pubmed-article:14561875 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14561875 | lifeskim:mentions | umls-concept:C0027834 | lld:lifeskim |
pubmed-article:14561875 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
pubmed-article:14561875 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:14561875 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:14561875 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:14561875 | pubmed:issue | 28 | lld:pubmed |
pubmed-article:14561875 | pubmed:dateCreated | 2003-10-16 | lld:pubmed |
pubmed-article:14561875 | pubmed:abstractText | Neurofilament assembly requires at minimum the polymerization of neurofilament light chain (NF-L) with either neurofilament medium chain (NF-M) or neurofilament heavy chain (NF-H) subunits, but requirements for their axonal transport have long been controversial. Using a gene deletion approach, we generated mice containing only NF-L or NF-M. In vivo pulse radiolabeling analyses in retinal ganglion cell neurons revealed that NF-L alone is incapable of efficient transport, whereas nearly one-half of the normal level of NF-M is transported along optic axons in the absence of the other triplet subunits. Under these conditions, however, NF-M transport is completely abolished by deleting alpha-internexin. Our results strongly suggest that efficient neurofilament protein transport in vivo minimally requires hetero-oligomer formation. They also show that NF-M can partner with intermediate filament proteins other than the NF-H and NF-L subunits in neurons to support slow transport and possibly other functions of neuronal intermediate filaments. | lld:pubmed |
pubmed-article:14561875 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:language | eng | lld:pubmed |
pubmed-article:14561875 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14561875 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14561875 | pubmed:month | Oct | lld:pubmed |
pubmed-article:14561875 | pubmed:issn | 1529-2401 | lld:pubmed |
pubmed-article:14561875 | pubmed:author | pubmed-author:NixonRalph... | lld:pubmed |
pubmed-article:14561875 | pubmed:author | pubmed-author:YuanAidongA | lld:pubmed |
pubmed-article:14561875 | pubmed:author | pubmed-author:JulienJean-Pi... | lld:pubmed |
pubmed-article:14561875 | pubmed:author | pubmed-author:RaoMala VMV | lld:pubmed |
pubmed-article:14561875 | pubmed:author | pubmed-author:KumarAsokA | lld:pubmed |
pubmed-article:14561875 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:14561875 | pubmed:day | 15 | lld:pubmed |
pubmed-article:14561875 | pubmed:volume | 23 | lld:pubmed |
pubmed-article:14561875 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14561875 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14561875 | pubmed:pagination | 9452-8 | lld:pubmed |
pubmed-article:14561875 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:14561875 | pubmed:meshHeading | pubmed-meshheading:14561875... | lld:pubmed |
pubmed-article:14561875 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14561875 | pubmed:articleTitle | Neurofilament transport in vivo minimally requires hetero-oligomer formation. | lld:pubmed |
pubmed-article:14561875 | pubmed:affiliation | Center for Dementia Research, Nathan Kline Institute, New York University School of Medicine, Orangeburg, New York 10962, USA. yuan@nki.rfmh.org | lld:pubmed |
pubmed-article:14561875 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14561875 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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