| pubmed-article:12424224 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:12424224 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12424224 | lifeskim:mentions | umls-concept:C0913844 | lld:lifeskim |
| pubmed-article:12424224 | lifeskim:mentions | umls-concept:C1423691 | lld:lifeskim |
| pubmed-article:12424224 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:12424224 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:12424224 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12424224 | pubmed:dateCreated | 2003-1-10 | lld:pubmed |
| pubmed-article:12424224 | pubmed:abstractText | Mutations of NPHS1 or NPHS2, the genes encoding for the glomerular podocyte proteins nephrin and podocin, cause steroid-resistant proteinuria. In addition, mice lacking NEPH1 develop a nephrotic syndrome that resembles NPHS mutations, suggesting that all three proteins are essential for the integrity of glomerular podocytes. Podocin interacts with the C-terminal domain of nephrin and facilitates nephrin-dependent signaling. NEPH1, a member of the immunoglobulin superfamily, is structurally related to nephrin. We report now that NEPH1 belongs to a family of three closely related proteins that interact with the C-terminal domain of podocin. All three NEPH proteins share a conserved podocin-binding motif; mutation of a centrally located tyrosine residue dramatically lowers the affinity of NEPH1 for podocin. NEPH1 triggers AP-1 activation similarly to nephrin but requires the presence of Tec family kinases for efficient transactivation. We conclude that NEPH1 defines a new family of podocin-binding molecules that are potential candidates for hereditary nephrotic syndromes not linked to either NPHS1 or NPHS2. | lld:pubmed |
| pubmed-article:12424224 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12424224 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12424224 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12424224 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:12424224 | pubmed:issn | 1530-6860 | lld:pubmed |
| pubmed-article:12424224 | pubmed:author | pubmed-author:SvenskHH | lld:pubmed |
| pubmed-article:12424224 | pubmed:author | pubmed-author:GerkePeterP | lld:pubmed |
| pubmed-article:12424224 | pubmed:author | pubmed-author:SellinLorenzL | lld:pubmed |
| pubmed-article:12424224 | pubmed:author | pubmed-author:WalzGerdG | lld:pubmed |
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| pubmed-article:12424224 | pubmed:author | pubmed-author:QuackIvoI | lld:pubmed |
| pubmed-article:12424224 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:12424224 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:12424224 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12424224 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12424224 | pubmed:pagination | 115-7 | lld:pubmed |
| pubmed-article:12424224 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12424224 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12424224 | pubmed:articleTitle | NEPH1 defines a novel family of podocin interacting proteins. | lld:pubmed |
| pubmed-article:12424224 | pubmed:affiliation | Department of Internal Medicine, Division of Nephrology, University Hospital Freiburg, Germany. | lld:pubmed |
| pubmed-article:12424224 | pubmed:publicationType | Journal Article | lld:pubmed |
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