Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers.

Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers.

The insertion of fully folded and assembled ion channels and pores into planar lipid bilayers for electrical recording has been facilitated by the use of conventional detergents at a final concentration below the critical micelle concentration (CMC). After the desired number of channels or pores (of...

Полное описание

Библиографические подробности
Главные авторы:	Raychaudhuri, P, Li, Q, Mason, A, Mikhailova, E, Heron, A, Bayley, H
Формат:	Journal article
Язык:	English
Опубликовано:	2011

Схожие документы

Bilayer formation with fluorinated amphiphiles and applications in membrane protein studies
по: Raychaudhuri, P
Опубликовано: (2013)

Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore.
по: Stoddart, D, и др.
Опубликовано: (2010)

Redirecting pore assembly of staphylococcal α-hemolysin by protein engineering
по: Koo, S, и др.
Опубликовано: (2019)

Redirecting Pore Assembly of Staphylococcal α‑Hemolysin by Protein Engineering
по: Sunwoo Koo, и др.
Опубликовано: (2019-03-01)

Aromatic Fluorination of Multiblock Amphiphile Enhances Its Incorporation into Lipid Bilayer Membranes
по: Ryo Sasaki, и др.
Опубликовано: (2020-03-01)

Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
по: Miles, G, и др.
Опубликовано: (2002)

An engineered dimeric protein pore that spans adjacent lipid bilayers.
по: Mantri, S, и др.
Опубликовано: (2013)

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
по: Song, L, и др.
Опубликовано: (1996)

Visualization of multivalent binding events using α-hemolysin
по: Gregoir, P, и др.
Опубликовано: (2020)

Pathway for insertion of amphiphilic nanoparticles into defect-free lipid bilayers from atomistic molecular dynamics simulations
по: Van Lehn, Reid C., и др.
Опубликовано: (2016)

Single-molecule chemistry studied using the protein pore -α-hemolysin
по: Choi, LS
Опубликовано: (2012)

Engineered α-hemolysin pores with chemically and genetically-fused functional proteins
по: Mantri, S
Опубликовано: (2013)

Engineered α-hemolysin pores with chemically and genetically-fused functional proteins
по: Mantri, S
Опубликовано: (2013)

Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin
по: Yu-Chuan Chiu, и др.
Опубликовано: (2023-09-01)

Translocating kilobase RNA through the Staphylococcal α-hemolysin nanopore.
по: Cracknell, J, и др.
Опубликовано: (2013)

Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.
по: Walker, B, и др.
Опубликовано: (1992)

Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
по: Krishnasastry, M, и др.
Опубликовано: (1994)

Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
по: Gouaux, J, и др.
Опубликовано: (1994)

Response of the lipid bilayer to membrane pore formation.
по: Bonev, B, и др.
Опубликовано: (1999)

Partition of Amphiphilic Molecules to Lipid Bilayers by ITC: Low-Affinity Solutes
по: Jaime Samelo, и др.
Опубликовано: (2017-10-01)

The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.
по: Jung, Y, и др.
Опубликовано: (2005)

Hybrid pore formation by directed insertion of α-haemolysin into solid-state nanopores.
по: Hall, A, и др.
Опубликовано: (2010)

Single-molecule chemistry studies with engineered alpha-hemolysin pores
по: Hammerstein, A
Опубликовано: (2011)

Architecture of human perforin pore in pure lipid bilayers
по: Serra, MD, и др.
Опубликовано: (2011)

RNase A does not translocate the alpha-hemolysin pore.
по: Besnik Krasniqi, и др.
Опубликовано: (2014-01-01)

DNA and lipid bilayers: self-assembly and insertion.
по: Khalid, S, и др.
Опубликовано: (2008)

Enhanced translocation of single DNA molecules through alpha-hemolysin nanopores by manipulation of internal charge.
по: Maglia, G, и др.
Опубликовано: (2008)

The energetics of transmembrane helix insertion into a lipid bilayer.
по: Chetwynd, A, и др.
Опубликовано: (2010)

Oroxylin A inhibits hemolysis via hindering the self-assembly of α-hemolysin heptameric transmembrane pore.
по: Jing Dong, и др.
Опубликовано: (2013-01-01)

Structure-Dependent Stability of Lipid-Based Polymer Amphiphiles Inserted on Erythrocytes
по: Chunsong Yu, и др.
Опубликовано: (2021-07-01)

Modulation of density and orientation of amphiphilic DNA anchored to phospholipid membranes. I. Supported lipid bilayers.
по: Gambinossi, F, и др.
Опубликовано: (2010)

Imaging the assembly of the Staphylococcal pore-forming toxin alpha-Hemolysin
по: Thompson, J, и др.
Опубликовано: (2009)

Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.
по: Walker, B, и др.
Опубликовано: (1995)

Orientation of the monomeric porin OmpG in planar lipid bilayers.
по: Chen, M, и др.
Опубликовано: (2008)

Energy landscape for the insertion of amphiphilic nanoparticles into lipid membranes: A computational study
по: Van Lehn, Reid C, и др.
Опубликовано: (2021)

Energy landscape for the insertion of amphiphilic nanoparticles into lipid membranes: A computational study.
по: Reid C Van Lehn, и др.
Опубликовано: (2019-01-01)

Unfolding and refolding of monomeric and heptameric α-hemolysin
по: Henricus, M, и др.
Опубликовано: (2010)

Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers.
по: Rakowska, P, и др.
Опубликовано: (2013)

Subunit dimers of alpha-hemolysin expand the engineering toolbox for protein nanopores.
по: Hammerstein, A, и др.
Опубликовано: (2011)

Synthesis and Antibacterial Activities of Amphiphilic Neomycin B-based Bilipid Conjugates and Fluorinated Neomycin B-based Lipids
по: Frank Schweizer, и др.
Опубликовано: (2012-08-01)