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Journal of Molecular Biology|May 16, 2001
Prokaryotic DNA polymerase I: evolution, structure, and "base flipping" mechanism for nucleotide selectionP H Patel, M Suzuki, E Adman, et al.The Journal of Biological Chemistry|March 30, 2001
The conserved active site motif A of Escherichia coli DNA polymerase I is highly mutableA Shinkai, P H Patel, L A LoebThe Journal of Biological Chemistry|November 9, 2000
A single highly mutable catalytic site amino acid is critical for DNA polymerase fidelityP H Patel, H Kawate, E Adman, et al.The Journal of Biological Chemistry|October 17, 2001
In vivo mutagenesis by Escherichia coli DNA polymerase I. Ile(709) in motif A functions in base selectionA Shinkai, L A LoebProceedings of the National Academy of Sciences of the United States of America|May 11, 2000
DNA polymerase active site is highly mutable: evolutionary consequencesP H Patel, L A LoebThe Journal of Biological Chemistry|September 27, 2000
Multiple amino acid substitutions allow DNA polymerases to synthesize RNAP H Patel, L A LoebProceedings of the National Academy of Sciences of the United States of America|September 3, 1996
Random mutagenesis of Thermus aquaticus DNA polymerase I: concordance of immutable sites in vivo with the crystal structureM Suzuki, D Baskin, L Hood, et al.The Journal of Biological Chemistry|April 25, 1997
Low fidelity mutants in the O-helix of Thermus aquaticus DNA polymerase IM Suzuki, A K Avicola, L Hood, et al.The Journal of Biological Chemistry|July 25, 2000
Thermus aquaticus DNA polymerase I mutants with altered fidelity. Interacting mutations in the O-helixM Suzuki, S Yoshida, E T Adman, et al.Pageof 434