B. Blaauw
Molecular Biology · Nature Communications · 2009–2020
A researcher in the Science corpus: 4 papers; trusts 2 researchers and is trusted by 0 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 86 citations into it
- Cell Biology — 28 citations into it
Whom B. Blaauw trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Papers from B. Blaauw's perspective
Ordered by how strongly the researchers B. Blaauw trusts endorse each paper. Same corpus, a different order for every researcher.
- Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. (Cell)
- Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (Journal of the American Society of Nephrology)
- The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. (Molecules and Cells)
- Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction (Nature)
- PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription (Proceedings of the National Academy of Sciences of the United States of America)
- In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. (Molecular Biology of the Cell)
- Autophagy fights disease through cellular self-digestion (Nature)
- Autophagy in the pathogenesis of disease. (Cell)
- Essential role for Nix in autophagic maturation of erythroid cells (Nature)
- Erratum: Autophagy suppresses tumorigenesis through elimination of p62 (Cell (2009) 137 (1062-1075))
Their papers
- Autophagy is required to maintain muscle mass. (2009) — 1,238 citations
- Regulation of autophagy and the ubiquitin–proteasome system by the FoxO transcriptional network during muscle atrophy (2015) — 660 citations
- Mechanisms regulating skeletal muscle growth and atrophy (2013) — 1,393 citations
- PHD1 controls muscle mTORC1 in a hydroxylation-independent manner by stabilizing leucyl tRNA synthetase (2020) — 689 citations