Beta-barrel membrane protein folding and structure viewed through the lens of alpha-hemolysin.
about
Development of an artificial cell, from self-organization to computation and self-reproductionCrystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structureMolecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxinsCrystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxinsThree-dimensional structure of different functional forms of the Vibrio cholerae hemolysin oligomer: a cryo-electron microscopic studyGrafting synthetic transmembrane units to the engineered low-toxicity α-hemolysin to restore its hemolytic activity.Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process.Geometrical membrane curvature as an allosteric regulator of membrane protein structure and function.Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membraneAssembly of the Bi-component leukocidin pore examined by truncation mutagenesis.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis.Interactions of peptides with a protein pore.Protein sequence analysis, cloning, and expression of flammutoxin, a pore-forming cytolysin from Flammulina velutipes. Maturation of dimeric precursor to monomeric active form by carboxyl-terminal truncation.The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formationInsights into alpha-hemolysin (Hla) evolution and expression among Staphylococcus aureus clones with hospital and community originBiological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells.The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes.Synthetic molecular evolution of pore-forming peptides by iterative combinatorial library screening.Cyclodextrin derivatives as anti-infectives.Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brainBacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin.Ion channels in microbes.Formation of very large conductance channels by Bacillus cereus Nhe in Vero and GH(4) cells identifies NheA + B as the inherent pore-forming structure.The aromatic ring of phenylalanine 334 is essential for oligomerization of Vibrio vulnificus hemolysin.Arresting and releasing Staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds.Unfolding of Vibrio cholerae hemolysin induces oligomerization of the toxin monomer.Exploring the molecular complexity of Triatoma dimidiata sialome.Electric migration of α-hemolysin in supported n-bilayers: a model for transmembrane protein microelectrophoresis.Pesticide vapor sensing using an aptamer, nanopore, and agarose gel on a chip.Astrocytes contain amyloid-β annular protofibrils in Alzheimer's disease brains.Lysenin-His, a sphingomyelin-recognizing toxin, requires tryptophan 20 for cation-selective channel assembly but not for membrane binding.Understanding antibiotic resistance via outer membrane permeability.c-Jun Proto-Oncoprotein Plays a Protective Role in Lung Epithelial Cells Exposed to Staphylococcal α-Toxin.
P2860
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P2860
Beta-barrel membrane protein folding and structure viewed through the lens of alpha-hemolysin.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Beta-barrel membrane protein f ...... h the lens of alpha-hemolysin.
@ast
Beta-barrel membrane protein f ...... h the lens of alpha-hemolysin.
@en
type
label
Beta-barrel membrane protein f ...... h the lens of alpha-hemolysin.
@ast
Beta-barrel membrane protein f ...... h the lens of alpha-hemolysin.
@en
prefLabel
Beta-barrel membrane protein f ...... h the lens of alpha-hemolysin.
@ast
Beta-barrel membrane protein f ...... h the lens of alpha-hemolysin.
@en
P1476
Beta-barrel membrane protein f ...... h the lens of alpha-hemolysin.
@en
P2093
Eric Gouaux
Michelle Montoya
P356
10.1016/S0005-2736(02)00663-6
P407
P577
2003-01-01T00:00:00Z