{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,1,12]],"date-time":"2024-01-12T22:26:11Z","timestamp":1705098371839},"reference-count":44,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":3687,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Motil. Cytoskeleton"],"published-print":{"date-parts":[[1995,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>We report the cloning and sequencing of genomic DNA encoding a cytoplasmic dynein heavy chain from the nematode <jats:italic>Caenorhabditis elegans.<\/jats:italic> In a contiguous stretch of 35,103 bp of DNA from the left arm of linkage group I, we have found a gene that is predicted to encode a protein of 4,568 amino acids. This gene is composed of 15 exons and 14 relatively short introns, and it has significant homology of the other dynein heavy chains in the databases. The deduced molecular mass of the derived polypeptide is 512,624 Da. As with other dynein heavy chains that have been sequenced to date, it contains four GXXGXGK(S\/T) motifs that form part of the consensus sequence for nucleotide triphosphate\u2010binding domains. Comparison of axonemal and cytoplasmic dynein heavy chains shows that regions of homology among all dyneins are clustered in the carboxyl terminal two\u2010thirds of the polypeptide, whereas the amino terminal one\u2010third of the heavy chains may contain domains that specify functions that differ between axonemal and cytoplasmic forms of the dynein heavy chain. \u00a9 1995 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/cm.970320104","type":"journal-article","created":{"date-parts":[[2005,2,24]],"date-time":"2005-02-24T01:48:46Z","timestamp":1109209726000},"page":"26-36","source":"Crossref","is-referenced-by-count":18,"title":["Genomic structure of a cytoplasmic dynein heavy chain gene from the nematode <i>Caenorhabditis elegans<\/i>"],"prefix":"10.1002","volume":"32","author":[{"given":"R. John","family":"Lye","sequence":"first","affiliation":[]},{"given":"Richard K.","family":"Wilson","sequence":"additional","affiliation":[]},{"given":"Robert H.","family":"Waterston","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(05)80360-2"},{"key":"e_1_2_1_3_1","first-page":"369a","article-title":"Cloning and sequencing of the ATP\u2010binding domains of novel isoforms of sea urchin dynein","volume":"115","author":"Asai D. J.","year":"1991","journal-title":"J. Cell Biol."},{"key":"e_1_2_1_4_1","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1242\/jcs.107.4.839","article-title":"The dynein genes of Paramecium tetraurelia. Sequences adjacent to the catalytic P\u2010loop identify cytoplasmic and axonemal heavy chain isoforms","volume":"107","author":"Asai D. J.","year":"1994","journal-title":"J. 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