Pore-forming protein structure analysis in membranes using multiple independent fluorescence techniques.

Pore-forming protein structure analysis in membranes using multiple independent fluorescence techniques.

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http://www.wikidata.org/entity/Q30330099
Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsStructural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structureTP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane proteinAssembly and topography of the prepore complex in cholesterol-dependent cytolysins.Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission.The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formationEfficient isolation of Pseudomonas aeruginosa type III secretion translocators and assembly of heteromeric transmembrane pores in model membranes.Synthetic molecular evolution of pore-forming peptides by iterative combinatorial library screening.Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer.Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Membrane insertion of the N-terminal alpha-helix of equinatoxin II, a sea anemone cytolytic toxin.Saccharides as Prospective Immobilizers of Nucleic Acids for Room-Temperature Structural EPR StudiesPulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb.Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes.A novel mechanism of pore formation: membrane penetration by the N-terminal amphipathic region of equinatoxin.
P2860

Pore-forming protein structure analysis in membranes using multiple independent fluorescence techniques.

Item
http://www.wikidata.org/entity/Q30330099
description
2002 nî lūn-bûn
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2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
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2002年论文
@wuu
name
Pore-forming protein structure ...... ndent fluorescence techniques.
@ast
Pore-forming protein structure ...... ndent fluorescence techniques.
@en
type
label
Pore-forming protein structure ...... ndent fluorescence techniques.
@ast
Pore-forming protein structure ...... ndent fluorescence techniques.
@en
prefLabel
Pore-forming protein structure ...... ndent fluorescence techniques.
@ast
Pore-forming protein structure ...... ndent fluorescence techniques.
@en
P1433
P1476
P2093
P2888
P304
P31
P356
P433
P478
P577
P5875
P6179
P698
P356
P1433
P1476
Pore-forming protein structure ...... ndent fluorescence techniques.
@en
P2093
P2888
P304
P31
P356
P433
P478
P577
P5875
P6179
P698