Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE. - Test2 - elhamkhani - TriplyDB

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

http://www.wikidata.org/entity/Q34429840

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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 Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor 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 Collaborative protein filaments A growing family: the expanding universe of the bacterial cytoskeleton Molecular Interactions of the Min Protein System Reproduce Spatiotemporal Patterning in Growing and Dividing Escherichia coli Cells FtsZ placement in nucleoid-free bacteria 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 The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature Cardiolipin domains in Bacillus subtilis marburg membranes A multistranded polymer model explains MinDE dynamics in E. coli cell division.Eicosapentaenoic acid plays a beneficial role in membrane organization and cell division of a cold-adapted bacterium, Shewanella livingstonensis Ac10.Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins.Changes in the Min oscillation pattern before and after cell birth A man-made ATP-binding protein evolved independent of nature causes abnormal growth in bacterial cells RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton 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.Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC 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 Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli ATP control of dynamic P1 ParA-DNA interactions: a key role for the nucleoid in plasmid partition Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli.Division accuracy in a stochastic model of Min oscillations in Escherichia coli.FtsZ and the division of prokaryotic cells and organelles.Role of MinD-membrane association in Min protein interactions Bacterial cell division spirals into control Membrane binding by MinD involves insertion of hydrophobic residues within the C-terminal amphipathic helix into the bilayer.The tail of the ParG DNA segregation protein remodels ParF polymers and enhances ATP hydrolysis via an arginine finger-like motif.A mechanical explanation for cytoskeletal rings and helices in bacteria.The switch I and II regions of MinD are required for binding and activating MinC.Soj (ParA) DNA binding is mediated by conserved arginines and is essential for plasmid segregation.

P2860

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P2860

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

http://www.wikidata.org/entity/Q34429840

description

2002 nî lūn-bûn

@nan

2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի դեկտեմբերին 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

@wuu

name

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@ast

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@en

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@nl

type

label

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@ast

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@en

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@nl

prefLabel

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@ast

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@en

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@nl

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P1433

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

P1476

Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE.

@en

P2093

Debabrata RayChaudhuri

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

Kyoko Suefuji

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

Regina Valluzzi

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

P2860

Cloning of a human cDNA encoding a putative nucleotide-binding protein related to Escherichia coli MinD

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

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 basis for the topological specificity function of MinE

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

NBP35 encodes an essential and evolutionary conserved protein in Saccharomyces cerevisiae with homology to a superfamily of bacterial ATPases.

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

Bacterial cell division.

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

P304

16776-16781

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scholarly article

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10.1073/PNAS.262671699

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P407

P433

26

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P478

99

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2002-12-13T00:00:00Z

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10990103

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12482939

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139220

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