rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1-2
|
pubmed:dateCreated |
1993-4-20
|
pubmed:abstractText |
RNase P and RNase MRP are related ribonucleoproteins. RNase MRP processes mitochondrial precursor- (primer) RNAs, whereas RNase P cleaves precursor-tRNAs to produce their mature 5'-ends. Both RNase P and RNase MRP are associated with the Th/To ribonucleoprotein suggesting possible interrelated pathways and/or functions. All known RNase P and RNase MRP RNAs contain conserved structural elements possibly involved in catalysis/substrate binding, but these elements do not predict all cellular functions of the RNPs.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
319
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1-4
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:7681014-Animals,
pubmed-meshheading:7681014-Base Sequence,
pubmed-meshheading:7681014-Biological Evolution,
pubmed-meshheading:7681014-Conserved Sequence,
pubmed-meshheading:7681014-Endoribonucleases,
pubmed-meshheading:7681014-Humans,
pubmed-meshheading:7681014-Molecular Sequence Data,
pubmed-meshheading:7681014-RNA,
pubmed-meshheading:7681014-RNA, Catalytic,
pubmed-meshheading:7681014-Ribonuclease P,
pubmed-meshheading:7681014-Structure-Activity Relationship
|
pubmed:year |
1993
|
pubmed:articleTitle |
RNase MRP/RNase P: a structure-function relation conserved in evolution?
|
pubmed:affiliation |
Institute of Tumor Biology, University of Vienna, Austria.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|