17471982

Source:http://linkedlifedata.com/resource/pubmed/id/17471982

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0033684, umls-concept:C0036536, umls-concept:C0036537, umls-concept:C0178566, umls-concept:C0181904, umls-concept:C0596972, umls-concept:C0728873, umls-concept:C1517378, umls-concept:C1521743, umls-concept:C1704646, umls-concept:C2603343
pubmed:issue	16 Suppl
pubmed:dateCreated	2007-5-2
pubmed:language	jpn
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0413762
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Codon, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide, http://linkedlifedata.com/resource/pubmed/chemical/SecA protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/SecM protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/signal sequence receptor, http://linkedlifedata.com/resource/pubmed/chemical/tRNA, proline-
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	0039-9450
pubmed:author	pubmed-author:ItoKoreakiK, pubmed-author:MutoHirokiH
pubmed:issnType	Print
pubmed:volume	51
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	2583-9
pubmed:meshHeading	pubmed-meshheading:17471982-Adenosine Triphosphatases, pubmed-meshheading:17471982-Bacterial Proteins, pubmed-meshheading:17471982-Calcium-Binding Proteins, pubmed-meshheading:17471982-Cell Membrane Permeability, pubmed-meshheading:17471982-Codon, pubmed-meshheading:17471982-Escherichia coli Proteins, pubmed-meshheading:17471982-Membrane Glycoproteins, pubmed-meshheading:17471982-Membrane Transport Proteins, pubmed-meshheading:17471982-Molecular Chaperones, pubmed-meshheading:17471982-Protein Biosynthesis, pubmed-meshheading:17471982-RNA, Transfer, Amino Acyl, pubmed-meshheading:17471982-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:17471982-Receptors, Peptide, pubmed-meshheading:17471982-Ribosomes, pubmed-meshheading:17471982-Transcription Factors
pubmed:year	2006
pubmed:articleTitle	[New concepts gained from the study of SecM, a secretion monitor protein].
pubmed:affiliation	hmuto@virus.kyoto-u.ac.jp
pubmed:publicationType	Journal Article, Review