Artículos de revistas sobre el tema "N-terminal modification enzymes"
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Nakano, Miyako, Sushil K. Mishra, Yuko Tokoro, Keiko Sato, Kazuki Nakajima, Yoshiki Yamaguchi, Naoyuki Taniguchi y Yasuhiko Kizuka. "Bisecting GlcNAc Is a General Suppressor of Terminal Modification of N-glycan". Molecular & Cellular Proteomics 18, n.º 10 (2 de agosto de 2019): 2044–57. http://dx.doi.org/10.1074/mcp.ra119.001534.
Texto completoSakato-Antoku, Miho, Jeremy L. Balsbaugh y Stephen M. King. "N-Terminal Processing and Modification of Ciliary Dyneins". Cells 12, n.º 20 (20 de octubre de 2023): 2492. http://dx.doi.org/10.3390/cells12202492.
Texto completoSTOUGHTON, Daniel M., Gerardo ZAPATA, Robert PICONE y Willie F. VANN. "Identification of Arg-12 in the active site of Escherichia coli K1 CMP-sialic acid synthetase". Biochemical Journal 343, n.º 2 (8 de octubre de 1999): 397–402. http://dx.doi.org/10.1042/bj3430397.
Texto completoRoll-Mecak, Antonina, Agnieszka Szyk y Vasilisa Kormendi. "Microtubule chemical complexity: mechanism of tubulin modification enzymes". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 de agosto de 2014): C1286. http://dx.doi.org/10.1107/s2053273314087130.
Texto completoLubelski, Jacek, Wout Overkamp, Leon D. Kluskens, Gert N. Moll y Oscar P. Kuipers. "Influence of Shifting Positions of Ser, Thr, and Cys Residues in Prenisin on the Efficiency of Modification Reactions and on the Antimicrobial Activities of the Modified Prepeptides". Applied and Environmental Microbiology 74, n.º 15 (6 de junio de 2008): 4680–85. http://dx.doi.org/10.1128/aem.00112-08.
Texto completoNakonieczna, Joanna, Tadeusz Kaczorowski, Agnieszka Obarska-Kosinska y Janusz M. Bujnicki. "Functional Analysis of MmeI from Methanol Utilizer Methylophilus methylotrophus, a Subtype IIC Restriction-Modification Enzyme Related to Type I Enzymes". Applied and Environmental Microbiology 75, n.º 1 (7 de noviembre de 2008): 212–23. http://dx.doi.org/10.1128/aem.01322-08.
Texto completoKelley, M. y D. A. Vessey. "Structural comparison between the mitochondrial aralkyl-CoA and arylacetyl-CoA N-acyltransferases". Biochemical Journal 288, n.º 1 (15 de noviembre de 1992): 315–17. http://dx.doi.org/10.1042/bj2880315.
Texto completoSmith, Clyde A., Marta Toth, Nichole K. Stewart, Lauren Maltz y Sergei B. Vakulenko. "Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside-2′′-phosphotransferases". Acta Crystallographica Section D Structural Biology 75, n.º 12 (29 de noviembre de 2019): 1129–37. http://dx.doi.org/10.1107/s2059798319015079.
Texto completoCaillava, Celine, Jean Sevalle y Frederic Checler. "P2-219: identification of enzymes involved in n-terminal truncation and modification of amyloid peptide". Alzheimer's & Dementia 7 (julio de 2011): S382. http://dx.doi.org/10.1016/j.jalz.2011.05.1101.
Texto completoNashed, Salomé, Houssam El Barbry, Médine Benchouaia, Angélie Dijoux-Maréchal, Thierry Delaveau, Nadia Ruiz-Gutierrez, Lucie Gaulier et al. "Functional mapping of N-terminal residues in the yeast proteome uncovers novel determinants for mitochondrial protein import". PLOS Genetics 19, n.º 8 (16 de agosto de 2023): e1010848. http://dx.doi.org/10.1371/journal.pgen.1010848.
Texto completoJayalath, Kumudie, Sean Frisbie, Minhchau To y Sanjaya Abeysirigunawardena. "Pseudouridine Synthase RsuA Captures an Assembly Intermediate That Is Stabilized by Ribosomal Protein S17". Biomolecules 10, n.º 6 (30 de mayo de 2020): 841. http://dx.doi.org/10.3390/biom10060841.
Texto completoLorenz, Sonja. "Structural mechanisms of HECT-type ubiquitin ligases". Biological Chemistry 399, n.º 2 (26 de enero de 2018): 127–45. http://dx.doi.org/10.1515/hsz-2017-0184.
Texto completoMann, Sarah A., Megan K. DeMart, Braidy May, Corey P. Causey y Bryan Knuckley. "Histone H4-based peptoids are inhibitors of protein arginine methyltransferase 1 (PRMT1)". Biochemical Journal 477, n.º 16 (21 de agosto de 2020): 2971–80. http://dx.doi.org/10.1042/bcj20200534.
