Cited by 251Cancer, Hypoxia, and MetabolismAngiogenesis and VEGF in CancerErythropoietin and Anemia Treatment

The DOI matches its Crossref record; 121 of the 122 references it cites were found in a registry or an index.

HIF-1 in cancer therapy: two decade long story of a transcription factor

Open access

Soni, Sourabh, Padwad, Yogendra S.·2017·Acta Oncologica

DOI 10.1080/0284186x.2017.1301680

Open this paper in CoChat — free account Open PDF

Abstract

Background: Oxygen (O2) homeostasis is an indispensable requirement of eukaryotes. O2 concentration in cellular milieu is defined as normoxia (∼21% O2), physoxia (∼1–13% O2) or hypoxia (∼0.1–1% O2). Hypoxia, a striking micro-environmental feature in tumorigenesis, is countered by tumor cells via induction of O2 governed transcription factor, hypoxia inducible factor-1 (HIF-1). Post discovery, HIF-1 has emerged as a promising anticancer therapeutic target during the last two decades. Recent reports have highlighted that enhanced levels of HIF-1 correlate with tumor metastasis leading to poor patient prognosis.Material and methods: A systematic search in PubMed and SciFinder for the literature on HIF-1 biology and therapeutic importance in cancer was carried out.Results: This review highlights the initial description as well as the recent insights into HIF-1 biology and regulation. We have focused on emerging data regarding varied classes of HIF-1 target genes affecting various levels of crosstalk among tumorigenic pathways. We have emphasized on the fact that HIF-1 acts as a networking hub coordinating activities of multiple signaling molecules influencing tumorigenesis. Emerging evidences indicate role of many HIF-induced proteomic and genomic alterations in malignant progression by mediating a myriad of genes stimulating angiogenesis, anaerobic metabolism and survival of cancer cells in O2-deficient microenvironment.Conclusions: Better understanding of the crucial role of HIF-1 in carcinogenesis could offer promising new avenues to researchers and aid in elucidating various open issues regarding the use of HIF-1 as an anticancer therapeutic target. In spite of large efforts in this field, many questions still remain unanswered. Hence, future investigations are necessary to devise, assess and refine methods for translating previous research efforts into novel clinical practices in cancer treatment.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1080/0284186x.2017.1301680

