Artigos de revistas sobre o tema "Peptidoglycan metabolism"
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Garcia, Daniel L., e Joseph P. Dillard. "Mutations in ampG or ampD Affect Peptidoglycan Fragment Release from Neisseria gonorrhoeae". Journal of Bacteriology 190, n.º 11 (4 de abril de 2008): 3799–807. http://dx.doi.org/10.1128/jb.01194-07.
Texto completo da fonteStrating, Hendrik, Chris Vandenende e Anthony J. Clarke. "Changes in peptidoglycan structure and metabolism during differentiation ofProteus mirabilisinto swarmer cells". Canadian Journal of Microbiology 58, n.º 10 (outubro de 2012): 1183–94. http://dx.doi.org/10.1139/w2012-102.
Texto completo da fontePérez Medina, Krizia, e Joseph Dillard. "Antibiotic Targets in Gonococcal Cell Wall Metabolism". Antibiotics 7, n.º 3 (21 de julho de 2018): 64. http://dx.doi.org/10.3390/antibiotics7030064.
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 fonteDörries, Kirsten, Rabea Schlueter e Michael Lalk. "Impact of Antibiotics with Various Target Sites on the Metabolome of Staphylococcus aureus". Antimicrobial Agents and Chemotherapy 58, n.º 12 (15 de setembro de 2014): 7151–63. http://dx.doi.org/10.1128/aac.03104-14.
Texto completo da fonteFernández, Ana, Astrid Pérez, Juan A. Ayala, Susana Mallo, Soraya Rumbo-Feal, Maria Tomás, Margarita Poza e Germán Bou. "Expression of OXA-Type and SFO-1 β-Lactamases Induces Changes in Peptidoglycan Composition and Affects Bacterial Fitness". Antimicrobial Agents and Chemotherapy 56, n.º 4 (30 de janeiro de 2012): 1877–84. http://dx.doi.org/10.1128/aac.05402-11.
Texto completo da fonteMaitra, Arundhati, Tulika Munshi, Jess Healy, Liam T. Martin, Waldemar Vollmer, Nicholas H. Keep e Sanjib Bhakta. "Cell wall peptidoglycan in Mycobacterium tuberculosis: An Achilles’ heel for the TB-causing pathogen". FEMS Microbiology Reviews 43, n.º 5 (10 de junho de 2019): 548–75. http://dx.doi.org/10.1093/femsre/fuz016.
Texto completo da fonteChan, Jia Mun, e Joseph P. Dillard. "Neisseria gonorrhoeae Crippled Its Peptidoglycan Fragment Permease To Facilitate Toxic Peptidoglycan Monomer Release". Journal of Bacteriology 198, n.º 21 (22 de agosto de 2016): 3029–40. http://dx.doi.org/10.1128/jb.00437-16.
Texto completo da fonteRojony, Rajoana, Lia Danelishvili, Anaamika Campeau, Jacob M. Wozniak, David J. Gonzalez e Luiz E. Bermudez. "Exposure of Mycobacterium abscessus to Environmental Stress and Clinically Used Antibiotics Reveals Common Proteome Response among Pathogenic Mycobacteria". Microorganisms 8, n.º 5 (9 de maio de 2020): 698. http://dx.doi.org/10.3390/microorganisms8050698.
Texto completo da fontePAYIE, KENNETH G., HENRI STRATING e ANTHONY J. CLARKE. "The Role ofO-Acetylation in the Metabolism of Peptidoglycan inProvidencia stuartii". Microbial Drug Resistance 2, n.º 1 (janeiro de 1996): 135–40. http://dx.doi.org/10.1089/mdr.1996.2.135.
Texto completo da fonteKurek, Anna, Anna M. Grudniak, Magdalena Szwed, Anna Klicka, Lukasz Samluk, Krystyna I. Wolska, Wirginia Janiszowska e Magdalena Popowska. "Oleanolic acid and ursolic acid affect peptidoglycan metabolism in Listeria monocytogenes". Antonie van Leeuwenhoek 97, n.º 1 (6 de novembro de 2009): 61–68. http://dx.doi.org/10.1007/s10482-009-9388-6.
