Artigos de revistas sobre o tema "Enzymes de modifications N-terminales"
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Pessatti, Tomás, Hernán Terenzi e Jean Bertoldo. "Protein Modifications: From Chemoselective Probes to Novel Biocatalysts". Catalysts 11, n.º 12 (30 de novembro de 2021): 1466. http://dx.doi.org/10.3390/catal11121466.
Texto completo da fonteJarrell, Ken F., Gareth M. Jones, Lina Kandiba, Divya B. Nair e Jerry Eichler. "S-Layer Glycoproteins and Flagellins: Reporters of Archaeal Posttranslational Modifications". Archaea 2010 (2010): 1–13. http://dx.doi.org/10.1155/2010/612948.
Texto completo da fonteChang, Yie-Hwa. "Impact of Protein Nα-Modifications on Cellular Functions and Human Health". Life 13, n.º 7 (24 de julho de 2023): 1613. http://dx.doi.org/10.3390/life13071613.
Texto completo da fonteSheeran, Freya L., e Salvatore Pepe. "Posttranslational modifications and dysfunction of mitochondrial enzymes in human heart failure". American Journal of Physiology-Endocrinology and Metabolism 311, n.º 2 (1 de agosto de 2016): E449—E460. http://dx.doi.org/10.1152/ajpendo.00127.2016.
Texto completo da fonteBond, Michelle R., e John A. Hanover. "A little sugar goes a long way: The cell biology of O-GlcNAc". Journal of Cell Biology 208, n.º 7 (30 de março de 2015): 869–80. http://dx.doi.org/10.1083/jcb.201501101.
Texto completo da fontePauli, Cornelius, Michael Kienhöfer, Stefanie Göllner e Carsten Müller-Tidow. "Epitranscriptomic modifications in acute myeloid leukemia: m6A and 2′-O-methylation as targets for novel therapeutic strategies". Biological Chemistry 402, n.º 12 (11 de outubro de 2021): 1531–46. http://dx.doi.org/10.1515/hsz-2021-0286.
Texto completo da fonteXiang, Meiyi, Wensu Liu, Wei Tian, Abin You e Dajun Deng. "RNA N-6-methyladenosine enzymes and resistance of cancer cells to chemotherapy and radiotherapy". Epigenomics 12, n.º 9 (maio de 2020): 801–9. http://dx.doi.org/10.2217/epi-2019-0358.
Texto completo da fontevan den Homberg, Daphne A. L., Reginald V. C. T. van der Kwast, Paul H. A. Quax e A. Yaël Nossent. "N-6-Methyladenosine in Vasoactive microRNAs during Hypoxia; A Novel Role for METTL4". International Journal of Molecular Sciences 23, n.º 3 (19 de janeiro de 2022): 1057. http://dx.doi.org/10.3390/ijms23031057.
Texto completo da fonteRoll-Mecak, Antonina, Agnieszka Szyk e 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 completo da fonteSouza, G. M., D. P. Mehta, M. Lammertz, J. Rodriguez-Paris, R. Wu, J. A. Cardelli e H. H. Freeze. "Dictyostelium lysosomal proteins with different sugar modifications sort to functionally distinct compartments". Journal of Cell Science 110, n.º 18 (15 de setembro de 1997): 2239–48. http://dx.doi.org/10.1242/jcs.110.18.2239.
Texto completo da fonteShima, Hiroki, e Kazuhiko Igarashi. "N 1-methyladenosine (m1A) RNA modification: the key to ribosome control". Journal of Biochemistry 167, n.º 6 (4 de março de 2020): 535–39. http://dx.doi.org/10.1093/jb/mvaa026.
Texto completo da fonteKuldell, James C., Harshani Luknauth, Anthony E. Ricigliano e Nathan W. Rigel. "Biogenesis of Lipoproteins in Gram-Negative Bacteria: 50 Years of Progress". Fine Focus 7, n.º 1 (3 de dezembro de 2021): 9–24. http://dx.doi.org/10.33043/ff.7.1.9-24.
Texto completo da fonteLorenz, Sonja. "Structural mechanisms of HECT-type ubiquitin ligases". Biological Chemistry 399, n.º 2 (26 de janeiro de 2018): 127–45. http://dx.doi.org/10.1515/hsz-2017-0184.
Texto completo da fonteOh, Jang-Hyun, Ju-Yeon Hyun, Shun-Jia Chen e Alexander Varshavsky. "Five enzymes of the Arg/N-degron pathway form a targeting complex: The concept of superchanneling". Proceedings of the National Academy of Sciences 117, n.º 20 (4 de maio de 2020): 10778–88. http://dx.doi.org/10.1073/pnas.2003043117.