Texto completoHayman, A. R., A. J. Dryden, T. J. Chambers y M. J. Warburton. "Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide". Biochemical Journal 277, n.º 3 (1 de agosto de 1991): 631–34. http://dx.doi.org/10.1042/bj2770631.
Texto completoJones, Carys S., David Sychantha, P. Lynne Howell y Anthony J. Clarke. "Structural basis for the O-acetyltransferase function of the extracytoplasmic domain of OatA from Staphylococcus aureus". Journal of Biological Chemistry 295, n.º 24 (29 de abril de 2020): 8204–13. http://dx.doi.org/10.1074/jbc.ra120.013108.
Texto completoNosrati, Meisam, Debayan Dey, Atousa Mehrani, Sarah E. Strassler, Natalia Zelinskaya, Eric D. Hoffer, Scott M. Stagg, Christine M. Dunham y Graeme L. Conn. "Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition". Journal of Biological Chemistry 294, n.º 46 (8 de octubre de 2019): 17642–53. http://dx.doi.org/10.1074/jbc.ra119.011181.
Texto completoKolli, Nagamalleswari, Jowita Mikolajczyk, Marcin Drag, Debaditya Mukhopadhyay, Nela Moffatt, Mary Dasso, Guy Salvesen y Keith D. Wilkinson. "Distribution and paralogue specificity of mammalian deSUMOylating enzymes". Biochemical Journal 430, n.º 2 (13 de agosto de 2010): 335–44. http://dx.doi.org/10.1042/bj20100504.
Texto completoJuntawong, Piyada, Pimprapai Butsayawarapat, Pattralak Songserm, Ratchaneeporn Pimjan y Supachai Vuttipongchaikij. "Overexpression of Jatropha curcas ERFVII2 Transcription Factor Confers Low Oxygen Tolerance in Transgenic Arabidopsis by Modulating Expression of Metabolic Enzymes and Multiple Stress-Responsive Genes". Plants 9, n.º 9 (20 de agosto de 2020): 1068. http://dx.doi.org/10.3390/plants9091068.
Texto completoGalati, Rossella, Alessandra Verdina, Giuliana Falasca y Alberto Chersi. "Increased Resistance of Peptides to Serum Proteases by Modification of their Amino Groups". Zeitschrift für Naturforschung C 58, n.º 7-8 (1 de agosto de 2003): 558–61. http://dx.doi.org/10.1515/znc-2003-7-819.
Texto completoBen-Arie, N., M. Khen y D. Lancet. "Glutathione S-transferases in rat olfactory epithelium: purification, molecular properties and odorant biotransformation". Biochemical Journal 292, n.º 2 (1 de junio de 1993): 379–84. http://dx.doi.org/10.1042/bj2920379.
Texto completoMillar, A. Harvey, Joshua L. Heazlewood, Carmela Giglione, Michael J. Holdsworth, Andreas Bachmair y Waltraud X. Schulze. "The Scope, Functions, and Dynamics of Posttranslational Protein Modifications". Annual Review of Plant Biology 70, n.º 1 (29 de abril de 2019): 119–51. http://dx.doi.org/10.1146/annurev-arplant-050718-100211.
Texto completoSu, Ping, Heejeong Im, Hsiaoling Hsieh, Simon Kang’A y Noel W. Dunn. "LlaFI, a Type III Restriction and Modification System in Lactococcus lactis". Applied and Environmental Microbiology 65, n.º 2 (1 de febrero de 1999): 686–93. http://dx.doi.org/10.1128/aem.65.2.686-693.1999.
Texto completoDavis, Katherine M., Kelsey R. Schramma, William A. Hansen, John P. Bacik, Sagar D. Khare, Mohammad R. Seyedsayamdost y Nozomi Ando. "Structures of the peptide-modifying radical SAM enzyme SuiB elucidate the basis of substrate recognition". Proceedings of the National Academy of Sciences 114, n.º 39 (11 de septiembre de 2017): 10420–25. http://dx.doi.org/10.1073/pnas.1703663114.
Texto completoPlavner, Noa y Jerry Eichler. "Defining the Topology of the N-Glycosylation Pathway in the Halophilic Archaeon Haloferax volcanii". Journal of Bacteriology 190, n.º 24 (17 de octubre de 2008): 8045–52. http://dx.doi.org/10.1128/jb.01200-08.
Texto completoChumpen Ramirez, Sabrina, Fernando M. Ruggiero, Jose Luis Daniotti y Javier Valdez Taubas. "Ganglioside glycosyltransferases are S-acylated at conserved cysteine residues involved in homodimerisation". Biochemical Journal 474, n.º 16 (7 de agosto de 2017): 2803–16. http://dx.doi.org/10.1042/bcj20170124.
