Year |
Citation |
Score |
2009 |
Quezada CM, Hicks SW, Galán JE, Stebbins CE. A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases. Proceedings of the National Academy of Sciences of the United States of America. 106: 4864-9. PMID 19273841 DOI: 10.1073/Pnas.0811058106 |
0.32 |
|
2005 |
Quezada CM, Hamel DJ, Gradinaru C, Bilwes AM, Dahlquist FW, Crane BR, Simon MI. Structural and chemical requirements for histidine phosphorylation by the chemotaxis kinase CheA. The Journal of Biological Chemistry. 280: 30581-5. PMID 15994328 DOI: 10.1074/Jbc.M505316200 |
0.511 |
|
2004 |
Quezada CM, Gradinaru C, Simon MI, Bilwes AM, Crane BR. Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima. Journal of Molecular Biology. 341: 1283-94. PMID 15321722 DOI: 10.1016/J.Jmb.2004.06.061 |
0.497 |
|
2004 |
Park SY, Quezada CM, Bilwes AM, Crane BR. Subunit exchange by CheA histidine kinases from the mesophile Escherichia coli and the thermophile Thermotoga maritima. Biochemistry. 43: 2228-40. PMID 14979719 DOI: 10.1021/Bi0352419 |
0.41 |
|
2002 |
Bilwes AM, Park SY, Quezada CM, Simon MI, Crane BR. Structure and Function of CheA, the Histidine Kinase Central to Bacterial Chemotaxis Histidine Kinases in Signal Transduction. 47-72. DOI: 10.1016/B978-012372484-7/50005-9 |
0.448 |
|
2001 |
Bilwes AM, Quezada CM, Croal LR, Crane BR, Simon MI. Nucleotide binding by the histidine kinase CheA. Nature Structural Biology. 8: 353-60. PMID 11276258 DOI: 10.1038/86243 |
0.504 |
|
1999 |
Takeuchi T, Böttcher A, Quezada CM, Meade TJ, Gray HB. Inhibition of thermolysin and human alpha-thrombin by cobalt(III) Schiff base complexes. Bioorganic & Medicinal Chemistry. 7: 815-9. PMID 10400334 DOI: 10.1016/S0968-0896(98)00272-7 |
0.353 |
|
1998 |
Takeuchi T, Bottcher A, Quezada CM, Simon MI, Meade TJ, Gray HB. Selective inhibition of human α-thrombin by cobalt(III) Schiff base complexes [20] Journal of the American Chemical Society. 120: 8555-8556. DOI: 10.1021/Ja981191X |
0.374 |
|
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