Статті в журналах з теми "Glycosyltransferase (GT61)"
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Ознайомтеся з топ-22 статей у журналах для дослідження на тему "Glycosyltransferase (GT61)".
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Wu, Ren, Meixian Zhou, and Hui Wu. "Purification and Characterization of an Active N-Acetylglucosaminyltransferase Enzyme Complex from Streptococci." Applied and Environmental Microbiology 76, no. 24 (October 22, 2010): 7966–71. http://dx.doi.org/10.1128/aem.01434-10.
Повний текст джерелаDuncan, Samuel M., and Michael A. J. Ferguson. "Common and unique features of glycosylation and glycosyltransferases in African trypanosomes." Biochemical Journal 479, no. 17 (September 6, 2022): 1743–58. http://dx.doi.org/10.1042/bcj20210778.
Повний текст джерелаBu, Su, Yirong Li, Meixian Zhou, Parastoo Azadin, Meiqin Zeng, Paula Fives-Taylor, and Hui Wu. "Interaction between Two Putative Glycosyltransferases Is Required for Glycosylation of a Serine-Rich Streptococcal Adhesin." Journal of Bacteriology 190, no. 4 (December 14, 2007): 1256–66. http://dx.doi.org/10.1128/jb.01078-07.
Повний текст джерелаMendoza, Fernanda, and Gonzalo A. Jaña. "The inverting mechanism of the metal ion-independent LanGT2: the first step to understand the glycosylation of natural product antibiotic precursors through QM/MM simulations." Organic & Biomolecular Chemistry 19, no. 26 (2021): 5888–98. http://dx.doi.org/10.1039/d1ob00544h.
Повний текст джерелаEvanovich, Eliane, Patricia Jeanne de Souza Mendonça-Mattos, and Maria Lúcia Harada. "Molecular Evolution of the Glycosyltransferase 6 Gene Family in Primates." Biochemistry Research International 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/9051727.
Повний текст джерелаTerrak, Mohammed, and Martine Nguyen-Distèche. "Kinetic Characterization of the Monofunctional Glycosyltransferase from Staphylococcus aureus." Journal of Bacteriology 188, no. 7 (April 1, 2006): 2528–32. http://dx.doi.org/10.1128/jb.188.7.2528-2532.2006.
Повний текст джерелаChang, Te-Sheng, Jiumn-Yih Wu, Tzi-Yuan Wang, Kun-Yuan Wu, and Chien-Min Chiang. "Uridine Diphosphate-Dependent Glycosyltransferases from Bacillus subtilis ATCC 6633 Catalyze the 15-O-Glycosylation of Ganoderic Acid A." International Journal of Molecular Sciences 19, no. 11 (November 5, 2018): 3469. http://dx.doi.org/10.3390/ijms19113469.
Повний текст джерелаZhang, Peng, Zheng Zhang, Lijuan Zhang, Jingjing Wang, and Changsheng Wu. "Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features." Computational and Structural Biotechnology Journal 18 (2020): 1383–90. http://dx.doi.org/10.1016/j.csbj.2020.06.003.
Повний текст джерелаForget, Stephanie M., Sydney B. Shepard, Ebrahim Soleimani, and David L. Jakeman. "On the Catalytic Activity of a GT1 Family Glycosyltransferase from Streptomyces venezuelae ISP5230." Journal of Organic Chemistry 84, no. 18 (August 20, 2019): 11482–92. http://dx.doi.org/10.1021/acs.joc.9b01130.
Повний текст джерелаMiyamoto, Yuji, Tetsu Mukai, Noboru Nakata, Yumi Maeda, Masanori Kai, Takashi Naka, Ikuya Yano, and Masahiko Makino. "Identification and Characterization of the Genes Involved in Glycosylation Pathways of Mycobacterial Glycopeptidolipid Biosynthesis." Journal of Bacteriology 188, no. 1 (January 1, 2006): 86–95. http://dx.doi.org/10.1128/jb.188.1.86-95.2006.
Повний текст джерелаZhou, Meixian, Zhixiang Peng, Paula Fives-Taylor, and Hui Wu. "A Conserved C-Terminal 13-Amino-Acid Motif of Gap1 Is Required for Gap1 Function and Necessary for the Biogenesis of a Serine-Rich Glycoprotein of Streptococcus parasanguinis." Infection and Immunity 76, no. 12 (October 13, 2008): 5624–31. http://dx.doi.org/10.1128/iai.00534-08.
