{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T11:09:55Z","timestamp":1791284995220,"version":"4.1.0"},"reference-count":49,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"6144","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2013,7,26]]},"abstract":"<jats:title>Not mTORCing<\/jats:title>\n                  <jats:p>\n                    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,\n                    <jats:bold>\n                      Kang\n                      <jats:italic>et al.<\/jats:italic>\n                    <\/jats:bold>\n                    (\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/www.sciencemag.org\/content\/341\/6144\/1236566.full\">1236566<\/jats:ext-link>\n                    ) 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.\n                  <\/jats:p>","DOI":"10.1126\/science.1236566","type":"journal-article","created":{"date-parts":[[2013,7,25]],"date-time":"2013-07-25T15:15:23Z","timestamp":1374765323000},"source":"Crossref","is-referenced-by-count":424,"title":["mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin"],"prefix":"10.1126","volume":"341","author":[{"given":"Seong A.","family":"Kang","sequence":"first","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA."},{"name":"Department of Biology, Massachusetts Institute of Technology (MIT), 77 Massachusetts Avenue, Cambridge, MA 02139, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael E.","family":"Pacold","sequence":"additional","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA."},{"name":"Department of Biology, Massachusetts Institute of Technology (MIT), 77 Massachusetts Avenue, Cambridge, MA 02139, USA."},{"name":"Department of Cancer Biology, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02115, USA."},{"name":"Department of Radiation Oncology, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02215, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher L.","family":"Cervantes","sequence":"additional","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA."},{"name":"Department of Biology, Massachusetts Institute of Technology (MIT), 77 Massachusetts Avenue, Cambridge, MA 02139, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Lim","sequence":"additional","affiliation":[{"name":"David H. 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