Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Regulation of HIF-1alpha stability through S-nitrosylation.

Molecular cell - 13 Apr 2007

Li Fang, Sonveaux Pierre, Rabbani Zahid N, Liu Shanling, Yan Bin, Huang Qian, Vujaskovic Zeljko, Dewhirst Mark W, Li Chuan-Yuan

Abstract excerpt

Hypoxia-inducible factor 1 (HIF-1) is a master transcriptional factor. Under normal oxygen tension, HIF-1 activity is usually suppressed due to the rapid, oxygen-dependent degradation of one of its two subunits, HIF-1alpha. Here we report that normoxic HIF-1 activity can be upregulated through NO-mediated S-nitrosylation and stabilization of HIF-1alpha. In murine tumors, exposure to ionizing radiation stimulated...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cysteine
Share to Gene Expression Regulation, Neoplastic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hypoxia-Inducible Factor 1, alpha Subunit

Share to Macrophages

Share to Nitric Oxide

Share to Nitric Oxide Synthase Type II

Share to Sequence Homology, Amino Acid

Share to Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 17434127
DOI: 10.1016/j.molcel.2007.02.024
PMCID: PMC2905600

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of HIF-1alpha stability through S-nitrosylation.PMID 17434127Read ↗

Regulatory mechanisms of hypoxia-inducible factor 1 activity: Two decades of knowledge.Semantic proximity Read ↗

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

Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch.Semantic proximity Read ↗

Identification of residues critical for regulation of protein stability and the transactivation function of the hypoxia-inducible factor-1alpha by the von Hippel-Lindau tumor suppressor gene product.Semantic proximity Read ↗

Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-alpha) proteins.Semantic proximity Read ↗

Identification and characterisation of the post-translational modifications that regulate the Hypoxia Inducible Factors, HIF-1α and HIF-2αSemantic proximity Read ↗

Activation of C-transactivation domain is essential for optimal HIF-1 alpha-mediated transcriptional and angiogenic effects.Semantic proximity Read ↗

GSNOR deficiency promotes tumor growth via FAK1 S-nitrosylationSemantic proximity Read ↗

Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein.Semantic proximity Read ↗

Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha.Semantic proximity Read ↗

Leu-574 of human HIF-1alpha is a molecular determinant of prolyl hydroxylation.Semantic proximity Read ↗

Polysulfide inhibits hypoxia-elicited hypoxia-inducible factor activation in a mitochondria-dependent manner.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.