The MinD membrane targeting sequence is a transplantable lipid-binding helix. - Wikidata - wikimedia - TriplyDB

The MinD membrane targeting sequence is a transplantable lipid-binding helix.

The MinD membrane targeting sequence is a transplantable lipid-binding helix.

http://www.wikidata.org/entity/Q44527107

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Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation Discovery of a selective NaV1.7 inhibitor from centipede venom with analgesic efficacy exceeding morphine in rodent pain models.The bacterial cytoskeleton The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site 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 Lipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein Targeting The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis Crystal structure of the N-terminal domain of MinC dimerized via domain swapping Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring How bacteria maintain location and number of flagella?Mapping out Min protein patterns in fully confined fluidic chambers TP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.Membrane potential is important for bacterial cell division Changes in the Min oscillation pattern before and after cell birth Chromosome segregation by the Escherichia coli Min system.Antimicrobial peptide cWFW kills by combining lipid phase separation with autolysis.Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction.MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.A polymerization-depolymerization model that accurately generates the self-sustained oscillatory system involved in bacterial division site placement Cellular polarity in prokaryotic organisms.Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli Macromolecules that prefer their membranes curvy.Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA.Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli.Role of MinD-membrane association in Min protein interactions Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes.MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.Polar flagellar biosynthesis and a regulator of flagellar number influence spatial parameters of cell division in Campylobacter jejuni Membrainy: a 'smart', unified membrane analysis tool.Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein Erns The product of tadZ, a new member of the parA/minD superfamily, localizes to a pole in Aggregatibacter actinomycetemcomitans Membrane Stored Curvature Elastic Stress Modulates Recruitment of Maintenance Proteins PspA and Vipp1 The switch I and II regions of MinD are required for binding and activating MinC.Spatial control of bacterial division-site placement.MinD and MinE interact with anionic phospholipids and regulate division plane formation in Escherichia coli.Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II.

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P2860

The MinD membrane targeting sequence is a transplantable lipid-binding helix.

http://www.wikidata.org/entity/Q44527107

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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The MinD membrane targeting sequence is a transplantable lipid-binding helix.

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The MinD membrane targeting sequence is a transplantable lipid-binding helix.

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type

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The MinD membrane targeting sequence is a transplantable lipid-binding helix.

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The MinD membrane targeting sequence is a transplantable lipid-binding helix.

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The MinD membrane targeting sequence is a transplantable lipid-binding helix.

@en

The MinD membrane targeting sequence is a transplantable lipid-binding helix.

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Journal of Biological Chemistry

P1476

The MinD membrane targeting sequence is a transplantable lipid-binding helix.

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P2093

Cheryl L Habrukowich

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

Susan L Rowland

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Tim H Szeto

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

P2860

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

Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.

Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site

Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ

Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles

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

Crystal structure of the bacterial cell division regulator MinD

Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase

FACS-optimized mutants of the green fluorescent protein (GFP)

Cytokinesis in bacteria

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40050-40056

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10.1074/JBC.M306876200

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41

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278

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2003-07-25T00:00:00Z

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12882967

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