Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function.
about
FtsA forms actin-like protofilaments.FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN.Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli.Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA.A mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundlingDetermination of bacterial rod shape by a novel cytoskeletal membrane protein.Dimer dynamics and filament organization of the bacterial cell division protein FtsATargeting FtsZ for antibacterial therapy: a promising avenue.Advances in understanding E. coli cell fission.Comparing contractile apparatus-driven cytokinesis mechanisms across kingdoms.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.FtsZ-ring Architecture and Its Control by MinCD.Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments.Roles of the essential protein FtsA in cell growth and division in Streptococcus pneumoniae.Validation of FRET Assay for the Screening of Growth Inhibitors of Escherichia coli Reveals Elongasome Assembly Dynamics.A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli.Key role of two terminal domains in the bidirectional polymerization of FtsA protein.Role of the FtsA C terminus as a switch for polymerization and membrane association.FtsA reshapes membrane architecture and remodels the Z-ring in Escherichia coli.
P2860
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P2860
Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function.
description
2008 nî lūn-bûn
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2008年の論文
@ja
2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
@zh-my
2008年学术文章
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2008年學術文章
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2008年學術文章
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2008年學術文章
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name
Compensation for the loss of t ...... ew insights into its function.
@ast
Compensation for the loss of t ...... ew insights into its function.
@en
type
label
Compensation for the loss of t ...... ew insights into its function.
@ast
Compensation for the loss of t ...... ew insights into its function.
@en
prefLabel
Compensation for the loss of t ...... ew insights into its function.
@ast
Compensation for the loss of t ...... ew insights into its function.
@en
P2860
P1476
Compensation for the loss of t ...... new insights into its function
@en
P2093
William Margolin
P2860
P304
P356
10.1111/J.1365-2958.2007.06085.X
P407
P577
2008-02-01T00:00:00Z