A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication - Wikidata - awgldk - TriplyDB

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

http://www.wikidata.org/entity/Q34013854

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Oxygen Sensing and Homeostasis Hypoxia signaling pathways: modulators of oxygen-related organelles PHD1 links cell-cycle progression to oxygen sensing through hydroxylation of the centrosomal protein Cep192 Ribonucleotide Reductase Requires Subunit Switching in Hypoxia to Maintain DNA Replication Cdc6 contributes to abrogating the G1 checkpoint under hypoxic conditions in HPV E7 expressing cells.Light exposure at night disrupts host/cancer circadian regulatory dynamics: impact on the Warburg effect, lipid signaling and tumor growth prevention Cyclin-dependent kinases regulate lysosomal degradation of hypoxia-inducible factor 1α to promote cell-cycle progression.Tumorigenicity of hypoxic respiring cancer cells revealed by a hypoxia-cell cycle dual reporter A cyclic peptide inhibitor of HIF-1 heterodimerization that inhibits hypoxia signaling in cancer cells.Intermittent induction of HIF-1α produces lasting effects on malignant progression independent of its continued expression.MicroRNA-18a inhibits hypoxia-inducible factor 1α activity and lung metastasis in basal breast cancers Pleiotropic modes of action in tumor cells of RNASET2, an evolutionary highly conserved extracellular RNase.Reprogramming the Transcriptional Response to Hypoxia with a Chromosomally Encoded Cyclic Peptide HIF-1 Inhibitor.Regulation of cell proliferation by hypoxia-inducible factors CDK-dependent phosphorylation of PHD1 on serine 130 alters its substrate preference in cells.Chaperone-mediated autophagy targets hypoxia-inducible factor-1α (HIF-1α) for lysosomal degradation.HIF-1 mediates metabolic responses to intratumoral hypoxia and oncogenic mutations Sirtuin-7 inhibits the activity of hypoxia-inducible factors.Complex role of HIF in cancer: the known, the unknown, and the unexpected.Anti-tumor activity of SL4 against breast cancer cells: induction of G2/M arrest through modulation of the MAPK-dependent p21 signaling pathway.Helicobacter pylori Induced Phosphatidylinositol-3-OH Kinase/mTOR Activation Increases Hypoxia Inducible Factor-1α to Promote Loss of Cyclin D1 and G0/G1 Cell Cycle Arrest in Human Gastric Cells.Tumor hypoxia as a driving force in genetic instability.Cell cycle progression in response to oxygen levels.Integration of hypoxic HIF-α signaling in blood cancers.Hypoxia-inducible factor 1 alpha is regulated by RBM38, a RNA-binding protein and a p53 family target, via mRNA translation.A compendium of proteins that interact with HIF-1α.Hypoxia on the Expression of Hepatoma Upregulated Protein in Prostate Cancer Cells.Role Of Hif2α Oxygen Sensing Pathway In Bronchial Epithelial Club Cell Proliferation HIF-3α1 promotes colorectal tumor cell growth by activation of JAK-STAT3 signaling.William Kaelin, Peter Ratcliffe, and Gregg Semenza receive the 2016 Albert Lasker Basic Medical Research Award.Biochemistry. How HIF-1α handles stress.The eIF4E2-Directed Hypoxic Cap-Dependent Translation Machinery Reveals Novel Therapeutic Potential for Cancer Treatment.Hypoxia-Inducible Factors and Cancer.HIF-1α expression and high microvessel density are characteristic features in serrated colorectal cancer.Mathematical modelling of interacting mechanisms for hypoxia mediated cell cycle commitment for mesenchymal stromal cells.Sphingosine 1-Phosphate Receptor 1 Is Required for MMP-2 Function in Bone Marrow Mesenchymal Stromal Cells: Implications for Cytoskeleton Assembly and Proliferation.

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A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

http://www.wikidata.org/entity/Q34013854

description

2013 nî lūn-bûn

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2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի փետրվարին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

@ast

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

@en

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

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type

label

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

@ast

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

@en

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

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prefLabel

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

@ast

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

@en

A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

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SCISIGNAL.2003417

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Science Signaling

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A nontranscriptional role for HIF-1α as a direct inhibitor of DNA replication

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Andre Levchenko

http://www.w3.org/2001/XMLSchema#string

Carmen C Wong

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Daniele M Gilkes

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Gregg L Semenza

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Kshitiz

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Maimon E Hubbi

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Sergio Rey

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Weibo Luo

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P2860

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

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

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

Self-assembling protein microarrays

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

HIF-2alpha promotes hypoxic cell proliferation by enhancing c-myc transcriptional activity

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

Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase

Phosphorylation of mammalian CDC6 by cyclin A/CDK2 regulates its subcellular localization

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

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10.1126/SCISIGNAL.2003417

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