Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
about
Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry and synthetic biologyInteraction of an amphipathic peptide with phosphatidycholine/phosphatidylethanolamine mixed membranesRegulation of ion channel function by the host lipid bilayer examined by a stopped-flow spectrofluorometric assay.Lipid recognition propensities of amino acids in membrane proteins from atomic resolution dataIdentification of FtsW as a transporter of lipid-linked cell wall precursors across the membraneInvestigating lipid composition effects on the mechanosensitive channel of large conductance (MscL) using molecular dynamics simulations.Co-translational association of cell-free expressed membrane proteins with supplied lipid bilayers.Detergent-free isolation, characterization, and functional reconstitution of a tetrameric K+ channel: the power of native nanodiscsFunctional equilibrium of the KcsA structure revealed by NMR.Effect of phosphatidylserine on unitary conductance and Ba2+ block of the BK Ca2+-activated K+ channel: re-examination of the surface charge hypothesis.Functional role and affinity of inorganic cations in stabilizing the tetrameric structure of the KcsA K+ channelMembranes: a meeting point for lipids, proteins and therapiesPreparation of uniformly isotope labeled KcsA for solid state NMR: expression, purification, reconstitution into liposomes and functional assay.Membrane protein synthesis in cell-free systems: from bio-mimetic systems to bio-membranes.The role of phosphatidic acid and cardiolipin in stability of the tetrameric assembly of potassium channel KcsA.The role of extramembranous cytoplasmic termini in assembly and stability of the tetrameric K(+)-channel KcsADo small headgroups of phosphatidylethanolamine and phosphatidic acid lead to a similar folding pattern of the K(+) channel?Inactivation of the KcsA potassium channel explored with heterotetramersCompeting Lipid-Protein and Protein-Protein Interactions Determine Clustering and Gating Patterns in the Potassium Channel from Streptomyces lividans (KcsA).Differential roles of blocking ions in KirBac1.1 tetramer stability.Anionic phospholipid interactions with the potassium channel KcsA: simulation studies.Interaction of the K+ channel KcsA with membrane phospholipids as studied by ESI mass spectrometry.Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane.Phosphatidic acid plays a special role in stabilizing and folding of the tetrameric potassium channel KcsA.Supramolecular Organization and Functional Implications of K+ Channel Clusters in Membranes.Detection and identification of stable oligomeric protein complexes in Escherichi coli inner membranes: a proteomics approach.The influence of a membrane environment on the structure and stability of a prokaryotic potassium channel, KcsA
P2860
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P2860
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
@en
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
@nl
type
label
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
@en
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
@nl
prefLabel
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
@en
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
@nl
P2093
P2860
P1433
P1476
Influence of lipids on membrane assembly and stability of the potassium channel KcsA.
@en
P2093
Annemieke van Dalen
Ben de Kruijff
J Antoinette Killian
Sander Hegger
P2860
P356
10.1016/S0014-5793(02)03061-2
P407
P577
2002-08-01T00:00:00Z