Cites

121 of 121 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

4 retracted

RETRACTED: Hypoxia-inducible factors are required for chemotherapy resistance of breast cancer stem cells
Samanta, D., Gilkes, D. M., Chaturvedi, P., Xiang, L., & Semenza, G. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421438111 · Cited by 460
Retracted
RETRACTED: Acriflavine inhibits HIF-1 dimerization, tumor growth, and vascularization
Lee, K., Zhang, H., Qian, D. Z., Rey, S., Liu, J. O., & Semenza, G. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909353106 · Cited by 451 · cited 1×
“In vivo investigations revealed that targeting HIF-1 function significantly inhibits tumor vascularization [79].”
Background
Retracted
RETRACTED ARTICLE: HIF-1-dependent expression of angiopoietin-like 4 and L1CAM mediates vascular metastasis of hypoxic breast cancer cells to the lungs
Zhang, H., Wong, C. C. L., Wei, H., Gilkes, D. M., Korangath, P., Chaturvedi, P., Schito, L., Chen, J., Krishnamachary, B., Winnard, P. T., et al. (2012) · Oncogene · doi:10.1038/onc.2011.365 · Cited by 326
Retracted
RETRACTED: Hypoxia induced E-cadherin involving regulators of Hippo pathway due to HIF-1α stabilization/nuclear translocation in bone metastasis from breast carcinoma
Maroni, P., Matteucci, E., Drago, L., Banfi, G., Bendinelli, P., & Desiderio, M. A. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.10.004 · Cited by 32
Retracted
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 · cited 1×
“HIF-1a, a basic-helix-loop-helix (bHLH)-PER (Period)ARNT-SIM (single minded) (PAS) superfamily member is the O2-labile subunit and is ubiquitously expressed in hypoxia [10].”
Background
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 · cited 1×
“[19] first demonstrated a central role of pVHL in HIF-1a regulation in 1999, and during the next decade mechanistic specifications of pVHL-HIF pathway and regulation of proteasomal degradation and polyubiquitylation were elucidated.”
Background
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 · cited 1×
“Under normal O2 tension, the PHDs become active and cause prolyl hydroxylation in HIF-1, leading to a recognition indicator for pVHL binding, ubiquitylation and subsequent degradation of HIF-1a [33].”
Background
Succinate is an inflammatory signal that induces IL-1β through HIF-1α
Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176 · cited 1×
“HIF-1 serves as an important moderator of the Warburg effect, the tumor-related metabolic switch, which helps cancer cells to create energy largely by disintegration of glucose in a non-oxidative manner rather than typical oxidative phosphorylation [64].”
Background
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 · cited 1×
“are hydroxylated by prolyl-4-hydroxylases (PHDs) [15].”
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
Untitled work
(1999) · PubMed · Cited by 2,204
Purification and Characterization of Hypoxia-inducible Factor 1
Wang, G. L., & Semenza, G. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1230 · Cited by 2,094 · cited 1×
“Since its discovery [4], biochemical purification and molecular characterization [5], there has been an exponential rise in the interest to study the importance of HIF-1 in tumor biology in the past two decades, which has been depicted in a timeline form in Figure 1.”
Background
HIF-1α pathway: role, regulation and intervention for cancer therapy
Masoud, G. N., & Li, W. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.05.007 · Cited by 1,871
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
Hypoxia-Inducible Factor-1 (HIF-1)
Ke, Q., & Costa, M. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.027029 · Cited by 1,690
Hypoxia-inducible Factor 1α (HIF-1α) Protein Is Rapidly Degraded by the Ubiquitin-Proteasome System under Normoxic Conditions
Salceda, S., & Caro, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22642 · Cited by 1,674
Hypoxia-inducible factors: mediators of cancer progression and targets for cancer therapy
Semenza, G. L. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.01.005 · Cited by 1,514
The metastatic niche: adapting the foreign soil
Psaila, B., & Lyden, D. C. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2621 · Cited by 1,344
Hypoxic control of metastasis
Rankin, E. B., & Giaccia, A. J. (2016) · Science · doi:10.1126/science.aaf4405 · Cited by 1,340 · cited 1×
“Hypoxia abundantly occurs in core of the tumors owing to high proliferation rates of cancer cells coupled with the presence of abnormal vasculature [2].”
Background
HIF-1 Regulates Cytochrome Oxidase Subunits to Optimize Efficiency of Respiration in Hypoxic Cells
Fukuda, R., Zhang, H., Kim, J.-W., Shimoda, L., Dang, C. V., & Semenza, G. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.047 · Cited by 1,225 · cited 1×
“Also it has been seen that under hypoxic condition, HIF-1a manipulates cytochrome c oxidase subunit 4 (COX4) switch, a homeostatic response optimizing respiration efficacy at varied O2 concentrations [71].”
Background
Oxygen Sensing, Hypoxia-Inducible Factors, and Disease Pathophysiology
Semenza, G. L. (2013) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104720 · Cited by 1,185 · cited 3×
“Oxygen (O2) homeostasis is a critically important factor for the survival of vertebrates [1].”
BackgroundInfluential
Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1
Manalo, D. J., Rowan, A., Lavoie, T., Natarajan, L., Kelly, B. D., Ye, S. Q., Garcia, J. G. N., & Semenza, G. L. (2005) · Blood · doi:10.1182/blood-2004-07-2958 · Cited by 1,154
Recommendations on the Use of 18 F-FDG PET in Oncology
Fletcher, J. W., Djulbegović, B., Soares, H. P., Siegel, B. A., Lowe, V. J., Lyman, G. H., Coleman, R. E., Wahl, R. L., Paschold, J. C., Avril, N. E., et al. (2008) · Journal of Nuclear Medicine · doi:10.2967/jnumed.107.047787 · Cited by 1,113 · cited 1×
“This is such a reliable indication that it acts as a basis for diagnosis of tumor in patients by 18-F-fluorodeoxyglucose-positron emission tomography (FDG-PET) to ascertain metastases by imaging of FDG tracer [63].”
