Artículos de revistas sobre el tema "Peptidoglycan polymerization"
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Arthur, Michel. "Regulation of Bacterial Peptidoglycan Polymerization". Trends in Microbiology 24, n.º 7 (julio de 2016): 519–21. http://dx.doi.org/10.1016/j.tim.2016.05.003.
Texto completoVasudevan, Pradeep, Jessica McElligott, Christa Attkisson, Michael Betteken y 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 julio de 2009): 6012–19. http://dx.doi.org/10.1128/jb.00604-09.
Texto completoChan, Yvonne G. Y., Matthew B. Frankel, Dominique Missiakas y 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 enero de 2016): 1123–36. http://dx.doi.org/10.1128/jb.00983-15.
Texto completoZuber, Benoît, Marisa Haenni, Tânia Ribeiro, Kathrin Minnig, Fátima Lopes, Philippe Moreillon y 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 septiembre de 2006): 6652–60. http://dx.doi.org/10.1128/jb.00391-06.
Texto completoRuiz, 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 octubre de 2008): 15553–57. http://dx.doi.org/10.1073/pnas.0808352105.
Texto completoYagi, Tetsuya, Sebabrata Mahapatra, Katarína Mikušová, Dean C. Crick y 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 completoArbeloa, Ana, Heidi Segal, Jean-Emmanuel Hugonnet, Nathalie Josseaume, Lionnel Dubost, Jean-Paul Brouard, Laurent Gutmann, Dominique Mengin-Lecreulx y 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 marzo de 2004): 1221–28. http://dx.doi.org/10.1128/jb.186.5.1221-1228.2004.
Texto completoRice, Louis B., Lenore L. Carias, Susan Rudin, Rebecca Hutton, Steven Marshall, Medhat Hassan, Nathalie Josseaume, Lionel Dubost, Arul Marie y 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 marzo de 2009): 3649–56. http://dx.doi.org/10.1128/jb.01834-08.
Texto completoAllen, N. E., J. N. Hobbs y 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 (octubre de 1996): 2356–62. http://dx.doi.org/10.1128/aac.40.10.2356.
Texto completoBraddick, Darren, Sandeep Sandhu, David I. Roper, Michael J. Chappell y 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 completoZheng, Sanduo, Lok-To Sham, Frederick A. Rubino, Kelly P. Brock, William P. Robins, John J. Mekalanos, Debora S. Marks, Thomas G. Bernhardt y 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 junio de 2018): 6709–14. http://dx.doi.org/10.1073/pnas.1802192115.
Texto completoYunck, Rachel, Hongbaek Cho y Thomas G. Bernhardt. "Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria". Molecular Microbiology 99, n.º 4 (19 de noviembre de 2015): 700–718. http://dx.doi.org/10.1111/mmi.13258.
Texto completovan Heijenoort, Jean. "Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan". Microbiology and Molecular Biology Reviews 71, n.º 4 (diciembre de 2007): 620–35. http://dx.doi.org/10.1128/mmbr.00016-07.
Texto completoAli 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 completoSjodt, 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 marzo de 2020): 813–20. http://dx.doi.org/10.1038/s41564-020-0687-z.
Texto completoPlocinski, 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 completoPunekar, Avinash S., Firdaus Samsudin, Adrian J. Lloyd, Christopher G. Dowson, David J. Scott, Syma Khalid y David I. Roper. "The role of the jaw subdomain of peptidoglycan glycosyltransferases for lipid II polymerization". Cell Surface 2 (junio de 2018): 54–66. http://dx.doi.org/10.1016/j.tcsw.2018.06.002.
Texto completoPerlstein, Deborah L., Tsung-Shing Andrew Wang, Emma H. Doud, Daniel Kahne y 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 enero de 2010): 48–49. http://dx.doi.org/10.1021/ja909325m.
Texto completoZawadzka-Skomiał, Joanna, Zdzislaw Markiewicz, Martine Nguyen-Distèche, Bart Devreese, Jean-Marie Frère y Mohammed Terrak. "Characterization of the Bifunctional Glycosyltransferase/Acyltransferase Penicillin-Binding Protein 4 of Listeria monocytogenes". Journal of Bacteriology 188, n.º 5 (1 de marzo de 2006): 1875–81. http://dx.doi.org/10.1128/jb.188.5.1875-1881.2006.
Texto completoQiao, Lei y 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 (junio de 1993): 3480–82. http://dx.doi.org/10.1021/jo00065a004.
Texto completoSchaefer, Kaitlin, Tristan W. Owens, Julia E. Page, Marina Santiago, Daniel Kahne y 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 noviembre de 2020): 34–43. http://dx.doi.org/10.1038/s41564-020-00808-5.
Texto completoVarma, Archana, Miguel A. de Pedro y Kevin D. Young. "FtsZ Directs a Second Mode of Peptidoglycan Synthesis in Escherichia coli". Journal of Bacteriology 189, n.º 15 (18 de mayo de 2007): 5692–704. http://dx.doi.org/10.1128/jb.00455-07.
Texto completoHamilton, Andrea, David L. Popham, David J. Carl, Xavier Lauth, Victor Nizet y Amanda L. Jones. "Penicillin-Binding Protein 1a Promotes Resistance of Group B Streptococcus to Antimicrobial Peptides". Infection and Immunity 74, n.º 11 (noviembre de 2006): 6179–87. http://dx.doi.org/10.1128/iai.00895-06.
