Artigos de revistas sobre o tema "Peptidoglycan polymerization"
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Arthur, Michel. "Regulation of Bacterial Peptidoglycan Polymerization". Trends in Microbiology 24, n.º 7 (julho de 2016): 519–21. http://dx.doi.org/10.1016/j.tim.2016.05.003.
Texto completo da fonteVasudevan, Pradeep, Jessica McElligott, Christa Attkisson, Michael Betteken e David L. Popham. "Homologues of the Bacillus subtilis SpoVB Protein Are Involved in Cell Wall Metabolism". Journal of Bacteriology 191, n.º 19 (31 de julho de 2009): 6012–19. http://dx.doi.org/10.1128/jb.00604-09.
Texto completo da fonteChan, Yvonne G. Y., Matthew B. Frankel, Dominique Missiakas e Olaf Schneewind. "SagB Glucosaminidase Is a Determinant of Staphylococcus aureus Glycan Chain Length, Antibiotic Susceptibility, and Protein Secretion". Journal of Bacteriology 198, n.º 7 (25 de janeiro de 2016): 1123–36. http://dx.doi.org/10.1128/jb.00983-15.
Texto completo da fonteZuber, Benoît, Marisa Haenni, Tânia Ribeiro, Kathrin Minnig, Fátima Lopes, Philippe Moreillon e Jacques Dubochet. "Granular Layer in the Periplasmic Space of Gram-Positive Bacteria and Fine Structures of Enterococcus gallinarum and Streptococcus gordonii Septa Revealed by Cryo-Electron Microscopy of Vitreous Sections". Journal of Bacteriology 188, n.º 18 (15 de setembro de 2006): 6652–60. http://dx.doi.org/10.1128/jb.00391-06.
Texto completo da fonteRuiz, Natividad. "Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase inEscherichia coli". Proceedings of the National Academy of Sciences 105, n.º 40 (1 de outubro de 2008): 15553–57. http://dx.doi.org/10.1073/pnas.0808352105.
Texto completo da fonteYagi, Tetsuya, Sebabrata Mahapatra, Katarína Mikušová, Dean C. Crick e Patrick J. Brennan. "Polymerization of Mycobacterial Arabinogalactan and Ligation to Peptidoglycan". Journal of Biological Chemistry 278, n.º 29 (28 de abril de 2003): 26497–504. http://dx.doi.org/10.1074/jbc.m302216200.
Texto completo da fonteArbeloa, Ana, Heidi Segal, Jean-Emmanuel Hugonnet, Nathalie Josseaume, Lionnel Dubost, Jean-Paul Brouard, Laurent Gutmann, Dominique Mengin-Lecreulx e Michel Arthur. "Role of Class A Penicillin-Binding Proteins in PBP5-Mediated β-Lactam Resistance in Enterococcus faecalis". Journal of Bacteriology 186, n.º 5 (1 de março de 2004): 1221–28. http://dx.doi.org/10.1128/jb.186.5.1221-1228.2004.
Texto completo da fonteRice, Louis B., Lenore L. Carias, Susan Rudin, Rebecca Hutton, Steven Marshall, Medhat Hassan, Nathalie Josseaume, Lionel Dubost, Arul Marie e Michel Arthur. "Role of Class A Penicillin-Binding Proteins in the Expression of β-Lactam Resistance in Enterococcus faecium". Journal of Bacteriology 191, n.º 11 (20 de março de 2009): 3649–56. http://dx.doi.org/10.1128/jb.01834-08.
Texto completo da fonteAllen, N. E., J. N. Hobbs e T. I. Nicas. "Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semisynthetic glycopeptide antibiotic." Antimicrobial Agents and Chemotherapy 40, n.º 10 (outubro de 1996): 2356–62. http://dx.doi.org/10.1128/aac.40.10.2356.
Texto completo da fonteBraddick, Darren, Sandeep Sandhu, David I. Roper, Michael J. Chappell e Timothy D. H. Bugg. "Observation of the time-course for peptidoglycan lipid intermediate II polymerization by Staphylococcus aureus monofunctional transglycosylase". Microbiology 160, n.º 8 (1 de agosto de 2014): 1628–36. http://dx.doi.org/10.1099/mic.0.079442-0.
