| pubmed-article:18226514 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18226514 | lifeskim:mentions | umls-concept:C0007613 | lld:lifeskim |
| pubmed-article:18226514 | lifeskim:mentions | umls-concept:C0041348 | lld:lifeskim |
| pubmed-article:18226514 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:18226514 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:18226514 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18226514 | pubmed:dateCreated | 2008-2-12 | lld:pubmed |
| pubmed-article:18226514 | pubmed:abstractText | All microtubules are built from a basic alpha/beta-tubulin building block, yet subpopulations of microtubules can be differentially marked by a number of post-translational modifications. These modifications, conserved throughout evolution, are thought to act individually or in combination to control specific microtubule-based functions, analogous to how histone modifications regulate chromatin functions. Here we review recent studies demonstrating that tubulin modifications influence microtubule-associated proteins such as severing proteins, plus-end tracking proteins, and molecular motors. In this way, tubulin modifications play an important role in regulating microtubule properties, such as stability and structure, as well as microtubule-based functions, such as ciliary beating, cell division, and intracellular trafficking. | lld:pubmed |
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| pubmed-article:18226514 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18226514 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18226514 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18226514 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18226514 | pubmed:issn | 0955-0674 | lld:pubmed |
| pubmed-article:18226514 | pubmed:author | pubmed-author:CaiDawenD | lld:pubmed |
| pubmed-article:18226514 | pubmed:author | pubmed-author:VerheyKristen... | lld:pubmed |
| pubmed-article:18226514 | pubmed:author | pubmed-author:HammondJennet... | lld:pubmed |
| pubmed-article:18226514 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18226514 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:18226514 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18226514 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18226514 | pubmed:pagination | 71-6 | lld:pubmed |
| pubmed-article:18226514 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
| pubmed-article:18226514 | pubmed:meshHeading | pubmed-meshheading:18226514... | lld:pubmed |
| pubmed-article:18226514 | pubmed:meshHeading | pubmed-meshheading:18226514... | lld:pubmed |
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| pubmed-article:18226514 | pubmed:meshHeading | pubmed-meshheading:18226514... | lld:pubmed |
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| pubmed-article:18226514 | pubmed:meshHeading | pubmed-meshheading:18226514... | lld:pubmed |
| pubmed-article:18226514 | pubmed:meshHeading | pubmed-meshheading:18226514... | lld:pubmed |
| pubmed-article:18226514 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18226514 | pubmed:articleTitle | Tubulin modifications and their cellular functions. | lld:pubmed |
| pubmed-article:18226514 | pubmed:affiliation | Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. | lld:pubmed |
| pubmed-article:18226514 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18226514 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:18226514 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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