Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli.
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Evolution of penicillin-binding protein 2 concentration and cell shape during a long-term experiment with Escherichia coliThe selective value of bacterial shapeBacterial wall as target for attack: past, present, and future researchAsymmetry of chromosome Replichores renders the DNA translocase activity of FtsK essential for cell division and cell shape maintenance in Escherichia coliThe crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding proteinCrystal structure of the 47-kDa lipoprotein of Treponema pallidum reveals a novel penicillin-binding proteinCrystal Structures of Penicillin-Binding Protein 6 from Escherichia coliInteraction of penicillin-binding protein 2 with soluble lytic transglycosylase B1 in Pseudomonas aeruginosaContribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli.The Rcs stress response and accessory envelope proteins are required for de novo generation of cell shape in Escherichia coli.Comparison of high-performance liquid chromatography and fluorophore-assisted carbohydrate electrophoresis methods for analyzing peptidoglycan composition of Escherichia coliElucidation of the structure of the membrane anchor of penicillin-binding protein 5 of Escherichia coliSeptal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment.Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli.Bacterial cell wall synthesis: new insights from localization studiesSynthesis and assembly of a novel glycan layer in Myxococcus xanthus sporesBranching of Escherichia coli cells arises from multiple sites of inert peptidoglycanThe putative hydrolase YycJ (WalJ) affects the coordination of cell division with DNA replication in Bacillus subtilis and may play a conserved role in cell wall metabolism.Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli.Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coliBranching sites and morphological abnormalities behave as ectopic poles in shape-defective Escherichia coliIsolation and characterization of mini-Tn5Km2 insertion mutants of Brucella abortus deficient in internalization and intracellular growth in HeLa cells.The requirement for pneumococcal MreC and MreD is relieved by inactivation of the gene encoding PBP1a.Mechanism for the antibacterial action of epigallocatechin gallate (EGCg) on Bacillus subtilis.Peptidoglycan hydrolases of Escherichia coli.Escherichia coli low-molecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching.A D, D-carboxypeptidase is required for Vibrio cholerae halotolerance.Shapes that Escherichia coli cells can achieve, as a paradigm for other bacteria.The Min system as a general cell geometry detection mechanism: branch lengths in Y-shaped Escherichia coli cells affect Min oscillation patterns and division dynamicsLoss of O-antigen increases cell shape abnormalities in penicillin-binding protein mutants of Escherichia coli.The Redundancy of Peptidoglycan Carboxypeptidases Ensures Robust Cell Shape Maintenance in Escherichia coliBacterial peptidoglycan (murein) hydrolases.Eliminating a set of four penicillin binding proteins triggers the Rcs phosphorelay and Cpx stress responses in Escherichia coli.Spore formation in Myxococcus xanthus is tied to cytoskeleton functions and polysaccharide spore coat deposition.Association of a D-alanyl-D-alanine carboxypeptidase gene with the formation of aberrantly shaped cells during the induction of viable but nonculturable Vibrio parahaemolyticus.FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli.Endopeptidase penicillin-binding proteins 4 and 7 play auxiliary roles in determining uniform morphology of Escherichia coliMechanisms of β-lactam killing and resistance in the context of Mycobacterium tuberculosis.Crystallization and preliminary X-ray crystallographic analysis of PBPD2 from Listeria monocytogenes.
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P2860
Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Contributions of PBP 5 and DD- ...... ell shape in Escherichia coli.
@ast
Contributions of PBP 5 and DD- ...... ell shape in Escherichia coli.
@en
type
label
Contributions of PBP 5 and DD- ...... ell shape in Escherichia coli.
@ast
Contributions of PBP 5 and DD- ...... ell shape in Escherichia coli.
@en
prefLabel
Contributions of PBP 5 and DD- ...... ell shape in Escherichia coli.
@ast
Contributions of PBP 5 and DD- ...... ell shape in Escherichia coli.
@en
P2860
P1476
Contributions of PBP 5 and DD- ...... cell shape in Escherichia coli
@en
P2093
D E Nelson
P2860
P304
P356
10.1128/JB.183.10.3055-3064.2001
P407
P577
2001-05-01T00:00:00Z