mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H+-ATPase
Copyright policy ) Zoncu, Roberto; Bar-Peled, Liron; Efeyan, Alejo; Sancak, Yasemin; Sabatini, David M.; Wang, Shuyu, Ph. D. Massachusetts Institute of Technology;
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H+-ATPase
Cellular sensing of amino acids occurs at the lysosome and is mediated by the vacuolar proton pump.
- Broad Institute United States
- Koch Institute for Integrative Cancer Research At MIT United States
- Howard Hughes Medical Institute United States
- Massachusetts Institute of Technology United States
- Whitehead Institute for Biomedical Research United States
Vacuolar Proton-Translocating ATPases, TOR Serine-Threonine Kinases, Proteins, Mechanistic Target of Rapamycin Complex 1, Cell Line, GTP Phosphohydrolases, Multiprotein Complexes, Animals, Humans, Drosophila, RNA Interference, Amino Acids, Lysosomes, Signal Transduction
Vacuolar Proton-Translocating ATPases, TOR Serine-Threonine Kinases, Proteins, Mechanistic Target of Rapamycin Complex 1, Cell Line, GTP Phosphohydrolases, Multiprotein Complexes, Animals, Humans, Drosophila, RNA Interference, Amino Acids, Lysosomes, Signal Transduction
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This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
Citations provided by BIP!popularityPopularity provided by BIP!
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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