Evidence map›Paper›PMID 17940884›Full record

ArticleNeurochemical research2008

Arachidonic acid binds 14-3-3zeta, releases 14-3-3zeta from phosphorylated BAD and induces aggregation of 14-3-3zeta.

Thomas G Brock

Abstract read
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In one paragraph

Article in Neurochemical research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

9 citing papers in PubMed, 16 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

1 author at 1 institution in 1 country.

Thomas G BrockDepartment of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA. brocko@umich.edu
University of Michigan–Ann Arbor · US

Funding

Regulation of Nuclear Import/Export of 5-LipoxygenaseR01AI043574 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROCK, THOMAS G · 2002 to 2006
$1.7M
NIAID NIH HHS R01 AI43574
6 · The paper itself

Abstract

Polyunsaturated fatty acids, like arachidonic acid, can bind proteins and affect their function. The 14-3-3 proteins bind phosphorylated sites on a diverse array of client proteins and, in this way, are involved in many intracellular signaling pathways. In this study, we used a novel approach to discover that 14-3-3zeta is able to directly bind arachidonic acid. Furthermore, arachidonic acid, at physiological concentrations, reduced the binding of 14-3-3zeta to phosphorylated BAD, an interaction that is important in regulating apoptosis. In addition, high concentrations of arachidonic acid caused the polymerization of 14-3-3zeta, an event observed in neurodegenerative disorders. Taken together, these results indicate that arachidonic acid directly interacts with 14-3-3zeta and that this interaction may be important in both normal and pathological cellular events. If so, then factors that mediate the release, metabolism and reacylation of arachidonic acid into membranes represent key points of regulation.

Indexed as

14-3-3 ProteinsAmino Acid SequenceAnimalsArachidonic Acidbcl-Associated Death ProteinCell Line, TumorElectrophoresis, Polyacrylamide GelImmunoprecipitationMolecular Sequence DataPhosphorylationProtein BindingRats14-3-3 ProteinsArachidonic Acidbcl-Associated Death Protein

Identifiers

PMID17940884
OpenAlexW2066324232

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.