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Anh Vu, Ph.D. - Publications

Affiliations: 
2011 Chemistry University of California, Santa Barbara, Santa Barbara, CA, United States 
Area:
protein structure and function, nuclear magnetic resonance
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2014 Wang X, Vallurupalli P, Vu A, Lee K, Sun S, Bai WJ, Wu C, Zhou H, Shea JE, Kay LE, Dahlquist FW. The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. Biochemistry. 53: 855-61. PMID 24444349 DOI: 10.1021/Bi4012379  0.612
2012 Wang X, Wu C, Vu A, Shea JE, Dahlquist FW. Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA. Journal of the American Chemical Society. 134: 16107-10. PMID 22992224 DOI: 10.1021/Ja3056694  0.616
2012 Wang X, Vu A, Lee K, Dahlquist FW. CheA-receptor interaction sites in bacterial chemotaxis. Journal of Molecular Biology. 422: 282-90. PMID 22659323 DOI: 10.1016/J.Jmb.2012.05.023  0.525
2012 Vu A, Wang X, Zhou H, Dahlquist FW. The receptor-CheW binding interface in bacterial chemotaxis. Journal of Molecular Biology. 415: 759-67. PMID 22155081 DOI: 10.1016/J.Jmb.2011.11.043  0.59
2011 Vu A, Hamel DJ, Zhou H, Dahlquist FW. The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima. Journal of Biomolecular Nmr. 51: 49-55. PMID 21947914 DOI: 10.1007/S10858-011-9540-2  0.644
2011 Vu A, Hamel D, Zhou H, Dahlquist F. Solution Structure of Histidine Phosphotransfer Domain of CheA Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Ld6/Pdb  0.634
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