Background
Dimerization, DNA Binding, and Transactivation Properties of Hypoxia-inducible Factor 1
Jiang, B.-H., Rue, E., Wang, G. L., Roe, R., & Semenza, G. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17771 · Cited by 1,106 · cited 1×
“On the other hand, the carboxy (COOH ) terminus possesses oxygen-dependent degradation domain (ODDD), which confers O2-dependent instability and also two autonomous transactivation domains (N-TAD and C-TAD) in addition to an inhibitory domain (ID, negative regulator of the transactivation domains) [11].”
Background
Oxygen Sensing, Homeostasis, and Disease
Semenza, G. L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1011165 · Cited by 1,014
Hypoxia-inducible nuclear factors bind to an enhancer element located 3' to the human erythropoietin gene.
Semenza, G. L., Nejfelt, M. K., Chi, S. M., & Antonarakis, S. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5680 · Cited by 990 · cited 1×
“Studies on the molecular mechanisms of hematopoietic growth hormone erythropoietin (EPO) induction, the most salient response to hypoxia, set the course for recognition of HIF-1 which operates ubiquitously in mammalian cells [3].”
Background
Recruitment of HIF-1α and HIF-2α to common target genes is differentially regulated in neuroblastoma: HIF-2α promotes an aggressive phenotype
Holmquist-Mengelbier, L., Fredlund, E., Löfstedt, T., Noguera, R., Navarro, S., Nilsson, H., Pietras, A., Vallon-Christersson, J., Borg, Å., Gradin, K., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.026 · Cited by 735
Metastatic Stem Cells: Sources, Niches, and Vital Pathways
Óskarsson, T., Batlle, E., & Massagué, J. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.02.002 · Cited by 726
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
Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer
Wigerup, C., Påhlman, S., & Bexell, D. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.04.009 · Cited by 687
Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of theCBP/p300 coactivator by the hypoxia‐induciblefactor‐1α
Kallio, P. J., Okamoto, K., O'Brien, S., Carrero, P., Makino, Y., Tanaka, H., & Poellinger, L. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6573 · Cited by 669 · cited 3×
“(NLS-N) and 718–721 (NLS-C) [13] (Figure 2).”
Influential
Antiangiogenic agents increase breast cancer stem cells via the generation of tumor hypoxia
Conley, S. J., Gheordunescu, E., Kakarala, P., Newman, B., Korkaya, H., Heath, A. N., Clouthier, S. G., & Wicha, M. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018866109 · Cited by 663
Disrupting proton dynamics and energy metabolism for cancer therapy
Parks, S. K., Chiche, J., & Pouysségur, J. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3579 · Cited by 631 · cited 1×
“Collectively, the acidic milieu and metabolic transformation provides plenty of metabolic intermediates that spur progression and aggressiveness of tumors [67].”
Background
The interplay between MYC and HIF in cancer
Dang, C. V., Kim, J., Gao, P., & Yustein, J. T. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2274 · Cited by 621
Cell type-specific regulation of angiogenic growth factor gene expression and induction of angiogenesis in nonischemic tissue by a constitutively active form of hypoxia-inducible factor 1
Kelly, B. D., Hackett, S. F., Hirota, K., Oshima, Y., Cai, Z., Berg-Dixon, S., Rowan, A., Yan, Z., Campochiaro, P. A., & Semenza, G. L. (2003) · Circulation Research · doi:10.1161/01.res.0000102937.50486.1b · Cited by 611
HIF ‐1 at the crossroads of hypoxia, inflammation, and cancer
Balamurugan, K. (2015) · International Journal of Cancer · doi:10.1002/ijc.29519 · Cited by 588 · cited 2×
“cell proliferation/viability, invasion and metastasis [9].”
Background
Mammalian target of rapamycin up-regulation of pyruvate kinase isoenzyme type M2 is critical for aerobic glycolysis and tumor growth
Sun, Q., Chen, X., Ma, J., Peng, H., Wang, F., Zha, X., Wang, Y., Jing, Y., Yang, H., Chen, R., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014769108 · Cited by 586
Induction of HIF–1α in response to hypoxia is instantaneous
Jewell, U. R., Kvietikova, I., Scheid, A., Bauer, C., Wenger, R. H., & Gassmann, M. (2001) · The FASEB Journal · doi:10.1096/fj.00-0732fje · Cited by 567 · cited 1×
“accurately projected as O2 sensors coupling HIF-mediated molecular responses to cellular O2 levels [16].”
Background
Hypoxia-inducible factor-1-dependent mechanisms of vascularization and vascular remodelling
Rey, S., & Semenza, G. L. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq045 · Cited by 555 · cited 2×
“inhibitors of matrix metalloproteinases (TIMP-1) [78].”
The contribution of VHL substrate binding and HIF1-α to the phenotype of VHL loss in renal cell carcinoma
Maranchie, J. K., Vasselli, J. R., Riss, J., Bonifacino, J. S., Linehan, W. M., & Klausner, R. D. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00044-2 · Cited by 442
Hypoxia-inducible factor 1 is a master regulator of breast cancer metastatic niche formation
Wong, C. C.-L., Gilkes, D. M., Zhang, H., Chen, J., Wei, H., Chaturvedi, P., Fraley, S. I., Wong, C.-M., Khoo, U.-S., Ng, I. O.-L., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113483108 · Cited by 437
HIF-1α Modulates Energy Metabolism in Cancer Cells by Inducing Over-Expression of Specific Glycolytic Isoforms
Marín‐Hernández, Á., Gallardo‐Pérez, J. C., Ralph, S. J., Rodríguez‐Enríquez, S., & Moreno‐Sánchez, R. (2009) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955709788922610 · Cited by 433 · cited 1×
“HIF-1 stimulates the expression and activation of glycolytic enzyme isoforms differing from those found in normal cells, thereby supporting the Warburg effect by potentiating macromolecular biosynthesis and energy production pathways in human cancers [65].”
Background
Hypoxia-Inducible Factor-1-Dependent Repression of E-cadherin in von Hippel-Lindau Tumor Suppressor–Null Renal Cell Carcinoma Mediated by TCF3, ZFHX1A, and ZFHX1B
