| pubmed-article:16129620 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16129620 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16129620 | lifeskim:mentions | umls-concept:C0524865 | lld:lifeskim |
| pubmed-article:16129620 | lifeskim:mentions | umls-concept:C0597177 | lld:lifeskim |
| pubmed-article:16129620 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16129620 | lifeskim:mentions | umls-concept:C1140675 | lld:lifeskim |
| pubmed-article:16129620 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:16129620 | lifeskim:mentions | umls-concept:C1553649 | lld:lifeskim |
| pubmed-article:16129620 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16129620 | pubmed:dateCreated | 2005-9-26 | lld:pubmed |
| pubmed-article:16129620 | pubmed:abstractText | Crustaceans form clots by the rapid crosslinking of a hemolymph clottable protein (CP) to form long, branched polymers. Clotting limits hemolymph loss from wounds as well as playing a part in the innate immune response. CP is a 420 kDa homodimer with a large quantity of associated lipid, primarily the carotenoid pigment astaxanthin. The three-dimensional structure of CP from the lobster Panulirus interruptus has been determined to 17 A resolution by single particle reconstruction from electron micrographs of the protein embedded in vitreous ice. The most prominent feature of this structure is a large cavity spanning the length of the molecule, which is the likely lipid binding pocket. The EM structure has been used in a low resolution molecular replacement search with data from orthorhombic CP crystals, and a solution is presented which describes the crystal packing. | lld:pubmed |
| pubmed-article:16129620 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16129620 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16129620 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16129620 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16129620 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16129620 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16129620 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16129620 | pubmed:issn | 1047-8477 | lld:pubmed |
| pubmed-article:16129620 | pubmed:author | pubmed-author:QuispeJoelJ | lld:pubmed |
| pubmed-article:16129620 | pubmed:author | pubmed-author:KollmanJustin... | lld:pubmed |
| pubmed-article:16129620 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16129620 | pubmed:volume | 151 | lld:pubmed |
| pubmed-article:16129620 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16129620 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16129620 | pubmed:pagination | 306-14 | lld:pubmed |
| pubmed-article:16129620 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:meshHeading | pubmed-meshheading:16129620... | lld:pubmed |
| pubmed-article:16129620 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16129620 | pubmed:articleTitle | The 17A structure of the 420 kDa lobster clottable protein by single particle reconstruction from cryoelectron micrographs. | lld:pubmed |
| pubmed-article:16129620 | pubmed:affiliation | Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093-0314, USA. jkollman@biomail.ucsd.edu | lld:pubmed |
| pubmed-article:16129620 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16129620 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16129620 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
