| Year |
Citation |
Score |
| 2021 |
Song H, Burton AJ, Shirran SL, Fahrig-Kamarauskaitė J, Kaspar H, Muir TW, Künzler M, Naismith JH. Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids. Angewandte Chemie (Weinheim An Der Bergstrasse, Germany). 133: 14440-14444. PMID 38505374 DOI: 10.1002/ange.202100818 |
0.537 |
|
| 2021 |
Matabaro E, Song H, Chepkirui C, Kaspar H, Witte L, Naismith JH, Freeman MF, Künzler M. Enzyme-mediated backbone N-methylation in ribosomally encoded peptides. Methods in Enzymology. 656: 429-458. PMID 34325794 DOI: 10.1016/bs.mie.2021.04.014 |
0.501 |
|
| 2021 |
Naismith JH, Song H, Burton AJ, Shirran SL, Fahrig-Kamarauskaitė J, Kaspar H, Muir TW, Künzler M. Engineering of a peptide α-N-methyltransferase to methylate non-proteinogenic amino acids. Angewandte Chemie (International Ed. in English). PMID 33856715 DOI: 10.1002/anie.202100818 |
0.537 |
|
| 2020 |
Song H, Naismith JH. Enzymatic methylation of the amide bond. Current Opinion in Structural Biology. 65: 79-88. PMID 32653730 DOI: 10.1016/J.Sbi.2020.06.004 |
0.597 |
|
| 2020 |
Song H, Fahrig-Kamarauskaitė J, Matabaro E, Kaspar H, Shirran SL, Zach C, Pace A, Stefanov BA, Naismith JH, Künzler M. Substrate plasticity of a fungal peptide α-N-methyltransferase. Acs Chemical Biology. PMID 32491837 DOI: 10.1021/Acschembio.0C00237 |
0.544 |
|
| 2020 |
Song H, Rao C, Deng Z, Yi Y, Naismith JH. The biosynthetic pathway of the benzoxazole in nataxazole proceeds via an unstable ester and has synthetic utility. Angewandte Chemie (International Ed. in English). PMID 31903677 DOI: 10.1002/Anie.201915685 |
0.628 |
|
| 2018 |
Qin M, Song H, Dai X, Chen Y, Guo Z. Two active site arginines are critical determinants of substrate binding and catalysis in MenD, a thiamine-dependent enzyme in menaquinone biosynthesis. The Biochemical Journal. PMID 30341164 DOI: 10.1042/Bcj20180548 |
0.762 |
|
| 2018 |
Song H, van der Velden NS, Shiran SL, Bleiziffer P, Zach C, Sieber R, Imani AS, Krausbeck F, Aebi M, Freeman MF, Riniker S, Künzler M, Naismith JH. A molecular mechanism for the enzymatic methylation of nitrogen atoms within peptide bonds. Science Advances. 4: eaat2720. PMID 30151425 DOI: 10.1126/Sciadv.Aat2720 |
0.555 |
|
| 2018 |
Guo Z, Qin M, Song H, Dai X, Chan CK, Chan W. Single turnover kinetics reveal a distinct mode of thiamine diphosphate-dependent catalysis in vitamin K biosynthesis. Chembiochem : a European Journal of Chemical Biology. PMID 29726079 DOI: 10.1002/Cbic.201800143 |
0.655 |
|
| 2016 |
Song H, Dong C, Qin M, Chen Y, Sun Y, Liu J, Chan W, Guo Z. A thiamine-dependent enzyme utilizes an active tetrahedral intermediate in vitamin K biosynthesis. Journal of the American Chemical Society. PMID 27213829 DOI: 10.1021/Jacs.6B03437 |
0.747 |
|
| 2015 |
Chen Y, Sun Y, Song H, Guo Z. Structural Basis for the ATP-dependent Configuration of Adenylation Active Site in Bacillus subtilis o-Succinylbenzoyl-CoA Synthetase. The Journal of Biological Chemistry. 290: 23971-83. PMID 26276389 DOI: 10.1074/Jbc.M115.676304 |
0.759 |
|
| 2015 |
Song H, Xu R, Guo Z. Identification and characterization of a methionine γ-lyase in the calicheamicin biosynthetic cluster of Micromonospora echinospora. Chembiochem : a European Journal of Chemical Biology. 16: 100-9. PMID 25404066 DOI: 10.1002/Cbic.201402489 |
0.682 |
|
| 2015 |
Chen Y, Sun Y, Song H, Guo Z. Structural basis for the atp-dependent configuration of adenylation active site in bacillus subtilis o-succinylbenzoyl-coa synthetase Journal of Biological Chemistry. 290: 23971-23983. DOI: 10.1074/jbc.M115.676304 |
0.708 |
|
| 2015 |
Song H, Xu R, Guo Z. Inside Cover: Identification and Characterization of a Methionine γ‐Lyase in the Calicheamicin Biosynthetic Cluster of Micromonospora echinospora (ChemBioChem 1/2015) Chembiochem. 16: 2-2. DOI: 10.1002/Cbic.201490068 |
0.484 |
|
| 2014 |
Song H, Sung HP, Tse YS, Jiang M, Guo Z. Ligand-dependent active-site closure revealed in the crystal structure of Mycobacterium tuberculosis MenB complexed with product analogues. Acta Crystallographica. Section D, Biological Crystallography. 70: 2959-69. PMID 25372686 DOI: 10.1107/S1399004714019440 |
0.69 |
|
| 2013 |
Sun Y, Song H, Li J, Li Y, Jiang M, Zhou J, Guo Z. Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme A synthase from the crotonase fold superfamily. Plos One. 8: e63095. PMID 23658663 DOI: 10.1371/Journal.Pone.0063095 |
0.689 |
|
| 2013 |
Chen M, Ma X, Chen X, Jiang M, Song H, Guo Z. Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli. Journal of Bacteriology. 195: 2768-75. PMID 23564174 DOI: 10.1128/Jb.00141-13 |
0.651 |
|
| 2012 |
Sun Y, Song H, Li J, Jiang M, Li Y, Zhou J, Guo Z. Active site binding and catalytic role of bicarbonate in 1,4-dihydroxy-2-naphthoyl coenzyme A synthases from vitamin K biosynthetic pathways. Biochemistry. 51: 4580-9. PMID 22606952 DOI: 10.1021/Bi300486J |
0.702 |
|
| 2012 |
Song H, Guo Z. Characterization of 1,4-dihydroxy-2-naphthoyl-coenzyme A synthase (MenB) in phylloquinone biosynthesis of Synechocystis sp. PCC 6803 Science China-Chemistry. 55: 98-105. DOI: 10.1007/S11426-011-4448-Y |
0.631 |
|
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