20302647

Source:http://linkedlifedata.com/resource/pubmed/id/20302647

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0205314, umls-concept:C0679622, umls-concept:C0681842, umls-concept:C1514562, umls-concept:C1880389, umls-concept:C1883204, umls-concept:C1883221
pubmed:dateCreated	2010-4-1
pubmed:abstractText	The mechanism by which the arthropod Oskar and vertebrate TDRD5/TDRD7 proteins nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. Using sequence profile searches we identify a novel domain in these proteins that is widely conserved across eukaryotes and bacteria.
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-11917006, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-12527760, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-15090597, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-15522763, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-15531603, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-15808743, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-15932519, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-16845078, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-17114934, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-17141210, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-17446385, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-17605815, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-17761879, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-18694567, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-18828840, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-19032786, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-19063939, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-19596481, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-19926723, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-19956676, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-20056882, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-770367, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-9254694, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-9399863, http://linkedlifedata.com/resource/pubmed/commentcorrection/20302647-9918945
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101258412
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/RNA, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins
pubmed:status	MEDLINE
pubmed:issn	1745-6150
pubmed:author	pubmed-author:AnantharamanVivekV, pubmed-author:AravindLL, pubmed-author:ZhangDapengD
pubmed:issnType	Electronic
pubmed:volume	5
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	13
pubmed:dateRevised	2010-9-30
pubmed:meshHeading	pubmed-meshheading:20302647-Amino Acid Sequence, pubmed-meshheading:20302647-Animals, pubmed-meshheading:20302647-Evolution, Molecular, pubmed-meshheading:20302647-Helix-Turn-Helix Motifs, pubmed-meshheading:20302647-Molecular Sequence Data, pubmed-meshheading:20302647-Phylogeny, pubmed-meshheading:20302647-Protein Structure, Tertiary, pubmed-meshheading:20302647-RNA, pubmed-meshheading:20302647-RNA-Binding Proteins, pubmed-meshheading:20302647-Sequence Alignment
pubmed:year	2010
pubmed:articleTitle	OST-HTH: a novel predicted RNA-binding domain.
pubmed:affiliation	National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
pubmed:publicationType	Journal Article, Research Support, N.I.H., Intramural