| pubmed-article:11106408 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11106408 | lifeskim:mentions | umls-concept:C1562025 | lld:lifeskim |
| pubmed-article:11106408 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:11106408 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:11106408 | lifeskim:mentions | umls-concept:C0887868 | lld:lifeskim |
| pubmed-article:11106408 | lifeskim:mentions | umls-concept:C0242759 | lld:lifeskim |
| pubmed-article:11106408 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:11106408 | pubmed:dateCreated | 2001-1-2 | lld:pubmed |
| pubmed-article:11106408 | pubmed:abstractText | Low density Triton X-100-insoluble plasma membrane microdomains can be isolated from different mammalian cell types and are proposed to be involved in membrane trafficking, cell morphogenesis and signal transduction. Heterotrimeric G-proteins and their receptors are often associated with such domains, suggesting that these structures are involved in G-protein-coupled signaling. Here we report that detergent-insoluble plasma membrane microdomains also exist in higher plants and contain about 15% of membrane-bound heterotrimeric G-protein beta-subunit (Gbeta). Plasma membrane microdomains were isolated from tobacco leaves. They have low buoyant density relative to the surrounding plasma membrane, and are insoluble in Triton X-100 at 4 degrees C. Detergent-insoluble vesicles were examined by freeze-fracture electron microscopy. They have sizes in the range 100-400 nm, and often contain aggregated protein complexes. The majority of plasma membrane proteins cannot be detected in the Triton X-100-insoluble fraction, while few polypeptides are highly enriched. We identified six proteins with molecular masses of 22, 28, 35, 60, 67 and 94 kDa in detergent-insoluble fractions that are glycosylphosphatidylinositol (GPI)-anchored. | lld:pubmed |
| pubmed-article:11106408 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11106408 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106408 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11106408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11106408 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11106408 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11106408 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:11106408 | pubmed:author | pubmed-author:OelmüllerRR | lld:pubmed |
| pubmed-article:11106408 | pubmed:author | pubmed-author:WestermannMM | lld:pubmed |
| pubmed-article:11106408 | pubmed:author | pubmed-author:PeskanTT | lld:pubmed |
| pubmed-article:11106408 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11106408 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:11106408 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11106408 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11106408 | pubmed:pagination | 6989-95 | lld:pubmed |
| pubmed-article:11106408 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:11106408 | pubmed:meshHeading | pubmed-meshheading:11106408... | lld:pubmed |
| pubmed-article:11106408 | pubmed:meshHeading | pubmed-meshheading:11106408... | lld:pubmed |
| pubmed-article:11106408 | pubmed:meshHeading | pubmed-meshheading:11106408... | lld:pubmed |
| pubmed-article:11106408 | pubmed:meshHeading | pubmed-meshheading:11106408... | lld:pubmed |
| pubmed-article:11106408 | pubmed:meshHeading | pubmed-meshheading:11106408... | lld:pubmed |
| pubmed-article:11106408 | pubmed:meshHeading | pubmed-meshheading:11106408... | lld:pubmed |
| pubmed-article:11106408 | pubmed:meshHeading | pubmed-meshheading:11106408... | lld:pubmed |
| pubmed-article:11106408 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11106408 | pubmed:articleTitle | Identification of low-density Triton X-100-insoluble plasma membrane microdomains in higher plants. | lld:pubmed |
| pubmed-article:11106408 | pubmed:affiliation | Institut für Allgemeine Botanik, Lehrstuhl Pflanzenphysiologie, Jena, Germany; Institut für Ultrastrukturforschung des Klinikums der Friedrich Schiller Universität Jena, Germany. | lld:pubmed |
| pubmed-article:11106408 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11106408 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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