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Cited by 431

The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.

mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin

Open access
Kang, Seong A., Pacold, Michael E., Cervantes, Christopher L., Lim, Daniel, Lou, Hua Jane, Ottina, Kathleen, Gray, Nathanael S., Turk, Benjamin E., Yaffe, Michael B., Sabatini, David M.·2013·Science

Abstract

Not mTORCing: Inhibition of the protein kinase complex mTORC1 has potentially beneficial therapeutic affects that include inhibition of cancer and extension of life span. However, effects of its inhibition in vivo have sometimes been disappointing. One reason may be that the well-studied inhibitor of mTORC1, rapamycin, inhibits some effects of mTORC1 but not others. In line with this idea, Kang et al. ( 1236566 ) show that the effect of rapamycin depends on the substrate. Characteristics of the phosphorylation sites on various substrates caused them to be phosphorylated with different efficiency by mTORC1. The substrates that were most efficiently phosphorylated were resistant to inhibition of mTORC1. The results explain how various sites, sometimes within the same protein, can differ in their sensitivity to rapamycin.

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Metadata

Authors
Kang, S. A., Pacold, M. E., Cervantes, C. L., Lim, D., Lou, H. J., Ottina, K., Gray, N. S., Turk, B. E., Yaffe, M. B., & Sabatini, D. M.
Venue
Science
Published
2013-07-26
Volume
341
Issue
6144
Pages
1236566-1236566
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1510881494
Cited by
431
References
48
FWCI
18.02
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin. https://app.cochat.ai/papers/10.1126/science.1236566
The paper
Kang, S. A., Pacold, M. E., Cervantes, C. L., Lim, D., Lou, H. J., Ottina, K., Gray, N. S., Turk, B. E., Yaffe, M. B., & Sabatini, D. M. (2013). mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin. Science. https://doi.org/10.1126/science.1236566

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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