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...

Cur síos iomlán

Sonraí bibleagrafaíochta
Príomhchruthaitheoirí:	Raychaudhuri, P, Li, Q, Mason, A, Mikhailova, E, Heron, A, Bayley, H
Formáid:	Journal article
Teanga:	English
Foilsithe / Cruthaithe:	2011

Míreanna comhchosúla

Bilayer formation with fluorinated amphiphiles and applications in membrane protein studies
de réir: Raychaudhuri, P
Foilsithe / Cruthaithe: (2013)

Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore.
de réir: Stoddart, D, et al.
Foilsithe / Cruthaithe: (2010)

Redirecting pore assembly of staphylococcal α-hemolysin by protein engineering
de réir: Koo, S, et al.
Foilsithe / Cruthaithe: (2019)

Redirecting Pore Assembly of Staphylococcal α‑Hemolysin by Protein Engineering
de réir: Sunwoo Koo, et al.
Foilsithe / Cruthaithe: (2019-03-01)

Aromatic Fluorination of Multiblock Amphiphile Enhances Its Incorporation into Lipid Bilayer Membranes
de réir: Ryo Sasaki, et al.
Foilsithe / Cruthaithe: (2020-03-01)

Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
de réir: Miles, G, et al.
Foilsithe / Cruthaithe: (2002)

An engineered dimeric protein pore that spans adjacent lipid bilayers.
de réir: Mantri, S, et al.
Foilsithe / Cruthaithe: (2013)

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
de réir: Song, L, et al.
Foilsithe / Cruthaithe: (1996)

Visualization of multivalent binding events using α-hemolysin
de réir: Gregoir, P, et al.
Foilsithe / Cruthaithe: (2020)

Pathway for insertion of amphiphilic nanoparticles into defect-free lipid bilayers from atomistic molecular dynamics simulations
de réir: Van Lehn, Reid C., et al.
Foilsithe / Cruthaithe: (2016)

Single-molecule chemistry studied using the protein pore -α-hemolysin
de réir: Choi, LS
Foilsithe / Cruthaithe: (2012)

Engineered α-hemolysin pores with chemically and genetically-fused functional proteins
de réir: Mantri, S
Foilsithe / Cruthaithe: (2013)

Engineered α-hemolysin pores with chemically and genetically-fused functional proteins
de réir: Mantri, S
Foilsithe / Cruthaithe: (2013)

Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin
de réir: Yu-Chuan Chiu, et al.
Foilsithe / Cruthaithe: (2023-09-01)

Translocating kilobase RNA through the Staphylococcal α-hemolysin nanopore.
de réir: Cracknell, J, et al.
Foilsithe / Cruthaithe: (2013)

Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.
de réir: Walker, B, et al.
Foilsithe / Cruthaithe: (1992)

Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
de réir: Krishnasastry, M, et al.
Foilsithe / Cruthaithe: (1994)

Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
de réir: Gouaux, J, et al.
Foilsithe / Cruthaithe: (1994)

Response of the lipid bilayer to membrane pore formation.
de réir: Bonev, B, et al.
Foilsithe / Cruthaithe: (1999)

Partition of Amphiphilic Molecules to Lipid Bilayers by ITC: Low-Affinity Solutes
de réir: Jaime Samelo, et al.
Foilsithe / Cruthaithe: (2017-10-01)

The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.
de réir: Jung, Y, et al.
Foilsithe / Cruthaithe: (2005)

Hybrid pore formation by directed insertion of α-haemolysin into solid-state nanopores.
de réir: Hall, A, et al.
Foilsithe / Cruthaithe: (2010)

Single-molecule chemistry studies with engineered alpha-hemolysin pores
de réir: Hammerstein, A
Foilsithe / Cruthaithe: (2011)

Architecture of human perforin pore in pure lipid bilayers
de réir: Serra, MD, et al.
Foilsithe / Cruthaithe: (2011)

RNase A does not translocate the alpha-hemolysin pore.
de réir: Besnik Krasniqi, et al.
Foilsithe / Cruthaithe: (2014-01-01)

DNA and lipid bilayers: self-assembly and insertion.
de réir: Khalid, S, et al.
Foilsithe / Cruthaithe: (2008)

Enhanced translocation of single DNA molecules through alpha-hemolysin nanopores by manipulation of internal charge.
de réir: Maglia, G, et al.
Foilsithe / Cruthaithe: (2008)

The energetics of transmembrane helix insertion into a lipid bilayer.
de réir: Chetwynd, A, et al.
Foilsithe / Cruthaithe: (2010)

Oroxylin A inhibits hemolysis via hindering the self-assembly of α-hemolysin heptameric transmembrane pore.
de réir: Jing Dong, et al.
Foilsithe / Cruthaithe: (2013-01-01)

Structure-Dependent Stability of Lipid-Based Polymer Amphiphiles Inserted on Erythrocytes
de réir: Chunsong Yu, et al.
Foilsithe / Cruthaithe: (2021-07-01)

Modulation of density and orientation of amphiphilic DNA anchored to phospholipid membranes. I. Supported lipid bilayers.
de réir: Gambinossi, F, et al.
Foilsithe / Cruthaithe: (2010)

Imaging the assembly of the Staphylococcal pore-forming toxin alpha-Hemolysin
de réir: Thompson, J, et al.
Foilsithe / Cruthaithe: (2009)

Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.
de réir: Walker, B, et al.
Foilsithe / Cruthaithe: (1995)

Orientation of the monomeric porin OmpG in planar lipid bilayers.
de réir: Chen, M, et al.
Foilsithe / Cruthaithe: (2008)

Energy landscape for the insertion of amphiphilic nanoparticles into lipid membranes: A computational study
de réir: Van Lehn, Reid C, et al.
Foilsithe / Cruthaithe: (2021)

Energy landscape for the insertion of amphiphilic nanoparticles into lipid membranes: A computational study.
de réir: Reid C Van Lehn, et al.
Foilsithe / Cruthaithe: (2019-01-01)

Unfolding and refolding of monomeric and heptameric α-hemolysin
de réir: Henricus, M, et al.
Foilsithe / Cruthaithe: (2010)

Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers.
de réir: Rakowska, P, et al.
Foilsithe / Cruthaithe: (2013)

Subunit dimers of alpha-hemolysin expand the engineering toolbox for protein nanopores.
de réir: Hammerstein, A, et al.
Foilsithe / Cruthaithe: (2011)

Synthesis and Antibacterial Activities of Amphiphilic Neomycin B-based Bilipid Conjugates and Fluorinated Neomycin B-based Lipids
de réir: Frank Schweizer, et al.
Foilsithe / Cruthaithe: (2012-08-01)