Texto completo da fonteBonis, Mathilde, Allison Williams, Stephanie Guadagnini, Catherine Werts e Ivo G. Boneca. "The Effect of Bulgecin A on Peptidoglycan Metabolism and Physiology ofHelicobacter pylori". Microbial Drug Resistance 18, n.º 3 (junho de 2012): 230–39. http://dx.doi.org/10.1089/mdr.2011.0231.
Texto completo da fonteRodionov, D. G., e E. E. Ishiguro. "Dependence of peptidoglycan metabolism on phospholipid synthesis during growth of Escherichia coli". Microbiology 142, n.º 10 (1 de outubro de 1996): 2871–77. http://dx.doi.org/10.1099/13500872-142-10-2871.
Texto completo da fonteMiao, Jiatong, Hanrui Liu, Yushan Qu, Weizhe Fu, Kangwei Qi, Shizhu Zang, Jiajia He, Shijia Zhao, Shixing Chen e Tao Jiang. "Effect of peptidoglycan amidase MSMEG_6281 on fatty acid metabolism in Mycobacterium smegmatis". Microbial Pathogenesis 140 (março de 2020): 103939. http://dx.doi.org/10.1016/j.micpath.2019.103939.
Texto completo da fonteHenze, U., T. Sidow, J. Wecke, H. Labischinski e B. Berger-Bächi. "Influence of femB on methicillin resistance and peptidoglycan metabolism in Staphylococcus aureus." Journal of Bacteriology 175, n.º 6 (1993): 1612–20. http://dx.doi.org/10.1128/jb.175.6.1612-1620.1993.
Texto completo da fonteGiefing-Kröll, Carmen, Kira E. Jelencsics, Siegfried Reipert e Eszter Nagy. "Absence of pneumococcal PcsB is associated with overexpression of LysM domain-containing proteins". Microbiology 157, n.º 7 (1 de julho de 2011): 1897–909. http://dx.doi.org/10.1099/mic.0.045211-0.
Texto completo da fonteAlvarez, Laura, Sara B. Hernandez e Felipe Cava. "Cell Wall Biology of Vibrio cholerae". Annual Review of Microbiology 75, n.º 1 (8 de outubro de 2021): 151–74. http://dx.doi.org/10.1146/annurev-micro-040621-122027.
Texto completo da fonteBæk, Kristoffer T., Angelika Gründling, René G. Mogensen, Louise Thøgersen, Andreas Petersen, Wilhelm Paulander e Dorte Frees. "β-Lactam Resistance in Methicillin-Resistant Staphylococcus aureus USA300 Is Increased by Inactivation of the ClpXP Protease". Antimicrobial Agents and Chemotherapy 58, n.º 8 (27 de maio de 2014): 4593–603. http://dx.doi.org/10.1128/aac.02802-14.
Texto completo da fonteRousseau, N., M. Dargis, P. Gourde, D. Beauchamp e F. Malouin. "Effect of beta-lactams on peptidoglycan metabolism of Haemophilus influenzae grown in animals." Antimicrobial Agents and Chemotherapy 36, n.º 10 (1 de outubro de 1992): 2147–55. http://dx.doi.org/10.1128/aac.36.10.2147.
Texto completo da fonteFujimoto, David F., e Kenneth W. Bayles. "Opposing Roles of the Staphylococcus aureus Virulence Regulators, Agr and Sar, in Triton X-100- and Penicillin-Induced Autolysis". Journal of Bacteriology 180, n.º 14 (15 de julho de 1998): 3724–26. http://dx.doi.org/10.1128/jb.180.14.3724-3726.1998.
Texto completo da fonteZhang, Xinshuai, Yao Ruan, Wukang Liu, Qian Chen, Lihong Gu e Ailing Guo. "Transcriptome Analysis of Gene Expression in Dermacoccus abyssi HZAU 226 under Lysozyme Stress". Microorganisms 8, n.º 5 (11 de maio de 2020): 707. http://dx.doi.org/10.3390/microorganisms8050707.
Texto completo da fonteLuan, Jun-Bo. "Insect Bacteriocytes: Adaptation, Development, and Evolution". Annual Review of Entomology 69, n.º 1 (25 de janeiro de 2024): 81–98. http://dx.doi.org/10.1146/annurev-ento-010323-124159.
