Year |
Citation |
Score |
2014 |
Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, et al. Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife. 3. PMID 24980702 DOI: 10.7554/Elife.03275 |
0.554 |
|
2014 |
Odokonyero D, Sakai A, Patskovsky Y, Malashkevich VN, Fedorov AA, Bonanno JB, Fedorov EV, Toro R, Agarwal R, Wang C, Ozerova ND, Yew WS, Sauder JM, Swaminathan S, Burley SK, et al. Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family. Proceedings of the National Academy of Sciences of the United States of America. 111: 8535-40. PMID 24872444 DOI: 10.1073/Pnas.1318703111 |
0.665 |
|
2014 |
Kumar R, Zhao S, Vetting MW, Wood BM, Sakai A, Cho K, Solbiati J, Almo SC, Sweedler JV, Jacobson MP, Gerlt JA, Cronan JE. Prediction and biochemical demonstration of a catabolic pathway for the osmoprotectant proline betaine. Mbio. 5: e00933-13. PMID 24520058 DOI: 10.1128/Mbio.00933-13 |
0.665 |
|
2014 |
Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, Francisco BS, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, et al. Author response: Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks Elife. DOI: 10.7554/Elife.03275.025 |
0.546 |
|
2013 |
Zhao S, Kumar R, Sakai A, Vetting MW, Wood BM, Brown S, Bonanno JB, Hillerich BS, Seidel RD, Babbitt PC, Almo SC, Sweedler JV, Gerlt JA, Cronan JE, Jacobson MP. Discovery of new enzymes and metabolic pathways by using structure and genome context. Nature. 502: 698-702. PMID 24056934 DOI: 10.1038/Nature12576 |
0.708 |
|
2012 |
Lukk T, Sakai A, Kalyanaraman C, Brown SD, Imker HJ, Song L, Fedorov AA, Fedorov EV, Toro R, Hillerich B, Seidel R, Patskovsky Y, Vetting MW, Nair SK, Babbitt PC, et al. Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily. Proceedings of the National Academy of Sciences of the United States of America. 109: 4122-7. PMID 22392983 DOI: 10.1073/Pnas.1112081109 |
0.617 |
|
2009 |
Sakai A, Fedorov AA, Fedorov EV, Schnoes AM, Glasner ME, Brown S, Rutter ME, Bain K, Chang S, Gheyi T, Sauder JM, Burley SK, Babbitt PC, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes. Biochemistry. 48: 1445-53. PMID 19220063 DOI: 10.1021/Bi802277H |
0.614 |
|
2009 |
Sakai A, Fedorov AA, Fedorov EV, Schnoes AM, Glasner ME, Brown S, Rutter ME, Bain K, Chang S, Gheyi T, Sauder JM, Burley SK, Babbitt PC, Almo SC, Gerlt JA. Evolution of Enzymatic Activities in the Enolase Superfamily: Stereochemically Distinct Mechanisms in Two Families ofcis,cis-Muconate Lactonizing Enzymes Biochemistry. 48: 2569-2570. DOI: 10.1021/Bi900265W |
0.444 |
|
2006 |
Glasner ME, Fayazmanesh N, Chiang RA, Sakai A, Jacobson MP, Gerlt JA, Babbitt PC. Evolution of Structure and Function in the o-Succinylbenzoate Synthase/N-Acylamino Acid Racemase Family of the Enolase Superfamily Journal of Molecular Biology. 360: 228-250. PMID 16740275 DOI: 10.1016/J.Jmb.2006.04.055 |
0.613 |
|
2006 |
Sakai A, Xiang DF, Xu C, Song L, Yew WS, Raushel FM, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway for the irreversible conversion of D- to L-amino acids. Biochemistry. 45: 4455-62. PMID 16584181 DOI: 10.1021/Bi060230B |
0.679 |
|
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