Evidence map›Paper›PMID 23359558›Full record

ArticleProtein science : a publication of the Protein Society2013

In silico study of human aquaporin AQP11 and AQP12 channels.

Luisa Calvanese, Marialuisa Pellegrini-Calace, Romina Oliva

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Presenting the Special Issue "Aquaporins: Dynamic Role and Regulation".International journal of molecular sciences · 2025
    Article
  5. Review
  6. Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023
    Review
  7. Classification and Gene Structure of Aquaporins.Advances in experimental medicine and biology · 2023
    Article
  8. Evolutionary Overview of Aquaporin Superfamily.Advances in experimental medicine and biology · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
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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

3 authors at 3 institutions in 1 country.

Luisa CalvaneseDepartment of Applied Sciences, University Parthenope of Naples, Centro Direzionale Isola C4, Naples I-80143, Italy.
Marialuisa Pellegrini-Calace
Romina Oliva
Parthenope University of Naples · ITUniversity of Bari Aldo Moro · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AQP11 and AQP12 are the most distantly related paralogs of the aquaporin family in human. They share indeed a low sequence similarity with other aquaporins and exhibit a modified N-terminal NPA signature motif. Furthermore, they have an anomalous subcellular localization. The AQP11 and AQP12 biological role remains to be fully clarified and their ability to allow transport of water is still debated. We have built accurate 3D-models for AQP11 and AQP12 and comprehensively compared their sequence and structure to other known aquaporins. In order to investigate whether they appear compatible or not with water permeability, we especially focused on the amino acid composition and electrostatics of their channels, keeping the structure of the low-water efficiency AQP0 as a reference system. Our analysis points out a possible alternative ar/R site and shows that these aquaporins feature unique residues at key pore-lining positions that make the shape, composition and electrostatics of their channel peculiar. Such residues can represent pivotal hints to study and explain the AQP11 and AQP12 biological and molecular function.

Indexed as

Amino Acid SequenceAquaporinsComputational BiologyComputer SimulationCysteineHumansModels, MolecularMolecular Sequence DataProtein ConformationSequence AlignmentStatic ElectricityWaterAQP11 protein, humanAQP12A protein, humanAquaporinsCysteineWater

Identifiers

PMID23359558
PMCPMC3610051
OpenAlexW1966676801

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.