| pubmed-article:17259172 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17259172 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:17259172 | lifeskim:mentions | umls-concept:C0039808 | lld:lifeskim |
| pubmed-article:17259172 | lifeskim:mentions | umls-concept:C0887839 | lld:lifeskim |
| pubmed-article:17259172 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:17259172 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:17259172 | pubmed:dateCreated | 2007-4-2 | lld:pubmed |
| pubmed-article:17259172 | pubmed:abstractText | The nuclear import of H1 linker histones is mediated by a heterodimer of transport receptors, known as importinbeta and importin7. Interestingly, both importins separately interact with H1, but only as a dimer they facilitate the translocation through the nuclear pore. We identified the H1 binding site of importin7, comprising two extended acidic loops near the C terminus of importin7. The analysis of the H1 import complex assembly by means of isothermal titration calorimetry revealed that the formation of a receptor heterodimer in vitro is an enthalpy-driven process, whereas subsequent binding of H1 to the heterodimer is entropy-driven. Furthermore, we show that the importinbeta binding domain of importin7 plays a key role in the activation of importin7 by importinbeta. This process is allosterically regulated by importinbeta and accounts for a specific tuning of the activity of the importinbeta.importin7 heterodimer. The results presented here provide new insights into cellular strategies to even energy balances in nuclear import and point toward a general regulation of importinbeta-related nuclear import processes. | lld:pubmed |
| pubmed-article:17259172 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17259172 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259172 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17259172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259172 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17259172 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17259172 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17259172 | pubmed:author | pubmed-author:DickmannsAchi... | lld:pubmed |
| pubmed-article:17259172 | pubmed:author | pubmed-author:DoeneckeDetle... | lld:pubmed |
| pubmed-article:17259172 | pubmed:author | pubmed-author:FicnerRalfR | lld:pubmed |
| pubmed-article:17259172 | pubmed:author | pubmed-author:StrasserAnjaA | lld:pubmed |
| pubmed-article:17259172 | pubmed:author | pubmed-author:WohlwendDanie... | lld:pubmed |
| pubmed-article:17259172 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17259172 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:17259172 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17259172 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17259172 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17259172 | pubmed:pagination | 10707-19 | lld:pubmed |
| pubmed-article:17259172 | pubmed:dateRevised | 2008-10-20 | lld:pubmed |
| pubmed-article:17259172 | pubmed:meshHeading | pubmed-meshheading:17259172... | lld:pubmed |
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| pubmed-article:17259172 | pubmed:meshHeading | pubmed-meshheading:17259172... | lld:pubmed |
| pubmed-article:17259172 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17259172 | pubmed:articleTitle | Thermodynamic analysis of H1 nuclear import: receptor tuning of importinbeta/importin7. | lld:pubmed |
| pubmed-article:17259172 | pubmed:affiliation | Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik and GZMB, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany. | lld:pubmed |
| pubmed-article:17259172 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17259172 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
