Sophia Y. Lunt

Molecular Biology · 2011–2012

A researcher in the Science corpus: 2 papers; trusts 30 researchers and is trusted by 3 researchers here, as inferred from the citation graph.

Subfields

Whom Sophia Y. Lunt trusts overall

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

  1. Ralph J. Deberardinis
  2. W. Kaelin
  3. Yusuf A. Hannun
  4. Javier A. Menéndez
  5. A. Futerman
  6. B. Ogretmen
  7. M. V. Vander Heiden
  8. S. Mazurek
  9. Heather L. Wieman
  10. Shomit Sengupta

Who trusts Sophia Y. Lunt overall

  1. Chih-Hao Chang
  2. Jie Zheng
  3. Ralph J. Deberardinis
  4. Navdeep S. Chandel
  5. Maria Liberti
  6. J. Cantor
  7. Andrew N. Lane
  8. Zhaoyong Li
  9. Shanmugasundaram Ganapathy-Kanniappan
  10. Yuanyuan An

Papers from Sophia Y. Lunt's perspective

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

  1. Akt Stimulates Aerobic Glycolysis in Cancer Cells (Cancer Research)
  2. Deregulation of Glucose Transporter 1 and Glycolytic Gene Expression by c-Myc* (Journal of Biological Chemistry)
  3. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. (Genes & Development)
  4. Cancer-associated IDH1 mutations produce 2-hydroxyglutarate (Nature)
  5. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. (Cell Metabolism)
  6. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth (Nature)
  7. c-Myc suppression of miR-23 enhances mitochondrial glutaminase and glutamine metabolism (Nature)
  8. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. (Cell Metabolism)
  9. Glioma-Derived Mutations in IDH1 Dominantly Inhibit IDH1 Catalytic Activity and Induce HIF-1α (Science)
  10. The common feature of leukemia-associated IDH1 and IDH2 mutations is a neomorphic enzymatic activity that converts α-ketoglutarate to 2-hydroxyglutarate (Cancer Cell)

Their papers