The Intracellular Distal Tail of the Na+/H+ Exchanger NHE1 Is Intrinsically Disordered: Implications for NHE1 Trafficking-Reference-Cited by-同舟云学术

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The Intracellular Distal Tail of the Na+/H+ Exchanger NHE1 Is Intrinsically Disordered: Implications for NHE1 Trafficking

Published:2011-04-08 Issue:17 Volume:50 Page:3469-3480
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Nørholm Ann-Beth¹²,Hendus-Altenburger Ruth¹²,Bjerre Gabriel¹,Kjaergaard Magnus²,Pedersen Stine F.¹,Kragelund Birthe B.²

Affiliation:

1. Cell and Developmental Biology, Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen Ø, Denmark

2. Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi1019989

Reference62 articles.

1. The Na+/H+ exchanger NHE1 in stress-induced signal transduction: implications for cell proliferation and cell death

2. Topological analysis of NHE1, the ubiquitous Na+/H+exchanger using chymotryptic cleavage

3. A Novel Topology Model of the Human Na+/H+ Exchanger Isoform 1

4. Nygaard, E. B., Lagerstedt, J. O., Bjerre, G., Poulsen, K. A., Meinild, S., Rigor, R. R., Pedersen, S. F., Voss, J. C., and Cala, P. M.Structural modeling and electron paramagnetic resonance spectroscopy of the human Na+/H+Exchanger isoform 1.J. Biol. Chem. 2010, in press.

5. The Na+/H+ exchanger isoform 1 (NHE1) is a novel member of the calmodulin-binding proteins. Identification and characterization of calmodulin-binding sites.

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