OSCR

Active conformations of neuronal Na<sup>+</sup>, K<sup>+</sup>-ATPase isoforms and a disease-causing mutant.

Overview

Authors: Mads Eskesen Christensen1,2, Michael Habeck1,2, Adriana Katz3, Marlene Uglebjerg Fruergaard1,2, Yoav Peleg4, Uri Pick3, Steven J. D. Karlish3, Poul Nissen1,2
  1. Danish Research Institute of Translational Neuroscience - DANDRITE, Nordic EMBL Partnership for Molecular Medicine, Aarhus University,Aarhus C, Denmark
  2. Dept. of Molecular Biology and Genetics, Aarhus University,Aarhus C, Denmark
  3. Dept. of Biomolecular Sciences, Weizmann Institute of Science,Rehovot, Israel
  4. Structural Proteomics Unit, Weizmann Institute of Science,Rehovot, Israel
Institutions: Aarhus University (Denmark); Weizmann Institute of Science (Israel)
Journal: Nature communications, volume 17, issue 1, article 9278
Dates: received 3 September 2025; accepted 15 July 2026; published online 29 July 2026
Type: Research article · Language: English
License: CC BY-NC-ND
Identifiers: DOI 10.1038/s41467-026-75997-4 · PMID 42669691 · PMCID PMC13526833 · OpenAlex W7171696665
Open access: gold, a free copy (OpenAlex)
Status: data only
Categories: histology / microscopy (modality), human (organism), other condition (population), cellular / molecular (subfield)
Methods: fMRI & imaging
Keywords: Cryoelectron microscopy, Ion transport, Mechanisms of disease, Molecular neuroscience, Neurodevelopmental disorders
MeSH: Neurons*, Sodium-Potassium-Exchanging ATPase*, Animals, Binding Sites, Cryoelectron Microscopy, Hemiplegia, Humans, Isoenzymes, Models, Molecular, Mutation, Protein Conformation, Sodium (* major topic)
Topic: Ion Transport and Channel Regulation (Molecular Biology, Biochemistry, Genetics and Molecular Biology), according to OpenAlex
Citations: not cited yet (Europe PMC); 84 references in the paper

Abstract

The abstract is not reproduced here: the paper's license (CC BY-NC-ND) does not allow it. Read it in the paper, at the publisher or on Europe PMC.

Code

The paper links to its data, not to its authors' code: see the Data section.

The paper's code and data availability statement is in the Data section.

Tracing map

A tracing map links a paper to the code its authors published: this paper has none, so it has no map.

Data

Datasets cited

Code and data availability statement

The paper has a code and data availability statement. Its license (CC BY-NC-ND) does not allow reproducing it here; in short, from what the harvester recognized in it:

Read it in the paper: doi.org/10.1038/s41467-026-75997-4.

Versions

The history of this record: each version stored by the harvester or made by a correction of its authors or of the maintainers of its code, and what changed in its facts. The texts of the paper (its abstract, its availability statements) are not part of it; versions that changed only those are not listed.

Version 1, 27 September 2026: the first record

Recorded: type, language, journal, volume, issue, pages, dates, 8 authors, 5 keywords, 12 MeSH terms, 4 funders, 83 references.

Cite

This paper

Christensen, M. E., Habeck, M., Katz, A., Fruergaard, M. U., Peleg, Y., Pick, U., Karlish, S. J. D., & Nissen, P. (2026). Active conformations of neuronal Na<sup>+</sup>, K<sup>+</sup>-ATPase isoforms and a disease-causing mutant. Nature communications, 17(1), 9278. https://doi.org/10.1038/s41467-026-75997-4

BibTeX

@article{christensen2026active,
author = {Christensen, Mads Eskesen and Habeck, Michael and Katz, Adriana and Fruergaard, Marlene Uglebjerg and Peleg, Yoav and Pick, Uri and Karlish, Steven J. D. and Nissen, Poul},
title = {{Active conformations of neuronal Na\<sup\>+\</sup\>, K\<sup\>+\</sup\>-ATPase isoforms and a disease-causing mutant}},
journal = {Nature communications},
year = {2026},
month = jul,
volume = {17},
number = {1},
pages = {9278},
publisher = {Nature Publishing Group},
issn = {2041-1723},
doi = {10.1038/s41467-026-75997-4},
url = {https://doi.org/10.1038/s41467-026-75997-4},
pmid = {42669691},
pmcid = {PMC13526833}
}

