Статті в журналах з теми "C-glycosyltransferase"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "C-glycosyltransferase".
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Pelzer, S., R. Süßmuth, D. Heckmann, J. Recktenwald, P. Huber, G. Jung, and W. Wohlleben. "Identification and Analysis of the Balhimycin Biosynthetic Gene Cluster and Its Use for Manipulating Glycopeptide Biosynthesis in Amycolatopsis mediterranei DSM5908." Antimicrobial Agents and Chemotherapy 43, no. 7 (July 1, 1999): 1565–73. http://dx.doi.org/10.1128/aac.43.7.1565.
Повний текст джерелаBirch, Helen L., Luke J. Alderwick, Doris Rittmann, Karin Krumbach, Helga Etterich, Anna Grzegorzewicz, Michael R. McNeil, Lothar Eggeling, and Gurdyal S. Besra. "Identification of a Terminal Rhamnopyranosyltransferase (RptA) Involved in Corynebacterium glutamicum Cell Wall Biosynthesis." Journal of Bacteriology 191, no. 15 (May 29, 2009): 4879–87. http://dx.doi.org/10.1128/jb.00296-09.
Повний текст джерелаFan, Jing, Chunxian Chen, Qibin Yu, Zheng-Guo Li, and Frederick G. Gmitter. "Characterization of three terpenoid glycosyltransferase genes in ‘Valencia’ sweet orange (Citrus sinensis L. Osbeck)." Genome 53, no. 10 (October 2010): 816–23. http://dx.doi.org/10.1139/g10-068.
Повний текст джерелаTegl, Gregor, and Bernd Nidetzky. "Leloir glycosyltransferases of natural product C-glycosylation: structure, mechanism and specificity." Biochemical Society Transactions 48, no. 4 (July 13, 2020): 1583–98. http://dx.doi.org/10.1042/bst20191140.
Повний текст джерелаKus, Julianne V., John Kelly, Luc Tessier, Hanjeong Harvey, Dennis G. Cvitkovitch, and Lori L. Burrows. "Modification of Pseudomonas aeruginosa Pa5196 Type IV Pilins at Multiple Sites with d-Araf by a Novel GT-C Family Arabinosyltransferase, TfpW." Journal of Bacteriology 190, no. 22 (September 19, 2008): 7464–78. http://dx.doi.org/10.1128/jb.01075-08.
Повний текст джерелаHsieh, Yin-Cheng, Hsi-Ho Chiu, Yen-Chieh Huang, Hoong-Kun Fun, Chia-Yu Lu, Yaw-Kuen Li, and Chun-Jung Chen. "Purification, crystallization and preliminary X-ray crystallographic analysis of glycosyltransferase-1 fromBacillus cereus." Acta Crystallographica Section F Structural Biology Communications 70, no. 9 (August 27, 2014): 1228–31. http://dx.doi.org/10.1107/s2053230x14014629.
Повний текст джерелаChen, Dawei, Ridao Chen, Kebo Xie, Tian Yue, Xiaolin Zhang, Fei Ye, and Jungui Dai. "Biocatalytic C-Glucosylation of Coumarins Using an Engineered C-Glycosyltransferase." Organic Letters 20, no. 6 (February 22, 2018): 1634–37. http://dx.doi.org/10.1021/acs.orglett.8b00378.
Повний текст джерелаGutmann, Alexander, and Bernd Nidetzky. "Enzymatic C-glycosylation: Insights from the study of a complementary pair of plant O- and C-glucosyltransferases." Pure and Applied Chemistry 85, no. 9 (September 1, 2013): 1865–77. http://dx.doi.org/10.1351/pac-con-12-11-24.
Повний текст джерелаGeshi, Naomi. "Arabinogalactan Glycosyltransferases: Enzyme Assay, Protein-Protein Interaction, Subcellular Localization, and Perspectives for Application." Advances in Botany 2014 (September 10, 2014): 1–7. http://dx.doi.org/10.1155/2014/434979.
Повний текст джерелаZou, Wei. "C-Glycosides and Aza-C-Glycosides as Potential Glycosidase and Glycosyltransferase Inhibitors." Current Topics in Medicinal Chemistry 5, no. 14 (November 1, 2005): 1363–91. http://dx.doi.org/10.2174/156802605774642999.
