Evidence map›Paper›PMID 16361443›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A.

John K Lee, David Kozono, Jonathan Remis, Yoshichika Kitagawa, Peter Agre, 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, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

69 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Evolutionary Overview of Aquaporin Superfamily.Advances in experimental medicine and biology · 2023
    Article
  5. Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023
    Article
  6. Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

9 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

6 authors at 2 institutions in 2 countries.

John K LeeMacromolecular Structure Group, Department of Biochemistry and Biophysics, University of California, S-412C Genentech Hall, 600 16th Street, San Francisco, CA 94143-2240, USA.
David Kozono
Jonathan Remis
Yoshichika Kitagawa
Peter Agre
Robert M Stroud
Akita Prefectural University · JPJohns Hopkins University · US

Funding

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 GM24485NIGMS NIH HHS R01 GM024485NIGMS NIH HHS R37 GM024485NIGMS NIH HHS U54 GM074929NIGMS NIH HHS U54 GM74929
6 · The paper itself

Abstract

To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis, we determined the structure of AqpM to 1.68-A resolution by x-ray crystallography. The structure establishes AqpM as being in a unique subdivision between the two major subdivisions of aquaporins, the water-selective aquaporins, and the water-plus-glycerol-conducting aquaglyceroporins. In AqpM, isoleucine replaces a key histidine residue found in the lumen of water channels, which becomes a glycine residue in aquaglyceroporins. As a result of this and other side-chain substituents in the walls of the channel, the channel is intermediate in size and exhibits differentially tuned electrostatics when compared with the other subfamilies.

Indexed as

Amino Acid SequenceAquaporinsArchaeaCrystallography, X-RayDetergentsGlycerolGlycineHot TemperatureHydrogen BondingHydrogen-Ion ConcentrationLiposomesMethanobacteriaceaeModels, MolecularMolecular Sequence DataProtein ConformationRecombinant ProteinsAquaporinsDetergentsGlycerolGlycineLiposomesRecombinant ProteinsWater

Identifiers

PMID16361443
PMCPMC1323191
OpenAlexW2151055502

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.