Texto completo da fontede Oliveira, Amanda C. P., Rafael M. Ferreira, Maria Inês T. Ferro, Jesus A. Ferro, Caio Zamuner, Henrique Ferreira e Alessandro M. Varani. "XAC4296 Is a Multifunctional and Exclusive Xanthomonadaceae Gene Containing a Fusion of Lytic Transglycosylase and Epimerase Domains". Microorganisms 10, n.º 5 (11 de maio de 2022): 1008. http://dx.doi.org/10.3390/microorganisms10051008.
Texto completo da fonteMARKOWSKA, KATARZYNA, ANNA MARIA GRUDNIAK, BARBARA MILCZAREK e KRYSTYNA IZABELLA WOLSKA. "The Effect of Silver Nanoparticles on Listeria monocytogenes PCM2191 Peptidoglycan Metabolism and Cell Permeability". Polish Journal of Microbiology 67, n.º 3 (2018): 315–20. http://dx.doi.org/10.21307/pjm-2018-037.
Texto completo da fonteArthur, Michel, Florence Depardieu, Peter Reynolds e Patrice Courvalin. "Quantitative analysis of the metabolism of soluble cytoplasmic peptidoglycan precursors of glycopeptide‐resistant enterococci". Molecular Microbiology 21, n.º 1 (julho de 1996): 33–44. http://dx.doi.org/10.1046/j.1365-2958.1996.00617.x.
Texto completo da fonteHervé, Mireille, Audrey Boniface, Stanislav Gobec, Didier Blanot e Dominique Mengin-Lecreulx. "Biochemical Characterization and Physiological Properties of Escherichia coli UDP-N-Acetylmuramate:l-Alanyl-γ-d-Glutamyl-meso- Diaminopimelate Ligase". Journal of Bacteriology 189, n.º 11 (23 de março de 2007): 3987–95. http://dx.doi.org/10.1128/jb.00087-07.
Texto completo da fonteQuintanilla, Samantha Y., Neda Habibi Arejan, Parthvi B. Patel e Cara C. Boutte. "PlrA (MSMEG_5223) is an essential polar growth regulator in Mycobacterium smegmatis". PLOS ONE 18, n.º 1 (12 de janeiro de 2023): e0280336. http://dx.doi.org/10.1371/journal.pone.0280336.
Texto completo da fontePapadopoulos, Andrea Olga, Christopher Ealand, Bhavna Gowan Gordhan, Michael VanNieuwenhze e Bavesh Davandra Kana. "Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis". PLOS ONE 16, n.º 11 (16 de novembro de 2021): e0259181. http://dx.doi.org/10.1371/journal.pone.0259181.
Texto completo da fonteSieradzki, Krzysztof, e Alexander Tomasz. "Gradual Alterations in Cell Wall Structure and Metabolism in Vancomycin-Resistant Mutants ofStaphylococcus aureus". Journal of Bacteriology 181, n.º 24 (15 de dezembro de 1999): 7566–70. http://dx.doi.org/10.1128/jb.181.24.7566-7570.1999.
Texto completo da fonteOliveira, Amanda C. P., Rafael M. Ferreira, Maria Inês T. Ferro, Jesus A. Ferro, Mick Chandler e Alessandro M. Varani. "Transposons and pathogenicity inXanthomonas: acquisition of murein lytic transglycosylases by TnXax1enhancesXanthomonas citrisubsp.citri306 virulence and fitness". PeerJ 6 (19 de dezembro de 2018): e6111. http://dx.doi.org/10.7717/peerj.6111.
Texto completo da fonteDaugelavičius, Rimantas, Virginija Cvirkaitė, Aušra Gaidelytė, Elena Bakienė, Rasa Gabrėnaitė-Verkhovskaya e Dennis H. Bamford. "Penetration of Enveloped Double-Stranded RNA Bacteriophages φ13 and φ6 into Pseudomonas syringae Cells". Journal of Virology 79, n.º 8 (15 de abril de 2005): 5017–26. http://dx.doi.org/10.1128/jvi.79.8.5017-5026.2005.