Texto completoLI, Lin, Song LING, Chun-lai WU, Wei-zhe YAO y Gen-jun XU. "Separate bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: the role of the C-terminal tail in modulating enzyme activity". Biochemical Journal 328, n.º 3 (15 de diciembre de 1997): 751–56. http://dx.doi.org/10.1042/bj3280751.
Texto completoRaz, A. y P. Needleman. "Differential modification of cyclo-oxygenase and peroxidase activities of prostaglandin endoperoxidase synthase by proteolytic digestion and hydroperoxides". Biochemical Journal 269, n.º 3 (1 de agosto de 1990): 603–7. http://dx.doi.org/10.1042/bj2690603.
Texto completoFOLEY, Vivienne y David SHEEHAN. "Glutathione S-transferases of the yeast Yarrowia lipolytica have unusually large molecular mass". Biochemical Journal 333, n.º 3 (1 de agosto de 1998): 839–45. http://dx.doi.org/10.1042/bj3330839.
Texto completoPeng, Gui-Xin, Yong Zhang, Qin-Qin Wang, Qing-Run Li, Hong Xu, En-Duo Wang y Xiao-Long Zhou. "The human tRNA taurine modification enzyme GTPBP3 is an active GTPase linked to mitochondrial diseases". Nucleic Acids Research 49, n.º 5 (22 de febrero de 2021): 2816–34. http://dx.doi.org/10.1093/nar/gkab104.
Texto completoRaj, Hanumantharao G., Ranju Kumari, Garima Gupta, Rajesh Kumar, Daman Saluja, Kambadoor M. Muralidhar, Ajit Kumar et al. "Novel function of calreticulin: Characterization of calreticulin as a transacetylase-mediating protein acetylator independent of acetyl CoA using polyphenolic acetates". Pure and Applied Chemistry 78, n.º 5 (1 de enero de 2006): 985–92. http://dx.doi.org/10.1351/pac200678050985.
Texto completoMOORE, Allison B. y Sheldon W. MAY. "Kinetic and inhibition studies on substrate channelling in the bifunctional enzyme catalysing C-terminal amidation". Biochemical Journal 341, n.º 1 (24 de junio de 1999): 33–40. http://dx.doi.org/10.1042/bj3410033.
Texto completoZhang, Yaoping, Edward L. Pohlmann, Jose Serate, Mary C. Conrad y Gary P. Roberts. "Mutagenesis and Functional Characterization of the Four Domains of GlnD, a Bifunctional Nitrogen Sensor Protein". Journal of Bacteriology 192, n.º 11 (2 de abril de 2010): 2711–21. http://dx.doi.org/10.1128/jb.01674-09.
Texto completoLidholt, K. y U. Lindahl. "Biosynthesis of heparin. The d-glucuronosyl- and N-acetyl-d-glucosaminyltransferase reactions and their relation to polymer modification". Biochemical Journal 287, n.º 1 (1 de octubre de 1992): 21–29. http://dx.doi.org/10.1042/bj2870021.
Texto completoSão-José, Carlos, Ricardo Parreira, Graça Vieira y Mário A. Santos. "The N-Terminal Region of the Oenococcus oeniBacteriophage fOg44 Lysin Behaves as a Bona Fide Signal Peptide inEscherichia coli and as a cis-Inhibitory Element, Preventing Lytic Activity on Oenococcal Cells". Journal of Bacteriology 182, n.º 20 (15 de octubre de 2000): 5823–31. http://dx.doi.org/10.1128/jb.182.20.5823-5831.2000.
Texto completoGoris, Marianne, Robert S. Magin, Håvard Foyn, Line M. Myklebust, Sylvia Varland, Rasmus Ree, Adrian Drazic et al. "Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80". Proceedings of the National Academy of Sciences 115, n.º 17 (26 de marzo de 2018): 4405–10. http://dx.doi.org/10.1073/pnas.1719251115.
Texto completoShang, Tao, Chee Mun Fang, Chin Eng Ong y Yan Pan. "Heterologous Expression of Recombinant Human Cytochrome P450 (CYP) in Escherichia coli: N-Terminal Modification, Expression, Isolation, Purification, and Reconstitution". BioTech 12, n.º 1 (7 de febrero de 2023): 17. http://dx.doi.org/10.3390/biotech12010017.
Texto completoYang, Chien-I., Hao-Hsuan Hsieh y Shu-ou Shan. "Timing and specificity of cotranslational nascent protein modification in bacteria". Proceedings of the National Academy of Sciences 116, n.º 46 (30 de octubre de 2019): 23050–60. http://dx.doi.org/10.1073/pnas.1912264116.
