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Adam C. Bastidas, Ph.D. - Publications

Affiliations: 
2014 Biomedical Sciences University of California, San Diego, La Jolla, CA 
Area:
Structure, Function, Dynamics, and Localization of PKA as a Prototype for the Protein Kinase Superfamily
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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
2015 Zhang P, Ye F, Bastidas AC, Kornev AP, Wu J, Ginsberg MH, Taylor SS. An Isoform-Specific Myristylation Switch Targets Type II PKA Holoenzymes to Membranes. Structure (London, England : 1993). PMID 26278174 DOI: 10.1016/J.Str.2015.07.007  0.537
2015 Niyitegeka JM, Bastidas AC, Newman RH, Taylor SS, Ongeri EM. Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury. American Journal of Physiology. Renal Physiology. 308: F56-68. PMID 25354939 DOI: 10.1152/Ajprenal.00167.2014  0.523
2015 Bastidas AC, Wu J, Taylor SS. Molecular features of product release for the PKA catalytic cycle. Biochemistry. 54: 2-10. PMID 25077557 DOI: 10.1021/Bi500684C  0.539
2013 Bastidas AC, Pierce LC, Walker RC, Johnson DA, Taylor SS. Influence of N-myristylation and ligand binding on the flexibility of the catalytic subunit of protein kinase A. Biochemistry. 52: 6368-79. PMID 24003983 DOI: 10.1021/Bi400575K  0.551
2013 Bastidas AC, Deal MS, Steichen JM, Guo Y, Wu J, Taylor SS. Phosphoryl transfer by protein kinase A is captured in a crystal lattice. Journal of the American Chemical Society. 135: 4788-98. PMID 23458248 DOI: 10.1021/Ja312237Q  0.552
2012 Bastidas AC, Deal MS, Steichen JM, Keshwani MM, Guo Y, Taylor SS. Role of N-terminal myristylation in the structure and regulation of cAMP-dependent protein kinase. Journal of Molecular Biology. 422: 215-29. PMID 22617327 DOI: 10.1016/J.Jmb.2012.05.021  0.56
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