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1696176
Source:
http://linkedlifedata.com/resource/pubmed/id/1696176
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60
)
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Statements in which the resource exists as a subject.
Predicate
Object
rdf:type
pubmed:Citation
lifeskim:mentions
umls-concept:C0014442
,
umls-concept:C0035668
,
umls-concept:C0073243
,
umls-concept:C0165198
,
umls-concept:C0449432
,
umls-concept:C0678594
,
umls-concept:C1179435
,
umls-concept:C1524073
,
umls-concept:C1548799
,
umls-concept:C1705248
,
umls-concept:C2348205
pubmed:issue
3
pubmed:dateCreated
1990-9-13
pubmed:grant
http://linkedlifedata.com/resource/pubmed/grant/GM19422
pubmed:language
eng
pubmed:journal
http://linkedlifedata.com/resource/pubmed/journal/0413066
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases
,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins
,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial
,
http://linkedlifedata.com/resource/pubmed/chemical/RPP14 protein, human
,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P
,
http://linkedlifedata.com/resource/pubmed/chemical/mitochondrial RNA-processing...
,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease P, E coli
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0092-8674
pubmed:author
pubmed-author:AltmanSS
,
pubmed-author:ForsterA CAC
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
407-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1696176-Bacillus subtilis
,
pubmed-meshheading:1696176-Base Sequence
,
pubmed-meshheading:1696176-Endoribonucleases
,
pubmed-meshheading:1696176-Escherichia coli
,
pubmed-meshheading:1696176-Escherichia coli Proteins
,
pubmed-meshheading:1696176-Genes, Bacterial
,
pubmed-meshheading:1696176-Genes, Fungal
,
pubmed-meshheading:1696176-HeLa Cells
,
pubmed-meshheading:1696176-Humans
,
pubmed-meshheading:1696176-Molecular Sequence Data
,
pubmed-meshheading:1696176-Nucleic Acid Conformation
,
pubmed-meshheading:1696176-RNA, Bacterial
,
pubmed-meshheading:1696176-Ribonuclease P
,
pubmed-meshheading:1696176-Saccharomyces cerevisiae
,
pubmed-meshheading:1696176-Sequence Homology, Nucleic Acid
pubmed:year
1990
pubmed:articleTitle
Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes.
pubmed:affiliation
Department of Biology, Yale University, New Haven, Connecticut 06520.
pubmed:publicationType
Journal Article
,
Comparative Study
,
Research Support, U.S. Gov't, P.H.S.
,
Research Support, U.S. Gov't, Non-P.H.S.
,
Research Support, Non-U.S. Gov't