Повний текст джерелаCai, Xiaofeng, Takaaki Taguchi, Huili Wang, Megumi Yuki, Megumi Tanaka, Kai Gong, Jinghua Xu, Yiming Zhao, Koji Ichinose, and Aiying Li. "Identification of a C-Glycosyltransferase Involved in Medermycin Biosynthesis." ACS Chemical Biology 16, no. 6 (June 3, 2021): 1059–69. http://dx.doi.org/10.1021/acschembio.1c00227.
Повний текст джерелаZhang, Ya-Qun, Zi-Long Wang, Zhuo Chen, Zheng-Tong Jin, Aobulikasimu Hasan, Hai-Dong Wang, Yu-Wei Sun, Xue Qiao, Yong Wang, and Min Ye. "A highly selective 2′′-O-glycosyltransferase from Ziziphus jujuba and De novo biosynthesis of isovitexin 2′′-O-glucoside." Chemical Communications 58, no. 15 (2022): 2472–75. http://dx.doi.org/10.1039/d1cc06949g.
Повний текст джерелаGutmann, Alexander, Corinna Krump, Linda Bungaruang, and Bernd Nidetzky. "A two-step O- to C-glycosidic bond rearrangement using complementary glycosyltransferase activities." Chem. Commun. 50, no. 41 (2014): 5465–68. http://dx.doi.org/10.1039/c4cc00536h.
Повний текст джерелаBlanco, K. C., F. F. de Moraes, N. S. Bernardi, M. H. P. B. Vettori, R. Monti, and J. Contiero. "Cyclodextrin production by Bacillus lehensis isolated from cassava starch: Characterisation of a novel enzyme." Czech Journal of Food Sciences 32, No. 1 (February 18, 2014): 48–53. http://dx.doi.org/10.17221/432/2012-cjfs.
Повний текст джерелаAmoah, Obed Jackson, Hue Thi Nguyen, and Jae Kyung Sohng. "N-Glucosylation in Corynebacterium glutamicum with YdhE from Bacillus lichenformis." Molecules 27, no. 11 (May 25, 2022): 3405. http://dx.doi.org/10.3390/molecules27113405.
Повний текст джерелаSun, Y., L. M. Willis, H. R. Batchelder, and M. Nitz. "Site specific protein O-glucosylation with bacterial toxins." Chemical Communications 52, no. 88 (2016): 13024–26. http://dx.doi.org/10.1039/c6cc06223g.
Повний текст джерелаHe, Junbin, Kuan Chen, Zhi-min Hu, Kai Li, Wei Song, Li-yan Yu, Chung-Hang Leung, Dik-Lung Ma, Xue Qiao, and Min Ye. "UGT73F17, a new glycosyltransferase from Glycyrrhiza uralensis, catalyzes the regiospecific glycosylation of pentacyclic triterpenoids." Chemical Communications 54, no. 62 (2018): 8594–97. http://dx.doi.org/10.1039/c8cc04215b.
Повний текст джерелаChen, Dawei, Ridao Chen, Kebo Xie, Yangyang Duan, and Jungui Dai. "Production of acetophenone C-glucosides using an engineered C-glycosyltransferase in Escherichia coli." Tetrahedron Letters 59, no. 19 (May 2018): 1875–78. http://dx.doi.org/10.1016/j.tetlet.2018.04.006.
Повний текст джерелаTao, Yehui, Ping Sun, Ruxin Cai, Yan Li, and Honghua Jia. "Exploring the Strategy of Fusing Sucrose Synthase to Glycosyltransferase UGT76G1 in Enzymatic Biotransformation." Applied Sciences 12, no. 8 (April 13, 2022): 3911. http://dx.doi.org/10.3390/app12083911.
Повний текст джерелаWang, Bo, Shang-Hui Jin, Hong-Qun Hu, Yan-Guo Sun, Yan-Wen Wang, Ping Han, and Bing-Kai Hou. "UGT87A2, an Arabidopsis glycosyltransferase, regulates flowering time viaFLOWERING LOCUS C." New Phytologist 194, no. 3 (March 9, 2012): 666–75. http://dx.doi.org/10.1111/j.1469-8137.2012.04107.x.
