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DOI stands for Digital Object Identifier ( D igital O bject I dentifier ) ,
and is the unique identifier for objects on the internet. It can be used to create persistent link and to cite articles.

Using DOI as a persistent link

To create a persistent link, add「」 「 」 before a DOI.
For instance, if the DOI of an article is 10.5297/ser.1201.002 , you can link persistently to the article by entering the following link in your browser: 10.5297/ser.1201.002
The DOI link will always direct you to the most updated article page no matter how the publisher changes the document's position, avoiding errors when engaging in important research.

Cite a document with DOI

When citing references, you should also cite the DOI if the article has one. If your citation guideline does not include DOIs, you may cite the DOI link.

DOIs allow accurate citations, improve academic contents connections, and allow users to gain better experience across different platforms. Currently, there are more than 70 million DOIs registered for academic contents. If you want to understand more about DOI, please visit airiti DOI ) 。

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Reference ( 34 ) 〈TOP〉
  1. 4. (a) de Kruijff, B.; van Dam, V.; Breukink, E., Lipid II: A central component in bacterial cell wall synthesis and a target for antibiotics. Prostaglandins, Leukotrienes Essent. Fatty Acids 2008, 79, 117-121. (b) Ritter, T. K.; Wong, C. H., Carbohydrate-based antibiotics: A new approach to tackling the problem of resistance. Angew. Chem., Int. Ed. 2001, 40, 3509-3533. (c) Cheng, T. J. R.; Sung, M. T.; Liao, H. Y.; Chang, Y. F.; Chen, C. W.; Huang, C. Y.; Chou, L. Y.; Wu, Y. D.; Chen, Y.; Cheng, Y. S. E.; Wong, C. H.; Ma, C.; Cheng, W. C., Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics. Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 431-436. (d) Shih, H. W.; Chen, K. T.; Chen, S. K.; Huang, C. Y.; Cheng, T. J. R.; Ma, C.; Wong, C. H.; Cheng, W. C., Combinatorial approach toward synthesis of small molecule libraries as bacterial transglycosylase inhibitors. Org. Biomol. Chem. 2010, 8, 2586-2593. (e) Cheng, T. J. R.; Wu, Y. T.; Yang, S. T.; Lo, K. H.; Chen, S. K.; Chen, Y. H.; Huang, W. I.; Yuan, C. H.; Guo, C. W.; Huang, L. Y.; Chen, K. T.; Shih, H. W.; Cheng, Y. S. E.; Cheng, W. C.; Wong, C. H., High-throughput identification of antibacterials against methicillin-resistant Staphylococcus aureus (MRSA) and the transglycosylase. Bioorg. Med. Chem. 2010, 18, 8512-8529. (f) Stembera, K.; Vogel, S.; Buchynskyy, A.; Ayala, J. A.; Welzel, P., A surface plasmon resonance analysis of the interaction between the antibiotic moenomycin A and penicillin-binding protein 1b. Chembiochem 2002, 3, 559-565.
  2. 5. (a) Lovering, A. L.; de Castro, L. H.; Lim, D.; Strynadka, N. C. J., Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science 2007, 315, 1402-1405. (b) Yuan, Y. Q.; Barrett, D.; Zhang, Y.; Kahne, D.; Sliz, P.; Walker, S., Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis. Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 5348-5353. (c) Sung, M. T.; Lai, Y. T.; Huang, C. Y.; Chou, L. Y.; Shih, H. W.; Cheng, W. C.; Wong, C. H.; Ma, C., Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 8824-8829.
  3. 6. (a) Ye, X. Y.; Lo, M. C.; Brunner, L.; Walker, D.; Kahne, D.; Walker, S., Better substrates for bacterial transglycosylases. J. Am. Chem. Soc. 2001, 123, 3155-3156. (b) Fraipont, C.; Sapunaric, F.; Zervosen, A.; Auger, G.; Devreese, B.; Lioux, T.; Blanot, D.; Mengin-Lecreulx, D.; Herdewijn, P.; Van Beeumen, J.; Frere, J. M.; Nguyen-Disteche, M., Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: Specificity profile for the substrate. Biochemistry 2006, 45, 4007-4013. (c) Liu, C. Y.; Guo, C. W.; Chang, Y. F.; Wang, J. T.; Shih, H. W.; Hsu, Y. F.; Chen, C. W.; Chen, S. K.; Wang, Y. C.; Cheng, T. J. R.; Ma, C.; Wong, C. H.; Fang, J. M.; Cheng, W. C., Synthesis and Evaluation of a New Fluorescent Transglycosylase Substrate: Lipid II-Based Molecule Possessing a Dansyl-C20 Polyprenyl Moiety. Org. Lett. 2010, 12, 1608-1611. (d) Perlstein, D. L.; Wang, T. S. A.; Doud, E. H.; Kahne, D.; Walker, S., The Role of the Substrate Lipid in Processive Glycan Polymerization by the Peptidoglycan Glycosyltransferases. J. Am. Chem. Soc. 2010, 132, 48-49.
  4. 9. (a) Schwartz, B.; Markwalder, J. A.; Wang, Y., Lipid II: Total synthesis of the bacterial cell wall precursor and utilization as a substrate for glycosyltransfer and transpeptidation by penicillin binding protein (PBP) 1b of Eschericia coli. J. Am. Chem. Soc. 2001, 123, 11638-11643. (b) VanNieuwenhze, M. S.; Mauldin, S. C.; Zia-Ebrahimi, M.; Winger, B. E.; Hornback, W. J.; Saha, S. L.; Aikins, J. A.; Blaszczak, L. C., The first total synthesis of lipid II: The final monomeric intermediate in bacterial cell wall biosynthesis. J. Am. Chem. Soc. 2002, 124, 3656-3660. (c) Schwartz, B.; Markwalder, J. A.; Seitz, S. P.; Wang, Y.; Stein, R. L., A kinetic characterization of the glycosyltransferase activity of Eschericia coli PBP1b and development of a continuous fluorescence assay. Biochemistry 2002, 41, 12552-12561. (d) Chang, Y. F.; Liu, C. Y.; Guo, C. W.; Wang, Y. C.; Fang, J. M.; Cheng, W. C., Solid-phase organic synthesis of polyisoprenoid alcohols with traceless sulfone linker. J. Org. Chem. 2008, 73, 7197-7203.
  5. 13. (a) Debenham, J. S.; Rodebaugh, R.; FraserReid, B., TCP- and phthalimide-protected n-pentenyl glucosaminide precursors for the synthesis of nodulation factors as illustrated by the total synthesis of NodRf-III (C18:1, MeFuc). J. Org. Chem. 1997, 62, 4591-4600. (b) Pollastri, M. P., Microwave-mediated synthesis: A green chemistry technology. Abstracts of Papers of the American Chemical Society 2005, 229, U575-U575.
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