Texto completoMillar, D. J., A. K. Allen, C. G. Smith, C. Sidebottom, A. R. Slabas y G. P. Bolwell. "Chitin-binding proteins in potato (Solanum tuberosum L.) tuber. Characterization, immunolocalization and effects of wounding". Biochemical Journal 283, n.º 3 (1 de mayo de 1992): 813–21. http://dx.doi.org/10.1042/bj2830813.
Texto completoScott, Hannah, Gideon J. Davies y Zachary Armstrong. "The structure of Phocaeicola vulgatus sialic acid acetylesterase". Acta Crystallographica Section D Structural Biology 78, n.º 5 (26 de abril de 2022): 647–57. http://dx.doi.org/10.1107/s2059798322003357.
Texto completoScott, Hannah, Gideon J. Davies y Zachary Armstrong. "The structure of Phocaeicola vulgatus sialic acid acetylesterase". Acta Crystallographica Section D Structural Biology 78, n.º 5 (26 de abril de 2022): 647–57. http://dx.doi.org/10.1107/s2059798322003357.
Texto completoScott, Hannah, Gideon J. Davies y Zachary Armstrong. "The structure of Phocaeicola vulgatus sialic acid acetylesterase". Acta Crystallographica Section D Structural Biology 78, n.º 5 (26 de abril de 2022): 647–57. http://dx.doi.org/10.1107/s2059798322003357.
Texto completoMahapatra, Sebabrata, Tetsuya Yagi, John T. Belisle, Benjamin J. Espinosa, Preston J. Hill, Michael R. McNeil, Patrick J. Brennan y Dean C. Crick. "Mycobacterial Lipid II Is Composed of a Complex Mixture of Modified Muramyl and Peptide Moieties Linked to Decaprenyl Phosphate". Journal of Bacteriology 187, n.º 8 (15 de abril de 2005): 2747–57. http://dx.doi.org/10.1128/jb.187.8.2747-2757.2005.
Texto completoBennick, A. "Structural and Genetic Aspects of Proline-rich Proteins". Journal of Dental Research 66, n.º 2 (febrero de 1987): 457–61. http://dx.doi.org/10.1177/00220345870660021201.
Texto completoRANGARAJAN, Minnie, Susan J. M. SMITH, Sally U y Michael A. CURTIS. "Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor". Biochemical Journal 323, n.º 3 (1 de mayo de 1997): 701–9. http://dx.doi.org/10.1042/bj3230701.
Texto completoTulsiani, D. R. P., M. D. Skudlarek, Y. Araki y M. C. Orgebin-Crist. "Purification and characterization of two forms of β-d-galactosidase from rat epididymal luminal fluid: evidence for their role in the modification of sperm plasma membrane glycoprotein(s)". Biochemical Journal 305, n.º 1 (1 de enero de 1995): 41–50. http://dx.doi.org/10.1042/bj3050041.
Texto completoPark, Suk-Youl, Hyun-Ju Lee, Jung-Mi Song, Jiali Sun, Hyo-Jeong Hwang, Kosuke Nishi y Jeong-Sun Kim. "Structural characterization of a modification subunit of a putative type I restriction enzyme fromVibrio vulnificusYJ016". Acta Crystallographica Section D Biological Crystallography 68, n.º 11 (18 de octubre de 2012): 1570–77. http://dx.doi.org/10.1107/s0907444912038826.
Texto completoBurenina, O. Yu, E. A. Fedotova, A. Yu Ryazanova, A. S. Protsenko, M. V. Zakharova, A. S. Karyagina, A. S. Solonin, T. S. Oretskaya y E. A. Kubareva. "Peculiarities of the Regulation of Gene Expression in the Ecl18kI Restriction–Modification System". Acta Naturae 5, n.º 2 (15 de junio de 2013): 70–80. http://dx.doi.org/10.32607/20758251-2013-5-2-70-80.
Texto completoSoupene, Eric y Frans A. Kuypers. "Dual Role of ACBD6 in the Acylation Remodeling of Lipids and Proteins". Biomolecules 12, n.º 12 (22 de noviembre de 2022): 1726. http://dx.doi.org/10.3390/biom12121726.
Texto completoSLEAT, David E., Stephen R. KRAUS, Istvan SOHAR, Henry LACKLAND y Peter LOBEL. "α-Glucosidase and N-acetylglucosamine-6-sulphatase are the major mannose-6-phosphate glycoproteins in human urine". Biochemical Journal 324, n.º 1 (15 de mayo de 1997): 33–39. http://dx.doi.org/10.1042/bj3240033.
Texto completoOikawa, Daisuke, Kouhei Shimizu y Fuminori Tokunaga. "Pleiotropic Roles of a KEAP1-Associated Deubiquitinase, OTUD1". Antioxidants 12, n.º 2 (1 de febrero de 2023): 350. http://dx.doi.org/10.3390/antiox12020350.
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