Imaging-based identification of a critical regulator of FtsZ protofilament curvature in Caulobacter.
about
A growing family: the expanding universe of the bacterial cytoskeletonBacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular FunctionsBacterial actin and tubulin homologs in cell growth and divisionThe bacterial divisome: ready for its close-upA New Essential Cell Division Protein in Caulobacter crescentus.Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersA Caulobacter MreB mutant with irregular cell shape exhibits compensatory widening to maintain a preferred surface area to volume ratio.Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.A NAD-dependent glutamate dehydrogenase coordinates metabolism with cell division in Caulobacter crescentus.Characterization of Caulobacter crescentus FtsZ protein using dynamic light scatteringStructural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in Caulobacter crescentus.Rapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.Prokaryotic cytokinesis: little rings bring big cylindrical things.Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.Shapeshifting to Survive: Shape Determination and Regulation in Caulobacter crescentus.Assembly of the Caulobacter cell division machine.Erin Goley: Catching the bug for studying the cytoskeleton.The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct robust cell wall construction.Bacterial cytokinesis: FzlA frizzes FtsZ filaments for fission force.ZipA and FtsA* stabilize FtsZ-GDP miniring structures.PomZ, a ParA-like protein, regulates Z-ring formation and cell division in Myxococcus xanthus.FtsZ Constriction Force - Curved Protofilaments Bending Membranes.Cytoskeletal Proteins in Caulobacter crescentus: Spatial Orchestrators of Cell Cycle Progression, Development, and Cell Shape.FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division.The intrinsically disordered C-terminal linker of FtsZ regulates protofilament dynamics and superstructure in vitro.A conserved coiled-coil protein pair focuses the cytokinetic Z-ring in Caulobacter crescentus.Beyond force generation: Why is a dynamic ring of FtsZ polymers essential for bacterial cytokinesis?Multiple effects of benzamide antibiotics on FtsZ function.
P2860
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P2860
Imaging-based identification of a critical regulator of FtsZ protofilament curvature in Caulobacter.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Imaging-based identification o ...... ment curvature in Caulobacter.
@ast
Imaging-based identification o ...... ment curvature in Caulobacter.
@en
Imaging-based identification o ...... ment curvature in Caulobacter.
@nl
type
label
Imaging-based identification o ...... ment curvature in Caulobacter.
@ast
Imaging-based identification o ...... ment curvature in Caulobacter.
@en
Imaging-based identification o ...... ment curvature in Caulobacter.
@nl
prefLabel
Imaging-based identification o ...... ment curvature in Caulobacter.
@ast
Imaging-based identification o ...... ment curvature in Caulobacter.
@en
Imaging-based identification o ...... ment curvature in Caulobacter.
@nl
P2093
P2860
P1433
P1476
Imaging-based identification o ...... ament curvature in Caulobacter
@en
P2093
John N Werner
Lucy Shapiro
Natalie A Dye
Zemer Gitai
P2860
P304
P356
10.1016/J.MOLCEL.2010.08.027
P50
P577
2010-09-01T00:00:00Z