Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
about
Obstructing toxin pathways by targeted pore blockageThe Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structureGrafting synthetic transmembrane units to the engineered low-toxicity α-hemolysin to restore its hemolytic activity.Predicting three-dimensional structures of transmembrane domains of β-barrel membrane proteins.Subunit dimers of alpha-hemolysin expand the engineering toolbox for protein nanoporesDistinction between pore assembly by staphylococcal alpha-toxin versus leukotoxins.Homologous versus heterologous interactions in the bicomponent staphylococcal gamma-haemolysin pore.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.Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membraneIon channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus.Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH.VacA from Helicobacter pylori: a hexameric chloride channel.Hydration force in the atomic force microscope: A computational study.Submolecular resolution of single macromolecules with atomic force microscopy.Large-scale analysis of high-speed atomic force microscopy data sets using adaptive image processing.Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscope.Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope.Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayersSynthetic protocells to mimic and test cell function.Tapping-mode atomic force microscopy produces faithful high-resolution images of protein surfaces.Polymeric nonelectrolytes to probe pore geometry: application to the alpha-toxin transmembrane channel.Atomic force microscopy and electron microscopy analysis of retrovirus Gag proteins assembled in vitro on lipid bilayers.Imaging domains in model membranes with atomic force microscopy.Engineering anthrax toxin variants that exclusively form octamers and their application to targeting tumorsPeptide-lipid interactions: insights and perspectives.Model-based prediction of the alpha-hemolysin structure in the hexameric state.Vertebrate membrane proteins: structure, function, and insights from biophysical approaches.Real-time visualization of assembling of a sphingomyelin-specific toxin on planar lipid membranes.Protein conducting channels-mechanisms, structures and applications.Imaging modes of atomic force microscopy for application in molecular and cell biology.Single molecule atomic force microscopy of aerolysin pore complexes reveals unexpected star-shaped topography.Amyloid ion channels: a porous argument or a thin excuse?Arresting and releasing Staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds.Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts.Electric migration of α-hemolysin in supported n-bilayers: a model for transmembrane protein microelectrophoresis.Compressive Force Spectroscopy: From Living Cells to Single Proteins.
P2860
Q26827489-A658DD6D-6177-452F-8333-E85216A8F0C1Q27656672-FCFA5979-8EC6-4CDA-95A5-1D2A4D7BBB64Q27666788-5092F9C4-A51E-4F3E-B686-A2A9B9DEAE28Q30153330-98B1FA96-FF2A-4DC8-866D-6388B3E430A5Q30155413-44D5873C-E5FF-4196-B4BF-52FBCD7A1189Q30155848-1693014E-769C-4CC4-9E57-F127215E759DQ30157977-314E0391-4307-46AF-A2AC-771FD54778D4Q30160102-404D9E89-D1E0-4C68-91B1-0A54ED0CC078Q30160110-162C85D3-C72A-40EC-894B-441594123D84Q30160120-FA2C4AAB-50F4-4A9B-89A5-C74E57CB010DQ30163889-A4200C9D-9E62-4F7E-B725-B831BD538A2DQ30164517-29109F05-293E-40B1-A490-A3EE47E64596Q30167424-C2D631D8-C371-40FF-9630-131401C8AD45Q30303622-B8367DA0-9DAC-47C1-8901-6D861A5DD512Q30304025-22DF98AD-8193-44DB-AA1D-3A5BBBB711DEQ30447529-36F335B3-9B21-4777-B6FB-5C7905B21CD4Q30472385-9EC789CA-8C59-4B75-AAA5-80B46FB0F71DQ30580242-5E04CC71-FF0D-48D6-A23E-C4C2B1F18295Q30884488-CF601D9A-B3FF-4E12-847E-B7FCB9B5B434Q31920509-2C3B9EA7-9AA2-41BB-810F-AF41C369B912Q33591266-C24F6AD0-2F35-4328-A1E1-1143FBB98BADQ33752103-2A08F594-8218-4BCC-A098-B0E307F2AA78Q34171183-EA537620-66D8-42A2-90DE-E9E742F1B0F7Q34171907-057802CD-3A0A-4D96-981F-C1AAE2B55E9FQ34172241-949DF7BE-5A00-4BF3-AC90-00AB1A861159Q34353319-3490997B-D946-4AFE-8BB4-3E690338270BQ34580781-8014E570-FCB7-4DD5-9811-60F8173DDA95Q36000295-4E5D16F7-4610-4258-A02B-883621EA8BACQ36838918-80B04FAB-691E-425C-A797-A907CA489AECQ36922687-09FD6E52-23B8-4E65-A5A2-A66971A5BCDDQ37204367-BAC617DB-C3A1-4DB1-94FE-A8CE6291258CQ37976983-9DFF1BE8-CB92-457A-8DD9-0FB4377976D0Q39223922-0A56644F-B105-427C-9F39-28D363309B95Q40355672-8AC689A0-40F5-48BD-AAF4-3DC54BC4461AQ42182458-065C93BE-5C21-4265-8FEC-E56A4FBF8EF8Q42255322-FCCA6401-2E8D-4582-ACBB-B98B5778A9F1Q46294211-06254D8B-9A9F-4DBF-B5DA-1D81D25E09EEQ47831870-89645BA7-5D56-44D0-9DF0-3ABAEFBD9A6AQ54249880-9ECE28DD-F8F4-4782-A851-F29354453C5C
P2860
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
@ast
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
@en
type
label
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
@ast
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
@en
prefLabel
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
@ast
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
@en
P2093
P356
P1476
Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers.
@en
P2093
P304
P356
10.1006/JMBI.1997.1535
P407
P577
1998-02-01T00:00:00Z