Krishnamachary, B., Zagzag, D., Nagasawa, H., Rainey, K., Okuyama, H., Baek, J. H., & Semenza, G. L. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3719 · Cited by 415
Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis
Xia, X., Lemieux, M. E., Li, W., Carroll, J. S., Brown, M., Liu, X. S., & Kung, A. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810067106 · Cited by 410
Targeting HIF1α Eliminates Cancer Stem Cells in Hematological Malignancies
Wang, Y., Liu, Y., Malek, S. N., Zheng, P., & Liu, Y. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.02.006 · Cited by 410
PKM2 promotes tumor angiogenesis by regulating HIF-1α through NF-κB activation
Azoitei, N., Becher, A., Steinestel, K., ROUHI, A. M., Diepold, K., Genze, F., Simmet, T., & Seufferlein, T. T. W. (2016) · Molecular Cancer · doi:10.1186/s12943-015-0490-2 · Cited by 346
Hypoxia-Inducible Factor-1-Dependent Repression of E-cadherin in von Hippel-Lindau Tumor Suppressor—Null Renal Cell Carcinoma Mediated by TCF3, ZFHX1A, and ZFHX1B
Gordon, M. S. (2007) · Yearbook of Oncology · doi:10.1016/s1040-1741(08)70352-x · Cited by 343
Regulation of Metabolism by Hypoxia-Inducible Factor 1
Semenza, G. L. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010678 · Cited by 342 · cited 2×
“In the glycolytic pathway, HIF-1 targets include hexokinase 1 and 2 (HK1, HK2) enzymes, glucose transporters 1 and 3 (GLUT1, GLUT3), lactate dehydrogenase-A (LDH-A), aldolase A and C (ALD-A, ALD-C), phosphofructokinase liver type (PFK-L), 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), enolase alpha…”
Background
The Oxygen Sensor Factor-Inhibiting Hypoxia-Inducible Factor-1 Controls Expression of Distinct Genes through the Bifunctional Transcriptional Character of Hypoxia-Inducible Factor-1α
Dayan, F., Roux, D., Brahimi-Horn, M. C., Pouyssegur, J., & Mazure, N. M. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4564 · Cited by 294
Loss of the Tumor Suppressor LKB1 Promotes Metabolic Reprogramming of Cancer Cells via HIF-1α
Faubert, B., Vincent, E. E., Griss, T., Samborska, B., Izreig, S., Svensson, R. U., Mamer, O. A., Avizonis, D., Shackelford, D. B., Shaw, R. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312570111 · Cited by 278
Reciprocal influence of the p53 and the hypoxic pathways
Sermeus, A., & Michiels, C. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.48 · Cited by 278
Oxygen-independent Regulation of HIF-1: Novel Involvement of PI3K/ AKT/mTOR Pathway in Cancer
Agani, F. H., & Jiang, B. (2013) · Current Cancer Drug Targets · doi:10.2174/1568009611313030003 · Cited by 265 · cited 4×
“Similarly, loss of PTEN can promote increased glucose uptake through elevated PI3K/Akt/mTOR signaling [103] while loss of the VHL also promotes a similar metabolic phenotype through stabilization of the HIF-1a [104].”
BackgroundInfluential
Structural Basis for Binding of Hypoxia-Inducible Factor to the Oxygen-Sensing Prolyl Hydroxylases
Chowdhury, R., McDonough, M. A., Mecinović, J., Loenarz, C., Flashman, E., Hewitson, K. S., Domene, C., & Schofield, C. J. (2009) · Structure · doi:10.1016/j.str.2009.06.002 · Cited by 241 · cited 1×
“humans) located in the LXXLAP motif [14] in ODDD of HIF-1a”
Background
Hypoxia-Inducible Factor 3 Is an Oxygen-Dependent Transcription Activator and Regulates a Distinct Transcriptional Response to Hypoxia
Zhang, P., Yao, Q., Lu, L., Li, Y., Chen, P.-J., & Duan, C. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.011 · Cited by 238 · cited 2×
“Recent reports have indicated that HIF-3a is hypoxia-activated and promotes a distinct transcriptional response in zebrafish embryos [30].”
Background
Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803
McNEILL, L. A., HEWITSON, K. S., CLARIDGE, T. D., SEIBEL, J. F., HORSFALL, L. E., & SCHOFIELD, C. J. (2002) · Biochemical Journal · doi:10.1042/bj20021162 · Cited by 215 · cited 2×
“This drives the blocking of interaction between C-TAD and CBP/p300 domains and further abrogation of gene transcription by HIF-1a [20].”
Background
The HIF-1 Hypoxia-Inducible Factor Modulates Lifespan in C. elegans
Zhang, Y., Shao, Z., Zhai, Z., Shen, C., & Powell-Coffman, J. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006348 · Cited by 211
The role of melanogenesis in regulation of melanoma behavior: Melanogenesis leads to stimulation of HIF-1α expression and HIF-dependent attendant pathways
Slominski, A. T., Kim, T.-K., Brożyna, A. A., Janjetović, Z., Brooks, D. L. P., Schwab, L. P., Skobowiat, C., Jóźwicki, W., & Seagroves, T. N. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.06.030 · Cited by 208
HIF1α is required for survival maintenance of chronic myeloid leukemia stem cells
Zhang, H., Li, H., Xi, H. S., & Li, S. (2012) · Blood · doi:10.1182/blood-2011-10-387381 · Cited by 196
Pyruvate kinase M2 regulates glucose metabolism by functioning as a coactivator for hypoxia-inducible factor 1 in cancer cells
Luo, W., & Semenza, G. L. (2011) · Oncotarget · doi:10.18632/oncotarget.299 · Cited by 193 · cited 1×
“Instead of PKM1, PKM2 physically joins HIF-1 stimulating its activity [66].”
Background
Hypoxia Inducible Factor Pathway and Physiological Adaptation: A Cell Survival Pathway?
Kumar, H., & Choi, D. (2015) · Mediators of Inflammation · doi:10.1155/2015/584758 · Cited by 192
Hypoxia-inducible factor 1 is required for remote ischemic preconditioning of the heart
Cai, Z. P., Luo, W., Zhan, H., & Semenza, G. L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317158110 · Cited by 190
Hypoxia-Inducible Factor 1α in Clear Cell Renal Cell Carcinoma
Klatte, T., Seligson, D. B., Riggs, S. B., Leppert, J. T., Berkman, M. K., Kleid, M. D., Yu, H., Kabbinavar, F. F., Pantuck, A. J., & Belldegrun, A. S. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-0411 · Cited by 187
Bcl-2 Family Members and Functional Electron Transport Chain Regulate Oxygen Deprivation-Induced Cell Death
McClintock, D. S., Santore, M. T., Lee, V. Y., Brunelle, J. K., Budinger, G. R. S., Zong, W., Thompson, C. B., Hay, N., & Chandel, N. S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.94-104.2002 · Cited by 187