Повний текст джерелаPlewe, Michael, Konrad Sandhoff, and Richard R. Schmidt. "Synthesis of 4-Epoxy-4-c-methyleneglycosylceramides, Potential Glycosyltransferase Inhibitors." Liebigs Annalen der Chemie 1992, no. 7 (July 24, 1992): 699–708. http://dx.doi.org/10.1002/jlac.1992199201118.
Повний текст джерелаArbeloa, Ana, Heidi Segal, Jean-Emmanuel Hugonnet, Nathalie Josseaume, Lionnel Dubost, Jean-Paul Brouard, Laurent Gutmann, Dominique Mengin-Lecreulx та Michel Arthur. "Role of Class A Penicillin-Binding Proteins in PBP5-Mediated β-Lactam Resistance in Enterococcus faecalis". Journal of Bacteriology 186, № 5 (1 березня 2004): 1221–28. http://dx.doi.org/10.1128/jb.186.5.1221-1228.2004.
Повний текст джерелаKhairullina, Alfia, Nikola Micic, Hans J. Lyngs Jørgensen, Nanna Bjarnholt, Leif Bülow, David B. Collinge, and Birgit Jensen. "Biocontrol Effect of Clonostachys rosea on Fusarium graminearum Infection and Mycotoxin Detoxification in Oat (Avena sativa)." Plants 12, no. 3 (January 21, 2023): 500. http://dx.doi.org/10.3390/plants12030500.
Повний текст джерелаNguyen, Hai P., and Kenichi Yokoyama. "Characterization of Acyl Carrier Protein-Dependent Glycosyltransferase in Mitomycin C Biosynthesis." Biochemistry 58, no. 25 (June 7, 2019): 2804–8. http://dx.doi.org/10.1021/acs.biochem.9b00379.
Повний текст джерелаDürr, Clemens, Dirk Hoffmeister, Sven-Eric Wohlert, Koji Ichinose, Monika Weber, Ursula von Mulert, Jon S. Thorson, and Andreas Bechthold. "The Glycosyltransferase UrdGT2 Catalyzes Both C- and O-Glycosidic Sugar Transfers." Angewandte Chemie International Edition 43, no. 22 (May 24, 2004): 2962–65. http://dx.doi.org/10.1002/anie.200453758.
Повний текст джерелаDürr, Clemens, Dirk Hoffmeister, Sven-Eric Wohlert, Koji Ichinose, Monika Weber, Ursula von Mulert, Jon S. Thorson, and Andreas Bechthold. "Die Glycosyltransferase UrdGT2 katalysiert sowohl C- als auch O-glycosidischen Zuckertransfer." Angewandte Chemie 116, no. 22 (May 24, 2004): 3022–25. http://dx.doi.org/10.1002/ange.200453758.
Повний текст джерелаChen, Dawei, Shuai Fan, Ridao Chen, Kebo Xie, Sen Yin, Lili Sun, Jimei Liu, et al. "Probing and Engineering Key Residues for Bis-C-glycosylation and Promiscuity of a C-Glycosyltransferase." ACS Catalysis 8, no. 6 (April 23, 2018): 4917–27. http://dx.doi.org/10.1021/acscatal.8b00376.
Повний текст джерелаShepherd, Micah D., Tao Liu, Carmen Méndez, Jose A. Salas, and Jürgen Rohr. "Engineered Biosynthesis of Gilvocarcin Analogues with Altered Deoxyhexopyranose Moieties." Applied and Environmental Microbiology 77, no. 2 (November 12, 2010): 435–41. http://dx.doi.org/10.1128/aem.01774-10.
Повний текст джерелаScherman, Hataichanok, Devinder Kaur, Ha Pham, Henrieta Škovierová, Mary Jackson, and Patrick J. Brennan. "Identification of a Polyprenylphosphomannosyl Synthase Involved in the Synthesis of Mycobacterial Mannosides." Journal of Bacteriology 191, no. 21 (August 28, 2009): 6769–72. http://dx.doi.org/10.1128/jb.00431-09.
Повний текст джерелаVoitsekhovskaia, Irina, Constanze Paulus, Charlotte Dahlem, Yuriy Rebets, Suvd Nadmid, Josef Zapp, Denis Axenov-Gribanov, et al. "Baikalomycins A-C, New Aquayamycin-Type Angucyclines Isolated from Lake Baikal Derived Streptomyces sp. IB201691-2A." Microorganisms 8, no. 5 (May 7, 2020): 680. http://dx.doi.org/10.3390/microorganisms8050680.
