Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore.

Nucleobase recognition in ssDNA at the central constriction of the alpha-hemolysin pore.

Nanopores are under investigation for single-molecule DNA sequencing. The alpha-hemolysin (alphaHL) protein nanopore contains three recognition points capable of nucleobase discrimination in individual immobilized ssDNA molecules. We have modified the recognition point R(1) by extensive mutagenesis...

Full description

Bibliographic Details
Main Authors:	Stoddart, D, Heron, A, Klingelhoefer, J, Mikhailova, E, Maglia, G, Bayley, H
Format:	Journal article
Language:	English
Published:	2010

Similar Items

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

Nucleobase recognition at alkaline pH and apparent pKa of single DNA bases immobilised within a biological nanopore.
by: Franceschini, L, et al.
Published: (2012)

Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers.
by: Raychaudhuri, P, et al.
Published: (2011)

Urea facilitates the translocation of single-stranded DNA and RNA through the alpha-hemolysin nanopore.
by: Japrung, D, et al.
Published: (2010)

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
by: Song, L, et al.
Published: (1996)

Expression of ssDNA in Mammalian Cells
by: Yin Chen, et al.
Published: (2003-01-01)

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

Structural Basis of SOSS1 Complex Assembly and Recognition of ssDNA
by: Wendan Ren, et al.
Published: (2014-03-01)

Multiple base-recognition sites in a biological nanopore: two heads are better than one.
by: Stoddart, D, et al.
Published: (2010)

Single-nucleotide discrimination in immobilized DNA oligonucleotides with a biological nanopore.
by: Stoddart, D, et al.
Published: (2009)

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

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

Biotechnological production of ssDNA with DNA-hydrolyzing deoxyribozymes
by: Jin Liu, et al.
Published: (2021-06-01)

RNase A does not translocate the alpha-hemolysin pore.
by: Besnik Krasniqi, et al.
Published: (2014-01-01)

The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.
by: Jung, Y, et al.
Published: (2005)

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

Structure, stability and specificity of the binding of ssDNA and ssRNA with proteins.
by: Arumay Pal, et al.
Published: (2019-04-01)

Studying the recognition mechanism of TcaR and ssDNA using molecular dynamic simulations
by: Fan, Jing-rong, et al.
Published: (2020)

Imaging the assembly of the Staphylococcal pore-forming toxin alpha-Hemolysin
by: Thompson, J, et al.
Published: (2009)

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

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

Identification of epigenetic DNA modifications with a protein nanopore.
by: Wallace, E, et al.
Published: (2010)

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

Proof of ssDNA degraded from dsDNA for ET recombination
by: Yuanxia Zheng, et al.
Published: (2024-09-01)

Selection and Identification of an ssDNA Aptamer for Fibroblast Activation Protein
by: Xiaomin Zhang, et al.
Published: (2023-02-01)

Computational Study on the Interaction and Moving of ssDNA through Nanosheets
by: Mansoor H. Alshehri
Published: (2021-08-01)

Selection, Characterization, and Application of ssDNA Aptamer against Furaneol
by: Natalia Komarova, et al.
Published: (2018-11-01)

Selection and targeting of EpCAM protein by ssDNA aptamer.
by: Walhan Alshaer, et al.
Published: (2017-01-01)

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

Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis.
by: Panchal, R, et al.
Published: (1995)

Watson-Crick Base-Pairing Requirements for ssDNA Recognition and Processing in Replication-Initiating HUH Endonucleases
by: Adam T. Smiley, et al.
Published: (2023-02-01)

Deciphering the mechanism of processive ssDNA digestion by the Dna2-RPA ensemble
by: Jiangchuan Shen, et al.
Published: (2022-01-01)

Physiological Tolerance to ssDNA Enables Strand Uncoupling during DNA Replication
by: Amaia Ercilla, et al.
Published: (2020-02-01)

Electric-field-driven translocation of ssDNA through hydrophobic nanopores
by: Haynes, T, et al.
Published: (2018)

Systematic Selection of High‐Affinity ssDNA Sequences to Carbon Nanotubes
by: Dakyeon Lee, et al.
Published: (2024-08-01)

CRISPR/Cas9‐enhanced ssDNA recombineering for Pseudomonas putida
by: Tomás Aparicio, et al.
Published: (2019-09-01)

Correction: Selection and targeting of EpCAM protein by ssDNA aptamer.
by: Walhan Alshaer, et al.
Published: (2018-01-01)

Development of a novel, high-affinity ssDNA trypsin inhibitor
by: Stanislaw Malicki, et al.
Published: (2019-01-01)

Generation of ssDNA aptamers as diagnostic tool for Newcastle avian virus.
by: Boutheina Marnissi, et al.
Published: (2020-01-01)

Dual functions for the ssDNA-binding protein RPA in meiotic recombination.
by: Baolu Shi, et al.
Published: (2019-02-01)