Copper activates HIF-1α/GPER/VEGF signalling in cancer cells
Rigiracciolo, D. C., Scarpelli, A., Lappano, R., Pisano, A., Santolla, M. F., Marco, P. D., Cirillo, F., Cappello, A. R., Dolce, V., Belfiore, A., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5779 · Cited by 185
Functional regulation of HIF‐1α under normoxia—is there more than post‐translational regulation?
Kuschel, A., Simon, P. D., & Tug, S. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22798 · Cited by 174 · cited 2×
“Conversely, hypoxic condition results in stability and transcriptional activity of HIF-1a (as discussed above), through several pathways and post-translational modifications (hydroxylation, acetylation, ubiquitylation, phosphorylation, sumoylation, S-nitrosation) [32].”
Background
Integrated analysis of microRNA and mRNA expression and association with HIF binding reveals the complexity of microRNA expression regulation under hypoxia
Camps, C., Saini, H. K., Mole, D. R., Choudhry, H., Reczko, M., Guerra‐Assunção, J. A., Tian, Y., Buffa, F. M., Harris, A. L., Hatzigeorgiou, A. G., et al. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-28 · Cited by 163 · cited 1×
“activating genes that encode microRNAs [6] and chromatin-”
Background
HIF-1: master and commander of the hypoxic world
Mazure, N. M., Brahimi-Horn, M. C., Berta, M., Benizri, E. I., Bilton, R. L., Dayan, F., Ginouvès, A., Berra, E., & Pouysségur, J. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.04.022 · Cited by 162
S‐nitrosation of Cys‐800 of HIF‐1α protein activates its interaction with p300 and stimulates its transcriptional activity
Yasinska, I. M., & Sumbayev, V. V. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00807-x · Cited by 156
Interaction of the PAS B Domain with HSP90 Accelerates Hypoxia-Inducible Factor-1α Stabilization
Katschinski, D. M., Le, L., Schindler, S., Thomas, T., Voss, A. K., & Wenger, R. H. (2004) · Cellular Physiology and Biochemistry · doi:10.1159/000080345 · Cited by 145
Hypoxia Induces VEGF-C Expression in Metastatic Tumor Cells via a HIF-1α-Independent Translation-Mediated Mechanism
Morfoisse, F., Kuchnio, A., Frainay, C., Gomez‐Brouchet, A., Delisle, M., Marzi, S., Helfer, A., Hantelys, F., Pujol, F., Guillermet‐Guibert, J., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2013.12.011 · Cited by 145
Hexokinase II and VEGF expression in liver tumors: correlation with hypoxia-inducible factor-1α and its significance
Yasuda, S., Arii, S., Mori, A. S., Isobe, N., Yang, W., Oe, H., Fujimoto, A., Yonenaga, Y., Sakashita, H., & Imamura, M. (2003) · Journal of Hepatology · doi:10.1016/s0168-8278(03)00503-8 · Cited by 142
The hypoxia‐inducible miR‐429 regulates hypoxia‐inducible factor‐1α expression in human endothelial cells through a negative feedback loop
Bartoszewska, S., Rochan, K., Piotrowski, A., Kamysz, W., Ochocka, J. R., Collawn, J. F., & Bartoszewski, R. (2014) · The FASEB Journal · doi:10.1096/fj.14-267054 · Cited by 139 · cited 1×
“miR-429 is induced during early stage of hypoxia in tumor cells and regulates HIF-1 mRNA levels [81].”
Background
Hypoxia in Tumors: Pathogenesis-Related Classification, Characterization of Hypoxia Subtypes, and Associated Biological and Clinical Implications
Vaupel, P. W., & Mayer, A. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-0620-8_3 · Cited by 132 · cited 1×
“Hypoxia, a prominent characteristic feature of the tumor milieu drives aggressiveness of a growing tumor [43].”
Background
Metabolic Targeting as an Anticancer Strategy: Dawn of a New Era?
Pan, J. G., & Mak, T. W. (2007) · Science s STKE · doi:10.1126/stke.3812007pe14 · Cited by 129
Hypoxia-inducible factors in cancer stem cells and inflammation
Peng, G., & Liu, Y. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.03.003 · Cited by 127
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
Beclin-1 Expression is a Predictor of Clinical Outcome in Patients with Esophageal Squamous Cell Carcinoma and Correlated to Hypoxia-Inducible Factor (HIF)-1α Expression
Chen, Y., Lü, Y., Lu, C., & Zhang, L. (2009) · Pathology & Oncology Research · doi:10.1007/s12253-008-9143-8 · Cited by 123
Recent agents targeting HIF‐1α for cancer therapy
Hu, Y., Liu, J., & Huang, H. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24390 · Cited by 113
An Akt/Hypoxia-Inducible Factor-1α/Platelet-Derived Growth Factor-BB Autocrine Loop Mediates Hypoxia-Induced Chemoresistance in Liver Cancer Cells and Tumorigenic Hepatic Progenitor Cells
Lau, C. K., Yang, Z. F., Ho, D. W., Ng, M. N., Yeoh, G. C., Poon, R. T. P., & Fan, S. T. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2127 · Cited by 113
Nitric Oxide Is a Factor in the Stabilization of Hypoxia-Inducible Factor-1α in Cancer: Role of Free Radical Formation
Quintero, M., Brennan, P. A., Thomas, G. J., & Moncada, S. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-0333 · Cited by 105 · cited 1×
“Additionally, it has been reported that elevated nitric oxide (NO) levels and enhanced expression of nitric oxide synthase (NOS) isoforms increases HIF-1a protein stability in human oral squamous cell carcinoma [42] (Table 1).”
Background
HIF-1α can act as a tumor suppressor gene in murine acute myeloid leukemia
Velasco-Hernández, T., Wittsten, A. H., Rehn, M., Bryder, D., & Cammenga, J. (2014) · Blood · doi:10.1182/blood-2014-04-567065 · Cited by 103
Tumor suppressor p53 negatively regulates glycolysis stimulated by hypoxia through its target RRAD
Zhang, C., Liu, J., Wu, R., Liang, Y., 林美华, Liu, J., Chan, C. S., Hu, W., & Feng, Z. (2014) · Oncotarget · doi:10.18632/oncotarget.2137 · Cited by 101 · cited 1×
“Recent reports have exhibited that p53 is stimulated by hypoxia and acts as a negative regulator of glycolysis [74] (Figure 4).”
Background
Hypoxia-Inducible Factor Prolyl Hydroxylase Inhibition: Robust New Target or Another Big Bust for Stroke Therapeutics?
Karuppagounder, S. S., & Ratan, R. R. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.28 · Cited by 97
