ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery.

By C. Jung, Chang-Bong Jun, Seung-Hyun Ro, Young-Mi Kim, N. Otto, Jing Cao, M. Kundu, Do-Hyung Kim. Molecular Biology of the Cell, 2009

2,018 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Physiology

View Paper: https://www.semanticscholar.org/paper/d328e43c4a68a67a1c1c70651803f86d7b596c70

How researchers see this paper

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

In Cell Biology

1. N. Mizushima
2. D. Klionsky
3. Beth Levine
4. Guido Kroemer
5. I. Slaninová
6. V. Deretic
7. Alec C. Kimmelman
8. A. Cuervo

In Epidemiology

1. Beth Levine
2. Guido Kroemer
3. N. Mizushima
4. D. Klionsky
5. I. Slaninová
6. V. Deretic
7. Douglas R. Green
8. Alec C. Kimmelman

In Physiology

1. Guido Kroemer
2. N. Mizushima
3. Beth Levine
4. Alec C. Kimmelman
5. D. Klionsky
6. I. Slaninová
7. L. Galluzzi
8. D. Rubinsztein

Citations in the corpus

• Regulation Mechanisms and Signaling Pathways of Autophagy (2009, background): “Regarding the substrates of the Atg1 kinase during autophagy, it is suggested that mammalian Atg13 and FIP200 are phosphorylated by ULKs (56), and ULKs also undergo autophosphorylation, which is conducive to a conformational change and autophagy induction (13).”
• Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy. (2009, result): “These results were also independently found by another group (Jung et al., 2009).”