Literatura científica selecionada sobre o tema "Peptidoglycan metabolism"
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Artigos de revistas sobre o assunto "Peptidoglycan metabolism"
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 fonteTeses / dissertações sobre o assunto "Peptidoglycan metabolism"
Regulski, Krzysztof. "Influence of peptidoglycan metabolism on immunomodulatory properties of Lactobacillus casei". Thesis, Paris 11, 2012. http://www.theses.fr/2012PA112313.
Texto completo da fontePeptidoglycan (PG) is the major component of the Gram-positive bacteria cell wall. It ensures bacterial cell shape and integrity. PG or PG-derived fragments have been shown to stimulate the host innate immune system, through Nod-2 receptors. In this work, we studied the influence of PG metabolism on immunomodulatory properties of Lactobacillus casei BL23, mainly its ability to modulate the response of human dendritic cells (DCs).We have first characterized the main peptidoglycan hydrolases (PGHs) of L. casei BL23. In silico search revealed that L. casei BL23 has a rather complex PGH complement including thirteen predicted PGHs with various catalytic domains. Proteomic analysis of bacterial cell wall extracts revealed the expression of seven of them during bacterial growth. We characterized four of them in details. Lc-p75 is the major PGH with a γ-D-glutamyl-L-lysyl-endopeptidase specificity and is responsible for daughter cell separation. Lc-p75 associated to the cell wall localizes at the cell septa. It is also one of the major secreted proteins of L. casei found in culture supernatant. Besides, we showed that L. casei Lc-p75 is a glycosylated protein. Lc-p40 is a PGH with a CHAP-domain endowed with endopeptidase hydrolytic specificity toward peptidoglycan cross-bridges and appears to localize on lateral cell wall. Lc-p45 is a second γ-D-glutamyl-L-lysyl endopeptidase with a role in cell shape maintenance. We further demonstrated that two prophage endolysins Lc-Lys and Lc-Lys2, encoded in L. casei BL23 genome, share a common novel type peptidoglycan-binding domain that recognizes specifically D-Asn cross-bridge, present in L. casei BL23 peptidoglycan.Deletion of the two endopeptidases, Lc-75 and Lc-p45, resulted in a complete loss ofdisaccharide-dipeptide, which is a ligand of Nod-2 receptor, in the muropeptide structure of L. casei BL23, whereas deletion of Lc-p75 gene led only to a reduction of disaccharide dipeptide. The two PGH-mutants, obtained by deletion of Lc-p75 gene alone or both Lc-p75 and Lc-p45 endopeptidase genes were compared with wild type L. casei BL23 for their capacity to stimulate signaling pathways in vitro in DCs derived from human monocytes. As a consequence of DC activation by L. casei strains, four pro-inflammatory cytokines IL-6, IL-8, IL-12 and TNF-α were produced. The concentrations of secreted cytokines in response to the single Lc-p75 and Lc-p75/p45 double mutant were lower than those induced by wild type L. casei BL23.In conclusion, L. casei BL23 has a complex PGH complement. The PGHs described in this work present unique features and play important role in cell division and morphology of L. casei. Our results indicate that wild type L. casei and endopeptidase-negative mutants, which differ in their PGH content and in their PG structure, have distinct effects on human DCs, with a higher anti-inflammatory character of the endopeptidase-negative mutants
Veeraraghavan, Usha. "Molecular and biochemical characterisation of mycobacterial peptidoglycan biosynthesis and glycogen metabolism". Thesis, University of Birmingham, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.522053.
Texto completo da fonteBroughton, Sarah Louise. "Studies on the metabolism and O-acetylation of peptidoglycan in Proteus mirabilis". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ33213.pdf.
Texto completo da fonteCherier, Dimitri. "CARACTERISATION BIOCHIMIQUE ET STRUCTURALE DE BACTERIOCINES CIBLANT LE METABOLISME DU PEPTIDOGLYCANE BACTERIEN, ALTERNATIVE POTENTIELLE AUX ANTIBIOTIQUES". Thesis, Université Paris-Saclay (ComUE), 2017. http://www.theses.fr/2017SACLS529/document.