Повний текст джерелаPLEWE, M., K. SANDHOFF, and R. R. SCHMIDT. "ChemInform Abstract: Synthesis of 4-Epoxy-4-C-methyleneglycosylceramides, Potential Glycosyltransferase Inhibitors." ChemInform 23, no. 46 (August 21, 2010): no. http://dx.doi.org/10.1002/chin.199246237.
Повний текст джерелаTam, Heng Keat, Johannes Härle, Stefan Gerhardt, Jürgen Rohr, Guojun Wang, Jon S. Thorson, Aurélien Bigot, et al. "Strukturelle Charakterisierung von O- und C-glycosylierenden Varianten der Landomycin-Glycosyltransferase LanGT2." Angewandte Chemie 127, no. 9 (January 7, 2015): 2853–57. http://dx.doi.org/10.1002/ange.201409792.
Повний текст джерелаWang, Fengbin, Maoquan Zhou, Shanteri Singh, Ragothaman M. Yennamalli, Craig A. Bingman, Jon S. Thorson, and George N. Phillips. "Crystal structure of SsfS6, the putative C -glycosyltransferase involved in SF2575 biosynthesis." Proteins: Structure, Function, and Bioinformatics 81, no. 7 (April 20, 2013): 1277–82. http://dx.doi.org/10.1002/prot.24289.
Повний текст джерелаHe, Jun‐Bin, Peng Zhao, Zhi‐Min Hu, Shuang Liu, Yi Kuang, Meng Zhang, Bin Li, Cai‐Hong Yun, Xue Qiao, and Min Ye. "Molecular and Structural Characterization of a Promiscuous C ‐Glycosyltransferase from Trollius chinensis." Angewandte Chemie International Edition 58, no. 33 (August 12, 2019): 11513–20. http://dx.doi.org/10.1002/anie.201905505.
Повний текст джерелаKelly, Steven D., Bradley R. Clarke, Olga G. Ovchinnikova, Ryan P. Sweeney, Monica L. Williamson, Todd L. Lowary, and Chris Whitfield. "Klebsiella pneumoniae O1 and O2ac antigens provide prototypes for an unusual strategy for polysaccharide antigen diversification." Journal of Biological Chemistry 294, no. 28 (May 28, 2019): 10863–76. http://dx.doi.org/10.1074/jbc.ra119.008969.
Повний текст джерелаJungui, Dai. "Biocatalytic bis-C-alkylation of phenolics using one-pot cascades with promiscuous C-glycosyltransferase and prenyltransferase." Journal of Chinese Pharmaceutical Sciences 2018, no. 4 (April 15, 2018): 241–50. http://dx.doi.org/10.5246/jcps.2018.04.025.
Повний текст джерелаGUÉRARDEL, Yann, Luis BALANZINO, Emmanuel MAES, Yves LEROY, Bernadette CODDEVILLE, Rafael ORIOL, and Gérard STRECKER. "The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides." Biochemical Journal 357, no. 1 (June 25, 2001): 167–82. http://dx.doi.org/10.1042/bj3570167.
Повний текст джерелаLarson, Eric T., Dirk Reiter, Mark Young, and C. Martin Lawrence. "Structure of A197 from Sulfolobus Turreted Icosahedral Virus: a Crenarchaeal Viral Glycosyltransferase Exhibiting the GT-A Fold." Journal of Virology 80, no. 15 (August 1, 2006): 7636–44. http://dx.doi.org/10.1128/jvi.00567-06.
Повний текст джерелаRajesh, Y., K. Narayanan, V. M. Subrahmanyam, and J. Venkata Rao. "BIOPROSPECTING FOR CYCLODEXTRIN GLYCOSYLTRANSFERASE PRODUCING BACTERIA." INDIAN DRUGS 51, no. 06 (June 28, 2014): 44–48. http://dx.doi.org/10.53879/id.51.06.p0044.
Повний текст джерелаLiu, Meizi, Dandan Wang, Yang Li, Xuemiao Li, Guangning Zong, Shuang Fei, Xue Yang, Jianping Lin, Xiaoqiang Wang, and Yuequan Shen. "Crystal Structures of the C-Glycosyltransferase UGT708C1 from Buckwheat Provide Insights into the Mechanism of C-Glycosylation." Plant Cell 32, no. 9 (July 22, 2020): 2917–31. http://dx.doi.org/10.1105/tpc.20.00002.
