Evidence map›Paper›PMID 39930196›Full record

ReviewAdvances in experimental medicine and biology2025

Calcium-Binding Protein 4 Is Fundamental for Retinal Structure and Function.

Billie Beckwith-Cohen, Simon M Petersen-Jones

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in experimental medicine and biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Billie Beckwith-CohenDepartment of Small Animal Clinical Sciences, Michigan State University, East Lansing, MI, USA. billiebc@msu.edu.
Simon M Petersen-JonesDepartment of Small Animal Clinical Sciences, Michigan State University, East Lansing, MI, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium-binding proteins (CaBPs) are a subfamily of calmodulin-like proteins, that modulate presynaptic calcium-dependent interactions with voltage-gated calcium channels. CaBPs play crucial roles in the development of normal sensorineural structure and function in both the visual and auditory systems. Disruption of CaBPs can result in a range of synaptic disorders of varying severity, which are dependent on the proteins or isoforms that predominate the affected system. In the retina, CaBP4 seems to be the isoform that is most important for the development of structure and function of the photoreceptor to ON bipolar synapse. Absence of CaBP4 results in synaptic ribbon immaturity in the first retinal synapse, disruption of ON-bipolar cell-driven responses, and a structurally thin outer plexiform layer. It has recently been demonstrated that at least some of the functional and anatomic disruption caused by CaBP mutations can be successfully addressed with gene augmentation therapy both in the eye and ear.

Indexed as

Calcium-Binding ProteinsRetinaAnimalsHumansSynapsesCalcium-Binding ProteinsAnimal modelsCaBPCone-rod synaptic disorderPlasticityRetinitis pigmentosaSynaptic ribbons

Identifiers

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.