · see citing works

The functional interplay between the HIF pathway and the ubiquitin system – more than a one-way road

Günter, J., Ruiz‐Serrano, A., Pickel, C., Wenger, R. H., & Scholz, C. C. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.027 · Cited by 39 · see citing works

Deubiquitinase UCHL1 Maintains Protein Homeostasis through the PSMA7–APEH–Proteasome Axis in High-grade Serous Ovarian Carcinoma

Tangri, A., Lighty, K., Loganathan, J., Mesmar, F., Podicheti, R., Zhang, C., Iwanicki, M., Drapkin, R., Nakshatri, H., & Mitra, S. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0883 · Cited by 40 · see citing works

SRSF1 and RBM4 differentially modulate the oncogenic effect of HIF-1α in lung cancer cells through alternative splicing mechanism

Chang, H.-L., & Lin, J.-C. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118550 · Cited by 38 · see citing works

Exploiting E3 ubiquitin ligases to reeducate the tumor microenvironment for cancer therapy

Li, X.-M., Zhao, Z., Xiao, Y., Xia, Q., Zhou, P., Wang, S., Wu, H., & Hu, J. (2023) · Experimental Hematology and Oncology · doi:10.1186/s40164-023-00394-2 · Cited by 38 · see citing works

Therapeutic Targeting of Epithelial Plasticity Programs: Focus on the Epithelial-Mesenchymal Transition

Malek, R. A., Wang, H., Taparra, K., & Tran, P. T. (2017) · Cells Tissues Organs · doi:10.1159/000447238 · Cited by 37 · see citing works

2D Core/Shell‐Structured Mesoporous Silicene@Silica for Targeted and Synergistic NIR‐II‐Induced Photothermal Ablation and Hypoxia‐Activated Chemotherapy of Tumors

Yin, H., Zhou, B., Zhao, C., Sun, L., Yue, W., Li, X., Li, H., Li, S., Xu, H., & Chen, Y. (2021) · Advanced Functional Materials · doi:10.1002/adfm.202102043 · Cited by 37 · see citing works

The role of hypoxic signalling in metastasis: towards translating knowledge of basic biology into novel anti-tumour strategies

Henríquez, J. A., Sleeman, J. P., & Garvalov, B. K. (2018) · Clinical & Experimental Metastasis · doi:10.1007/s10585-018-9930-x · Cited by 37 · see citing works

Ubiquitin carboxyl-terminal esterase L1 (UCHL1) is associated with stem-like cancer cell functions in pediatric high-grade glioma

Sánchez-Díaz, P. C., Chang, J. C., Moses, E. S., Dao, T., Chen, Y., & Hung, J. Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176879 · Cited by 34 · see citing works

HIF-1 maintains a functional relationship between pancreatic cancer cells and stromal fibroblasts by upregulating expression and secretion of Sonic hedgehog

Katagiri, T., Kobayashi, M., Yoshimura, M., Morinibu, A., Itasaka, S., Hiraoka, M., & Harada, H. (2018) · Oncotarget · doi:10.18632/oncotarget.24156 · Cited by 34 · 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

Hypoxia-Inducible Factor-Dependent and Independent Mechanisms Underlying Chemoresistance of Hypoxic Cancer Cells

Lee, P. W. T., Koseki, L. R., Haitani, T., Harada, H., & Kobayashi, M. (2024) · Cancers · doi:10.3390/cancers16091729 · Cited by 34 · see citing works

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 33 · see citing works

Astrocytes & Astrocyte derived Extracellular Vesicles in Morphine Induced Amyloidopathy: Implications for Cognitive Deficits in Opiate Abusers

Sil, S., Singh, S., Chemparathy, D. T., Chivero, E. T., Gordon, L., & Buch, S. J. (2021) · Aging and Disease · doi:10.14336/ad.2021.0406 · Cited by 32 · see citing works

UCHL1 Regulates Melanogenesis through Controlling MITF Stability in Human Melanocytes

Seo, E. Y., Jin, S., Sohn, K., Park, C., Lee, D. H., & Chung, J. H. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.03.024 · Cited by 33 · see citing works

C-Terminal Farnesylation of UCH-L1 Plays a Role in Transport of Epstein-Barr Virus Primary Oncoprotein LMP1 to Exosomes

Kobayashi, E., Aga, M., Kondo, S., Whitehurst, C. B., Yoshizaki, T., Pagano, J. S., & Shackelford, J. (2018) · mSphere · doi:10.1128/msphere.00030-18 · Cited by 32 · see citing works

