Year |
Citation |
Score |
2023 |
Lim LR, Wong G, Go MK, Yew WS. Increasing lysergic acid levels for ergot alkaloid biosynthesis: Directing catalysis the F-G loop of Clavine oxidases. Frontiers in Microbiology. 14: 1150937. PMID 37007471 DOI: 10.3389/fmicb.2023.1150937 |
0.781 |
|
2023 |
Go MK, Zhu T, Lim KJH, Hartono YD, Xue B, Fan H, Yew WS. Cannabinoid Biosynthesis Using Noncanonical Cannabinoid Synthases. International Journal of Molecular Sciences. 24. PMID 36674774 DOI: 10.3390/ijms24021259 |
0.771 |
|
2022 |
Han P, Teo WZ, Yew WS. Biologically engineered microbes for bioremediation of electronic waste: Wayposts, challenges and future directions. Engineering Biology. 6: 23-34. PMID 36968558 DOI: 10.1049/enb2.12020 |
0.734 |
|
2022 |
Yap SHK, Pan J, Linh DV, Zhang X, Wang X, Teo WZ, Zamburg E, Tham CK, Yew WS, Poh CL, Thean AV. Engineered Nucleotide Chemicapacitive Microsensor Array Augmented with Physics-Guided Machine Learning for High-Throughput Screening of Cannabidiol. Small (Weinheim An Der Bergstrasse, Germany). e2107659. PMID 35521934 DOI: 10.1002/smll.202107659 |
0.722 |
|
2022 |
Wong G, Lim LR, Tan YQ, Go MK, Bell DJ, Freemont PS, Yew WS. Reconstituting the complete biosynthesis of D-lysergic acid in yeast. Nature Communications. 13: 712. PMID 35132076 DOI: 10.1038/s41467-022-28386-6 |
0.767 |
|
2021 |
Krishna Deepak RNV, Verma RK, Hartono YD, Yew WS, Fan H. Recent Advances in Structure, Function, and Pharmacology of Class A Lipid GPCRs: Opportunities and Challenges for Drug Discovery. Pharmaceuticals (Basel, Switzerland). 15. PMID 35056070 DOI: 10.3390/ph15010012 |
0.763 |
|
2021 |
Han P, Go MK, Chow JY, Xue B, Lim YP, Crone MA, Storch M, Freemont PS, Yew WS. A high-throughput pipeline for scalable kit-free RNA extraction. Scientific Reports. 11: 23260. PMID 34853385 DOI: 10.1038/s41598-021-02742-w |
0.735 |
|
2021 |
Jung H, Ling H, Tan YQ, Chua NH, Yew WS, Chang MW. Heterologous expression of cyanobacterial gas vesicle proteins in Saccharomyces cerevisiae. Biotechnology Journal. e2100059. PMID 34499423 DOI: 10.1002/biot.202100059 |
0.479 |
|
2021 |
Tan YQ, Ali S, Xue B, Teo WZ, Ling LH, Go MK, Lv H, Robinson RC, Narita A, Yew WS. Structure of a Minimal α-Carboxysome-Derived Shell and Its Utility in Enzyme Stabilization. Biomacromolecules. PMID 34384019 DOI: 10.1021/acs.biomac.1c00533 |
0.774 |
|
2021 |
Lim KJH, Lim YP, Hartono YD, Go MK, Fan H, Yew WS. Biosynthesis of Nature-Inspired Unnatural Cannabinoids. Molecules (Basel, Switzerland). 26. PMID 34068935 DOI: 10.3390/molecules26102914 |
0.754 |
|
2021 |
Tan YQ, Xue B, Yew WS. Genetically Encodable Scaffolds for Optimizing Enzyme Function. Molecules (Basel, Switzerland). 26. PMID 33806660 DOI: 10.3390/molecules26051389 |
0.595 |
|
2020 |
Chua PSJ, Go MK, Osothprarop T, Mcdonald S, Karabadzhak AG, Yew WS, Peisajovich S, Nirantar S. Evolving a thermostable terminal deoxynucleotidyl transferase. Acs Synthetic Biology. PMID 32497424 DOI: 10.1021/acssynbio.0c00078 |
0.742 |
|
2020 |
Go MK, Zhao LN, Xue B, Supekar S, Robinson RC, Fan H, Yew WS. Directed Computational Evolution of Quorum-Quenching Lactonases from the Amidohydrolase Superfamily. Structure (London, England : 1993). PMID 32320671 DOI: 10.1016/j.str.2020.03.011 |
0.753 |
|
2020 |
Liow LT, Go MK, Chang MW, Yew WS. Toolkit development for cyanogenic and gold biorecovery chassis . Acs Synthetic Biology. PMID 32160465 DOI: 10.1021/Acssynbio.0C00064 |
0.743 |
|
2018 |
Lim YP, Go MK, Raida M, Inoue T, Wenk MR, Keasling JD, Chang MW, Yew WS. Synthetic Enzymology and the Fountain of Youth: Repurposing Biology for Longevity. Acs Omega. 3: 11050-11061. PMID 30320257 DOI: 10.1021/acsomega.8b01620 |
0.778 |
|
2018 |
Go MK, Chow JY, Yew WS. Directed Evolution of Quorum-Quenching Enzymes: A Method for the Construction of a Directed Evolution Platform and Characterization of a Quorum-Quenching Lactonase from Geobacillus kaustophilus. Methods in Molecular Biology (Clifton, N.J.). 1673: 311-323. PMID 29130183 DOI: 10.1007/978-1-4939-7309-5_24 |