Texto completo da fonteZheng, Sanduo, Lok-To Sham, Frederick A. Rubino, Kelly P. Brock, William P. Robins, John J. Mekalanos, Debora S. Marks, Thomas G. Bernhardt e Andrew C. Kruse. "Structure and mutagenic analysis of the lipid II flippase MurJ fromEscherichia coli". Proceedings of the National Academy of Sciences 115, n.º 26 (11 de junho de 2018): 6709–14. http://dx.doi.org/10.1073/pnas.1802192115.
Texto completo da fonteYunck, Rachel, Hongbaek Cho e Thomas G. Bernhardt. "Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria". Molecular Microbiology 99, n.º 4 (19 de novembro de 2015): 700–718. http://dx.doi.org/10.1111/mmi.13258.
Texto completo da fontevan Heijenoort, Jean. "Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan". Microbiology and Molecular Biology Reviews 71, n.º 4 (dezembro de 2007): 620–35. http://dx.doi.org/10.1128/mmbr.00016-07.
Texto completo da fonteAli Hasan, Waseem. "Differential Study of Antimicrobial Activity of Vancomycin and Teicoplanin (Targocid) against Strains of Staphylococcus aureus and Streptococci sp." Tikrit Journal of Pharmaceutical Sciences 5, n.º 2 (13 de abril de 2023): 203–7. http://dx.doi.org/10.25130/tjphs.2009.5.2.11.203.207.
Texto completo da fonteSjodt, Megan, Patricia D. A. Rohs, Morgan S. A. Gilman, Sarah C. Erlandson, Sanduo Zheng, Anna G. Green, Kelly P. Brock et al. "Structural coordination of polymerization and crosslinking by a SEDS–bPBP peptidoglycan synthase complex". Nature Microbiology 5, n.º 6 (9 de março de 2020): 813–20. http://dx.doi.org/10.1038/s41564-020-0687-z.
Texto completo da fontePlocinski, P., M. Ziolkiewicz, M. Kiran, S. I. Vadrevu, H. B. Nguyen, J. Hugonnet, C. Veckerle et al. "Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes". Journal of Bacteriology 193, n.º 13 (29 de abril de 2011): 3246–56. http://dx.doi.org/10.1128/jb.00188-11.
Texto completo da fontePunekar, Avinash S., Firdaus Samsudin, Adrian J. Lloyd, Christopher G. Dowson, David J. Scott, Syma Khalid e David I. Roper. "The role of the jaw subdomain of peptidoglycan glycosyltransferases for lipid II polymerization". Cell Surface 2 (junho de 2018): 54–66. http://dx.doi.org/10.1016/j.tcsw.2018.06.002.
Texto completo da fontePerlstein, Deborah L., Tsung-Shing Andrew Wang, Emma H. Doud, Daniel Kahne e Suzanne Walker. "The Role of the Substrate Lipid in Processive Glycan Polymerization by the Peptidoglycan Glycosyltransferases". Journal of the American Chemical Society 132, n.º 1 (13 de janeiro de 2010): 48–49. http://dx.doi.org/10.1021/ja909325m.
Texto completo da fonteZawadzka-Skomiał, Joanna, Zdzislaw Markiewicz, Martine Nguyen-Distèche, Bart Devreese, Jean-Marie Frère e Mohammed Terrak. "Characterization of the Bifunctional Glycosyltransferase/Acyltransferase Penicillin-Binding Protein 4 of Listeria monocytogenes". Journal of Bacteriology 188, n.º 5 (1 de março de 2006): 1875–81. http://dx.doi.org/10.1128/jb.188.5.1875-1881.2006.
Texto completo da fonteQiao, Lei, e John C. Vederas. "Synthesis of a C-phosphonate disaccharide as a potential inhibitor of peptidoglycan polymerization by transglycosylase". Journal of Organic Chemistry 58, n.º 13 (junho de 1993): 3480–82. http://dx.doi.org/10.1021/jo00065a004.