Texto completoMarkovski, Monica, Jessica L. Bohrhunter, Tania J. Lupoli, Tsuyoshi Uehara, Suzanne Walker, Daniel E. Kahne y 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 completoRohs, 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 octubre de 2018): e1007726. http://dx.doi.org/10.1371/journal.pgen.1007726.
Texto completoCremniter, Julie, Jean-Luc Mainardi, Nathalie Josseaume, Jean-Charles Quincampoix, Lionel Dubost, Jean-Emmanuel Hugonnet, Arul Marie, Laurent Gutmann, Louis B. Rice y 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 completoChang, Chungyu, Chenggang Wu, Jerzy Osipiuk, Sara D. Siegel, Shiwei Zhu, Xiangan Liu, Andrzej Joachimiak, Robert T. Clubb, Asis Das y 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 completoDi Guilmi, Anne Marie, Andréa Dessen, Otto Dideberg y 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 completoMarmont, Lindsey S. y 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 septiembre de 2020): 23879–85. http://dx.doi.org/10.1073/pnas.2004598117.
Texto completoAllen, N. E., D. L. LeTourneau y 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 (enero de 1997): 66–71. http://dx.doi.org/10.1128/aac.41.1.66.
Texto completoBoll, Joseph M., Alexander A. Crofts, Katharina Peters, Vincent Cattoir, Waldemar Vollmer, Bryan W. Davies y 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 septiembre de 2016): E6228—E6237. http://dx.doi.org/10.1073/pnas.1611594113.
Texto completoTerrak, Mohammed y 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 completoSteed, Molly E., Céline Vidaillac y 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 noviembre de 2011): 955–59. http://dx.doi.org/10.1128/aac.05849-11.
Texto completoXayarath, Bobbi y 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 febrero de 2007): 3369–81. http://dx.doi.org/10.1128/jb.01938-06.
Texto completoVoedts, Henri, Sean P. Kennedy, Guennadi Sezonov, Michel Arthur y 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 diciembre de 2022). http://dx.doi.org/10.1038/s41467-022-35528-3.
Texto completoAtze, Heiner, Yucheng Liang, Jean-Emmanuel Hugonnet, Arnaud Gutierrez, Filippo Rusconi y Michel Arthur. "Heavy isotope labeling and mass spectrometry reveal unexpected remodeling of bacterial cell wall expansion in response to drugs". eLife 11 (9 de junio de 2022). http://dx.doi.org/10.7554/elife.72863.
Texto completoSichel, Sophie R., Benjamin P. Bratton y Nina Reda Salama. "Distinct regions of H. pylori's bactofilin CcmA regulate protein-protein interactions to control helical cell shape". eLife 11 (8 de septiembre de 2022). http://dx.doi.org/10.7554/elife.80111.
Texto completoGarde, Shambhavi, Pavan Kumar Chodisetti y Manjula Reddy. "Peptidoglycan: Structure, Synthesis, and Regulation". EcoSal Plus, 20 de enero de 2021. http://dx.doi.org/10.1128/ecosalplus.esp-0010-2020.
Texto completoShlosman, Irina, Elayne M. Fivenson, Morgan S. A. Gilman, Tyler A. Sisley, Suzanne Walker, Thomas G. Bernhardt, Andrew C. Kruse y Joseph J. Loparo. "Allosteric activation of cell wall synthesis during bacterial growth". Nature Communications 14, n.º 1 (10 de junio de 2023). http://dx.doi.org/10.1038/s41467-023-39037-9.
Texto completoNygaard, 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 completoLi, Franco K. K., Liam J. Worrall, Robert T. Gale, Eric D. Brown y 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 (marzo de 2024). http://dx.doi.org/10.1126/sciadv.adj3864.
Texto completoHugonnet, 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 octubre de 2016). http://dx.doi.org/10.7554/elife.19469.
Texto completoTeh, Hui Wen, Marimuthu Citartan, Hazrina Yusof Hamdani, Mohamad Zaki Salleh, Lay Kek Teh, Mohd Nur Fakhruzzaman Noorizhab y 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 diciembre de 2023, 49–58. http://dx.doi.org/10.35118/apjmbb.2023.031.4.06.
Texto completoSütterlin, Laetitia, Zainab Edoo, Jean-Emmanuel Hugonnet, Jean-Luc Mainardi y 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 octubre de 2017). http://dx.doi.org/10.1128/aac.01607-17.
Texto completoStamsås, Gro Anita, Marine Restelli, Adrien Ducret, Céline Freton, Pierre Simon Garcia, Leiv Sigve Håvarstein, Daniel Straume, Christophe Grangeasse y Morten Kjos. "A CozE Homolog Contributes to Cell Size Homeostasis of Streptococcus pneumoniae". mBio 11, n.º 5 (27 de octubre de 2020). http://dx.doi.org/10.1128/mbio.02461-20.
Texto completoVélez, Marisela. "How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?" Frontiers in Microbiology 13 (3 de mayo de 2022). http://dx.doi.org/10.3389/fmicb.2022.757711.
Texto completoMidonet, Caroline, Sean Bisset, Irina Shlosman, Felipe Cava, David Z. Rudner y 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 octubre de 2023. http://dx.doi.org/10.1128/mbio.02390-23.
Texto completoSacco, Emmanuelle, Mélanie Cortes, Nathalie Josseaume, Louis B. Rice, Jean-Luc Mainardi y 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 julio de 2014). http://dx.doi.org/10.1128/mbio.01446-14.
Texto completoSadecki, Patric W., Alexander M. Justen, Jordan S. Ho y 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 completoMadeswaran, Arumugam y 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 febrero de 2022). http://dx.doi.org/10.2174/1570180819666220202155320.
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