| pubmed-article:16046906 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16046906 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:16046906 | lifeskim:mentions | umls-concept:C1519624 | lld:lifeskim |
| pubmed-article:16046906 | lifeskim:mentions | umls-concept:C2350345 | lld:lifeskim |
| pubmed-article:16046906 | lifeskim:mentions | umls-concept:C1523924 | lld:lifeskim |
| pubmed-article:16046906 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:16046906 | lifeskim:mentions | umls-concept:C1550030 | lld:lifeskim |
| pubmed-article:16046906 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16046906 | pubmed:dateCreated | 2005-7-27 | lld:pubmed |
| pubmed-article:16046906 | pubmed:abstractText | It has long been recognized that the coupling of membrane transport to underlying cellular metabolic status is critical because transport processes consume a large portion of total cellular energy. Recently, the finely tuned metabolic sensor AMP-activated protein kinase (AMPK) has emerged as a membrane transport regulator, which may permit sensitive transport-metabolism crosstalk. This review will discuss how AMPK may play an important role in the regulation of ion and solute transport across the plasma membrane under both physiological and pathological conditions in epithelia and other tissues. | lld:pubmed |
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| pubmed-article:16046906 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16046906 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16046906 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16046906 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16046906 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16046906 | pubmed:issn | 1062-4821 | lld:pubmed |
| pubmed-article:16046906 | pubmed:author | pubmed-author:HallowsKennet... | lld:pubmed |
| pubmed-article:16046906 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16046906 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:16046906 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16046906 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16046906 | pubmed:pagination | 464-71 | lld:pubmed |
| pubmed-article:16046906 | pubmed:dateRevised | 2011-9-22 | lld:pubmed |
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| pubmed-article:16046906 | pubmed:meshHeading | pubmed-meshheading:16046906... | lld:pubmed |
| pubmed-article:16046906 | pubmed:meshHeading | pubmed-meshheading:16046906... | lld:pubmed |
| pubmed-article:16046906 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16046906 | pubmed:articleTitle | Emerging role of AMP-activated protein kinase in coupling membrane transport to cellular metabolism. | lld:pubmed |
| pubmed-article:16046906 | pubmed:affiliation | Renal-Electrolyte Division, Department of Medicine and Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, S976 Scaife Hall, 3550 Terrace Street, Pittsburgh, PA 15261, USA. hallows@pitt.edu | lld:pubmed |
| pubmed-article:16046906 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16046906 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16046906 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:16046906 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16046906 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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