Texto completo da fonteMillar, A. Harvey, Joshua L. Heazlewood, Carmela Giglione, Michael J. Holdsworth, Andreas Bachmair e 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 completo da fonteSchaumburg, Anke, Hansjörg A. W. Schneider-Poetsch e C. Eckerskorn. "Characterization of Plastid 5-Aminolevulinate Dehydratase (ALAD; EC 4.2.1.24) from Spinach (Spinacia olevacea L.) by Sequencing and Comparison with Non-Plant ALAD Enzymes". Zeitschrift für Naturforschung C 47, n.º 1-2 (1 de fevereiro de 1992): 77–84. http://dx.doi.org/10.1515/znc-1992-1-214.
Texto completo da fontePortero-Otin, M., M. J. Bellmunt, J. R. Requena e R. Pamplona. "Protein modification by advanced Maillard adducts can be modulated by dietary polyunsaturated fatty acids". Biochemical Society Transactions 31, n.º 6 (1 de dezembro de 2003): 1403–5. http://dx.doi.org/10.1042/bst0311403.
Texto completo da fonteMishra, Suresh, Geetika Bassi e BL Grégoire Nyomba. "Inter-proteomic posttranslational modifications of the SARS-CoV-2 and the host proteins ‒ A new frontier". Experimental Biology and Medicine 246, n.º 7 (19 de janeiro de 2021): 749–57. http://dx.doi.org/10.1177/1535370220986785.
Texto completo da fonteGlassey, Emerson, Andrew M. King, Daniel A. Anderson, Zhengan Zhang e Christopher A. Voigt. "Functional expression of diverse post-translational peptide-modifying enzymes in Escherichia coli under uniform expression and purification conditions". PLOS ONE 17, n.º 9 (19 de setembro de 2022): e0266488. http://dx.doi.org/10.1371/journal.pone.0266488.
Texto completo da fonteSteinbrecher, Tina, e Gerhard Leubner-Metzger. "Xyloglucan remodelling enzymes and the mechanics of plant seed and fruit biology". Journal of Experimental Botany 73, n.º 5 (2 de março de 2022): 1253–57. http://dx.doi.org/10.1093/jxb/erac020.
Texto completo da fonteVarland, Sylvia, Camilla Osberg e Thomas Arnesen. "N‐terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects". PROTEOMICS 15, n.º 14 (16 de junho de 2015): 2385–401. http://dx.doi.org/10.1002/pmic.201400619.
Texto completo da fonteKeffer-Wilkes, Laura Carole, Govardhan Reddy Veerareddygari e Ute Kothe. "RNA modification enzyme TruB is a tRNA chaperone". Proceedings of the National Academy of Sciences 113, n.º 50 (14 de novembro de 2016): 14306–11. http://dx.doi.org/10.1073/pnas.1607512113.
Texto completo da fonteChung, Ben C., Jinshi Zhao, Robert A. Gillespie, Do-Yeon Kwon, Ziqiang Guan, Jiyong Hong, Pei Zhou e Seok-Yong Lee. "Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis". Science 341, n.º 6149 (29 de agosto de 2013): 1012–16. http://dx.doi.org/10.1126/science.1236501.
Texto completo da fonteFernández-Hernando, Carlos, Masaki Fukata, Pascal N. Bernatchez, Yuko Fukata, Michelle I. Lin, David S. Bredt e William C. Sessa. "Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase". Journal of Cell Biology 174, n.º 3 (24 de julho de 2006): 369–77. http://dx.doi.org/10.1083/jcb.200601051.
Texto completo da fonteGalati, Rossella, Alessandra Verdina, Giuliana Falasca e 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 completo da fonteYamauchi, Mitsuo, e Marnisa Sricholpech. "Lysine post-translational modifications of collagen". Essays in Biochemistry 52 (25 de maio de 2012): 113–33. http://dx.doi.org/10.1042/bse0520113.
Texto completo da fonteIze, Bérengère, Sarah J. Coulthurst, Kostas Hatzixanthis, Isabelle Caldelari, Grant Buchanan, Elaine C. Barclay, David J. Richardson, Tracy Palmer e Frank Sargent. "Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains". Microbiology 155, n.º 12 (1 de dezembro de 2009): 3992–4004. http://dx.doi.org/10.1099/mic.0.033647-0.
