Membrane pores: from structure and assembly, to medicine and technology

Membrane pores: from structure and assembly, to medicine and technology

Bibliográfalaš dieđut
Váldodahkkit:	Gilbert, RJC, Bayley, H, Anderluh, G
Materiálatiipa:	Journal article
Giella:	English
Almmustuhtton:	Royal Society 2017

Geahča maid

Cryo-EM structures of perforin-2 in isolation and assembled on a membrane suggest a mechanism for pore formation
Dahkki: Yu, X, et al.
Almmustuhtton: (2022)

Rapid assembly of a multimeric membrane protein pore.
Dahkki: Thompson, JR, et al.
Almmustuhtton: (2011)

Membrane pore formation at protein-lipid interfaces.
Dahkki: Gilbert, R, et al.
Almmustuhtton: (2014)

Rapid Assembly of a Multimeric Membrane Protein Pore Observed by Single Molecule Fluorescence
Dahkki: Cronin, B, et al.
Almmustuhtton: (2012)

Electron microscopy as a critical tool in the determination of pore forming mechanisms in proteins.
Dahkki: Gilbert, RJC
Almmustuhtton: (2021)

Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.
Dahkki: Walker, B, et al.
Almmustuhtton: (1992)

Redirecting pore assembly of staphylococcal α-hemolysin by protein engineering
Dahkki: Koo, S, et al.
Almmustuhtton: (2019)

Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
Dahkki: Podobnik, M, et al.
Almmustuhtton: (2016)

Redirecting Pore Assembly of Staphylococcal α‑Hemolysin by Protein Engineering
Dahkki: Sunwoo Koo, et al.
Almmustuhtton: (2019-03-01)

Single-molecule tracking of perfringolysin O assembly and membrane insertion uncoupling
Dahkki: Senior, MJT, et al.
Almmustuhtton: (2022)

Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
Dahkki: Marjetka Podobnik, et al.
Almmustuhtton: (2016-05-01)

Templated Assembly of Pore-forming Peptides in Lipid Membranes
Dahkki: Aziz Fennouri, et al.
Almmustuhtton: (2019-02-01)

Outer membrane protein G: Engineering a quiet pore for biosensing.
Dahkki: Chen, M, et al.
Almmustuhtton: (2008)

Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae.
Dahkki: Gilbert, R, et al.
Almmustuhtton: (1999)

Protein-lipid interactions and non-lamellar lipidic structures in membrane pore formation and membrane fusion
Dahkki: Gilbert, R
Almmustuhtton: (2015)

Permeation of styryl dyes through nanometer-scale pores in membranes.
Dahkki: Wu, Y, et al.
Almmustuhtton: (2011)

Effects of the eukaryotic pore-forming cytolysin Equinatoxin II on lipid membranes and the role of sphingomyelin.
Dahkki: Bonev, B, et al.
Almmustuhtton: (2003)

Single-molecule kinetics of pore assembly by the membrane attack complex
Dahkki: Edward S. Parsons, et al.
Almmustuhtton: (2019-05-01)

Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
Dahkki: Krishnasastry, M, et al.
Almmustuhtton: (1994)

Inhibition of Pore-Forming Proteins
Dahkki: Neža Omersa, et al.
Almmustuhtton: (2019-09-01)

Architecture of human perforin pore in pure lipid bilayers
Dahkki: Serra, MD, et al.
Almmustuhtton: (2011)

Interview: Enriching the pore. Interviewed by Hannah Stanwix.
Dahkki: Bayley, H
Almmustuhtton: (2012)

Incomplete pneumolysin oligomers form membrane pores.
Dahkki: Sonnen, A, et al.
Almmustuhtton: (2014)

Engineered transmembrane pores.
Dahkki: Ayub, M, et al.
Almmustuhtton: (2016)

Membrane-protein structure: Piercing insights.
Dahkki: Bayley, H
Almmustuhtton: (2009)

PH dependence of listeriolysin O aggregation and pore-forming ability
Dahkki: Bavdek, A, et al.
Almmustuhtton: (2012)

Temperature-responsive protein pores.
Dahkki: Jung, Y, et al.
Almmustuhtton: (2006)

Stochastic sensing with protein pores
Dahkki: Bayley, H, et al.
Almmustuhtton: (2000)

pH dependence of listeriolysin O aggregation and pore-forming ability.
Dahkki: Bavdek, A, et al.
Almmustuhtton: (2012)

Incomplete pneumolysin oligomers form membrane pores
Dahkki: Andreas F.-P. Sonnen, et al.
Almmustuhtton: (2014-01-01)

Assembly of transmembrane pores from mirror-image peptides
Dahkki: Smrithi Krishnan R, et al.
Almmustuhtton: (2022-09-01)

Dunking into the Lipid Bilayer: How Direct Membrane Binding of Nucleoporins Can Contribute to Nuclear Pore Complex Structure and Assembly
Dahkki: Mohamed Hamed, et al.
Almmustuhtton: (2021-12-01)

C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeability
Dahkki: Santhosh Kumar Nagarajan, et al.
Almmustuhtton: (2025-01-01)

Exportins can inhibit major mitotic assembly events in vitro: membrane fusion, nuclear pore formation, and spindle assembly
Dahkki: Matthew S. Nord, et al.
Almmustuhtton: (2020-01-01)

Polymers through pores: single-molecule experiments with nucleic acids, polypeptides and polysaccharides
Dahkki: Bayley, H
Almmustuhtton: (2013)

Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
Dahkki: Gouaux, J, et al.
Almmustuhtton: (1994)

Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
Dahkki: Miles, G, et al.
Almmustuhtton: (2002)

Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin.
Dahkki: Bakrac, B, et al.
Almmustuhtton: (2008)

Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin
Dahkki: Bakrač, B, et al.
Almmustuhtton: (2008)

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