Texto completo da fonteSchaefer, Kaitlin, Tristan W. Owens, Julia E. Page, Marina Santiago, Daniel Kahne e Suzanne Walker. "Structure and reconstitution of a hydrolase complex that may release peptidoglycan from the membrane after polymerization". Nature Microbiology 6, n.º 1 (9 de novembro de 2020): 34–43. http://dx.doi.org/10.1038/s41564-020-00808-5.
Texto completo da fonteVarma, Archana, Miguel A. de Pedro e Kevin D. Young. "FtsZ Directs a Second Mode of Peptidoglycan Synthesis in Escherichia coli". Journal of Bacteriology 189, n.º 15 (18 de maio de 2007): 5692–704. http://dx.doi.org/10.1128/jb.00455-07.
Texto completo da fonteHamilton, Andrea, David L. Popham, David J. Carl, Xavier Lauth, Victor Nizet e Amanda L. Jones. "Penicillin-Binding Protein 1a Promotes Resistance of Group B Streptococcus to Antimicrobial Peptides". Infection and Immunity 74, n.º 11 (novembro de 2006): 6179–87. http://dx.doi.org/10.1128/iai.00895-06.
Texto completo da fonteMarkovski, Monica, Jessica L. Bohrhunter, Tania J. Lupoli, Tsuyoshi Uehara, Suzanne Walker, Daniel E. Kahne e Thomas G. Bernhardt. "Cofactor bypass variants reveal a conformational control mechanism governing cell wall polymerase activity". Proceedings of the National Academy of Sciences 113, n.º 17 (11 de abril de 2016): 4788–93. http://dx.doi.org/10.1073/pnas.1524538113.
Texto completo da fonteRohs, Patricia D. A., Jackson Buss, Sue I. Sim, Georgia R. Squyres, Veerasak Srisuknimit, Mandy Smith, Hongbaek Cho et al. "A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery". PLOS Genetics 14, n.º 10 (18 de outubro de 2018): e1007726. http://dx.doi.org/10.1371/journal.pgen.1007726.
Texto completo da fonteCremniter, Julie, Jean-Luc Mainardi, Nathalie Josseaume, Jean-Charles Quincampoix, Lionel Dubost, Jean-Emmanuel Hugonnet, Arul Marie, Laurent Gutmann, Louis B. Rice e Michel Arthur. "Novel Mechanism of Resistance to Glycopeptide Antibiotics in Enterococcus faecium". Journal of Biological Chemistry 281, n.º 43 (29 de agosto de 2006): 32254–62. http://dx.doi.org/10.1074/jbc.m606920200.
Texto completo da fonteChang, Chungyu, Chenggang Wu, Jerzy Osipiuk, Sara D. Siegel, Shiwei Zhu, Xiangan Liu, Andrzej Joachimiak, Robert T. Clubb, Asis Das e Hung Ton-That. "Cell-to-cell interaction requires optimal positioning of a pilus tip adhesin modulated by gram-positive transpeptidase enzymes". Proceedings of the National Academy of Sciences 116, n.º 36 (19 de agosto de 2019): 18041–49. http://dx.doi.org/10.1073/pnas.1907733116.
Texto completo da fonteDi Guilmi, Anne Marie, Andréa Dessen, Otto Dideberg e Thierry Vernet. "The Glycosyltransferase Domain of Penicillin-Binding Protein 2a from Streptococcus pneumoniae Catalyzes the Polymerization of Murein Glycan Chains". Journal of Bacteriology 185, n.º 15 (1 de agosto de 2003): 4418–23. http://dx.doi.org/10.1128/jb.185.15.4418-4423.2003.
Texto completo da fonteMarmont, Lindsey S., e Thomas G. Bernhardt. "A conserved subcomplex within the bacterial cytokinetic ring activates cell wall synthesis by the FtsW-FtsI synthase". Proceedings of the National Academy of Sciences 117, n.º 38 (9 de setembro de 2020): 23879–85. http://dx.doi.org/10.1073/pnas.2004598117.
Texto completo da fonteAllen, N. E., D. L. LeTourneau e J. N. Hobbs. "Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-D-alanine and D-alanyl-D-lactate residues." Antimicrobial Agents and Chemotherapy 41, n.º 1 (janeiro de 1997): 66–71. http://dx.doi.org/10.1128/aac.41.1.66.
