Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE - Wikidata - awgldk - TriplyDB

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

http://www.wikidata.org/entity/Q24531258

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The Min system and other nucleoid-independent regulators of Z ring positioning Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation Complete Genome Sequence of the Genetically Tractable Hydrogenotrophic Methanogen Methanococcus maripaludis Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor Dynamic structures in Escherichia coli: spontaneous formation of MinE rings and MinD polar zones The bacterial cytoskeleton Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles Functional taxonomy of bacterial hyperstructures The ParA/MinD family puts things in their place Molecular Interactions of the Min Protein System Reproduce Spatiotemporal Patterning in Growing and Dividing Escherichia coli Cells Theoretical Prediction of Disrupted Min Oscillation in Flattened Escherichia coli.Membrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD.An Optimal Free Energy Dissipation Strategy of the MinCDE Oscillator in Regulating Symmetric Bacterial Cell Division Noise-induced Min phenotypes in E. coli.Streptococcus pyogenes pSM19035 requires dynamic assembly of ATP-bound ParA and ParB on parS DNA during plasmid segregation Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis Structure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localization Crystal structure of the N-terminal domain of MinC dimerized via domain swapping Spatial regulators for bacterial cell division self-organize into surface waves in vitro The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature Structural features of glycosyltransferases synthesizing major bilayer and nonbilayer-prone membrane lipids in Acholeplasma laidlawii and Streptococcus pneumoniae Mapping out Min protein patterns in fully confined fluidic chambers A multistranded polymer model explains MinDE dynamics in E. coli cell division.Critical waves and the length problem of biology.Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins.Changes in the Min oscillation pattern before and after cell birth Chromosome segregation by the Escherichia coli Min system.Asymmetric constriction of dividing Escherichia coli cells induced by expression of a fusion between two min proteins.Cytokinesis in bacteria A plant MinD homologue rescues Escherichia coli HL1 mutant (DeltaMinDE) in the absence of MinE Subcellular Min oscillations as a single-cell reporter of the action of polycations, protamine, and gentamicin on Escherichia coli Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction.A polymerization-depolymerization model that accurately generates the self-sustained oscillatory system involved in bacterial division site placement Mesoscale spatial patterning in the Escherichia coli Min system: reaction-diffusion versus mechanical communication.Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability

P2860

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P2860

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

http://www.wikidata.org/entity/Q24531258

description

2002 nî lūn-bûn

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2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2002 թվականի մայիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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type

label

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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prefLabel

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

@ast

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

@en

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

@en

P2093

Edward P Gogol

http://www.w3.org/2001/XMLSchema#string

Joe Lutkenhaus

http://www.w3.org/2001/XMLSchema#string

Zonglin Hu

http://www.w3.org/2001/XMLSchema#string

P2860

The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site

Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli

Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus.

Crystal structure of the bacterial cell division inhibitor MinC.

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis

Gonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction.

MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli

The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.

Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site.

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6761-6

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scholarly article

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963538

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10.1073/PNAS.102059099

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P433

10

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99

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2002-05-14T00:00:00Z

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11385625

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11983867

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124476

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