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Cited by 490

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Aquaporin water channels: molecular mechanisms for human diseases1

Open access
Agre, Peter, Kozono, David·2003·FEBS Letters

Abstract

Although water is the major component of all biological fluids, the molecular pathways for water transport across cell membranes eluded identification until the discovery of the aquaporin family of water channels. The atomic structure of mammalian AQP1 illustrates how this family of proteins is freely permeated by water but not protons (hydronium ions, H 3 O+). Definition of the subcellular sites of expression predicted their physiological functions and potential clinical disorders. Analysis of several human disease states has confirmed that aquaporins are involved in multiple different illnesses including abnormalities of kidney function, loss of vision, onset of brain edema, starvation, and arsenic toxicity.

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Crossref · 10.1016/s0014-5793(03)01083-4

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Metadata

Authors
Agre, P., & Kozono, D.
Venue
FEBS Letters
Publisher
Wiley
Published
2003-10-02
Volume
555
Issue
1
Pages
72-78
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2105892382
Cited by
490
References
2
FWCI
10.62
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Aquaporin water channels: molecular mechanisms for human diseases1. https://app.cochat.ai/papers/10.1016/s0014-5793(03)01083-4
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Agre, P., & Kozono, D. (2003). Aquaporin water channels: molecular mechanisms for human diseases1. FEBS Letters. https://doi.org/10.1016/s0014-5793(03)01083-4

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.