RIS

TY - JOUR
AU - Christensen, Mads Eskesen
AU - Habeck, Michael
AU - Katz, Adriana
AU - Fruergaard, Marlene Uglebjerg
AU - Peleg, Yoav
AU - Pick, Uri
AU - Karlish, Steven J. D.
AU - Nissen, Poul
TI - Active conformations of neuronal Na<sup>+</sup>, K<sup>+</sup>-ATPase isoforms and a disease-causing mutant
T2 - Nature communications
J2 - Nat Commun
PY - 2026
DA - 2026/07/29
VL - 17
IS - 1
SP - 9278
SN - 2041-1723
PB - Nature Publishing Group
DO - 10.1038/s41467-026-75997-4
UR - https://doi.org/10.1038/s41467-026-75997-4
LA - en
ER -

CSL-JSON

{
"id": "10.1038/s41467-026-75997-4",
"type": "article-journal",
"title": "Active conformations of neuronal Na<sup>+</sup>, K<sup>+</sup>-ATPase isoforms and a disease-causing mutant",
"container-title": "Nature communications",
"author": [
{
"family": "Christensen",
"given": "Mads Eskesen"
},
{
"family": "Habeck",
"given": "Michael"
},
{
"family": "Katz",
"given": "Adriana"
},
{
"family": "Fruergaard",
"given": "Marlene Uglebjerg"
},
{
"family": "Peleg",
"given": "Yoav"
},
{
"family": "Pick",
"given": "Uri"
},
{
"family": "Karlish",
"given": "Steven J. D."
},
{
"family": "Nissen",
"given": "Poul"
}
],
"container-title-short": "Nat Commun",
"volume": "17",
"issue": "1",
"page": "9278",
"DOI": "10.1038/s41467-026-75997-4",
"PMID": "42669691",
"PMCID": "PMC13526833",
"ISSN": "2041-1723",
"publisher": "Nature Publishing Group",
"URL": "https://doi.org/10.1038/s41467-026-75997-4",
"language": "en",
"issued": {
"date-parts": [
[
2026,
7,
29
]
]
}
}

Similar papers

The papers with a page that share the most with this one: the tools found in their code, their categories, datasets, cited references and authors, the rarest counting most.

[1] doi:10.1038/s41594-026-01866-9 [code]
Structural and mechanistic insights into gating and allosteric modulation of GluN1-GluN3A NMDA receptors.
Journal: Nature structural & molecular biology
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 3 references
[2] doi:10.1038/s41594-026-01845-0
Conformational plasticity of human acid-sensing ion channel 1a.
Journal: Nature structural & molecular biology
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 3 references
[3] doi:10.1038/s41467-026-74814-2
Structural mechanism of Necrocide 1 activation of human TRPM4 that triggers necrosis by sodium overload.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 3 references
[4] doi:10.1038/s41594-026-01789-5 [code]
Calcium dependent activation of the TMEM16F scramblase and ion channel.
Journal: Nature structural & molecular biology
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 2 references
[5] doi:10.1038/s41467-026-75877-x
Structure of NHE6 and its lipid-mediated interactions regulating endosomal pH.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 2 references
[6] doi:10.1038/s41467-026-75444-4 [code]
Structural insights enable drug discovery for the neuronal NBCn2 carbonate transporter.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 2 references
[7] doi:10.1038/s41467-026-75806-y [code]
Cryo-EM insights into isoform-specific properties of the IP<sub>3</sub>R2 channel.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 2 references
[8] doi:10.1038/s41467-026-75564-x
Cooperative mechanism of neurotransmitter recognition and transport by the human vesicular polyamine transporter.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 2 references
[9] doi:10.1038/s41467-026-74087-9 [code]
Cryo-EM structures of heteromeric Kir4.1/5.1 channel suggest mechanisms of inward rectification and channel blockage.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 2 references
[10] doi:10.1371/journal.pbio.3003777
Structure of the human P2X3 receptor reveals the basis for subtype-selective inhibition by sivopixant.
Journal: PLoS biology
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 2 references

Contribute

The authors of this paper can claim it, correct its record and validate its tracing map, and the maintainers of its code (its owner, or a public member of its organization) correct what it says of their repository; anyone signed in can ask for its removal. Every request goes to OSCR's own machine, which answers it; your account page follows them.

Sign in with ORCID to claim this paper as one of its authors, correct its record or validate its tracing map: when the paper's metadata lists your ORCID iD, you are recognized at once. Maintainers of its code: sign in with GitHub, then claim the repository on your account page.

Request its removal

To ask OSCR to remove this record, the copies of its authors' scripts or its tracing map, use the removal request page: signed in, you say who you are, what to remove and why, then review and confirm the request. Published rules decide every request (how).

Discussion, reproductions, activity

Discussion: questions and error reports about this paper and its code, from signed-in readers and its authors. It opens with sign-in.

Reproductions: reports from readers who ran the authors' code: what they reproduced, with which environment, commit and data. It opens with sign-in.

Activity: what happens around this paper: new versions of its record, its map's validation, discussions and reproductions. It opens with sign-in.