M
Murray P. Deutscher
Researcher at University of Miami
Publications - 184
Citations - 11738
Murray P. Deutscher is an academic researcher from University of Miami. The author has contributed to research in topics: RNase P & RNase PH. The author has an hindex of 60, co-authored 184 publications receiving 11193 citations. Previous affiliations of Murray P. Deutscher include University of Connecticut Health Center & National Institute for Medical Research.
Papers
More filters
Journal ArticleDOI
Preparation of Cells Permeable to Macromolecules by Treatment with Toluene: Studies of Transfer Ribonucleic Acid Nucleotidyltransferase
TL;DR: Transfer ribonucleic acid (tRNA) nucleotidyltransferase was studied after making cells permeable to macromolecules by treatment with toluene, and the usefulness of such a procedure as an initial step in purification of such enzymes is discussed.
Journal ArticleDOI
Escherichia coli RNase T Functions in Vivo as a Dimer Dependent on Cysteine 168
TL;DR: RNase T dimerizes in vivo, that the dimer form is required for RNase T activity, and that Cys-168 is needed for dimerization of the enzyme.
Journal Article
Escherichia coli RNase M is a multiply altered form of RNase I.
TL;DR: It is shown that RNase M is, in fact, a multiply altered form of RNase I, and is just one of several previously described endoribonuclease activities that are actually manifestations ofRNase I.
Journal ArticleDOI
Mode of Action of RNase BN/RNase Z on tRNA Precursors: RNase BN DOES NOT REMOVE THE CCA SEQUENCE FROM tRNA*
Tanmay Dutta,Murray P. Deutscher +1 more
TL;DR: Findings provide important information on the ability of RNase BN to process tRNA precursors and help explain the known physiological properties of this enzyme and call into question the removal of CCA sequences by RNases BN.
Journal ArticleDOI
Aminoacyl transfer ribonucleic acid synthesis in toluene treated liver cells
TL;DR: It is reported that aminoacyl-tRNA synthetases can be studied within such toluene-treated liver cells, and that these cells are permeable to exogenous tRNA.