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Proceedings of the National Academy of Sciences of the United States of America|October 19, 2001
Metal ion cooperativity in ribozyme cleavage of RNAM Brännvall, L A KirsebomMolecular Biology Reports|January 1, 1995
RNase P from bacteria. Substrate recognition and function of the protein subunitL A Kirsebom, A VioqueRNA (New York, N.Y.)|July 22, 1998
The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domainJ Kufel, L A KirsebomNucleic Acids Research|January 11, 1993
Product release is a rate-limiting step during cleavage by the catalytic RNA subunit of Escherichia coli RNase PA Tallsjö, L A KirsebomProceedings of the National Academy of Sciences of the United States of America|June 11, 1996
Different cleavage sites are aligned differently in the active site of M1 RNA, the catalytic subunit of Escherichia coli RNase PJ Kufel, L A KirsebomJournal of Molecular Biology|June 20, 1989
Reaction in vitro of some mutants of RNase P with wild-type and temperature-sensitive substratesL A Kirsebom, S AltmanJournal of Molecular Biology|December 16, 1994
Cleavage site selection by M1 RNA the catalytic subunit of Escherichia coli RNase P, is influenced by pHJ Kufel, L A KirsebomJournal of Molecular Biology|November 15, 1996
Residues in Escherichia coli RNase P RNA important for cleavage site selection and divalent metal ion bindingJ Kufel, L A KirsebomPageof 4