Johnson, Jeffrey R; Santos, Silvia D; Johnson, Tasha et al. (2015) Prediction of Functionally Important Phospho-Regulatory Events in Xenopus laevis Oocytes. PLoS Comput Biol 11:e1004362
|
Zhang, Xinshuai; Kumar, Ritesh; Vetting, Matthew W et al. (2015) A unique cis-3-hydroxy-l-proline dehydratase in the enolase superfamily. J Am Chem Soc 137:1388-91
|
Ghasempur, Salehe; Eswaramoorthy, Subramaniam; Hillerich, Brandan S et al. (2014) Discovery of a novel L-lyxonate degradation pathway in Pseudomonas aeruginosa PAO1. Biochemistry 53:3357-66
|
Zhao, Suwen; Sakai, Ayano; Zhang, Xinshuai et al. (2014) Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife 3:
|
Wichelecki, Daniel J; Balthazor, Bryan M; Chau, Anthony C et al. (2014) Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the D-mannonate dehydratase subgroup. Biochemistry 53:2722-31
|
Groninger-Poe, Fiona P; Bouvier, Jason T; Vetting, Matthew W et al. (2014) Evolution of enzymatic activities in the enolase superfamily: galactarate dehydratase III from Agrobacterium tumefaciens C58. Biochemistry 53:4192-203
|
Kim, Seung Joong; Fernandez-Martinez, Javier; Sampathkumar, Parthasarathy et al. (2014) Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex. Mol Cell Proteomics 13:2911-26
|
Odokonyero, Denis; Sakai, Ayano; Patskovsky, Yury et al. (2014) Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family. Proc Natl Acad Sci U S A 111:8535-40
|
Wichelecki, Daniel J; Vendiola, Jean Alyxa Ferolin; Jones, Amy M et al. (2014) Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily: pathways for the catabolism of L-gulonate and L-idonate. Biochemistry 53:5692-9
|
Manjasetty, Babu A; Chance, Mark R; Burley, Stephen K et al. (2014) Crystal structure of Clostridium acetobutylicum Aspartate kinase (CaAK): An important allosteric enzyme for amino acids production. Biotechnol Rep (Amst) 3:73-85
|
Showing the most recent 10 out of 92 publications