Targeting HIF-1 for cancer therapy (Q27860504)

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

Europe PubMed Central

title

Targeting HIF-1 for cancer therapy (English)

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1

Gregg L Semenza

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language of work or name

English

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publication date

October 2003

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published in

Nature Reviews Cancer

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volume

3

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page(s)

721-32

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issue

10

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cites work

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Purification and characterization of hypoxia-inducible factor 1

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

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Hypoxia--a key regulatory factor in tumour growth

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HIF-1 alpha is required for solid tumor formation and embryonic vascularization.

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Hypoxia promotes invasive growth by transcriptional activation of the met protooncogene

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Identification and classification of p53-regulated genes

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A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development

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HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is closely related to hypoxia-inducible factor-1 alpha and developmentally expressed in blood vessels

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Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway

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Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells

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Hypoxia-inducible factor-2alpha (HIF-2alpha) is involved in the apoptotic response to hypoglycemia but not to hypoxia

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Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus

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

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

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HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

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Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

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

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HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation

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Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein

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Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex

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

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Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein

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Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein

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Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension

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Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation

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Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension

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Activation of Hypoxia-inducible Factor-1; Definition of Regulatory Domains within the α Subunit

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

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

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

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

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Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response

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Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha

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Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL

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Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

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Aerobic glycolysis by proliferating cells: a protective strategy against reactive oxygen species.

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Transcription factor HIF-1 is a necessary mediator of the pasteur effect in mammalian cells.

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Insulin-like growth factor 1 induces hypoxia-inducible factor 1-mediated vascular endothelial growth factor expression, which is dependent on MAP kinase and phosphatidylinositol 3-kinase signaling in colon cancer cells

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p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1.

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MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300

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Regulation of hypoxia-inducible factor 1alpha expression and function by the mammalian target of rapamycin.

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The Expression and Distribution of the Hypoxia-Inducible Factors HIF-1α and HIF-2α in Normal Human Tissues, Cancers, and Tumor-Associated Macrophages

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Relation of hypoxia inducible factor 1 alpha and 2 alpha in operable non-small cell lung cancer to angiogenic/molecular profile of tumours and survival

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Hypoxia-inducible factor-1 modulates gene expression in solid tumors and influences both angiogenesis and tumor growth.

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The hypoxia-inducible factor-1 alpha is a negative factor for tumor therapy.

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Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1

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Dominant-negative hypoxia-inducible factor-1 alpha reduces tumorigenicity of pancreatic cancer cells through the suppression of glucose metabolism

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Suppression of tumor growth through disruption of hypoxia-inducible transcription

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Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein

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The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma

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Loss of pVHL is sufficient to cause HIF dysregulation in primary cells but does not promote tumor growth

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Stabilization of wild-type p53 by hypoxia-inducible factor 1alpha

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Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia

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Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours

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Levels of hypoxia-inducible factor-1 alpha during breast carcinogenesis

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Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway

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Geldanamycin inhibits migration of glioma cells in vitro: a potential role for hypoxia-inducible factor (HIF-1alpha) in glioma cell invasion

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2ME2 inhibits tumor growth and angiogenesis by disrupting microtubules and dysregulating HIF.

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HIF activation identifies early lesions in VHL kidneys: evidence for site-specific tumor suppressor function in the nephron

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Expression of hypoxia-inducible factor 1? in brain tumors

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Gliomagenesis: genetic alterations and mouse models

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Cancer modeling in the modern era: progress and challenges

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Can small animal imaging accelerate drug development?

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Prostaglandin E2 induces hypoxia-inducible factor-1alpha stabilization and nuclear localization in a human prostate cancer cell line

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The p14ARF tumor suppressor protein facilitates nucleolar sequestration of hypoxia-inducible factor-1alpha (HIF-1alpha ) and inhibits HIF-1-mediated transcription

31 March 2020

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Bcl-2 overexpression in human melanoma cells increases angiogenesis through VEGF mRNA stabilization and HIF-1-mediated transcriptional activity

31 March 2020

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Significant correlation of hypoxia-inducible factor-1alpha with treatment outcome in cervical cancer treated with radical radiotherapy

31 March 2020

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Levels of hypoxia-inducible factor-1alpha independently predict prognosis in patients with lymph node negative breast carcinoma

31 March 2020

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Expression of hypoxia-inducible factor-1 alpha in oligodendrogliomas: its impact on prognosis and on neoangiogenesis.

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Association of hypoxia-inducible factors 1alpha and 2alpha with activated angiogenic pathways and prognosis in patients with endometrial carcinoma

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31 March 2020

Identifiers

DOI

10.1038/NRC1187

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

86313

1034382167

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86313

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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