11245200

Source:http://linkedlifedata.com/resource/pubmed/id/11245200

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0026376, umls-concept:C0035544, umls-concept:C0179400, umls-concept:C1167298, umls-concept:C1638312, umls-concept:C1706087, umls-concept:C2347930
pubmed:issue	5510
pubmed:dateCreated	2001-3-12
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0404511
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Acid Anhydride Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/MUD2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Triphosphatase, http://linkedlifedata.com/resource/pubmed/chemical/PRP28 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA-dependent ATPase, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoprotein, U1 Small Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, Small Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/U1A protein
pubmed:status	MEDLINE
pubmed:month	Mar
pubmed:issn	0036-8075
pubmed:author	pubmed-author:LührmannRR, pubmed-author:WillC LCL
pubmed:issnType	Print
pubmed:day	9
pubmed:volume	291
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1916-7
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:11245200-Acid Anhydride Hydrolases, pubmed-meshheading:11245200-Adenosine Triphosphatases, pubmed-meshheading:11245200-Adenosine Triphosphate, pubmed-meshheading:11245200-DEAD-box RNA Helicases, pubmed-meshheading:11245200-Fungal Proteins, pubmed-meshheading:11245200-Kinetics, pubmed-meshheading:11245200-Nucleoside-Triphosphatase, pubmed-meshheading:11245200-RNA, Double-Stranded, pubmed-meshheading:11245200-RNA, Small Nuclear, pubmed-meshheading:11245200-RNA Nucleotidyltransferases, pubmed-meshheading:11245200-RNA Precursors, pubmed-meshheading:11245200-RNA-Binding Proteins, pubmed-meshheading:11245200-Ribonucleoprotein, U1 Small Nuclear, pubmed-meshheading:11245200-Ribonucleoproteins, pubmed-meshheading:11245200-Ribonucleoproteins, Small Nuclear, pubmed-meshheading:11245200-Saccharomyces cerevisiae, pubmed-meshheading:11245200-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11245200-Spliceosomes, pubmed-meshheading:11245200-Vaccinia virus
pubmed:year	2001
pubmed:articleTitle	Molecular biology. RNP remodeling with DExH/D boxes.
pubmed:affiliation	Cellular Biochemistry Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. cwill1@gwdg.de
pubmed:publicationType	Journal Article