| pubmed-article:12351838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12351838 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12351838 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:12351838 | lifeskim:mentions | umls-concept:C0086149 | lld:lifeskim |
| pubmed-article:12351838 | pubmed:issue | Pt 10 Pt 2 | lld:pubmed |
| pubmed-article:12351838 | pubmed:dateCreated | 2002-9-27 | lld:pubmed |
| pubmed-article:12351838 | pubmed:abstractText | Cyclase-associated protein (CAP) is a conserved two-domain protein that helps to activate the catalytic activity of adenylyl cyclase in the cyclase-bound state through interaction with Ras, which binds to the cyclase in a different region. With its other domain, CAP can bind monomeric actin and therefore also carries a cytoskeletal function. The protein is thus involved in Ras/cAMP-dependent signal transduction and most likely serves as an adapter protein translocating the adenylyl cyclase complex to the actin cytoskeleton. Crystals belonging to the orthorhombic space group C222, with unit-cell parameters a = 71.2, b = 75.1, c = 162.9 A, have been obtained from Dictyostelium discoideum CAP carrying a C-terminal His tag. A complete native data set extending to 2.2 A resolution was collected from a single crystal using an in-house X-ray system. The asymmetric unit contains one molecule of CAP. | lld:pubmed |
| pubmed-article:12351838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12351838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12351838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12351838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12351838 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12351838 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:12351838 | pubmed:author | pubmed-author:HofmannAndrea... | lld:pubmed |
| pubmed-article:12351838 | pubmed:author | pubmed-author:WlodawerAlexa... | lld:pubmed |
| pubmed-article:12351838 | pubmed:author | pubmed-author:HessSonjaS | lld:pubmed |
| pubmed-article:12351838 | pubmed:author | pubmed-author:SchleicherMic... | lld:pubmed |
| pubmed-article:12351838 | pubmed:author | pubmed-author:NoegelAngelik... | lld:pubmed |
| pubmed-article:12351838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12351838 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:12351838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12351838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12351838 | pubmed:pagination | 1858-61 | lld:pubmed |
| pubmed-article:12351838 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:meshHeading | pubmed-meshheading:12351838... | lld:pubmed |
| pubmed-article:12351838 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12351838 | pubmed:articleTitle | Crystallization of cyclase-associated protein from Dictyostelium discoideum. | lld:pubmed |
| pubmed-article:12351838 | pubmed:affiliation | Macromolecular Crystallography Laboratory, NCI at Frederick, Frederick, MD 21702, USA. andreas.hofmann@ed.ac.uk | lld:pubmed |
| pubmed-article:12351838 | pubmed:publicationType | Journal Article | lld:pubmed |
