Relevant bibliographies by topics / Sortase-mediated ligation

Academic literature on the topic 'Sortase-mediated ligation'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Sortase-mediated ligation"

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Wang, Hejia Henry, Burcin Altun, Kido Nwe, and Andrew Tsourkas. "Proximity-Based Sortase-Mediated Ligation." Angewandte Chemie 129, no. 19 (April 7, 2017): 5433–36. http://dx.doi.org/10.1002/ange.201701419.

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Wang, Hejia Henry, Burcin Altun, Kido Nwe, and Andrew Tsourkas. "Proximity-Based Sortase-Mediated Ligation." Angewandte Chemie International Edition 56, no. 19 (April 4, 2017): 5349–52. http://dx.doi.org/10.1002/anie.201701419.

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Valgardson, Jordan D., Sarah A. Struyvenberg, Zachary R. Sailer, Isabel M. Piper, Justin E. Svendsen, D. Alex Johnson, Brandon A. Vogel, John M. Antos, Michael J. Harms, and Jeanine F. Amacher. "Comparative Analysis and Ancestral Sequence Reconstruction of Bacterial Sortase Family Proteins Generates Functional Ancestral Mutants with Different Sequence Specificities." Bacteria 1, no. 2 (June 9, 2022): 121–35. http://dx.doi.org/10.3390/bacteria1020011.

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Gram-positive bacteria are some of the earliest known life forms, diverging from gram-negative bacteria 2 billion years ago. These organisms utilize sortase enzymes to attach proteins to their peptidoglycan cell wall, a structural feature that distinguishes the two types of bacteria. The transpeptidase activity of sortases make them an important tool in protein engineering applications, e.g., in sortase-mediated ligations or sortagging. However, due to relatively low catalytic efficiency, there are ongoing efforts to create better sortase variants for these uses. Here, we use bioinformatics tools, principal component analysis and ancestral sequence reconstruction, in combination with protein biochemistry, to analyze natural sequence variation in these enzymes. Principal component analysis on the sortase superfamily distinguishes previously described classes and identifies regions of relatively high sequence variation in structurally-conserved loops within each sortase family, including those near the active site. Using ancestral sequence reconstruction, we determined sequences of ancestral Staphylococcus and Streptococcus Class A sortase proteins. Enzyme assays revealed that the ancestral Streptococcus enzyme is relatively active and shares similar sequence variation with other Class A Streptococcus sortases. Taken together, we highlight how natural sequence variation can be utilized to investigate this important protein family, arguing that these and similar techniques may be used to discover or design sortases with increased catalytic efficiency and/or selectivity for sortase-mediated ligation experiments.
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Dai, Xiaolin, Diana Mate, Ulrich Glebe, Tayebeh Mirzaei Garakani, Andrea Körner, Ulrich Schwaneberg, and Alexander Böker. "Sortase-Mediated Ligation of Purely Artificial Building Blocks." Polymers 10, no. 2 (February 6, 2018): 151. http://dx.doi.org/10.3390/polym10020151.

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Han, Ying, Yifan Da, Mingjia Yu, Yaping Cheng, Xin Wang, Jiale Xiong, Guoying Guo, Yan Li, Xianxing Jiang, and Xiaoqing Cai. "Protein labeling approach to improve lysosomal targeting and efficacy of antibody–drug conjugates." Organic & Biomolecular Chemistry 18, no. 17 (2020): 3229–33. http://dx.doi.org/10.1039/d0ob00265h.

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Chen, Qi, Qing Sun, Nicholas M. Molino, Szu-Wen Wang, Eric T. Boder, and Wilfred Chen. "Sortase A-mediated multi-functionalization of protein nanoparticles." Chemical Communications 51, no. 60 (2015): 12107–10. http://dx.doi.org/10.1039/c5cc03769g.

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A new strategy was developed to create multi-functionalizaton of protein nanoparticles using Sortase A-mediated ligation, resulting in modified protein nanoparticles that are both thermally responsive and catalytic active.
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Dai, Xiaolin, Alexander Böker, and Ulrich Glebe. "Broadening the scope of sortagging." RSC Advances 9, no. 9 (2019): 4700–4721. http://dx.doi.org/10.1039/c8ra06705h.

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Williamson, Daniel J., Michael E. Webb, and W. Bruce Turnbull. "Depsipeptide substrates for sortase-mediated N-terminal protein ligation." Nature Protocols 9, no. 2 (January 9, 2014): 253–62. http://dx.doi.org/10.1038/nprot.2014.003.

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Liu, Fa, Ethan Y. Luo, David B. Flora, and Adam R. Mezo. "Irreversible Sortase A-Mediated Ligation Driven by Diketopiperazine Formation." Journal of Organic Chemistry 79, no. 2 (January 6, 2014): 487–92. http://dx.doi.org/10.1021/jo4024914.

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Matsumoto, Takuya, Kou Furuta, Tsutomu Tanaka, and Akihiko Kondo. "Sortase A-Mediated Metabolic Enzyme Ligation in Escherichia coli." ACS Synthetic Biology 5, no. 11 (October 11, 2016): 1284–89. http://dx.doi.org/10.1021/acssynbio.6b00194.

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Dissertations / Theses on the topic "Sortase-mediated ligation"

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Dai, Xiaolin [Verfasser], Alexander [Akademischer Betreuer] Böker, Ulrich Gutachter] Schwaneberg, and Rainer [Gutachter] [Haag. "Synthesis of artificial building blocks for sortase-mediated ligation and their enzymatic linkage / Xiaolin Dai ; Gutachter: Ulrich Schwaneberg, Rainer Haag ; Betreuer: Alexander Böker." Potsdam : Universität Potsdam, 2018. http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-420060.

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Dai, Xiaolin [Verfasser], Alexander [Akademischer Betreuer] Böker, Ulrich [Gutachter] Schwaneberg, and Rainer [Gutachter] Haag. "Synthesis of artificial building blocks for sortase-mediated ligation and their enzymatic linkage / Xiaolin Dai ; Gutachter: Ulrich Schwaneberg, Rainer Haag ; Betreuer: Alexander Böker." Potsdam : Universität Potsdam, 2018. http://d-nb.info/1218404132/34.

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Book chapters on the topic "Sortase-mediated ligation"

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Wang, Hejia Henry, and Andrew Tsourkas. "Overcoming the Limitations of Sortase with Proximity-Based Sortase-Mediated Ligation (PBSL)." In Methods in Molecular Biology, 165–77. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9537-0_13.

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Wang, Hejia Henry, and Andrew Tsourkas. "Site-Specific C-Terminal Labeling of Recombinant Proteins with Proximity-Based Sortase-Mediated Ligation (PBSL)." In Methods in Molecular Biology, 15–28. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9546-2_2.

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