Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
Q Lu, S Wierzbicki, AS Krasilnikov, ME Schmitt - RNA, 2010 - rnajournal.cshlp.org
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
Q Lu, S Wierzbicki, AS Kraslinikov, ME Schmitt - RNA, 2010 - rnajournal.cshlp.org
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
Q Lu, S Wierzbicki, AS Krasilnikov, ME Schmitt - RNA, 2010 - pure.psu.edu
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
Q Lu, S Wierzbicki, AS Krasilnikov… - RNA (New York …, 2010 - pubmed.ncbi.nlm.nih.gov
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
[PDF][PDF] Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
Q LU, S WIERZBICKI, AS KRASILNIKOV, ME SCHMITT - RNA, 2010 - researchgate.net
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
[HTML][HTML] Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
Q Lu, S Wierzbicki, AS Krasilnikov, ME Schmitt - RNA, 2010 - ncbi.nlm.nih.gov
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components.
Q Lu, S Wierzbicki, AS Krasilnikov… - RNA (New York, NY), 2010 - europepmc.org
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …