| pubmed-article:16508085 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16508085 | lifeskim:mentions | umls-concept:C2350346 | lld:lifeskim |
| pubmed-article:16508085 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:16508085 | pubmed:dateCreated | 2006-3-1 | lld:pubmed |
| pubmed-article:16508085 | pubmed:abstractText | AMP-activated protein kinase (AMPK) is an intracellular energy sensor that regulates metabolism in response to energy demand and supply by adjusting the ATP-generating and ATP-consuming pathways. AMPK potentially plays a critical role in diabetes and obesity as it is known to be activated by metforin and rosiglitazone, drugs used for the treatment of type II diabetes. AMPK is a heterotrimer composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. Mutations in the gamma subunit are known to cause glycogen accumulation, leading to cardiac arrhythmias. Recently, a functional glycogen-binding domain (GBD) has been identified in the beta subunit. Here, the crystallization of GBD in the presence of beta-cyclodextrin is reported together with preliminary X-ray data analysis allowing the determination of the structure by single isomorphous replacement and threefold averaging using in-house X-ray data collected from a selenomethionine-substituted protein. | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16508085 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16508085 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16508085 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16508085 | pubmed:issn | 1744-3091 | lld:pubmed |
| pubmed-article:16508085 | pubmed:author | pubmed-author:PolekhinaGali... | lld:pubmed |
| pubmed-article:16508085 | pubmed:author | pubmed-author:ParkerMichael... | lld:pubmed |
| pubmed-article:16508085 | pubmed:author | pubmed-author:StapletonDavi... | lld:pubmed |
| pubmed-article:16508085 | pubmed:author | pubmed-author:GuptaAbhilash... | lld:pubmed |
| pubmed-article:16508085 | pubmed:author | pubmed-author:FeilSusanne... | lld:pubmed |
| pubmed-article:16508085 | pubmed:author | pubmed-author:O'DonnellPaul... | lld:pubmed |
| pubmed-article:16508085 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16508085 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16508085 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:16508085 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16508085 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16508085 | pubmed:pagination | 39-42 | lld:pubmed |
| pubmed-article:16508085 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:meshHeading | pubmed-meshheading:16508085... | lld:pubmed |
| pubmed-article:16508085 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16508085 | pubmed:articleTitle | Crystallization of the glycogen-binding domain of the AMP-activated protein kinase beta subunit and preliminary X-ray analysis. | lld:pubmed |
| pubmed-article:16508085 | pubmed:affiliation | St Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia. gpolekhina@svi.edu.au | lld:pubmed |
| pubmed-article:16508085 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16508085 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:83803 | entrezgene:pubmed | pubmed-article:16508085 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16508085 | lld:entrezgene |