Texto completo da fonteLubelski, Jacek, Wout Overkamp, Leon D. Kluskens, Gert N. Moll e 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 junho de 2008): 4680–85. http://dx.doi.org/10.1128/aem.00112-08.
Texto completo da fonteChin, Hang Gyeong, Pierre-Olivier Esteve, Cristian Ruse, Jiyoung Lee, Scott E. Schaus, Sriharsa Pradhan e Ulla Hansen. "The microtubule-associated histone methyltransferase SET8, facilitated by transcription factor LSF, methylates α-tubulin". Journal of Biological Chemistry 295, n.º 14 (28 de fevereiro de 2020): 4748–59. http://dx.doi.org/10.1074/jbc.ra119.010951.
Texto completo da fonteMikolajczyk, Krzysztof, Radoslaw Kaczmarek e Marcin Czerwinski. "How glycosylation affects glycosylation: the role of N-glycans in glycosyltransferase activity". Glycobiology 30, n.º 12 (4 de maio de 2020): 941–69. http://dx.doi.org/10.1093/glycob/cwaa041.
Texto completo da fonteBakshi, Tania, David Pham, Raminderjeet Kaur e Bingyun Sun. "Hidden Relationships between N-Glycosylation and Disulfide Bonds in Individual Proteins". International Journal of Molecular Sciences 23, n.º 7 (29 de março de 2022): 3742. http://dx.doi.org/10.3390/ijms23073742.
Texto completo da fonteMathur, Bhoomika, Asif Shajahan, Waqar Arif, Qiushi Chen, Nicholas J. Hand, Lara K. Abramowitz, Kristina Schoonjans et al. "Nuclear receptors FXR and SHP regulate protein N-glycan modifications in the liver". Science Advances 7, n.º 17 (abril de 2021): eabf4865. http://dx.doi.org/10.1126/sciadv.abf4865.
Texto completo da fonteNair, Arathi, e Bhaskar Saha. "Regulation of Ras-GTPase Signaling and Localization by Post-Translational Modifications". Kinases and Phosphatases 1, n.º 2 (21 de abril de 2023): 97–116. http://dx.doi.org/10.3390/kinasesphosphatases1020007.
Texto completo da fonteKolli, Nagamalleswari, Jowita Mikolajczyk, Marcin Drag, Debaditya Mukhopadhyay, Nela Moffatt, Mary Dasso, Guy Salvesen e 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 completo da fonteLarsen, Karen, Roberto Najle, Adrián Lifschitz, María L. Maté, Carlos Lanusse e Guillermo L. Virkel. "Effects of Sublethal Exposure to a Glyphosate-Based Herbicide Formulation on Metabolic Activities of Different Xenobiotic-Metabolizing Enzymes in Rats". International Journal of Toxicology 33, n.º 4 (julho de 2014): 307–18. http://dx.doi.org/10.1177/1091581814540481.
Texto completo da fonteHøegh, Inge, Shamkant Patkar, Torben Halkier e Mogens T. Hansen. "Two lipases from Candida antarctica: cloning and expression in Aspergillus oryzae". Canadian Journal of Botany 73, S1 (31 de dezembro de 1995): 869–75. http://dx.doi.org/10.1139/b95-333.
Texto completo da fontePerez-Rizquez, Carlos, David Lopez-Tejedor, Laura Plaza-Vinuesa, Blanca de las Rivas, Rosario Muñoz, Jose Cumella e Jose M. Palomo. "Chemical Modification of Novel Glycosidases from Lactobacillus plantarum Using Hyaluronic Acid: Effects on High Specificity against 6-Phosphate Glucopyranoside". Coatings 9, n.º 5 (9 de maio de 2019): 311. http://dx.doi.org/10.3390/coatings9050311.
Texto completo da fonteMahapatra, Sebabrata, Tetsuya Yagi, John T. Belisle, Benjamin J. Espinosa, Preston J. Hill, Michael R. McNeil, Patrick J. Brennan e 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 completo da fonteMcEllistrem, M. Catherine, Janet E. Stout e Lee H. Harrison. "Simplified Protocol for Pulsed-Field Gel Electrophoresis Analysis of Streptococcus pneumoniae". Journal of Clinical Microbiology 38, n.º 1 (janeiro de 2000): 351–53. http://dx.doi.org/10.1128/jcm.38.1.351-353.2000.
Texto completo da fonteSpooren, Anita AMG, e Chris TA Evelo. "Only the glutathione dependent antioxidant enzymes are inhibited by haematotoxic hydroxylamines". Human & Experimental Toxicology 17, n.º 10 (outubro de 1998): 554–59. http://dx.doi.org/10.1177/096032719801701005.
