Evidence map›Paper›PMID 30826060›Full record

ArticleBiochemical and biophysical research communications2019

A predominant form of C-terminally end-cleaved AQP0 functions as an open water channel and an adhesion protein in AQP0

S Sindhu Kumari, Kulandaiappan Varadaraj

Open access · bronzeAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. CatExperimental eye research · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. C-Terminal End of Aquaporin 0 Regulates Lens Gap Junction Channel Function.Investigative ophthalmology & visual science · 2019
    Article
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

2 authors at 1 institution in 1 country.

S Sindhu KumariPhysiology and Biophysics, Stony Brook University, NY, USA.
Kulandaiappan VaradarajPhysiology and Biophysics, Stony Brook University, NY, USA; SUNY Eye Institute, Syracuse, NY, USA. Electronic address: kulandaiappan.varadaraj@stonybrook.edu.
Stony Brook University · US

Funding

Role of aquaporins in mammalian lens development,transparency and homeostasisR01EY026155 · NEI · STATE UNIVERSITY NEW YORK STONY BROOK · PI VARADARAJ, KULANDAIAPPAN · 2016 to 2019
$1.6M
NEI NIH HHS R01 EY026155
6 · The paper itself

Abstract

The purpose of this investigation was to find out whether C-terminally end-cleaved aquaporin 0 (AQP0), that is present predominantly in the lens mature fiber cells of the WT, functions as a water channel and a cell-to-cell adhesion (CTCA) protein in a knockin (KI) mouse model (AQP0

Indexed as

AnimalsAquaporinsCataractCell AdhesionCell Membrane PermeabilityEye ProteinsLens, CrystallineMiceMice, Inbred C57BLMutationWateraquaporin 0AquaporinsEye ProteinsWaterAQP0Cell-to-cell adhesionC-terminally end-cleaved AQP0Water permeability

Identifiers

PMID30826060
PMCPMC6588171
OpenAlexW2917712579

What OpenQuestion holds

Textmetadata
LicenceTDM
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.