Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization.
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Structure and Membrane Interactions of the Antibiotic Peptide Dermadistinctin K by Multidimensional Solution and Oriented 15N and 31P Solid-State NMR SpectroscopyThe complete general secretory pathway in gram-negative bacteriaRegulation of the ribosome-membrane junction at early stages of presecretory protein translocation in the mammalian endoplasmic reticulum.Role of lipids in the translocation of proteins across membranes.Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB proteinEffect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence.Protein transport via amino-terminal targeting sequences: common themes in diverse systems.Conformational and membrane-binding properties of a signal sequence are largely unaltered by its adjacent mature region.Surfactant protein B: lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain.Phospholipids enhance the binding of peptides to class II major histocompatibility moleculesLipid involvement in protein translocation in Escherichia coli.Signal peptides: new markers in cardiovascular disease?Participation of acid phospholipids in protein translocation across the bacterial cytoplasmic membrane.Anionic phospholipids and protein translocation.Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coliThe stable BRP signal peptide causes lethality but is unable to provoke the translocation of cloacin DF13 across the cytoplasmic membrane of Escherichia coli.Induction of non-bilayer lipid structures by functional signal peptidesInteraction of wild-type signal sequences and their charged variants with model and natural membranesThe presence of a helix breaker in the hydrophobic core of signal sequences of secretory proteins prevents recognition by the signal-recognition particle in Escherichia coli.Apparent Inhibition of Chloroplast Protein Import by Cold Temperatures Is Due to Energetic Considerations Not Membrane Fluidity.Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes.Delta mu H+ dependency of in vitro protein translocation into Escherichia coli inner-membrane vesicles varies with the signal-sequence core-region composition.
P2860
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P2860
Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization.
description
1988 nî lūn-bûn
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1988年の論文
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1988年学术文章
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1988年学术文章
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1988年学术文章
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1988年學術文章
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name
Penetration of the signal sequ ...... rations of lipid organization.
@ast
Penetration of the signal sequ ...... rations of lipid organization.
@en
type
label
Penetration of the signal sequ ...... rations of lipid organization.
@ast
Penetration of the signal sequ ...... rations of lipid organization.
@en
prefLabel
Penetration of the signal sequ ...... rations of lipid organization.
@ast
Penetration of the signal sequ ...... rations of lipid organization.
@en
P2093
P356
P1433
P1476
Penetration of the signal sequ ...... rations of lipid organization.
@en
P2093
Batenburg AM
Verkleij AJ
de Kruijff B
P304
P356
10.1021/BI00415A043
P407
P577
1988-07-01T00:00:00Z