Document Detail


mTOR signaling for biological control and cancer.
MedLine Citation:
PMID:  23460185     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mammalian target of rapamycin (mTOR) is a major intersection that connects signals from the extracellular milieu to corresponding changes in intracellular processes. When abnormally regulated, the mTOR signaling pathway is implicated in a wide spectrum of cancers, neurological diseases, and proliferative disorders. Therefore, pharmacological agents that restore the regulatory balance of the mTOR pathway could be beneficial for a great number of diseases. This review summarizes current understanding of mTOR signaling and some unanswered questions in the field. We describe the composition of the mTOR complexes, upstream signals that activate mTOR, and physiological processes that mTOR regulates. We also discuss the role of mTOR and its downstream effectors in cancer, obesity and diabetes, and autism.
Authors:
Anya Alayev; Marina K Holz
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review    
Journal Detail:
Title:  Journal of cellular physiology     Volume:  228     ISSN:  1097-4652     ISO Abbreviation:  J. Cell. Physiol.     Publication Date:  2013 Aug 
Date Detail:
Created Date:  2013-04-22     Completed Date:  2013-06-24     Revised Date:  2013-12-13    
Medline Journal Info:
Nlm Unique ID:  0050222     Medline TA:  J Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1658-64     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 Wiley Periodicals, Inc.
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MeSH Terms
Descriptor/Qualifier:
Animals
Humans
Multiprotein Complexes / antagonists & inhibitors,  physiology
Neoplasms / enzymology*
Signal Transduction / physiology*
TOR Serine-Threonine Kinases / antagonists & inhibitors,  physiology*
Grant Support
ID/Acronym/Agency:
CA151112/CA/NCI NIH HHS; R15 CA151112/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Multiprotein Complexes; 0/TOR complex 2; 0/mechanistic target of rapamycin complex 1; EC 2.7.1.1/TOR Serine-Threonine Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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