Texto completo da fonteBoll, Joseph M., Alexander A. Crofts, Katharina Peters, Vincent Cattoir, Waldemar Vollmer, Bryan W. Davies e M. Stephen Trent. "A penicillin-binding protein inhibits selection of colistin-resistant, lipooligosaccharide-deficientAcinetobacter baumannii". Proceedings of the National Academy of Sciences 113, n.º 41 (28 de setembro de 2016): E6228—E6237. http://dx.doi.org/10.1073/pnas.1611594113.
Texto completo da fonteTerrak, Mohammed, e Martine Nguyen-Distèche. "Kinetic Characterization of the Monofunctional Glycosyltransferase from Staphylococcus aureus". Journal of Bacteriology 188, n.º 7 (1 de abril de 2006): 2528–32. http://dx.doi.org/10.1128/jb.188.7.2528-2532.2006.
Texto completo da fonteSteed, Molly E., Céline Vidaillac e Michael J. Rybak. "Evaluation of Telavancin Activity versus Daptomycin and Vancomycin against Daptomycin-Nonsusceptible Staphylococcus aureus in anIn VitroPharmacokinetic/Pharmacodynamic Model". Antimicrobial Agents and Chemotherapy 56, n.º 2 (28 de novembro de 2011): 955–59. http://dx.doi.org/10.1128/aac.05849-11.
Texto completo da fonteXayarath, Bobbi, e Janet Yother. "Mutations Blocking Side Chain Assembly, Polymerization, or Transport of a Wzy-Dependent Streptococcus pneumoniae Capsule Are Lethal in the Absence of Suppressor Mutations and Can Affect Polymer Transfer to the Cell Wall". Journal of Bacteriology 189, n.º 9 (23 de fevereiro de 2007): 3369–81. http://dx.doi.org/10.1128/jb.01938-06.
Texto completo da fonteVoedts, Henri, Sean P. Kennedy, Guennadi Sezonov, Michel Arthur e Jean-Emmanuel Hugonnet. "Genome-wide identification of genes required for alternative peptidoglycan cross-linking in Escherichia coli revealed unexpected impacts of β-lactams". Nature Communications 13, n.º 1 (27 de dezembro de 2022). http://dx.doi.org/10.1038/s41467-022-35528-3.
Texto completo da fonteAtze, Heiner, Yucheng Liang, Jean-Emmanuel Hugonnet, Arnaud Gutierrez, Filippo Rusconi e Michel Arthur. "Heavy isotope labeling and mass spectrometry reveal unexpected remodeling of bacterial cell wall expansion in response to drugs". eLife 11 (9 de junho de 2022). http://dx.doi.org/10.7554/elife.72863.
Texto completo da fonteSichel, Sophie R., Benjamin P. Bratton e Nina Reda Salama. "Distinct regions of H. pylori's bactofilin CcmA regulate protein-protein interactions to control helical cell shape". eLife 11 (8 de setembro de 2022). http://dx.doi.org/10.7554/elife.80111.
Texto completo da fonteGarde, Shambhavi, Pavan Kumar Chodisetti e Manjula Reddy. "Peptidoglycan: Structure, Synthesis, and Regulation". EcoSal Plus, 20 de janeiro de 2021. http://dx.doi.org/10.1128/ecosalplus.esp-0010-2020.
Texto completo da fonteShlosman, Irina, Elayne M. Fivenson, Morgan S. A. Gilman, Tyler A. Sisley, Suzanne Walker, Thomas G. Bernhardt, Andrew C. Kruse e Joseph J. Loparo. "Allosteric activation of cell wall synthesis during bacterial growth". Nature Communications 14, n.º 1 (10 de junho de 2023). http://dx.doi.org/10.1038/s41467-023-39037-9.
Texto completo da fonteNygaard, Rie, Chris L. B. Graham, Meagan Belcher Dufrisne, Jonathan D. Colburn, Joseph Pepe, Molly A. Hydorn, Silvia Corradi et al. "Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex". Nature Communications 14, n.º 1 (24 de agosto de 2023). http://dx.doi.org/10.1038/s41467-023-40483-8.
