| pubmed-article:12076536 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12076536 | lifeskim:mentions | umls-concept:C0007292 | lld:lifeskim |
| pubmed-article:12076536 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:12076536 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12076536 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:12076536 | pubmed:dateCreated | 2002-6-21 | lld:pubmed |
| pubmed-article:12076536 | pubmed:abstractText | Membranes are important sites for the regulation of metabolic functions because they contain transport molecules, which often catalyze the first step in a pathway, and signal-transduction components, which allow the cell to communicate with the environment. Given the catalytic importance of transport proteins and their role in membrane stability, it is possible that oligomerization is used to regulate their function. This review evaluates knowledge of the functions that are associated with the oligomeric organization of secondary transport proteins, which are a major class of solute-translocation systems in all living species. | lld:pubmed |
| pubmed-article:12076536 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12076536 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12076536 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12076536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12076536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12076536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12076536 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12076536 | pubmed:month | May | lld:pubmed |
| pubmed-article:12076536 | pubmed:issn | 0968-0004 | lld:pubmed |
| pubmed-article:12076536 | pubmed:author | pubmed-author:PoolmanBertB | lld:pubmed |
| pubmed-article:12076536 | pubmed:author | pubmed-author:HeubergerEsth... | lld:pubmed |
| pubmed-article:12076536 | pubmed:author | pubmed-author:VeenhoffLiesb... | lld:pubmed |
| pubmed-article:12076536 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12076536 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:12076536 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12076536 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12076536 | pubmed:pagination | 242-9 | lld:pubmed |
| pubmed-article:12076536 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12076536 | pubmed:meshHeading | pubmed-meshheading:12076536... | lld:pubmed |
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| pubmed-article:12076536 | pubmed:meshHeading | pubmed-meshheading:12076536... | lld:pubmed |
| pubmed-article:12076536 | pubmed:meshHeading | pubmed-meshheading:12076536... | lld:pubmed |
| pubmed-article:12076536 | pubmed:meshHeading | pubmed-meshheading:12076536... | lld:pubmed |
| pubmed-article:12076536 | pubmed:meshHeading | pubmed-meshheading:12076536... | lld:pubmed |
| pubmed-article:12076536 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12076536 | pubmed:articleTitle | Quaternary structure and function of transport proteins. | lld:pubmed |
| pubmed-article:12076536 | pubmed:affiliation | Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4 9747 AG Groningen, The Netherlands. | lld:pubmed |
| pubmed-article:12076536 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12076536 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:12076536 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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