The MinD membrane targeting sequence is a transplantable lipid-binding helix.
about
Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formationDiscovery of a selective NaV1.7 inhibitor from centipede venom with analgesic efficacy exceeding morphine in rodent pain models.The bacterial cytoskeletonThe Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell ProtrusionsDynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis MembraneThe structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting siteDetermination 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 MinCLipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein TargetingThe Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate CytokinesisCrystal structure of the N-terminal domain of MinC dimerized via domain swappingStructural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ringHow bacteria maintain location and number of flagella?Mapping out Min protein patterns in fully confined fluidic chambersTP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.Membrane potential is important for bacterial cell divisionChanges in the Min oscillation pattern before and after cell birthChromosome 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 placementCellular 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 vitroZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coliMacromolecules 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 interactionsCardiolipin 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 jejuniMembrainy: a 'smart', unified membrane analysis tool.Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein ErnsThe product of tadZ, a new member of the parA/minD superfamily, localizes to a pole in Aggregatibacter actinomycetemcomitansMembrane Stored Curvature Elastic Stress Modulates Recruitment of Maintenance Proteins PspA and Vipp1The 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.
P2860
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P2860
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
@en
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
@nl
type
label
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
@en
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
@nl
prefLabel
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
@en
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
@nl
P2093
P2860
P356
P1476
The MinD membrane targeting sequence is a transplantable lipid-binding helix.
@en
P2093
Cheryl L Habrukowich
Susan L Rowland
Tim H Szeto
P2860
P304
40050-40056
P356
10.1074/JBC.M306876200
P407
P50
P577
2003-07-25T00:00:00Z