Evidence map›Paper›PMID 21713671›Full record

ReviewAdvances in experimental medicine and biology2011

BTB-Kelch proteins and ubiquitination of kainate receptors.

John Marshall, Leslie A C Blair, Jeffrey D Singer

Open access · greenAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

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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 1 institution in 1 country.

John MarshallDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island 02912, USA. John_Marshall@brown.edu
Leslie A C Blair
Jeffrey D Singer
John Brown University · US

Funding

STRUCTURE AND FUNCTION OF AN E3/UBIQUTIN LIGASER01GM082940 · NIGMS · PORTLAND STATE UNIVERSITY · PI SINGER, JEFFREY D · 2008 to 2012
$1.3M
NIGMS NIH HHS 1R01GM082940-01A1NIGMS NIH HHS R01 GM082940PHS HHS R21.2970803
6 · The paper itself

Abstract

Kainate receptors (KAR) form a class of glutamate receptors that have been implicated in epilepsy, stroke, Alzheimer's and neuropathic pain.1 KAR subtypes are known to be segregated to specific locations within neurons and play significant roles in synaptic transmission and plasticity.2 Increasing evidence suggests a the role for ubiqutination in regulating the number of synaptic neurotransmitter receptors.3-5 The ubiquitin pathway consists of activation (E1), conjugation (E2) and ligation (E3). Cullins form the largest family of E3 ligase complexes. We have recently shown that the BTB/Kelch domain proteins, actinfilin and mayven, bind both Cul3 and specific KAR subtypes (GluR6 and GluR5-2b) to target these KARs for ubiquitination and degradation.5 In this chapter we will review how these interactions occur, what they mean for the stability of KARs and their associated proteins and how, in turn, they may affect synaptic functions in the central nervous system.

Indexed as

AnimalsHumansKainic Acid ReceptorsProteinsUbiquitinationKainic Acid ReceptorsProteins

Identifiers

PMID21713671
PMCPMC3929045
OpenAlexW180366708

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.