Zobrazeno 1 - 10
of 82
pro vyhledávání: '"Pseudopeptidoglycan"'
Autor:
Cécile Morlot, Yves V. Brun, J. Bonnet, Nathalie Campo, Thierry Vernet, Maxime Jacq, Michael S. VanNieuwenhze, Claire Durmort, Isabelle Mortier-Barrière, Christine Moriscot, Anne Marie Di Guilmi, Christopher Arthaud, Benoit Gallet
Publikováno v:
Molecular Microbiology. 106:832-846
Summary The peptidoglycan is a rigid matrix required to resist turgor pressure and to maintain the cellular shape. It is formed by linear glycan chains composed of N-acetylmuramic acid-(β-1,4)-N-acetylglucosamine (MurNAc-GlcNAc) disaccharides associ
Autor:
Ariam F. TecleMariam, Taylor C. Brown, Christian A. Peterson, Mary E. Snavely, Allison M. Blake, Sydney C. Schneider, Om P. Neelay, Jennifer A. Campbell, Matthew E. Cremeens
Publikováno v:
Journal of Molecular Structure. 1146:329-336
Traditional therapeutics are losing effectiveness as bacterial resistance increases, and antimicrobial peptides (AMPs) can serve as an alternative source for antimicrobial agents. Their mode of action is commonly hypothesized to involve pore formatio
d-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii
Autor:
In Geol Choi, Je Chul Lee, Kwon Joo Yeo, Saeyoung Lee, Woo Cheol Lee, Hye-Yeon Kim, Seung Il Kim, Eunha Hwang, Young Ho Jeon, Chaejoon Cheong, Jeong Soon Park
Publikováno v:
Process Biochemistry. 55:110-115
OmpA-like domain proteins bind to peptidoglycan by interacting with the d -amino acid moiety of meso -diaminopimelate in peptidoglycan, but it is still not clear how this domain recognizes the d -amino region of peptidoglycan. To study their d -stere
Publikováno v:
Chemistry (Weinh., Print) 24 (2018): 2533–+. doi:10.1002/chem.201702973
info:cnr-pdr/source/autori:Squeglia, Flavia; Ruggiero, Alessia; Berisio, Rita/titolo:Chemistry of Peptidoglycan in Mycobacterium tuberculosis Life Cycle: An off-the-wall Balance of Synthesis and Degradation/doi:10.1002%2Fchem.201702973/rivista:Chemistry (Weinh., Print)/anno:2018/pagina_da:2533/pagina_a:+/intervallo_pagine:2533–+/volume:24
info:cnr-pdr/source/autori:Squeglia, Flavia; Ruggiero, Alessia; Berisio, Rita/titolo:Chemistry of Peptidoglycan in Mycobacterium tuberculosis Life Cycle: An off-the-wall Balance of Synthesis and Degradation/doi:10.1002%2Fchem.201702973/rivista:Chemistry (Weinh., Print)/anno:2018/pagina_da:2533/pagina_a:+/intervallo_pagine:2533–+/volume:24
The cell wall envelope of mycobacteria is structurally distinct from that of both Gram-positive and Gram-negative bacteria. In Mycobacterium tuberculosis, this cell wall has unique structural features and plays a crucial role in drug resistance and m
Autor:
Waldemar Vollmer
Publikováno v:
Molecular Microbiology. 86:1031-1035
Summary Most bacteria surround their cytoplasmic membrane with a net-like, elastic heteropolymer, the peptidoglycan sacculus, to protect themselves from bursting due to the turgor and to maintain cell shape. It has been assumed that growing bacteria
Autor:
Xiaoxue Zhou, Lynette Cegelski
Publikováno v:
Biochemistry. 51:8143-8153
The bacterial cell wall is essential to cell survival and is a major target of antibiotics. The main component of the bacterial cell wall is peptidoglycan, a cage-like macromolecule that preserves cellular integrity and maintains cell shape. The inso
Autor:
Joris M. Van Herreweghe, Arnout Voet, Chris W. Michiels, Lise Vanderkelen, Seppe Leysen, Lien Callewaert
Publikováno v:
Trends in Microbiology. 20:501-510
Peptidoglycan is the major structural component of the bacterial cell wall. It provides resistance against turgor and its cleavage by hydrolases such as lysozymes results in bacteriolysis. Most, if not all, animals produce lysozymes as key effectors
Autor:
Dirk-Jan Scheffers, Menno B. Tol
Publikováno v:
PLoS Pathogens, Vol 11, Iss 12, p e1005213 (2015)
PLoS Pathogens, 11(12):e1005213. PUBLIC LIBRARY SCIENCE
PLoS Pathogens
PLoS Pathogens, 11(12):e1005213. PUBLIC LIBRARY SCIENCE
PLoS Pathogens
Nearly all bacteria contain a peptidoglycan cell wall. The peptidoglycan precursor molecule is LipidII, containing the basic peptidoglycan building block attached to a lipid. Although the suitability of LipidII as an antibacterial target has long bee
Autor:
Yumiko Takatsuka, Yoshifumi Itoh, Yoshiyuki Kamio, Seiji Kojima, Jun Kaneko, Kyong Cheol Ko, Naoki Abe
Publikováno v:
Journal of Bacteriology. 192:5953-5961
The peptidoglycan of Selenomonas ruminantium is covalently bound to cadaverine (PG-cadaverine), which likely plays a significant role in maintaining the integrity of the cell surface structure. The outer membrane of this bacterium contains a 45-kDa m
Autor:
Helena Veiga, Magda L. Atilano, James Yates, Sergio R. Filipe, Mariana G. Pinho, Patricia Reed, Pedro M. Pereira
Publikováno v:
Proceedings of the National Academy of Sciences. 107:18991-18996
The cell wall of Staphylococcus aureus is characterized by an extremely high degree of cross-linking within its peptidoglycan (PGN). Penicillin-binding protein 4 (PBP4) is required for the synthesis of this highly cross-linked peptidoglycan. We found