Three-dimensional structure of ribonuclease H from E. coli
- K. Katayanagi, M. Miyagawa, K. Morikawa
- Biology, ChemistryNature
- 20 September 1990
THE three-dimensional structure of RNase H from Escherichia coli was determined at 1.8 Å resolution by X-ray crystallography. The enzyme was found to belong to the α + β class of structures,…
NMR studies of a DNA containing 8-hydroxydeoxyguanosine.
- Y. Oda, S. Uesugi, E. Ohtsuka
- Chemistry, BiologyNucleic Acids Research
- 11 April 1991
NMR data indicate that the 8-hydroxyguanine (oh8G) base takes a 6,8-diketo tautomeric form and is base-paired to C with Watson-Crick type hydrogen bonds in a B-form structure.
Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution.
- K. Katayanagi, M. Miyagawa, K. Morikawa
- Chemistry, BiologyJournal of Molecular Biology
- 20 February 1992
Essential structure of E. coli promoter: effect of spacer length between the two consensus sequences on promoter function.
- T. Aoyama, M. Takanami, M. Ikehara
- BiologyNucleic Acids Research
- 10 September 1983
A promoter with the consensus sequence(TTGACA and TATAAT) at -35 and -10 regions was constructed, and the distance between the two consensus sequences was independently altered at two restriction…
An alternative approach to deoxyoligonucleotides as hybridization probes by insertion of deoxyinosine at ambiguous codon positions.
- E. Ohtsuka, S. Matsuki, M. Ikehara, Y. Takahashi, K. Matsubara
- Biology, ChemistryJournal of Biological Chemistry
- 10 March 1985
Identification of the amino acid residues involved in an active site of Escherichia coli ribonuclease H by site-directed mutagenesis.
- S. Kanaya, A. Kohara, M. Ikehara
- Biology, ChemistryJournal of Biological Chemistry
- 15 March 1990
X-ray structure of T4 endonuclease V: an excision repair enzyme specific for a pyrimidine dimer.
- K. Morikawa, O. Matsumoto, E. Ohtsuka
- Chemistry, BiologyScience
- 24 April 1992
The x-ray structure of T4 endonuclease V, an enzyme responsible for the first step of a pyrimidine-dimer-specific excision-repair pathway, was determined at a 1.6-angstrom resolution and suggests the residues involved in the substrate binding and the catalysis of the glycosylation reaction.
Carbon-13 magnetic resonance spectra of 8-substituted purine nucleosides. Characteristic shifts for the syn conformation.
- S. Uesugi, M. Ikehara
- ChemistryJournal of the American Chemical Society
- 11 May 1977
Secretion in yeast of human lysozymes with different specific activities created by replacing valine-110 with proline by site-directed mutagenesis.
- M. Kikuchi, Y. Yamamoto, M. Ikehara
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 December 1988
The results suggest that cis/trans isomerization of prolyl peptide bonds probably occurs in vivo and that the conformational change of protein as well as point mutations in genes might influence the molecular evolution of the protein.
Role of the basic amino acid cluster and Glu-23 in pyrimidine dimer glycosylase activity of T4 endonuclease V.
- T. Doi, A. Recktenwald, E. Ohtsuka
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 15 October 1992
Results indicate that Glu-23 plays an important role in catalysis of the DNA glycosylase reaction, and that Arg-3 is a crucial residue for substrate binding in T4 endonuclease V.
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