Evidence map›Paper›PMID 22103298›Full record

ArticleJournal of proteome research2012

Protein composition of immunoprecipitated synaptic ribbons.

A Kantardzhieva, M Peppi, W S Lane, W F Sewell

Abstract read
In one paragraph

Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Recurrent connectivity supports carbon dioxide sensitivity inbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Role of Ribeye PXDLS/T-binding cleft in normal synaptic ribbon function.bioRxiv : the preprint server for biology · 2023
    Article
  5. Ribbon Synapses and Retinal Disease: Review.International journal of molecular sciences · 2023
    Review
  6. Transmission at rod and cone ribbon synapses in the retina.Pflugers Archiv : European journal of physiology · 2021
    Review
  7. Photoreceptor Compartment-Specific TULP1 Interactomes.International journal of molecular sciences · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Transmission Disrupted: Modeling Auditory Synaptopathy in Zebrafish.Frontiers in cell and developmental biology · 2018
    Review
  14. Activity-Dependent Phosphorylation by CaMKIIδ Alters the CaFrontiers in synaptic neuroscience · 2017
    Article
  15. Review
  16. Article
  17. Article
  18. Global Ca2+ signaling drives ribbon-independent synaptic transmission at rod bipolar cell synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  19. Article
  20. 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

4 authors at 3 institutions in 1 country.

A KantardzhievaEaton-Peabody Laboratory, Department of Otology and Laryngology, Massachusetts Eye and Ear Infirmary and Harvard Medical School, 243 Charles Street, Boston, Massachusetts 02114, United States.
M Peppi
W S Lane
W F Sewell
Massachusetts Eye and Ear Infirmary · USCenter for Systems Biology · USHarvard University · US

Funding

PHARMACOLOGY OF NEUROTRANSMITTERS IN HAIR-CELL ORGANSR01DC000767 · NIDCD · MASSACHUSETTS EYE AND EAR INFIRMARY · PI SEWELL, WILLIAM F · 1991 to 2010
$3.6M
Proteomic analysis of synaptic ribbons in the inner earR21DC009651 · NIDCD · MASSACHUSETTS EYE AND EAR INFIRMARY · PI SEWELL, WILLIAM F · 2008 to 2009
$415k
NIDCD NIH HHS R01 DC000767NIDCD NIH HHS R21 DC009651
6 · The paper itself

Abstract

The synaptic ribbon is an electron-dense structure found in hair cells and photoreceptors. The ribbon is surrounded by neurotransmitter-filled vesicles and considered to play a role in vesicle release. We generated an objective, quantitative analysis of the protein composition of the ribbon complex using a mass spectrometry-based proteomics analysis. Our use of affinity-purified ribbons and control IgG immunoprecipitations ensure that the identified proteins are indeed associated with the ribbon complex. The use of mouse tissue, where the proteome is complete, generated a comprehensive analysis of the candidates. We identified 30 proteins (comprising 56 isoforms and subunits) associated with the ribbon complex. The ribbon complex primarily comprises proteins found in conventional synapses, which we categorized into 6 functional groups: vesicle handling (38.5%), scaffold (7.3%), cytoskeletal molecules (20.6%), phosphorylation enzymes (10.6%), molecular chaperones (8.2%), and transmembrane proteins from the presynaptic membrane firmly attached to the ribbon (11.3%). The 3 CtBP isoforms represent the major protein in the ribbon whether calculated by molar amount (30%) or by mass (20%). The relatively high quantity of phosphorylation enzymes suggests a very active and regulated structure. The ribbon appears to comprise a concentrated cluster of proteins dealing with vesicle creation, retention and distribution, and consequent exocytosis.

Indexed as

AnimalsCattleCell NucleusExocytosisImmunoglobulin GImmunohistochemistryImmunoprecipitationMass SpectrometryMiceModels, MolecularNerve Tissue ProteinsPhotoreceptor CellsProteomeProteomicsRetinaSynapsesImmunoglobulin GNerve Tissue ProteinsProteome

Identifiers

PMID22103298
PMCPMC3274173
OpenAlexW2042356908

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.