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Department of Biology
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Residues in the conserved His domain of fruit fly tRNase Z that function in catalysis are not involved in substrate recognition or binding.
Journal of molecular biology Jul, 2005 | Pubmed ID: 15935379
Naturally occurring mutations in human mitochondrial pre-tRNASer(UCN) can affect the transfer ribonuclease Z cleavage site, processing kinetics, and substrate secondary structure.
The Journal of biological chemistry Feb, 2006 | Pubmed ID: 16361254
Residues in two homology blocks on the amino side of the tRNase Z His domain contribute unexpectedly to pre-tRNA 3' end processing.
RNA (New York, N.Y.) Jun, 2006 | Pubmed ID: 16618969
Columbia University
Neela Zareen1,
Lloyd A. Greene2
1Department of Biology, Columbia University,
2Department of Pathology and Cell Biology, Columbia University
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