Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements

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Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements. / Lundby, Alicia; Mutoh, Hiroki; Dimitrov, Dimitar; Akemann, Walther; Knöpfel, Thomas.

In: PLoS ONE, Vol. 3, No. 6, 2008, p. e2514.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Lundby, A, Mutoh, H, Dimitrov, D, Akemann, W & Knöpfel, T 2008, 'Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements', PLoS ONE, vol. 3, no. 6, pp. e2514. https://doi.org/10.1371/journal.pone.0002514

APA

Lundby, A., Mutoh, H., Dimitrov, D., Akemann, W., & Knöpfel, T. (2008). Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements. PLoS ONE, 3(6), e2514. https://doi.org/10.1371/journal.pone.0002514

Vancouver

Lundby A, Mutoh H, Dimitrov D, Akemann W, Knöpfel T. Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements. PLoS ONE. 2008;3(6):e2514. https://doi.org/10.1371/journal.pone.0002514

Author

Lundby, Alicia ; Mutoh, Hiroki ; Dimitrov, Dimitar ; Akemann, Walther ; Knöpfel, Thomas. / Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements. In: PLoS ONE. 2008 ; Vol. 3, No. 6. pp. e2514.

Bibtex

@article{9aef8d30955a11df928f000ea68e967b,
title = "Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements",
abstract = "Ci-VSP contains a voltage-sensing domain (VSD) homologous to that of voltage-gated potassium channels. Using charge displacement ('gating' current) measurements we show that voltage-sensing movements of this VSD can occur within 1 ms in mammalian membranes. Our analysis lead to development of a genetically encodable fluorescent protein voltage sensor (VSFP) in which the fast, voltage-dependent conformational changes of the Ci-VSP voltage sensor are transduced to similarly fast fluorescence read-outs.",
author = "Alicia Lundby and Hiroki Mutoh and Dimitar Dimitrov and Walther Akemann and Thomas Kn{\"o}pfel",
note = "Keywords: Animals; Fluorescence; Genetic Engineering; Ion Channel Gating; PC12 Cells; Potassium Channels; Protein Conformation; Rats",
year = "2008",
doi = "10.1371/journal.pone.0002514",
language = "English",
volume = "3",
pages = "e2514",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "6",

}

RIS

TY - JOUR

T1 - Engineering of a genetically encodable fluorescent voltage sensor exploiting fast Ci-VSP voltage-sensing movements

AU - Lundby, Alicia

AU - Mutoh, Hiroki

AU - Dimitrov, Dimitar

AU - Akemann, Walther

AU - Knöpfel, Thomas

N1 - Keywords: Animals; Fluorescence; Genetic Engineering; Ion Channel Gating; PC12 Cells; Potassium Channels; Protein Conformation; Rats

PY - 2008

Y1 - 2008

N2 - Ci-VSP contains a voltage-sensing domain (VSD) homologous to that of voltage-gated potassium channels. Using charge displacement ('gating' current) measurements we show that voltage-sensing movements of this VSD can occur within 1 ms in mammalian membranes. Our analysis lead to development of a genetically encodable fluorescent protein voltage sensor (VSFP) in which the fast, voltage-dependent conformational changes of the Ci-VSP voltage sensor are transduced to similarly fast fluorescence read-outs.

AB - Ci-VSP contains a voltage-sensing domain (VSD) homologous to that of voltage-gated potassium channels. Using charge displacement ('gating' current) measurements we show that voltage-sensing movements of this VSD can occur within 1 ms in mammalian membranes. Our analysis lead to development of a genetically encodable fluorescent protein voltage sensor (VSFP) in which the fast, voltage-dependent conformational changes of the Ci-VSP voltage sensor are transduced to similarly fast fluorescence read-outs.

U2 - 10.1371/journal.pone.0002514

DO - 10.1371/journal.pone.0002514

M3 - Journal article

C2 - 18575613

VL - 3

SP - e2514

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 6

ER -

ID: 20969902