General Reference: | - Bardwell, J. C., Craig, E. A. (1987). "Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli." Proc Natl Acad Sci U S A 84:5177-5181. Pubmed: 3299380
- Berry, M. B., Meador, B., Bilderback, T., Liang, P., Glaser, M., Phillips, G. N. Jr (1994). "The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP." Proteins 19:183-198. Pubmed: 7937733
- Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Brune, M., Schumann, R., Wittinghofer, F. (1985). "Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli." Nucleic Acids Res 13:7139-7151. Pubmed: 2997739
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
- Miyamoto, K., Nakahigashi, K., Nishimura, K., Inokuchi, H. (1991). "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12." J Mol Biol 219:393-398. Pubmed: 2051480
- Muller, C. W., Schlauderer, G. J., Reinstein, J., Schulz, G. E. (1996). "Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding." Structure 4:147-156. Pubmed: 8805521
- Muller, C. W., Schulz, G. E. (1992). "Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state." J Mol Biol 224:159-177. Pubmed: 1548697
- Muller, C. W., Schulz, G. E. (1993). "Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop." Proteins 15:42-49. Pubmed: 8451239
- Munier-Lehmann, H., Burlacu-Miron, S., Craescu, C. T., Mantsch, H. H., Schultz, C. P. (1999). "A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study." Proteins 36:238-248. Pubmed: 10398370
- Reinstein, J., Brune, M., Wittinghofer, A. (1988). "Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli." Biochemistry 27:4712-4720. Pubmed: 2844237
- Reinstein, J., Schlichting, I., Wittinghofer, A. (1990). "Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli." Biochemistry 29:7451-7459. Pubmed: 2223776
- Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
- Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842
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