Texto completo da fonteHeywood, Astra, e Iain L. Lamont. "Cell envelope proteases and peptidases of Pseudomonas aeruginosa: multiple roles, multiple mechanisms". FEMS Microbiology Reviews 44, n.º 6 (17 de agosto de 2020): 857–73. http://dx.doi.org/10.1093/femsre/fuaa036.
Texto completo da fonteDillard, Joseph P., e Kathleen T. Hackett. "Mutations Affecting Peptidoglycan Acetylation in Neisseria gonorrhoeae and Neisseria meningitidis". Infection and Immunity 73, n.º 9 (setembro de 2005): 5697–705. http://dx.doi.org/10.1128/iai.73.9.5697-5705.2005.
Texto completo da fonteAliev, R. B., N. V. Stryzhak, A. S. Shapovalova, S. I. Abuvatfa, O. S. Kunytska e P. G. Kovalenko. "CLINICAL SIGNIFICANCE OF THE INFLUENCE OF CELL WALL ANTIGENS OF STAPHYLOCOCCUS AUREUS ON PHAGOCYTIC CELLS OF THE PERIPHERAL BLOOD IN CHILDREN WITH PURULENT AND INFLAMMATORY DISEASES OF STAPHYLOCOCCAL ETIOLOGY". Medical and Ecological Problems 27, n.º 3-4 (31 de agosto de 2023): 13–16. http://dx.doi.org/10.31718/mep.2023.27.3-4.02.
Texto completo da fonteRajeeve, Karthika, Nadine Vollmuth, Sudha Janaki-Raman, Thomas F. Wulff, Apoorva Baluapuri, Francesca R. Dejure, Claudia Huber et al. "Reprogramming of host glutamine metabolism during Chlamydia trachomatis infection and its key role in peptidoglycan synthesis". Nature Microbiology 5, n.º 11 (3 de agosto de 2020): 1390–402. http://dx.doi.org/10.1038/s41564-020-0762-5.
Texto completo da fonteDE ROUBIN, M. R., D. MENGIN-LECREULX e J. VAN HEIJENOORT. "Peptidoglycan biosynthesis in Escherichia coli: variations in the metabolism of alanine and D-alanyl-D-alanine". Journal of General Microbiology 138, n.º 8 (1 de agosto de 1992): 1751–57. http://dx.doi.org/10.1099/00221287-138-8-1751.
Texto completo da fonteBancroft, Peter J., Obolbek Turapov, Heena Jagatia, Kristine B. Arnvig, Galina V. Mukamolova e Jeffrey Green. "Coupling of Peptidoglycan Synthesis to Central Metabolism in Mycobacteria: Post-transcriptional Control of CwlM by Aconitase". Cell Reports 32, n.º 13 (setembro de 2020): 108209. http://dx.doi.org/10.1016/j.celrep.2020.108209.
Texto completo da fonteBannikova, Svetlana, Tamara Khlebodarova, Asya Vasilieva, Irina Mescheryakova, Alla Bryanskaya, Elizaveta Shedko, Vasily Popik, Tatiana Goryachkovskaya e Sergey Peltek. "Specific Features of the Proteomic Response of Thermophilic Bacterium Geobacillus icigianus to Terahertz Irradiation". International Journal of Molecular Sciences 23, n.º 23 (2 de dezembro de 2022): 15216. http://dx.doi.org/10.3390/ijms232315216.
Texto completo da fontePavelić, K., R. J. Bernacki e S. Vuk-Pavlović. "Insulin-modulated interleukin-2 production by murine splenocytes and a T-cell hybridoma". Journal of Endocrinology 114, n.º 1 (julho de 1987): 89–94. http://dx.doi.org/10.1677/joe.0.1140089.
Texto completo da fonteChaput, Catherine, Chantal Ecobichon, Nadine Pouradier, Jean-Claude Rousselle, Abdelkader Namane e Ivo G. Boneca. "Role of theN-Acetylmuramoyl-l-Alanyl Amidase, AmiA, ofHelicobacter pyloriin Peptidoglycan Metabolism, Daughter Cell Separation, and Virulence". Microbial Drug Resistance 22, n.º 6 (setembro de 2016): 477–86. http://dx.doi.org/10.1089/mdr.2016.0070.