Повний текст джерелаYing, Yanling, Xiaozhen Hong, Shu Chen, Ji He, and Faming Zhu. "c.518T > C missense mutation in the B glycosyltransferase gene responsible for a weak B variant." Transfusion 58, no. 1 (November 6, 2017): 269–70. http://dx.doi.org/10.1111/trf.14381.
Повний текст джерелаFischbach, M. A., H. Lin, D. R. Liu, and C. T. Walsh. "From The Cover: In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase." Proceedings of the National Academy of Sciences 102, no. 3 (December 14, 2004): 571–76. http://dx.doi.org/10.1073/pnas.0408463102.
Повний текст джерелаChen, Dawei, Ridao Chen, Ruishan Wang, Jianhua Li, Kebo Xie, Chuancai Bian, Lili Sun, et al. "Probing the Catalytic Promiscuity of a Regio- and Stereospecific C-Glycosyltransferase fromMangifera indica." Angewandte Chemie 127, no. 43 (September 10, 2015): 12869–73. http://dx.doi.org/10.1002/ange.201506505.
Повний текст джерелаVidal, Sébastien, Isabelle Bruyère, Annie Malleron, Claudine Augé, and Jean-Pierre Praly. "Non-isosteric C-glycosyl analogues of natural nucleotide diphosphate sugars as glycosyltransferase inhibitors." Bioorganic & Medicinal Chemistry 14, no. 21 (November 2006): 7293–301. http://dx.doi.org/10.1016/j.bmc.2006.06.057.
Повний текст джерелаChen, Dawei, Ridao Chen, Ruishan Wang, Jianhua Li, Kebo Xie, Chuancai Bian, Lili Sun, et al. "Probing the Catalytic Promiscuity of a Regio- and Stereospecific C-Glycosyltransferase fromMangifera indica." Angewandte Chemie International Edition 54, no. 43 (September 1, 2015): 12678–82. http://dx.doi.org/10.1002/anie.201506505.
Повний текст джерелаTam, Heng Keat, Johannes Härle, Stefan Gerhardt, Jürgen Rohr, Guojun Wang, Jon S. Thorson, Aurélien Bigot, et al. "Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2." Angewandte Chemie International Edition 54, no. 9 (January 7, 2015): 2811–15. http://dx.doi.org/10.1002/anie.201409792.
Повний текст джерелаOvchinnikova, Olga G., Evan Mallette, Akihiko Koizumi, Todd L. Lowary, Matthew S. Kimber та Chris Whitfield. "Bacterial β-Kdo glycosyltransferases represent a new glycosyltransferase family (GT99)". Proceedings of the National Academy of Sciences 113, № 22 (19 травня 2016): E3120—E3129. http://dx.doi.org/10.1073/pnas.1603146113.
Повний текст джерелаWang, Guohong, Jiaxi Li, Shuxin Xie, Zhengyuan Zhai, and Yanling Hao. "The N-terminal domain of rhamnosyltransferase EpsF influences exopolysaccharide chain length determination in Streptococcus thermophilus 05-34." PeerJ 8 (February 12, 2020): e8524. http://dx.doi.org/10.7717/peerj.8524.
Повний текст джерелаChang, Y. C., A. Jong, S. Huang, P. Zerfas, and K. J. Kwon-Chung. "CPS1, a Homolog of the Streptococcus pneumoniae Type 3 Polysaccharide Synthase Gene, Is Important for the Pathobiology of Cryptococcus neoformans." Infection and Immunity 74, no. 7 (July 2006): 3930–38. http://dx.doi.org/10.1128/iai.00089-06.
Повний текст джерелаAllison, Sarah E., Michael A. D'Elia, Sharif Arar, Mario A. Monteiro, and Eric D. Brown. "Studies of the Genetics, Function, and Kinetic Mechanism of TagE, the Wall Teichoic Acid Glycosyltransferase in Bacillus subtilis 168." Journal of Biological Chemistry 286, no. 27 (May 10, 2011): 23708–16. http://dx.doi.org/10.1074/jbc.m111.241265.
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