Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction.
about
Crystal Structures of Complexes of Bacterial dd-Peptidases with Peptidoglycan-Mimetic Ligands: The Substrate Specificity PuzzleA new family of cyanobacterial penicillin-binding proteins. A missing link in the evolution of class A beta-lactamases.Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment.Flk prevents premature secretion of the anti-sigma factor FlgM into the periplasm.Bacterial peptidoglycan (murein) hydrolases.New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysisEchoLOCATION: an in silico analysis of the subcellular locations of Escherichia coli proteins and comparison with experimentally derived locations.Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.
P2860
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P2860
Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction.
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name
Investigations into the mechan ...... d 6b for membrane interaction.
@en
Investigations into the mechan ...... d 6b for membrane interaction.
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Investigations into the mechan ...... d 6b for membrane interaction.
@en
Investigations into the mechan ...... d 6b for membrane interaction.
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Investigations into the mechan ...... d 6b for membrane interaction.
@en
Investigations into the mechan ...... d 6b for membrane interaction.
@nl
P2093
P2860
P1433
P1476
Investigations into the mechan ...... d 6b for membrane interaction.
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P2093
David Phoenix
Frederick Harris
Ulrich Seydel
P2860
P304
P356
10.1046/J.1432-1033.2002.03295.X
P407
P577
2002-12-01T00:00:00Z