Повний текст джерелаSingh, Sunil Kumar, Cathlene Eland, Jesper Harholt, Henrik Vibe Scheller, and Alan Marchant. "Cell adhesion in Arabidopsis thaliana is mediated by ECTOPICALLY PARTING CELLS 1 - a glycosyltransferase (GT64) related to the animal exostosins." Plant Journal 43, no. 3 (June 30, 2005): 384–97. http://dx.doi.org/10.1111/j.1365-313x.2005.02455.x.
Повний текст джерелаPham, Tram T. K., Brittany Stinson, Nethaji Thiyagarajan, Michelle Lizotte-Waniewski, Keith Brew, and K. Ravi Acharya. "Structures of Complexes of a Metal-independent Glycosyltransferase GT6 fromBacteroides ovatuswith UDP-N-Acetylgalactosamine (UDP-GalNAc) and Its Hydrolysis Products." Journal of Biological Chemistry 289, no. 12 (January 23, 2014): 8041–50. http://dx.doi.org/10.1074/jbc.m113.545384.
Повний текст джерелаJung, Jihye, Doreen Schachtschabel, Michael Speitling та Bernd Nidetzky. "Controllable Iterative β-Glucosylation from UDP-Glucose by Bacillus cereus Glycosyltransferase GT1: Application for the Synthesis of Disaccharide-Modified Xenobiotics". Journal of Agricultural and Food Chemistry 69, № 48 (24 листопада 2021): 14630–42. http://dx.doi.org/10.1021/acs.jafc.1c05788.
Повний текст джерелаAkbar, Sehrish, Wei Yao, Lifang Qin, Yuan Yuan, Charles A. Powell, Baoshan Chen, and Muqing Zhang. "Comparative Analysis of Sugar Metabolites and Their Transporters in Sugarcane Following Sugarcane mosaic virus (SCMV) Infection." International Journal of Molecular Sciences 22, no. 24 (December 17, 2021): 13574. http://dx.doi.org/10.3390/ijms222413574.
Повний текст джерелаPetit, Daniel, Roxana Elin Teppa та Anne Harduin-Lepers. "A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family". Glycobiology, 3 вересня 2020. http://dx.doi.org/10.1093/glycob/cwaa086.
Повний текст джерелаKadirvelraj, Renuka, Jeong-Yeh Yang, Hyun Woo Kim, Justin H. Sanders, Kelley W. Moremen, and Zachary A. Wood. "Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites." Journal of Biological Chemistry, November 23, 2020, jbc.RA120.015305. http://dx.doi.org/10.1074/jbc.ra120.015305.
Повний текст джерелаZhong, Ruiqin, Dongtao Cui, Dennis R. Phillips, Nathanael T. Sims, and Zheng-Hua Ye. "Functional analysis of GT61 glycosyltransferases from grass species in xylan substitutions." Planta 254, no. 6 (November 25, 2021). http://dx.doi.org/10.1007/s00425-021-03794-y.
Повний текст джерелаZhu, Li, Xiting Wei, Jianming Cong, Jing Zou, Lihao Wan, and Shutong Xu. "Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY." Nature Communications 13, no. 1 (December 2, 2022). http://dx.doi.org/10.1038/s41467-022-35234-0.
Повний текст джерелаTeze, David, Gonzalo Nahuel Bidart, and Ditte Hededam Welner. "Family 1 glycosyltransferases (GT1, UGTs) are subject to dilution-induced inactivation and low chemo stability toward their own acceptor substrates." Frontiers in Molecular Biosciences 9 (July 22, 2022). http://dx.doi.org/10.3389/fmolb.2022.909659.
Повний текст джерелаTaujale, Rahil, Zhongliang Zhou, Wayland Yeung, Kelley W. Moremen, Sheng Li, and Natarajan Kannan. "Mapping the glycosyltransferase fold landscape using interpretable deep learning." Nature Communications 12, no. 1 (September 27, 2021). http://dx.doi.org/10.1038/s41467-021-25975-9.
Повний текст джерелаNarciso, Joan Oñate, Wei Zeng, Kris Ford, Edwin R. Lampugnani, John Humphries, Ingvild Austarheim, Allison van de Meene, Antony Bacic та Monika S. Doblin. "Biochemical and Functional Characterization of GALT8, an Arabidopsis GT31 β-(1,3)-Galactosyltransferase That Influences Seedling Development". Frontiers in Plant Science 12 (25 травня 2021). http://dx.doi.org/10.3389/fpls.2021.678564.
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