Global Identification of New Substrates for the Yeast Endoribonuclease, RNase Mitochondrial RNA Processing (MRP)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference41 articles.
1. Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component;Salinas;J. Biol. Chem.,2005
2. Interactions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase P;Houser-Scott;Proc. Natl. Acad. Sci. U.S.A.,2002
3. Yeast site-specific ribonucleoprotein endoribonuclease MRP contains an RNA component homologous to mammalian RNase MRP RNA and essential for cell viability;Schmitt;Genes Dev.,1994
4. Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes;Forster;Cell,1990
5. Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae;Schmitt;Mol. Cell. Biol.,1993
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2. Structural insight into precursor ribosomal RNA processing by ribonuclease MRP;Science;2020-08-07
3. Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP;Nature Communications;2020-07-10
4. Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP;2020-03-18
5. Asymmetric secretion in budding yeast reinforces daughter cell identity;2018-11-29
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