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| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C0753114 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C0682972 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C1518792 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:9446593 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9446593 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9446593 | pubmed:dateCreated | 1998-2-23 | lld:pubmed |
| pubmed-article:9446593 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9446593 | pubmed:abstractText | The solution structure of an extended pleckstrin homology (PH) domain from the beta-adrenergic receptor kinase is obtained by high resolution NMR. The structure establishes that the beta-adrenergic receptor kinase extended PH domain has the same fold and topology as other PH domains, and there are several unique features, most notably an extended C-terminal alpha-helix that behaves as a molten helix, and a surface charge polarity that is extensively modified by positive residues in the extended alpha-helix and the C terminus. These observations complement biochemical evidence that the C-terminal portion of this PH domain participates in protein-protein interactions with Gbetagamma subunits. This suggests that the C-terminal segment of the PH domain may function to mediate protein-protein interactions with the targets of PH domains. | lld:pubmed |
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| pubmed-article:9446593 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9446593 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9446593 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9446593 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9446593 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9446593 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9446593 | pubmed:author | pubmed-author:CowburnDD | lld:pubmed |
| pubmed-article:9446593 | pubmed:author | pubmed-author:LeVineHH3rd | lld:pubmed |
| pubmed-article:9446593 | pubmed:author | pubmed-author:ZhengJJ | lld:pubmed |
| pubmed-article:9446593 | pubmed:author | pubmed-author:CahillSS | lld:pubmed |
| pubmed-article:9446593 | pubmed:author | pubmed-author:FushmanDD | lld:pubmed |
| pubmed-article:9446593 | pubmed:author | pubmed-author:Najmabadi-Has... | lld:pubmed |
| pubmed-article:9446593 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9446593 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:9446593 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9446593 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9446593 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9446593 | pubmed:pagination | 2835-43 | lld:pubmed |
| pubmed-article:9446593 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9446593 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9446593 | pubmed:articleTitle | The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. | lld:pubmed |
| pubmed-article:9446593 | pubmed:affiliation | Laboratory of Physical Biochemistry, The Rockefeller University, New York, New York 10021-6399, USA. | lld:pubmed |
| pubmed-article:9446593 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9446593 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9446593 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9446593 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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