Expression of hypoxia-inducible factor-1α in cervical carcinomas: correlation with tumor oxygenation
Haugland, H. K., Vukovic, V. M., Pintilie, M., Fyles, A., Milosevic, M., Hill, R. P., & Hedley, D. W. (2002) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/s0360-3016(02)02815-8 · Cited by 97
Overexpression and nuclear translocation of hypoxia-inducible factor prolyl hydroxylase PHD2 in head and neck squamous cell carcinoma is associated with tumor aggressiveness.
Jokilehto, T., Rantanen, K., Luukkaa, M., Heikkinen, P. T., Grenman, R. A., Minn, H. R. I., Kronqvist, P., & Jaakkola, P. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-2022 · Cited by 97
Anoxia-induced apoptosis occurs through a mitochondria-dependent pathway in lung epithelial cells
Santore, M. T., McClintock, D. S., Lee, V. Y., Budinger, G. R. S., & Chandel, N. S. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00281.2001 · Cited by 95
Hypoxia-inducible factor-1α expression and angiogenesis in gastrointestinal stromal tumor of the stomach
Takahashi, R., Tanaka, S., Hiyama, T., Ito, M., Kitadai, Y., Sumii, M., Haruma, K., & Chayama, K. (2003) · Oncology Reports · doi:10.3892/or.10.4.797 · Cited by 78
Poly(ADP-Ribose) Polymerase 1 Promotes Tumor Cell Survival by Coactivating Hypoxia-Inducible Factor-1–Dependent Gene Expression
Elser, M., Borsig, L., Hassa, P. O., Erener, S., Messner, S., Valovka, T., Keller, S., Gassmann, M., & Hottiger, M. O. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-0377 · Cited by 78 · cited 1×
“Poly (ADP-ribose) polymerase 1 (PARP1) is one more NADþ-dependent enzyme, which was reported to interact with and promote HIF-1a transactivation [41].”
Background
Inhibition of hypoxia-inducible factors limits tumor progression in a mouse model of colorectal cancer
Shay, J. E. S., Imtiyaz, H. Z., Sivanand, S., Durham, A. C., Skuli, N., Hsu, S., Mucaj, V., Eisinger‐Mathason, T. S. K., Krock, B. L., Giannoukos, D. N., et al. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu004 · Cited by 73
Differential roles of Sirt1 in HIF-1α and HIF-2α mediated hypoxic responses
Yoon, H., Shin, S.-H., Shin, D. H., Chun, Y., & Park, J. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.001 · Cited by 69 · cited 2×
“These nicotinamide adenine dinucleotide (NADþ)-dependent enzymes have exhibited potential to regulate HIF activity, thereby strengthening the association between HIF responses and cellular stress [40].”
Background
VEGF as a Biomarker for Metastatic Uveal Melanoma in Humans
Barak, V., Pe’er, J., Kalickman, I., & Frenkel, S. (2011) · Current Eye Research · doi:10.3109/02713683.2010.534573 · Cited by 62
miR-21 Is Linked to Glioma Angiogenesis
Hermansen, S. K., Nielsen, B. S., Aaberg-Jessen, C., & Kristensen, B. W. (2015) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155415623515 · Cited by 60
Targeting hypoxia-inducible factor-1α (HIF-1α) in combination with antiangiogenic therapy: A phase I trial of bortezomib plus bevacizumab
Falchook, G. S., Wheler, J. J., Naing, A., Jackson, E. F., Jankú, F., Hong, D. S., Ng, C. S., Tannir, N. M., Lawhorn, K., Huang, M., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2163 · Cited by 59
The effect of HIF-1α on glucose metabolism, growth and apoptosis of pancreatic cancerous cells.
He, G., Jiang, Y., Zhang, B., & Wu, G. (2014) · PubMed · doi:10.6133/apjcn.2014.23.1.14 · Cited by 54 · cited 1×
“Interestingly, HIF-1a induces glycolysis and actively restrains mitochondrial function and O2 utilization by inducing pyruvate dehydrogenase kinase-1 (PDK-1) activity [68].”
Background
Mutant p53 facilitates pro-angiogenic, hyperproliferative phenotype in response to chronic relative hypoxia
Kamat, C. D., Green, D. E., Warnke, L. A., Thorpe, J. E., Ceriello, A., & Ihnat, M. A. (2006) · Cancer Letters · doi:10.1016/j.canlet.2006.08.017 · Cited by 53
Overexpression of nuclear NHERF1 in advanced colorectal cancer: Association with hypoxic microenvironment and tumor invasive phenotype
Malfettone, A., Silvestris, N., Paradiso, A., Mattioli, E., Simone, G., & Mangia, A. (2012) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2012.03.004 · Cited by 50
IGF-1 induced HIF-1α-TLR9 cross talk regulates inflammatory responses in glioma
Sinha, S., Koul, N., Dixit, D., Sharma, V., & Sen, E. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.06.024 · Cited by 47 · cited 2×
“These include platelet-derived growth factor (PDGF) [37], insulin [38] and insulin-like growth factors (IGF) [39], which induces HIF-1a translation (Table 1).”
Background
Thymosin β4 induces the expression of vascular endothelial growth factor (VEGF) in a hypoxia-inducible factor (HIF)-1α-dependent manner
Jo, J.-O., Kim, S.-R., Bae, M.-K., Kang, Y., Ock, M. S., Kleinman, H. K., & Cha, H. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.07.005 · Cited by 46
Hypoxia-inducible factor (HIF) inhibitors: a patent survey (2011-2015)
Ban, H. S., Uto, Y., Won, M., & Nakamura, H. (2016) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2016.1146252 · Cited by 45
Loss of VHL expression contributes to epithelial–mesenchymal transition in oral squamous cell carcinoma
Zhang, S., Zhou, X., Wang, B., Zhang, K., Liu, S., Yue, K., Zhang, L., & Wang, X. (2014) · Oral Oncology · doi:10.1016/j.oraloncology.2014.06.007 · Cited by 43
Hypoxia inhibits mesenchymal stem cell proliferation through HIF1α-dependent regulation of P27
Kumar, S., & Vaidya, M. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2674-5 · Cited by 43
Effects of 2-methoxyestradiol on apoptosis and HIF-1α and HIF-2α expression in lung cancer cells under normoxia and hypoxia
Aquino‐Gálvez, A., González-Ávila, G., DELGADO-TELLO, J., Castillejos-López, M. D. J., Mendoza-Milla, C., Zúñiga, J., Checa, M., Maldonado-Martínez, H. A., TRINIDAD-LÓPEZ, A., Cisneros, J., et al. (2015) · Oncology Reports · doi:10.3892/or.2015.4399 · Cited by 40
bcl-2/Adenovirus E1B 19-kd Interacting Protein 3 (BNIP3) Regulates Hypoxia-Induced Neural Precursor Cell Death
Walls, K. C., Ghosh, A. P., Ballestas, M. E., Klocke, B. J., & Roth, K. A. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181c3b9be · Cited by 39 · cited 1×
