| pubmed-article:11535825 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11535825 | lifeskim:mentions | umls-concept:C0521449 | lld:lifeskim |
| pubmed-article:11535825 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11535825 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:11535825 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11535825 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11535825 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:11535825 | pubmed:dateCreated | 2001-9-12 | lld:pubmed |
| pubmed-article:11535825 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11535825 | pubmed:abstractText | The TRP (transient receptor potential) superfamily includes a group of subfamilies of channel-like proteins mediating a multitude of physiological signaling processes. The TRP-melastatin (TRPM) subfamily includes the putative tumor suppressor melastatin (MLSN) and is a poorly characterized group of TRP-related proteins. Here, we describe the identification and characterization of an additional TRPM protein TRPM4. We reveal that TRPM4 and MLSN each mediate Ca(2+) entry when expressed in HEK293 cells. Furthermore, we demonstrate that a short form of MLSN (MLSN-S) interacts directly with and suppresses the activity of full-length MLSN (MLSN-L). This suppression seems to result from the inhibition of translocation of MLSN-L to the plasma membrane. We propose that control of translocation through interaction between MLSN-S and MLSN-L represents a mode for regulating ion channel activity. | lld:pubmed |
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| pubmed-article:11535825 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11535825 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11535825 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11535825 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11535825 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11535825 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11535825 | pubmed:author | pubmed-author:GillD LDL | lld:pubmed |
| pubmed-article:11535825 | pubmed:author | pubmed-author:MontellCC | lld:pubmed |
| pubmed-article:11535825 | pubmed:author | pubmed-author:XuX ZXZ | lld:pubmed |
| pubmed-article:11535825 | pubmed:author | pubmed-author:MoebiusFF | lld:pubmed |
| pubmed-article:11535825 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11535825 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:11535825 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:11535825 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11535825 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11535825 | pubmed:pagination | 10692-7 | lld:pubmed |
| pubmed-article:11535825 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11535825 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11535825 | pubmed:articleTitle | Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform. | lld:pubmed |
| pubmed-article:11535825 | pubmed:affiliation | Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. | lld:pubmed |
| pubmed-article:11535825 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11535825 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11535825 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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