JunD reduces tumor angiogenesis by protecting cells from oxidative stress.

By Damien Gerald, E. Berra, Y. Frapart, D. Chan, Amato J. Giaccia, D. Mansuy, J. Pouysségur, M. Yaniv, F. Mechta‐Grigoriou. Cell, 2004

598 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/6aee4198ac5dca4085c830135e8b287d9b3bb6e6

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. G. Semenza
2. W. Kaelin
3. P. Schumacker
4. P. Ratcliffe
5. Eyal Gottlieb
6. J. Chiche
7. R. Guzy
8. M. Brahimi-Horn

In Molecular Biology

1. W. Kaelin
2. G. Semenza
3. P. Ratcliffe
4. P. Schumacker
5. Arkaitz Carracedo
6. J. Chiche
7. Eyal Gottlieb
8. R. Guzy

In Oncology

1. Arkaitz Carracedo
2. Eyal Gottlieb
3. B. A. Hocevar
4. W. Kaelin
5. J. Pouysségur
6. P. Pandolfi
7. L. Kamendulis
8. J. Klaunig

Citations in the corpus

• Vitamins C and E: Beneficial effects from a mechanistic perspective (2011, background): “Alternatively or additionally,H2O2 and other ROS may also interfere with HIF prolyl hydroxylase by decreasing Fe in the catalytic site [29].”
• Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy. (2008, background): “[142] D.”
• Tumour hypoxia induces a metabolic shift causing acidosis: a common feature in cancer (2009, background): “However, studies © 2009 The Authors Journal compilation © 2010 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd 778 into pulmonary arterial myocytes showed that the expression and activity of NHE-1 was enhanced in hypoxia [116], but no implication of ROS was investigated.”
• Redox Regulation of Cell Survival (2008, unknown): “Interest-ingly, genes encoding two isoforms of PHD proteins ( phd 2 & 3) are HIF targets.”
• Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia (2006, background): “One possibility is that the ROS act directly at the Fe2+ ion associated with prolyl hydroxylase, rendering the enzyme inactive by preventing its redox cycling (Gerald et al. 2004).”
• Physical and biological mechanisms of direct plasma interaction with living tissue (2009, background): “Indeed, ROS induce stress in mammalian cells and while in some cases it may lead to apoptosis in other cases this stress can actually promote or control angiogenesis, the growth of new blood vessels or repair/regeneration of existing ones [62]–[64].”
• Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-alpha activation. (2005, unknown): “Recently, redox changes through the depletion of ascorbate by CoCl2 (Salnikow et al., 2004) or via oxidation of cellular iron by persistent ROS production (Gerald et al., 2004) have been shown to inhibit hydroxylase activity leading to stabilization of HIF-α subunits.”
• Oxidative Stress and Oxidative Damage in Carcinogenesis (2010, background): “While most reported functions of JunD are related to decreased cellular oxidative stress, recent reports show that JunD can inhibit cell proliferation through activation of p21 promoter and reduce tumor angiogenesis by protecting cells from oxidative stress (L. Li et al. 2002; Gerald et al. 2004).”
• Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer (2006, background): “Reactive oxygen species were reported to inhibit PHD activity under normoxic conditions by oxidizing the PHD cofactors ferrous iron and ascorbate (Figure 3) (Gerald et al., 2004).”
• SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization (2011, background): “Notably, ROS have been shown to inhibit the PHDs and stabilize HIF1a (Gerald et al., 2004; Kaelin and Ratcliffe, 2008).”