Evidence map›Paper›PMID 23608234›Full record

ReviewProgress in lipid research2013

Mammalian phosphatidylinositol 4-kinases as modulators of membrane trafficking and lipid signaling networks.

Emma L Clayton, Shane Minogue, Mark G Waugh

Open access · hybridAbstract readReview
In one paragraph

Review in Progress in lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 83 citations in OpenAlex.

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  6. Human GBP1 Is Involved in the Repair of Damaged Phagosomes/Endolysosomes.International journal of molecular sciences · 2023
    Article
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  8. Cholesterol and Phosphoinositides in Cilia Biology.Advances in experimental medicine and biology · 2023
    Review
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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 3 institutions in 1 country.

Emma L ClaytonUCL Institute for Liver & Digestive Health, UCL Royal Free Campus, Rowland Hill Street, London NW3 2PF, United Kingdom.
Shane Minogue
Mark G Waugh
Roland Hill (United Kingdom) · GBThe Royal Free Hospital · GBUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council bb/G021163/1Biotechnology and Biological Sciences Research Council BB/G021163/1
6 · The paper itself

Abstract

The four mammalian phosphatidylinositol 4-kinases modulate inter-organelle lipid trafficking, phosphoinositide signalling and intracellular vesicle trafficking. In addition to catalytic domains required for the synthesis of PI4P, the phosphatidylinositol 4-kinases also contain isoform-specific structural motifs that mediate interactions with proteins such as AP-3 and the E3 ubiquitin ligase Itch, and such structural differences determine isoform-specific roles in membrane trafficking. Moreover, different permutations of phosphatidylinositol 4-kinase isozymes may be required for a single cellular function such as occurs during distinct stages of GPCR signalling and in Golgi to lysosome trafficking. Phosphatidylinositol 4-kinases have recently been implicated in human disease. Emerging paradigms include increased phosphatidylinositol 4-kinase expression in some cancers, impaired functioning associated with neurological pathologies, the subversion of PI4P trafficking functions in bacterial infection and the activation of lipid kinase activity in viral disease. We discuss how the diverse and sometimes overlapping functions of the phosphatidylinositol 4-kinases present challenges for the design of isoform-specific inhibitors in a therapeutic context.

Indexed as

1-Phosphatidylinositol 4-KinaseAnimalsBacterial InfectionsGlycosphingolipidsHumansIsoenzymesNeoplasmsNervous System DiseasesPhosphatidylinositol PhosphatesReceptors, G-Protein-CoupledSignal TransductionSphingomyelinsVirus Diseases1-Phosphatidylinositol 4-KinaseGlycosphingolipidsIsoenzymesphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesReceptors, G-Protein-CoupledSphingomyelins

Identifiers

PMID23608234
PMCPMC3989048
OpenAlexW1994803385

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.