Hypermethylation of UCHL1 Promotes Metastasis of Nasopharyngeal Carcinoma by Suppressing Degradation of Cortactin (CTTN)

Zhao, Y., Lei, Y., He, S., Li, Y., Wang, Y., Hong, X.-H., Liang, Y., Li, J., Chen, Y., Luo, W.-J., et al. (2020) · Cells · doi:10.3390/cells9030559 · Cited by 31 · see citing works

BAP1 is a novel regulator of HIF-1α

Bononi, A., Wang, Q., Zolondick, A. A., Bai, F., Steele-Tanji, M., Suarez, J. S., Pastorino, S., Sipes, A., Signorato, V., Ferro, A., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217840120 · Cited by 32 · see citing works

Ubiquitin C‑terminal hydrolase‑L1: A new cancer marker and therapeutic target with dual effects (Review)

Wang, X., Zhang, N., Li, M., Hong, T., Meng, W., & Ouyang, T. (2023) · Oncology Letters · doi:10.3892/ol.2023.13709 · Cited by 31 · see citing works

Inhibition of UCH-L1 Deubiquitinating Activity with Two Forms of LDN-57444 Has Anti-Invasive Effects in Metastatic Carcinoma Cells

Kobayashi, E., Hwang, D., Bheda-Malge, A., Whitehurst, C. B., Kabanov, A. V., Kondo, S., Aga, M., Yoshizaki, T., Pagano, J. S., Sokolsky‐Papkov, M., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153733 · Cited by 30 · see citing works

Roles of ubiquitination in the crosstalk between tumors and the tumor microenvironment (Review)

Zhang, X., Meng, T., Cui, S., Liu, D., Pang, Q., & Wang, P. (2022) · International Journal of Oncology · doi:10.3892/ijo.2022.5374 · Cited by 29 · see citing works

The essential role of PRAK in tumor metastasis and its therapeutic potential

Wang, Y., Wang, W., Wu, H., Zhou, Y. J., Qin, X., Wang, Y., Wu, J., Sun, X., Yang, Y. G., Xu, H. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21993-9 · Cited by 28 · see citing works

Ubiquitin C-Terminal Hydrolase L1 (UCH-L1) Promotes Hippocampus-Dependent Memory via Its Deubiquitinating Effect on TrkB

Guo, Y., Lu, Y., Zheng, Y., Chen, X., Dong, J., Yuan, R.-R., Huang, S., Yu, H., Wang, Y., Chen, Z.-Y., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3148-16.2017 · Cited by 28 · see citing works

Ubiquitin C‐terminal hydrolase L1 promotes expression of programmed cell death‐ligand 1 in non‐small‐cell lung cancer cells

Mao, R., Tan, X., Xiao, Y., Wang, X., Wei, Z., Wang, J., Wang, X., Zhou, H., Zhang, L., & Shi, Y. (2020) · Cancer Science · doi:10.1111/cas.14529 · Cited by 26 · see citing works

Overexpression of ubiquitin carboxyl-terminal hydrolase L1 (UCHL1) in serum of children after thermal injury

Matuszczak, E., Tylicka, M., Dębek, W., Sankiewicz, A., Gorodkiewicz, E., & Hermanowicz, A. (2017) · Advances in Medical Sciences · doi:10.1016/j.advms.2016.07.004 · Cited by 26 · see citing works

Ubiquitin carboxyl‐terminal hydrolase L1 promotes hypoxia‐inducible factor 1‐dependent tumor cell malignancy in spheroid models

Li, X., Hattori, A., Takahashi, S., Gotö, Y., Harada, H., & Kakeya, H. (2019) · Cancer Science · doi:10.1111/cas.14236 · Cited by 25 · see citing works

LINE-1 methylation level and prognosis in pancreas cancer: pyrosequencing technology and literature review

Yamamura, K., Kosumi, K., Baba, Y., Harada, K., Gao, F., Zhang, X., Zhou, L., Kitano, Y., Arima, K., Kaida, T., et al. (2017) · Surgery Today · doi:10.1007/s00595-017-1539-1 · Cited by 25 · see citing works

Comprehensive single-cell transcriptome analysis reveals heterogeneity in endometrioid adenocarcinoma tissues

Hashimoto, S., Tabuchi, Y., Yurino, H., Hirohashi, Y., Deshimaru, S., Asano, T., Mariya, T., Oshima, K., Takamura, Y., Ukita, Y., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-14676-3 · Cited by 26 · see citing works

