Tuning the size and properties of ClyA nanopores assisted by directed evolution.
about
Nanopore-based analysis of biochemical speciesEngineered transmembrane pores.Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.Multi-compartment encapsulation of communicating droplets and droplet networks in hydrogel as a model for artificial cells.The assembly dynamics of the cytolytic pore toxin ClyA.Engineering a nanopore with co-chaperonin function.Single molecule analysis by biological nanopore sensors.Detection of two isomeric binding configurations in a protein-aptamer complex with a biological nanopore.The Transmembrane Domain of a Bicomponent ABC Transporter Exhibits Channel-Forming Activity.Nanopore Sensing.Fingerprinting of Peptides with a Large Channel of Bacteriophage Phi29 DNA Packaging Motor.Assembly mechanism of the α-pore-forming toxin cytolysin A from Escherichia coli.Single-molecule nanopore enzymology.Channel of viral DNA packaging motor for real time kinetic analysis of peptide oxidation states.Single-Molecule Analyte Recognition with ClyA Nanopores Equipped with Internal Protein AdaptorsDetection of 5-methylcytosine and 5-hydroxymethylcytosine in DNA via host-guest interactions inside α-hemolysin nanopores.DNA Translocation through Nanopores at Physiological Ionic Strengths Requires Precise Nanoscale EngineeringNanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein NanoporeLabel-Free and Real-Time Detection of Protein Ubiquitination with a Biological NanoporeA Protein Rotaxane Controls the Translocation of Proteins Across a ClyA Nanopore.DNA-assisted oligomerization of pore-forming toxin monomers into precisely-controlled protein channels.Electro-osmotic capture and ionic discrimination of peptide and protein biomarkers with FraC nanopores.Real-Time Conformational Changes and Controlled Orientation of Native Proteins Inside a Protein Nanoreactor.Alpha-Helical Fragaceatoxin C Nanopore Engineered for Double-Stranded and Single-Stranded Nucleic Acid Analysis.Behavior of α-synuclein-drug complexes during nanopore analysis with a superimposed AC field.pH controlled gating of toxic protein pores by dendrimers.Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore.Modular pore-forming immunotoxins with caged cytotoxicity tailored by directed evolution
P2860
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P2860
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年學術文章
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name
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
@en
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
@nl
type
label
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
@en
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
@nl
prefLabel
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
@en
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
@nl
P2093
P2860
P356
P1476
Tuning the size and properties of ClyA nanopores assisted by directed evolution.
@en
P2093
Annemie Biesemans
Giovanni Maglia
Misha Soskine
P2860
P304
13456-13463
P356
10.1021/JA4053398
P407
P577
2013-08-27T00:00:00Z