0.781 |
|
2016 |
Lim YP, Go MK, Yew WS. Exploiting the Biosynthetic Potential of Type III Polyketide Synthases. Molecules (Basel, Switzerland). 21. PMID 27338328 DOI: 10.3390/molecules21060806 |
0.803 |
|
2016 |
Tay SB, Chow JY, Go MK, Yew WS. Anti-virulent Disruption of Pathogenic Biofilms using Engineered Quorum-quenching Lactonases. Journal of Visualized Experiments : Jove. PMID 26779961 DOI: 10.3791/53243 |
0.785 |
|
2015 |
Go MK, Wongsantichon J, Cheung VWN, Chow JY, Robinson RC, Yew WS. Synthetic Polyketide Enzymology: Platform for Biosynthesis of Antimicrobial Polyketides Acs Catalysis. 5: 4033-4042. DOI: 10.1021/acscatal.5b00477 |
0.746 |
|
2014 |
Cheung VW, Xue B, Hernandez-Valladares M, Go MK, Tung A, Aguda AH, Robinson RC, Yew WS. Identification of polyketide inhibitors targeting 3-dehydroquinate dehydratase in the shikimate pathway of Enterococcus faecalis. Plos One. 9: e103598. PMID 25072253 DOI: 10.1371/journal.pone.0103598 |
0.782 |
|
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 |
0.537 |
|
2014 |
Go MK, Zhang WC, Lim B, Yew WS. Glycine decarboxylase is an unusual amino acid decarboxylase involved in tumorigenesis. Biochemistry. 53: 947-56. PMID 24467211 DOI: 10.1021/Bi4014227 |
0.731 |
|
2014 |
Chow JY, Yang Y, Tay SB, Chua KL, Yew WS. Disruption of biofilm formation by the human pathogen Acinetobacter baumannii using engineered quorum-quenching lactonases. Antimicrobial Agents and Chemotherapy. 58: 1802-5. PMID 24379199 DOI: 10.1128/AAC.02410-13 |
0.598 |
|
2013 |
Xue B, Chow JY, Baldansuren A, Yap LL, Gan YH, Dikanov SA, Robinson RC, Yew WS. Structural evidence of a productive active site architecture for an evolved quorum-quenching GKL lactonase. Biochemistry. 52: 2359-70. PMID 23461395 DOI: 10.1021/Bi4000904 |
0.67 |
|
2012 |
Go MK, Chow JY, Cheung VW, Lim YP, Yew WS. Establishing a toolkit for precursor-directed polyketide biosynthesis: exploring substrate promiscuities of acid-CoA ligases. Biochemistry. 51: 4568-79. PMID 22587726 DOI: 10.1021/bi300425j |
0.785 |
|
2010 |
Chow JY, Xue B, Lee KH, Tung A, Wu L, Robinson RC, Yew WS. Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily. The Journal of Biological Chemistry. 285: 40911-20. PMID 20980257 DOI: 10.1074/jbc.M110.177139 |
0.66 |
|
2009 |
Chow JY, Wu L, Yew WS. Directed evolution of a quorum-quenching lactonase from Mycobacterium avium subsp. paratuberculosis K-10 in the amidohydrolase superfamily. Biochemistry. 48: 4344-53. PMID 19374350 DOI: 10.1021/bi9004045 |
0.642 |
|
2006 |
Yew WS, Fedorov AA, Fedorov EV, Wood BM, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: D-tartrate dehydratase from Bradyrhizobium japonicum Biochemistry. 45: 14598-14608. PMID 17144653 DOI: 10.1021/Bi061688G |
0.717 |
|
2006 |
Yew WS, Fedorov AA, Fedorov EV, Rakus JF, Pierce RW, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris Biochemistry. 45: 14582-14597. PMID 17144652 DOI: 10.1021/Bi061687O |
0.776 |
|
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 |
0.691 |
|
2005 |
Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 44: 1816-23. PMID 15697207 DOI: 10.1021/Bi0478143 |
0.781 |
|
2005 |
Yew WS, Akana J, Wise EL, Rayment I, Gerlt JA. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 44: 1807-15. PMID 15697206 DOI: 10.1021/Bi047815V |
0.773 |
|
2004 |
Wise EL, Yew WS, Gerlt JA, Rayment I. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 43: 6438-46. PMID 15157078 DOI: 10.1021/bi0497392 |
0.547 |
|
2004 |
Yew WS, Wise EL, Rayment I, Gerlt JA. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 43: 6427-37. PMID 15157077 DOI: 10.1021/Bi049741T |
0.548 |
|
2003 |
Wise EL, Yew WS, Gerlt JA, Rayment I. Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily. Biochemistry. 42: 12133-42. PMID 14567674 DOI: 10.1021/Bi0348819 |
0.552 |
|
2002 |
Wise E, Yew WS, Babbitt PC, Gerlt JA, Rayment I. Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 41: 3861-9. PMID 11900527 DOI: 10.1021/Bi012174E |
0.548 |
|
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