Comprehensive Proteomic Characterization Reveals Subclass-Specific Molecular Aberrations within Triple-negative Breast Cancer

Kosok, M., Shaik, A. A., Bay, B., & Gunaratne, J. (2020) · iScience · doi:10.1016/j.isci.2020.100868 · Cited by 25 · see citing works

Hypoxia inducible factor signaling in breast tumors controls spontaneous tumor dissemination in a site-specific manner

Todd, V. M., Vecchi, L. A., Clements, M. E., Snow, K. P., Ontko, C. D., Himmel, L. E., Pinelli, C. J., Rafat, M., & Johnson, R. W. (2021) · Communications Biology · doi:10.1038/s42003-021-02648-3 · Cited by 24 · see citing works

SPINK1 as a plasma marker for tumor hypoxia and a therapeutic target for radiosensitization

Suwa, T., Kobayashi, M., Shirai, Y., Nam, J., Tabuchi, Y., Takeda, N., Akamatsu, S., Ogawa, O., Mizowaki, T., Hammond, E. M., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.148135 · Cited by 24 · see citing works

HIF-2α, acting via miR-191, is involved in angiogenesis and metastasis of arsenite-transformed HBE cells

Xu, W., Luo, F., Sun, B., Ye, H., Li, J., Shi, L., Liu, Y., Lü, X., Wang, B., Wang, Q., et al. (2015) · Toxicology Research · doi:10.1039/c5tx00225g · Cited by 24 · see citing works

Mitochondrial apoptosis and curtailment of hypoxia‐inducible factor‐1α/fatty acid synthase: A dual edge perspective of gamma linolenic acid in ER+ mammary gland cancer

Roy, S., Singh, M., Rawat, A. K., Kumar, D., & Kaithwas, G. (2020) · Cell Biochemistry and Function · doi:10.1002/cbf.3513 · Cited by 24 · see citing works

Comprehensive analysis of ubiquitin-proteasome system genes related to prognosis and immunosuppression in head and neck squamous cell carcinoma

Wang, J., Li, J., Zhang, L., Qin, Y., Zhang, F., Hu, R., Chen, H., Tian, Y., Liu, Z., Tian, Y., et al. (2021) · Aging · doi:10.18632/aging.203411 · Cited by 23 · see citing works

AK-1, a SIRT2 inhibitor, destabilizes HIF-1α and diminishes its transcriptional activity during hypoxia

Lee, S. D., Kim, W., Jeong, J., Park, J., & Kim, J. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.01.031 · Cited by 23 · see citing works

Concentration of UHCL1 in the Serum of Children with Acute Appendicitis, Before and After Surgery, and Its Correlation with CRP and Prealbumin

Matuszczak, E., Tylicka, M., Dębek, W., Tokarzewicz, A., Gorodkiewicz, E., & Hermanowicz, A. (2017) · Journal of Investigative Surgery · doi:10.1080/08941939.2017.1282559 · Cited by 23 · see citing works

The emerging roles of the ubiquitination/deubiquitination system in tumor radioresistance regarding DNA damage responses, cell cycle regulation, hypoxic responses, and antioxidant properties: Insight into the development of novel radiosensitizing strategies

Gotö, Y., Koyasu, S., Kobayashi, M., & Harada, H. (2017) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2017.07.007 · Cited by 23 · see citing works

Abstract A201: UCHL1 promotes distant tumor metastasis through its deubiquitinating effect on HIF-1α

Harada, H. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.targ-15-a201

175 UCHL1 promotes distant tumor metastasis through its deubiquitinating effect on HIF-1α

Harada, H. (2015) · European Journal of Cancer · doi:10.1016/s0959-8049(16)30072-7

ARTICLE

Sowa, T., Menju, T., Sonobe, M., Kakeya, H., Toi, M., Date, H., Hammond, E. M., Hiraoka, M., & Harada, H. (2016)

Abstract B119: Inhibition of UCHL1 blocks proliferation and metastasis in HIF-1 dependent tumor malignancy

Li, X., Hattori, A., Takahashi, S., Gotö, Y., Harada, H., & Kakeya, H. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.targ-19-b119

Ubiquitin carboxyl‐terminal hydrolase L1 promotes hypoxia‐inducible factor 1‐dependent tumor cell malignancy in spheroid models

Li, X., Hattori, A., Takahashi, S., Gotö, Y., Harada, H., & Kakeya, H. (2019) · Cancer Science · doi:10.1111/cas.14236 · Cited by 25 · see citing works