Evidence map›Paper›PMID 29370879›Full record

ArticleVisual neuroscience2018

Differential epitope masking reveals synapse-specific complexes of TRPM1.

Melina A Agosto, Ivan A Anastassov, Theodore G Wensel

Open access · greenAbstract read
In one paragraph

Article in Visual neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 42% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Trans-synaptic Interaction with mGluR6 Contributes to ELFN1 Presynaptic Enrichment in Rod Photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  3. Article
  4. American journal of ophthalmology case reports · 2024
    Article
  5. Article
  6. Article
  7. 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

3 authors at 1 institution in 1 country.

Melina A AgostoVerna and Marrs McLean Department of Biochemistry and Molecular Biology,Baylor College of Medicine,Houston,Texas 77030.ORCID 0000-0002-3647-1926
Ivan A AnastassovVerna and Marrs McLean Department of Biochemistry and Molecular Biology,Baylor College of Medicine,Houston,Texas 77030.
Theodore G WenselVerna and Marrs McLean Department of Biochemistry and Molecular Biology,Baylor College of Medicine,Houston,Texas 77030.
Baylor College of Medicine · US

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI Michael M Ittmann · 2007 to 2026
$73.9M
VISION RESEARCH CENTERP30EY002520 · NEI · BAYLOR COLLEGE OF MEDICINE · PI Samuel M Wu · 1985 to 2026
$14.8M
Trasnducin Interactions with Photoreceptor MembranesR01EY007981 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1989 to 2016
$6.1M
Cilium-Associated Structures in Rod CellsR01EY026545 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 2016 to 2024
$3.7M
Light regulation of retinal phosphoinositidesR01EY025218 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 2016 to 2019
$1.6M
Characterization of TRPM1 isoforms and binding partners in ON bipolar cellsF32EY024815 · NEI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ANASTASSOV, IVAN · 2014 to 2016
$164k
The role of transient receptor potential channel TRPM1 in vertebrate visionF32EY020067 · NEI · BAYLOR COLLEGE OF MEDICINE · PI AGOSTO, MELINA A · 2010 to 2011
$99k
NCI NIH HHS P30 CA125123NEI NIH HHS F32 EY020067NEI NIH HHS F32 EY024815NEI NIH HHS P30 EY002520NEI NIH HHS R01 EY007981NEI NIH HHS R01 EY025218NEI NIH HHS R01 EY026545
6 · The paper itself

Abstract

The transient receptor potential channel TRPM1 is required for synaptic transmission between photoreceptors and the ON subtype of bipolar cells (ON-BPC), mediating depolarization in response to light. TRPM1 is present in the somas and postsynaptic dendritic tips of ON-BPCs. Monoclonal antibodies generated against full-length TRPM1 were found to have differential labeling patterns when used to immunostain the mouse retina, with some yielding reduced labeling of dendritic tips relative to the labeling of cell bodies. Epitope mapping revealed that those antibodies that poorly label the dendritic tips share a binding site (N2d) in the N-terminal arm near the transmembrane domain. A major splice variant of TRPM1 lacking exon 19 does not contain the N2d binding site, but quantitative immunoblotting revealed no enrichment of this variant in synaptsomes. One explanation of the differential labeling is masking of the N2d epitope by formation of a synapse-specific multiprotein complex. Identifying the binding partners that are specific for the fraction of TRPM1 present at the synapses is an ongoing challenge for understanding TRPM1 function.

Indexed as

AnimalsAntibodies, MonoclonalBlotting, WesternEpitope MappingEpitopesMiceMice, Inbred C57BLMicroscopy, ConfocalPolymerase Chain ReactionProtein IsoformsRetinal Bipolar CellsSynapsesSynaptic TransmissionTRPM Cation ChannelsAntibodies, MonoclonalEpitopesProtein IsoformsTrpm1 protein, mouseTRPM Cation ChannelsEpitope mappingEpitope maskingON bipolar cellTRPM1

Identifiers

PMID29370879
PMCPMC5788301
OpenAlexW2794086415

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.