Texto completo da fontevan Heijenoort, Y., M. Gómez, M. Derrien, J. Ayala e J. van Heijenoort. "Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: possible roles of PBP 1b and PBP 3." Journal of Bacteriology 174, n.º 11 (1992): 3549–57. http://dx.doi.org/10.1128/jb.174.11.3549-3557.1992.
Texto completo da fonteMengin-Lecreulx, Dominique, e Bruno Lemaitre. "Structure and metabolism of peptidoglycan and molecular requirements allowing its detection by the Drosophila innate immune system". Journal of Endotoxin Research 11, n.º 2 (abril de 2005): 105–11. http://dx.doi.org/10.1177/09680519050110020601.
Texto completo da fonteBisicchia, Paola, Efthimia Lioliou, David Noone, Letal I. Salzberg, Eric Botella, Sebastian Hübner e Kevin M. Devine. "Peptidoglycan metabolism is controlled by the WalRK (YycFG) and PhoPR two-component systems in phosphate-limitedBacillus subtiliscells". Molecular Microbiology 75, n.º 4 (fevereiro de 2010): 972–89. http://dx.doi.org/10.1111/j.1365-2958.2009.07036.x.
Texto completo da fontede Sarrau, Benoît, Thierry Clavel, Isabelle Bornard e Christophe Nguyen-the. "Low temperatures and fermentative metabolism limit peptidoglycan digestion of Bacillus cereus. Impact on colony forming unit counts". Food Microbiology 33, n.º 2 (abril de 2013): 213–20. http://dx.doi.org/10.1016/j.fm.2012.09.019.
Texto completo da fonteValinger, Zdenka, Branko Ladešić, Ivo Hršak e Jelka Tomašić. "Relationship of metabolism and immunostimulating activity of peptidoglycan monomer in mice after three different routes of administration". International Journal of Immunopharmacology 9, n.º 3 (janeiro de 1987): 325–32. http://dx.doi.org/10.1016/0192-0561(87)90057-9.
Texto completo da fonteMiyamoto, Tetsuya, Masumi Katane, Yasuaki Saitoh, Masae Sekine e Hiroshi Homma. "Cystathionine β-lyase is involved in d-amino acid metabolism". Biochemical Journal 475, n.º 8 (23 de abril de 2018): 1397–410. http://dx.doi.org/10.1042/bcj20180039.
Texto completo da fonteBriers, Yves, Maarten Walmagh, Barbara Grymonprez, Manfred Biebl, Jean-Paul Pirnay, Valerie Defraine, Jan Michiels et al. "Art-175 Is a Highly Efficient Antibacterial against Multidrug-Resistant Strains and Persisters of Pseudomonas aeruginosa". Antimicrobial Agents and Chemotherapy 58, n.º 7 (21 de abril de 2014): 3774–84. http://dx.doi.org/10.1128/aac.02668-14.
Texto completo da fonteBarreteau, Hélène, Ahmed Bouhss, Martine Fourgeaud, Jean-Luc Mainardi, Thierry Touzé, Fabien Gérard, Didier Blanot, Michel Arthur e Dominique Mengin-Lecreulx. "Human- and Plant-Pathogenic Pseudomonas Species Produce Bacteriocins Exhibiting Colicin M-Like Hydrolase Activity towards Peptidoglycan Precursors". Journal of Bacteriology 191, n.º 11 (3 de abril de 2009): 3657–64. http://dx.doi.org/10.1128/jb.01824-08.
Texto completo da fonteMir, Mushtaq, Sladjana Prisic, Choong-Min Kang, Shichun Lun, Haidan Guo, Jeffrey P. Murry, Eric J. Rubin e Robert N. Husson. "Mycobacterial GenecuvAIs Required for Optimal Nutrient Utilization and Virulence". Infection and Immunity 82, n.º 10 (21 de julho de 2014): 4104–17. http://dx.doi.org/10.1128/iai.02207-14.
Texto completo da fonteKim, Jungman, Jae Ho Choi, Taehwan Oh, Byungjae Ahn e Tatsuya Unno. "Codium fragile Ameliorates High-Fat Diet-Induced Metabolism by Modulating the Gut Microbiota in Mice". Nutrients 12, n.º 6 (21 de junho de 2020): 1848. http://dx.doi.org/10.3390/nu12061848.
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