Texto completo da fonteThe misuse of antibiotics during the last decades led to the emergence of multidrug resistant pathogenic bacteria. This phenomenon constitutes a major public health issue. Given that urgency, the finding of new antibacterials in the short term is crucial.Colicins, due to their antimicrobials properties, constitute good candidates. They are protein toxins produced by E. coli to kill competitors belonging to the same or related species. In most cases, they exhibit their cytotoxic activity through an ionophoric or nucleasic activity. Among the twenty colicins known to date, colicin M (ColM) is the only one known to interfere with peptidoglycan biosynthesis. It develops its lethal activity in the E. coli periplasm, in three steps deeply linked to its structural organization in three domains. Once in the periplasm, ColM degrades the lipid II, i.e. the last precursor in the peptidoglycan biosynthesis pathway, in two products that cannot be reused, thereby leading to cell lysis. Several ColM homologues have been identified in other bacterial genera, such as Pseudomonas, Pectobacterium and Burkholderia, but no cross activity has been shown to date, explaining the narrow antibacterial spectrum displayed by the members of this new family of antibacterial enzymes.This work deals with the structural and biochemical study of ColM and some of its homologues. Structural studies on several variants of PaeM, the ColM homologue from P. aeruginosa, led to identify a conserved water molecule in the active site, probably playing a central role in the catalytic mechanism of this enzyme family. Moreover, expression of ColM homologues from Pseudomonas or Pectobacterium species directly in the E. coli periplasm showed that all these homologues were able to induce E. coli cell lysis, thus demonstrating the great potential of these bacteriocins as an alternative to antibiotics. Following these results, several chimera colicins were created between ColM and its homologues, which were shown to degrade lipid II in vitro and to induce E. coli cell lysis after their periplasmic expression, opening the way to future new therapeutic options
Waterworth, James Stephen. "Anaerobic biodegradation of Peptidoglycan and Chitin by freshwater and marine sediment bacteria". Thesis, Queen Mary, University of London, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.266849.
Texto completo da fonteLe, Roux Pierre. "Recherche d'inhibiteurs et d'antibacteriques peptidiques synthetiques, ayant pour cible le metabolisme du peptidoglycane bacterien". Paris 11, 1990. http://www.theses.fr/1990PA112114.
Texto completo da fonteDai, Dexi. "Five new genetic loci involved in cell wall peptidoglycan metabolism of Escherichia coli". Thesis, 1990. https://dspace.library.uvic.ca//handle/1828/9479.
Texto completo da fonteGraduate
Livros sobre o assunto "Peptidoglycan metabolism"
A, De pedro M., Höltje J. V. 1941-, Löffelhardt W e Federation of European Microbiological Societies., eds. Bacterial growth and lysis: Metabolism and structure of the bacterial sacculus. New York: Plenum Press, 1993.
Encontre o texto completo da fonteE, Vance Dennis, e Vance Jean E, eds. Biochemistry of lipids, lipoproteins, and membranes. Amsterdam: Elsevier, 1991.
Encontre o texto completo da fonteM.A. de Pedro (Editor), J. V. Höltje (Editor) e Wolfgang Löffelhardt (Editor), eds. Bacterial Growth & Lysis: Metabolism and Structure of the Bacterial Sacculus. Springer, 1993.
Encontre o texto completo da fonteCapítulos de livros sobre o assunto "Peptidoglycan metabolism"
van Heijenoort, Jean, Dominique Mengin-Lecreulx, Yveline van Heijenoort, Didier Blanot, Bernard Flouret, Catherine Michaud, Claudine Parquet, Flore Pratviel-Sosa, Manolo Gomez e Juan A. Ayala. "Variations in the Metabolism of Peptidoglycan Prior to Polymerization". In Bacterial Growth and Lysis, 127–38. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4757-9359-8_15.
Texto completo da fonteTomasić, J., Z. Valinger, I. Hrsak e B. Ladesić. "Metabolic Fate of Peptidoglycan Monomer from Brevibacterium divaricatum and Biological Activity of its Metabolites". In Biological Properties of Peptidoglycan, editado por Peter H. Seidl e Karl H. Schleifer, 203–8. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110874297-026.
Texto completo da fonteSeidl, P. H., e K. H. Schleifer. "SECRETION OF FRAGMENTS FROM BACTERIAL CELL WALL PEPTIDOGLYCAN". In Environmental Regulation of Microbial Metabolism, 443–50. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-12-428580-4.50050-2.
Texto completo da fonteBattistuzzi, Fabia U., e S. Blair Hedges. "Archaebacteria". In The Timetree of Life, 101–5. Oxford University PressOxford, 2009. http://dx.doi.org/10.1093/oso/9780199535033.003.0006.
Texto completo da fonteBHAGAVAN, N. V. "Carbohydrate Metabolism III: Glycoproteins, Glycolipids, GPI Anchors, Proteoglycans, and Peptidoglycans". In Medical Biochemistry, 307–30. Elsevier, 2002. http://dx.doi.org/10.1016/b978-012095440-7/50018-4.
Texto completo da fonte"Postbiotics: A comprehensive Review of Classification, Application and Health Benefits". In Prospective Research and Technological Advancements in Food and Health Sciences, 361–407. Skyfox Publishing Group, 2023. http://dx.doi.org/10.22573/spg.023.978-93-90357-07-9/13.
Texto completo da fonteEmmett, Stevan R., Nicola Hill e Federico Dajas-Bailador. "Infectious disease". In Clinical Pharmacology for Prescribing. Oxford University Press, 2019. http://dx.doi.org/10.1093/oso/9780199694938.003.0019.
Texto completo da fonteBakar, Elvan, Nebiye Pelin Türker e Zeynep Erim. "Biosynthesis and Function of Glycoconjugates". In Recent Progress in Pharmaceutical Nanobiotechnology: A Medical Perspective, 166–222. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815179422123080009.
Texto completo da fonte