| pubmed-article:11158577 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0020275 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0425245 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0442726 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:11158577 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11158577 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11158577 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11158577 | pubmed:abstractText | Changes in protein mobility accompany changes in conformation during the trans-activation of enzymes; however, few studies exist that validate or characterize this behavior. In this study, amide hydrogen/deuterium exchange/mass spectrometry was used to probe the conformational flexibility of extracellular signal-regulated protein kinase-2 before and after activation by phosphorylation. The exchange data indicated that extracellular regulated protein kinase-2 activation caused altered backbone flexibility in addition to the conformational changes previously established by x-ray crystallography. The changes in flexibility occurred in regions involved in substrate binding and turnover, suggesting their importance in enzyme regulation. | lld:pubmed |
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| pubmed-article:11158577 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11158577 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11158577 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11158577 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11158577 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11158577 | pubmed:author | pubmed-author:HANT STS | lld:pubmed |
| pubmed-article:11158577 | pubmed:author | pubmed-author:GoldsmithE... | lld:pubmed |
| pubmed-article:11158577 | pubmed:author | pubmed-author:ResingK AKA | lld:pubmed |
| pubmed-article:11158577 | pubmed:author | pubmed-author:HoofnagleA... | lld:pubmed |
| pubmed-article:11158577 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11158577 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:11158577 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:11158577 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11158577 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11158577 | pubmed:pagination | 956-61 | lld:pubmed |
| pubmed-article:11158577 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11158577 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11158577 | pubmed:articleTitle | Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange. | lld:pubmed |
| pubmed-article:11158577 | pubmed:affiliation | Department of Chemistry and Biochemistry, and Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309, USA. ahn@spot.colorado.edu | lld:pubmed |
| pubmed-article:11158577 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11158577 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11158577 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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