Amphipol mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein pb5. (Q34274118)

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1 February 2020

title

Amphipol mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein pb5 (English)

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1 February 2020

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Angéline Van der Heyden

3

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1 February 2020

Pascal Dumy

6

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1 February 2020

7

Françoise M Winnik

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author name string

Hajra Basit

1

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1 February 2020

K Shivaji Sharma

2

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Chantal Gondran

4

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Cécile Breyton

5

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Pierre Labbé

8

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language of work or name

English

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publication date

11 May 2012

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1 February 2020

published in

Chemical Communications

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volume

48

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issue

48

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page(s)

6037-6039

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Bacteriophage-host interactions leading to genome internalization

1 February 2020

cites work

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FhuA-mediated phage genome transfer into liposomes: a cryo-electron tomography study

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DNA delivery by phage as a strategy for encapsulating toroidal condensates of arbitrary size into liposomes

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Characterization of a high-affinity complex between the bacterial outer membrane protein FhuA and the phage T5 protein pb5.

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Bacteriophages as twenty-first century antibacterial tools for food and medicine

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Amphipols, nanodiscs, and fluorinated surfactants: three nonconventional approaches to studying membrane proteins in aqueous solutions

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The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.

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Promotion of sugar-lectin recognition through the multiple sugar presentation offered by regioselectively addressable functionalized templates (RAFT): a QCM-D and SPR study

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Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet

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Aptamer biosensor for label-free impedance spectroscopy detection of proteins based on recognition-induced switching of the surface charge

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Label-free femtomolar detection of target DNA by impedimetric DNA sensor based on poly(pyrrole-nitrilotriacetic acid) film

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Complexation of integral membrane proteins by phosphorylcholine-based amphipols

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