Linked Life Data

17095930

Source:http://linkedlifedata.com/resource/pubmed/id/17095930

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2006-11-10
pubmed:abstractText
The AMP-activated protein kinase (AMPK) has been referred to as an "energy sensor" because it binds to and is regulated by both AMP and ATP. The binding of AMP to AMPK allows it to be phosphorylated by upstream kinases, resulting in its activation. In contrast, the binding of ATP prevents its activation. AMPK regulates a multitude of metabolic processes that cumulatively function to maintain cellular energy homeostasis through repression of a number of energy-consuming processes with simultaneous enhancement of energy-producing processes. One downstream AMPK target that has been recently identified is the mammalian target of rapamycin (mTOR), a positive effector of cell growth and division. The focus of the present review is to briefly summarize current knowledge concerning the regulation of mTOR signaling by AMPK.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0195-9131
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1958-64
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Interaction between the AMP-activated protein kinase and mTOR signaling pathways.
pubmed:affiliation
Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA. skimball@psu.edu
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural