Evidence map›Paper›PMID 19383790›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance.

Joseph D Ho, Ronald Yeh, Andrew Sandstrom, Ilya Chorny, William E C Harries, Rebecca A Robbins, Larry J W Miercke, Robert M Stroud

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 169 papers.

0numbers the graph read from it
0cells of the map it votes in
169citing papers in PubMed
11.2field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

169 citing papers in PubMed, 320 citations in OpenAlex.

  1. Article
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  9. Review
  10. Article
  11. Review
  12. Article
  13. Molecular basis for human aquaporin inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Thermodynamics andThe journal of physical chemistry. B · 2024
    Article
  15. Article
  16. Article
  17. Mechanosensitive aquaporins.Biophysical reviews · 2023
    Review
  18. Article
  19. Article
  20. Aquaporins and COFrontiers in physiology · 2023
    Review

109 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Joseph D HoGraduate Program in Chemistry and Chemical Biology and Department of Biochemistry and Biophysics, Genentech Hall, University of California, 600 16th Street, San Francisco, CA 94158-2517, USA.
Ronald Yeh
Andrew Sandstrom
Ilya Chorny
William E C Harries
Rebecca A Robbins
Larry J W Miercke
Robert M Stroud
University of California, San Francisco · US

Funding

Yeast ExpressionP50GM073210 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2004 to 2013
$21.5M
SPECIALIZED CENTER FOR THE PROTEIN STRUCTURE INITIATIVEU54GM074929 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KABACK, HOWARD RONALD · 2005 to 2009
$16.6M
STRUCTURE/FUNCTION OF PROTEINS AT MOLECULAR LEVELR01GM024485 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2024
$7.5M
Molecular Basis for Transmembrane Conduction & SignalingR37GM024485 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2007 to 2016
$4.7M
NIGMS NIH HHS GM074929NIGMS NIH HHS GM24485NIGMS NIH HHS P50 GM073210NIGMS NIH HHS R01 GM024485NIGMS NIH HHS R37 GM024485NIGMS NIH HHS U54 GM074929
6 · The paper itself

Abstract

Aquaporin (AQP) 4 is the predominant water channel in the mammalian brain, abundantly expressed in the blood-brain and brain-cerebrospinal fluid interfaces of glial cells. Its function in cerebral water balance has implications in neuropathological disorders, including brain edema, stroke, and head injuries. The 1.8-A crystal structure reveals the molecular basis for the water selectivity of the channel. Unlike the case in the structures of water-selective AQPs AqpZ and AQP1, the asparagines of the 2 Asn-Pro-Ala motifs do not hydrogen bond to the same water molecule; instead, they bond to 2 different water molecules in the center of the channel. Molecular dynamics simulations were performed to ask how this observation bears on the proposed mechanisms for how AQPs remain totally insulating to any proton conductance while maintaining a single file of hydrogen bonded water molecules throughout the channel.

Indexed as

Aquaporin 4Cell AdhesionCrystallography, X-RayHumansProtein ConformationProtein FoldingWaterAQP4 protein, humanAquaporin 4Water

Identifiers

PMID19383790
PMCPMC2678640
OpenAlexW2103511429

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.