Texto completo da fonteLi, Franco K. K., Liam J. Worrall, Robert T. Gale, Eric D. Brown e Natalie C. J. Strynadka. "Cryo-EM analysis of S. aureus TarL, a polymerase in wall teichoic acid biogenesis central to virulence and antibiotic resistance". Science Advances 10, n.º 9 (março de 2024). http://dx.doi.org/10.1126/sciadv.adj3864.
Texto completo da fonteHugonnet, Jean-Emmanuel, Dominique Mengin-Lecreulx, Alejandro Monton, Tanneke den Blaauwen, Etienne Carbonnelle, Carole Veckerlé, Yves, V. Brun et al. "Factors essential for L,D-transpeptidase-mediated peptidoglycan cross-linking and β-lactam resistance in Escherichia coli". eLife 5 (21 de outubro de 2016). http://dx.doi.org/10.7554/elife.19469.
Texto completo da fonteTeh, Hui Wen, Marimuthu Citartan, Hazrina Yusof Hamdani, Mohamad Zaki Salleh, Lay Kek Teh, Mohd Nur Fakhruzzaman Noorizhab e Thean-Hock Tang. "Identification of potential mutations associated with multidrug resistance among isolates of Mycobacterium tuberculosis in Malaysia by in silico screening". Asia Pacific Journal of Molecular Biology and Biotechnology, 27 de dezembro de 2023, 49–58. http://dx.doi.org/10.35118/apjmbb.2023.031.4.06.
Texto completo da fonteSütterlin, Laetitia, Zainab Edoo, Jean-Emmanuel Hugonnet, Jean-Luc Mainardi e Michel Arthur. "Peptidoglycan Cross-Linking Activity of L,D-Transpeptidases from Clostridium difficile and Inactivation of These Enzymes by β-Lactams". Antimicrobial Agents and Chemotherapy 62, n.º 1 (23 de outubro de 2017). http://dx.doi.org/10.1128/aac.01607-17.
Texto completo da fonteStamsås, Gro Anita, Marine Restelli, Adrien Ducret, Céline Freton, Pierre Simon Garcia, Leiv Sigve Håvarstein, Daniel Straume, Christophe Grangeasse e Morten Kjos. "A CozE Homolog Contributes to Cell Size Homeostasis of Streptococcus pneumoniae". mBio 11, n.º 5 (27 de outubro de 2020). http://dx.doi.org/10.1128/mbio.02461-20.
Texto completo da fonteVélez, Marisela. "How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?" Frontiers in Microbiology 13 (3 de maio de 2022). http://dx.doi.org/10.3389/fmicb.2022.757711.
Texto completo da fonteMidonet, Caroline, Sean Bisset, Irina Shlosman, Felipe Cava, David Z. Rudner e Thomas G. Bernhardt. "MacP bypass variants of Streptococcus pneumoniae PBP2a suggest a conserved mechanism for the activation of bifunctional cell wall synthases". mBio, 17 de outubro de 2023. http://dx.doi.org/10.1128/mbio.02390-23.
Texto completo da fonteSacco, Emmanuelle, Mélanie Cortes, Nathalie Josseaume, Louis B. Rice, Jean-Luc Mainardi e Michel Arthur. "Serine/Threonine Protein Phosphatase-Mediated Control of the Peptidoglycan Cross-Linking l,d-Transpeptidase Pathway in Enterococcus faecium". mBio 5, n.º 4 (8 de julho de 2014). http://dx.doi.org/10.1128/mbio.01446-14.
Texto completo da fonteSadecki, Patric W., Alexander M. Justen, Jordan S. Ho e Laura L. Kiessling. "Regiospecificity of Galactan Polymerization by Divergent GlfT2 Orthologs". FASEB Journal 31, S1 (abril de 2017). http://dx.doi.org/10.1096/fasebj.31.1_supplement.951.2.
Texto completo da fonteMadeswaran, Arumugam, e Premavathi Gunasekaran Midhuna. "In Silico Evaluation Of Some Commercially Available Flavonoids As Galactofuranoyltransferase-2 Inhibitors In The Management Of Tuberculosis". Letters in Drug Design & Discovery 19 (2 de fevereiro de 2022). http://dx.doi.org/10.2174/1570180819666220202155320.
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