“BCL2/ adenovirus E1B 19 kDa protein-interacting protein 3 (BNIP3) is a HIF-1 target gene correlated to autophagy [72] through disruption of interaction between Beclin-1 (a highly conserved autophagy inducer protein) and B-cell lymphoma 2 (Bcl-2) or B-cell lymphoma-extra-large (Bcl-xL) [73].”
Background
Leu-574 of HIF-1α Is Essential for the von Hippel-Lindau (VHL)-mediated Degradation Pathway
Huang, E. L., Pete, E. A., Schau, M., Milligan, J., & Gu, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207280200 · Cited by 38 · cited 1×
“Collectively, these alterations lead to 26S proteasomal degradation of HIF-1a subunit by tethering to the b-domain of von Hippel-Lindau protein (pVHL), an E3 ubiquitin ligase at Leucine-574 (L574) [18].”
Background
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
The Role of the HIF-1α Transcription Factor in Increased Cell Division at Physiological Oxygen Tensions
Carrera, S., Senra, J. M., Acosta, M. I., Althubiti, M., Hammond, E. M., de Verdier, P. J., & Macip, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097938 · Cited by 37 · cited 1×
“Recently HIF-1a has been reported to be activated at physiological O2 levels in a p42/44 mitogen-activated protein kinase (MAPK)dependent manner determining increased cellular proliferation commonly found in these conditions [36].”
Background
MicroRNAs in Hypoxia Response
Greco, S., & Martelli, F. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6083 · Cited by 34 · cited 1×
“Previous studies have demonstrated number of miRNAs induced during hypoxia and they play critical roles in angiogenesis [80].”
Background
Curcumin induces p53-independent necrosis in H1299 cells via a mitochondria-associated pathway
Li, F., Chen, X., XU, B., & Zhou, H. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.4395 · Cited by 32
Hypoxia-induced downregulation of autophagy mediator Beclin-1 reduces the susceptibility of malignant intestinal epithelial cells to hypoxia-dependent apoptosis
Yoo, B. H., Wu, X., Derouet, M. F., Haniff, M., Eskelinen, E., & Rosen, K. V. (2009) · Autophagy · doi:10.4161/auto.5.8.10167 · Cited by 32
Insulin Regulates Hypoxia-Inducible Factor-1α Transcription by Reactive Oxygen Species Sensitive Activation of Sp1 in 3T3-L1 Preadipocyte
Biswas, S., Mukherjee, R., Tapryal, N., Singh, A. K., & Mukhopadhyay, C. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062128 · Cited by 24 · cited 1×
“These include platelet-derived growth factor (PDGF) [37], insulin [38] and insulin-like growth factors (IGF) [39], which induces HIF-1a translation (Table 1).”
Background
Hypoxia‐inducible factor 1α is essential for hypoxic p27 induction in endometrioid endometrial carcinoma
Horrée, N., Gort, E. H., van der Groep, P., Heintz, A. P. M., Vooijs, M., & van Diest, P. J. (2007) · The Journal of Pathology · doi:10.1002/path.2244 · Cited by 23
Antagonistic crosstalk between APC and HIF-1α
Näthke, I. S., & Rocha, S. (2011) · Cell Cycle · doi:10.4161/cc.10.10.15638 · Cited by 19
Expression of cFLIPL Determines the Basal Interaction of Bcl‐2 With Beclin‐1 and Regulates p53 Dependent Ubiquitination of Beclin‐1 During Autophagic Stress
Ranjan, K., & Pathak, C. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25474 · Cited by 19 · cited 1×
“BCL2/ adenovirus E1B 19 kDa protein-interacting protein 3 (BNIP3) is a HIF-1 target gene correlated to autophagy [72] through disruption of interaction between Beclin-1 (a highly conserved autophagy inducer protein) and B-cell lymphoma 2 (Bcl-2) or B-cell lymphoma-extra-large (Bcl-xL) [73].”
Background
PTEN status mediates 2ME2 anti-tumor efficacy in preclinical glioblastoma models: role of HIF1α suppression
Muh, C. R., Joshi, S., Singh, A. R., Kesari, S., Durden, D. L., & Makale, M. (2013) · Journal of Neuro-Oncology · doi:10.1007/s11060-013-1283-3 · Cited by 16
Expression of Hypoxia Inducible Factor-1α and Its Significance in Laryngeal Carcinoma
Xh, W., Lu, Y.-F., Hu, X.-D., Mao, J.-Y., Ji, X.-X., Yao, H.-T., & Zhou, S.-H. (2010) · Journal of International Medical Research · doi:10.1177/147323001003800618 · Cited by 13
Hypoxia-inducible factor-1-regulated protein expression and oligodendroglioma patient outcome: comparison with established biomarkers and preoperative UCSF low-grade scoring system
Abraham, S. M., Hu, N., & Jensen, R. L. (2012) · Journal of Neuro-Oncology · doi:10.1007/s11060-012-0839-y · Cited by 12
Nucleocytoplasmic shuttling of IPAS by its unique nuclear import and export signals unshared with other HIF-3α splice variants
Torii, S., Sakaki, K., Otomo, M., Saka, K., Yasumoto, K., & Sogawa, K. (2013) · The Journal of Biochemistry · doi:10.1093/jb/mvt088 · Cited by 11 · cited 1×
“Very little was known about the newest isoform HIF-3a until the identification of its spliced variant, inhibitory PAS (IPAS) which in a dominant negative way regulates HIF-1 DNA binding ability [29].”
Background
HIF1A expression in localized prostate cancer treated with dose escalation radiation therapy
Zapatero, A., Morente, M. M., de Vidales, C. M., Adrados, M., López, C., Nieto, S., González, M. J. A., Arellano, R., Conde, A. C., & Vicente, F. G. (2015) · Cancer Biomarkers · doi:10.3233/cbm-140439 · Cited by 7
Differential effects of HIF-α isoforms on apoptosis in renal carcinoma cell lines
Doonachar, A., Gallo, M. D., Doukas, D., Pasricha, R., Lantsberg, I., & Schoenfeld, A. R. (2015) · Cancer Cell International · doi:10.1186/s12935-015-0175-3 · Cited by 7 · cited 1×
“HRE, they are functionally non-redundant [26].”
Hypoxia-Inducible Factor 1A in Clear Cell Renal Cell Carcinoma
Klatte, T., Seligson, D. B., Riggs, S. B., Berkman, M. K., Kleid, M. D., Kabbinavar, F. F., Pantuck, A. J., & Belldegrun, A. S. (2007) · Cited by 7
A chronic obstructive pulmonary disease negatively influences the prognosis of patients with bladder urothelial carcinoma via hypoxia inducible factor-1α.
Huang, Z., Xu, R., Lv, C., Zhong, Z., Zhang, L., Zhu, L., Tang, Y., & Zhao, X. (2014) · PubMed · Cited by 5