Texto completo da fonteAmjadi, Mohammad, Tooba Hallaj e Niko Hildebrandt. "A sensitive homogeneous enzyme assay for euchromatic histone-lysine-N-methyltransferase 2 (G9a) based on terbium-to-quantum dot time-resolved FRET". BioImpacts 11, n.º 3 (8 de julho de 2020): 173–79. http://dx.doi.org/10.34172/bi.2021.23.
Texto completo da fonteSim, E., K. Pinter, A. Mushtaq, A. Upton, J. Sandy, S. Bhakta e M. Noble. "Arylamine N-acetyltransferases: a pharmacogenomic approach to drug metabolism and endogenous function". Biochemical Society Transactions 31, n.º 3 (1 de junho de 2003): 615–19. http://dx.doi.org/10.1042/bst0310615.
Texto completo da fonteZheng, Suting, John J. Wyrick e Joseph C. Reese. "Novel trans-Tail Regulation of H2B Ubiquitylation and H3K4 Methylation by the N Terminus of Histone H2A". Molecular and Cellular Biology 30, n.º 14 (24 de maio de 2010): 3635–45. http://dx.doi.org/10.1128/mcb.00324-10.
Texto completo da fonteNæssan, Cecilia L., Wolfgang Egge-Jacobsen, Ryan W. Heiniger, Matthew C. Wolfgang, Finn Erik Aas, Åsmund Røhr, Hanne C. Winther-Larsen e Michael Koomey. "Genetic and Functional Analyses of PptA, a Phospho-Form Transferase Targeting Type IV Pili in Neisseria gonorrhoeae". Journal of Bacteriology 190, n.º 1 (19 de outubro de 2007): 387–400. http://dx.doi.org/10.1128/jb.00765-07.
Texto completo da fontePatel, Chaitanya, Haddas Saad, Marina Shenkman e Gerardo Z. Lederkremer. "Oxidoreductases in Glycoprotein Glycosylation, Folding, and ERAD". Cells 9, n.º 9 (22 de setembro de 2020): 2138. http://dx.doi.org/10.3390/cells9092138.
Texto completo da fonteRan, Di, Yong-guo Zhang e Jun Sun. "IHIBITION OF TRNA QUEUOSINE MODIFICATION CAUSE MITOCHONDRIAL DYSFUNCTION AND APOPTOSIS IN THE INTESTINAL EPITHELIAL CELLS". Inflammatory Bowel Diseases 30, Supplement_1 (25 de janeiro de 2024): S67—S68. http://dx.doi.org/10.1093/ibd/izae020.145.
Texto completo da fonteAvila, C., R. Huang, M. Stevens, A. Aponte, D. Tripodi, K. Kim e M. Sack. "Platelet Mitochondrial Dysfunction is Evident in Type 2 Diabetes in Association with Modifications of Mitochondrial Anti-Oxidant Stress Proteins". Experimental and Clinical Endocrinology & Diabetes 120, n.º 04 (15 de setembro de 2011): 248–51. http://dx.doi.org/10.1055/s-0031-1285833.
Texto completo da fontePotter, Beth A., Rebecca P. Hughey e Ora A. Weisz. "Role of N- and O-glycans in polarized biosynthetic sorting". American Journal of Physiology-Cell Physiology 290, n.º 1 (janeiro de 2006): C1—C10. http://dx.doi.org/10.1152/ajpcell.00333.2005.
Texto completo da fonteLucas, Jose Antonio, Ana Garcia-Villaraco, Maria Belen Montero-Palmero, Blanca Montalban, Beatriz Ramos Solano e Francisco Javier Gutierrez-Mañero. "Physiological and Genetic Modifications Induced by Plant-Growth-Promoting Rhizobacteria (PGPR) in Tomato Plants under Moderate Water Stress". Biology 12, n.º 7 (23 de junho de 2023): 901. http://dx.doi.org/10.3390/biology12070901.
Texto completo da fonteGarcia-Oliva, Cecilia, Pilar Hoyos, Lucie Petrásková, Natalia Kulik, Helena Pelantová, Alfredo H. Cabanillas, Ángel Rumbero, Vladimír Křen, María J. Hernáiz e Pavla Bojarová. "Acceptor Specificity of β-N-Acetylhexosaminidase from Talaromyces flavus: A Rational Explanation". International Journal of Molecular Sciences 20, n.º 24 (7 de dezembro de 2019): 6181. http://dx.doi.org/10.3390/ijms20246181.
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