C. Pugh

Cancer Research · 2000–2011

A researcher in the Science corpus: 11 papers; trusts 2 researchers and is trusted by 11 researchers here, as inferred from the citation graph.

Subfields

• Cancer Research — 68 citations into it; #246 of 1,780 by trust here, #96 by citations
• Molecular Biology — 67 citations into it; #3,728 of 17,773 by trust here, #1,205 by citations

Whom C. Pugh trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. G. Semenza
2. W. Kaelin
3. Roland H. Wenger
4. K. Kondo

Who trusts C. Pugh overall

1. G. Semenza
2. N. Ferrara
3. Christopher J. Schofield
4. S. P. Herbert
5. Alicia S. Chung
6. Roland H. Wenger

Papers from C. Pugh's perspective

Ordered by how strongly the researchers C. Pugh trusts endorse each paper. Same corpus, a different order for every researcher.

1. Differential Roles of Hypoxia-Inducible Factor 1α (HIF-1α) and HIF-2α in Hypoxic Gene Regulation (Molecular and Cellular Biology)
2. Transcription Factor HIF-1 Is a Necessary Mediator of the Pasteur Effect in Mammalian Cells (Molecular and Cellular Biology)
3. Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects. (Journal of the National Cancer Institute)
4. Molecular basis of the VHL hereditary cancer syndrome (Nature Reviews. Cancer)
5. Hypoxia — a key regulatory factor in tumour growth (Nature Reviews. Cancer)
6. Targeting HIF-1 for cancer therapy (Nature Reviews. Cancer)
7. Differentiating the functional role of hypoxia‐inducible factor (HIF)‐1α and HIF‐2α (EPAS‐1) by the use of RNA interference: erythropoietin is a HIF‐2α target gene in Hep3B and Kelly cells
8. Early expression of angiogenesis factors in acute myocardial ischemia and infarction. (New England Journal of Medicine)
9. Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. (Proceedings of the National Academy of Sciences of the United States of America)
10. Inhibition of HIF2α Is Sufficient to Suppress pVHL-Defective Tumor Growth (PLoS Biology)

Their papers

• Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O2-Regulated Prolyl Hydroxylation (2001) — 4,904 citations
• Regulation of angiogenesis by hypoxia: role of the HIF system (2003) — 2,531 citations
• C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. (2001) — 3,389 citations
• Hypoxia Inducible Factor-α Binding and Ubiquitylation by the von Hippel-Lindau Tumor Suppressor Protein* (2000) — 822 citations
• Independent function of two destruction domains in hypoxia‐inducible factor‐α chains activated by prolyl hydroxylation (2001) — 1,106 citations
• Differential Function of the Prolyl Hydroxylases PHD1, PHD2, and PHD3 in the Regulation of Hypoxia-inducible Factor* (2004) — 1,117 citations
• Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family* (2002) — 716 citations
• High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq. (2011) — 724 citations
• Contrasting Properties of Hypoxia-Inducible Factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-Associated Renal Cell Carcinoma (2005) — 993 citations
• Hypoxia-inducible expression of tumor-associated carbonic anhydrases. (2000) — 1,347 citations
• The expression and distribution of the hypoxia-inducible factors HIF-1α and HIF-2α in normal human tissues, cancers, and tumor-associated macrophages (2000) — 1,144 citations