The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli. - Wikidata - wikimedia - TriplyDB

The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli.

The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli.

http://www.wikidata.org/entity/Q53521792

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Activities and regulation of peptidoglycan synthases Molecular mechanisms for the evolution of bacterial morphologies and growth modes Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.Structural Insights into the Lipoprotein Outer Membrane Regulator of Penicillin-binding Protein 1B Outer-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1B Crystal Structure of Penicillin-Binding Protein 3 (PBP3) from Escherichia coli The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain Cell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJ Artificial septal targeting of Bacillus subtilis cell division proteins in Escherichia coli: an interspecies approach to the study of protein-protein interactions in multiprotein complexes A New Essential Cell Division Protein in Caulobacter crescentus.Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli.Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA Interaction and modulation of two antagonistic cell wall enzymes of mycobacteria.From the regulation of peptidoglycan synthesis to bacterial growth and morphology.Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases.A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators.A DNA damage-induced, SOS-independent checkpoint regulates cell division in Caulobacter crescentus.PBP1a/LpoA but not PBP1b/LpoB are involved in regulation of the major β-lactamase gene blaA in Shewanella oneidensis.Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN.Forming cross-linked peptidoglycan from synthetic gram-negative Lipid II Cofactor bypass variants reveal a conformational control mechanism governing cell wall polymerase activity.The Redundancy of Peptidoglycan Carboxypeptidases Ensures Robust Cell Shape Maintenance in Escherichia coli Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN Function and localization dynamics of bifunctional penicillin-binding proteins in Caulobacter crescentus.Advances in understanding E. coli cell fission.The physiology of bacterial cell division.From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?Penicillin-binding protein 5 can form a homo-oligomeric complex in the inner membrane of Escherichia coli.Determinants of Bacterial Morphology: From Fundamentals to Possibilities for Antimicrobial Targeting.The stoichiometric divisome: a hypothesis.PBP1B Glycosyltransferase and Transpeptidase Activities Play Different Essential Roles during the De Novo Regeneration of Rod Morphology in Escherichia coli.Subunit Arrangement in GpsB, a Regulator of Cell Wall Biosynthesis.An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: mutational analysis of Thr338.Importance of the conserved residues in the peptidoglycan glycosyltransferase module of the class A penicillin-binding protein 1b of Escherichia coli.A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.Interplay between Penicillin-binding proteins and SEDS proteins promotes bacterial cell wall synthesis

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The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli.

http://www.wikidata.org/entity/Q53521792

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2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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The essential cell division pr ...... ase PBP1B in Escherichia coli.

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The essential cell division protein FtsN interacts with the murein

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The essential cell division pr ...... ase PBP1B in Escherichia coli.

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The essential cell division protein FtsN interacts with the murein

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The essential cell division pr ...... ase PBP1B in Escherichia coli.

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The essential cell division protein FtsN interacts with the murein

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Journal of Biological Chemistry

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The essential cell division pr ...... ase PBP1B in Escherichia coli.

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Carolin Ewers

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Claudine Fraipont

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Maria Anstett

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Martine Nguyen-Distèche

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Mohammed Terrak

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Patrick Müller

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Tanja Kallis

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Ute Bertsche

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P2860

Analysis of gene control signals by DNA fusion and cloning in Escherichia coli

Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold.

Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli.

Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell.

Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli.

Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis.

On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins.

The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site.

Penicillin-binding proteins 1a and 1b form independent dimers in Escherichia coli.

Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN.

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10.1074/JBC.M706390200

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50

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282

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Martine Nguyen-Distèche

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Waldemar Vollmer

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2007-10-15T00:00:00Z

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17938168

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