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  Transmembrane domain length of viral K+ channels is a signal for mitochondria targeting

Balss, J., Papatheodorou, P., Mehmel, M., Baumeister, D., Hertel, B., Delaroque, N., et al. (2008). Transmembrane domain length of viral K+ channels is a signal for mitochondria targeting. Proceedings of the National Academy of Sciences of the United States of America, 105(34), 12313-12318. doi:10.1073/pnas.0805709105.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-9E7E-8 Version Permalink: https://hdl.handle.net/21.11116/0000-0005-3A37-D
Genre: Journal Article

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2518832 (Publisher version)
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 Creators:
Balss, J., Author
Papatheodorou, P., Author
Mehmel, M., Author
Baumeister, D., Author
Hertel, B., Author
Delaroque, N.1, Author           
Chatelain, F. C., Author
Minor, D. L., Author
Etten, Van, Author
Rassow, J., Author
Moroni, A., Author
Thiel, G., Author
Affiliations:
1Department of Bioorganic Chemistry, MPI for Chemical Ecology, Max Planck Society, ou_24028              

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Free keywords: Algal viruses Dual targeting K plus channel sorting Pbcv-1 Esv-1 Potassium channel Protein import Membrane Virus Mechanisms Kcv Multidisciplinary in Current Contents(R)/Life Sciences
 Abstract: K+ channels operate in the plasma membrane and in membranes of organelles including mitochondria. The mechanisms and topogenic information for their differential synthesis and targeting is unknown. This article describes 2 similar viral K+ channels that

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 Dates: 2008
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: BOL466
DOI: 10.1073/pnas.0805709105
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 105 (34) Sequence Number: - Start / End Page: 12313 - 12318 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230