Research works printed but not linked: 5

Huang Z, 2014, Int J Clin Exp Med, 7, 3344
Takahashi R, 2003, Oncol Rep, 10, 797
He GD, 2014, Asia Pac J Clin Nutr, 23, 174
Pan JG, 2007, Sci STKE, 381, e14
Zhong H, 1999, Cancer Res, 59, 5830

Sorted by citations

Mechanisms of Chemotherapy Resistance in Triple-Negative Breast Cancer—How We Can Rise to the Challenge
Nedeljković, M., & Damjanović, A. (2019) · Cells · doi:10.3390/cells8090957 · Cited by 910
“Since the discovery of HIFs, many inhibitors with diverse modes of action have been identified, but none have progressed to clinical use [119].”
Background
The anti-cancer effect of quercetin: molecular implications in cancer metabolism
Reyes-Farias, M., & Carrasco-Pozo, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133177 · Cited by 689
“In fact, HIF-1α is the primary driver of increased glycolysis and lactate production during hypoxia [35].”
Background
The Drug-Resistance Mechanisms of Five Platinum-Based Antitumor Agents
Zhou, J., Kang, Y., Chen, L., Wang, H., Liu, J., Zeng, S., & Yu, L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00343 · Cited by 481
“Whereas under hypoxic conditions, impaired hydroxylation process stabilizes the HIF1a protein, furthermore HIF1a will translocate into nuclear and dimerize with HIF1b to transactivate the target genes which relate with glucose metabolism, angiogenesis, cell proliferation, invasion and metastasis (reviewed in Pawlus an…”
Background
Practical classification of triple-negative breast cancer: intratumoral heterogeneity, mechanisms of drug resistance, and novel therapies
Marra, A., Trapani, D., Viale, G., Criscitiello, C., & Curigliano, G. (2020) · npj Breast Cancer · doi:10.1038/s41523-020-00197-2 · Cited by 332
HIF-1α signaling: Essential roles in tumorigenesis and implications in targeted therapies
Zhao, Y., Xing, C., Deng, Y., Ye, C., & Peng, H. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.02.039 · Cited by 231
“It has been reported that HIF-1a is highly expressed in tumors such as breast, liver, bladder, cervical, colorectal, endometrial, lung, etc.(77) NANOG is a protein required for the self-renewal of breast cancer stem cells (BCSCs), and high expression of NANOG in tumor tissues of breast cancer patients is correlated wi…”
Background

See all 251

Authors: Soni, S., & Padwad, Y. S.
Affiliations: Institute of Himalayan Bioresource Technology (IN)
Corresponding author: Padwad, Yogendra S.
ORCID: Soni, Sourabh
Padwad, Yogendra S.
Venue: Acta Oncologica
Publisher: MJS Publishing, Medical Journals Sweden AB
Published: 2017-03-30
Volume: 56
Issue: 4
Pages: 503-515
ISSN: 0284-186X (ISSN-L)
1651-226X
DOI: 10.1080/0284186x.2017.1301680
OpenAlex: W2599085091
Cited by: 251
References: 122
Citations by year: 2026: 6 · 2025: 16 · 2024: 16 · 2023: 35 · 2022: 34 · 2021: 38 · 2020: 41 · 2019: 43 · 2018: 20 · 2017: 1
FWCI: 2.92
Type: journal article
Language: en
Open access: diamond
doi.org
Locations: Acta Oncologica (publishedVersion)
PubMed (publishedVersion)
Funders: Council of Scientific and Industrial Research
Council for Scientific and Industrial Research (MLP0039)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
Keywords: HIF-1, tumor hypoxia, oxygen homeostasis, transcription factor regulation, HIF-1 target genes, tumor angiogenesis, anaerobic metabolism, metastasis, carcinogenesis, cancer therapy targets, tumor microenvironment
MeSH terms: Animals, Humans, Neoplasms, Cell Hypoxia, Hypoxia-Inducible Factor 1, alpha Subunit

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

HIF-1 in cancer therapy: two decade long story of a transcription factor

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks