Evidence map›Paper›PMID 24604726›Full record

ArticleMolecular biology reports2014

Identification of PLP2 and RAB5C as novel TPD52 binding partners through yeast two-hybrid screening.

Hamideh Shahheydari, Sarah Frost, Brian J Smith, Guy E Groblewski, Yuyan Chen, Jennifer A Byrne

Open access · greenAbstract read
In one paragraph

Article in Molecular biology reports, 2014. 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
0.4field-weighted citation impact, top 35% 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, 15 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

6 authors at 4 institutions in 2 countries.

Hamideh ShahheydariChildren's Cancer Research Unit, Kids Research Institute, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia.
Sarah Frost
Brian J Smith
Guy E Groblewski
Yuyan Chen
Jennifer A Byrne
Children's Hospital at Westmead · AUUniversity of Sydney · AULa Trobe University · AUUniversity of Wisconsin–Madison · US

Funding

Vector and Human Acinar CoreP01DK098108 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PANDOL, STEPHEN J. · 2014 to 2018
$8.1M
Acinar Cell Biology and Pancreatic DiseaseR01DK070888 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI GROBLEWSKI, GUY E · 2006 to 2021
$4.0M
NIDDK NIH HHS P01 DK098108NIDDK NIH HHS R01 DK070888
6 · The paper itself

Abstract

Tumor protein D52 (TPD52) is overexpressed in different cancers, but its molecular functions are poorly defined. A large, low-stringency yeast two-hybrid screen using full-length TPD52 bait identified known partners (TPD52, TPD52L1, TPD52L2, MAL2) and four other preys that reproducibly bound TPD52 and TPD52L1 baits (PLP2, RAB5C, GOLGA5, YIF1A). PLP2 and RAB5 interactions with TPD52 were confirmed in pull down assays, with interaction domain mapping experiments indicating that both proteins interact with a novel binding region of TPD52. This study provides insights into TPD52 functions, and ways to maximise the efficiency of low-stringency yeast two-hybrid screens.

Indexed as

Binding SitesCell Line, TumorEscherichia coliGene ExpressionHumansMARVEL Domain-Containing ProteinsNeoplasm ProteinsPlasmidsProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingProteolipidsrab5 GTP-Binding ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeTransfectionMARVEL Domain-Containing ProteinsNeoplasm ProteinsPLP2 protein, humanProteolipidsRAB5C protein, humanrab5 GTP-Binding ProteinsRecombinant Fusion ProteinsTPD52 protein, human

Identifiers

PMID24604726
PMCPMC4069224
OpenAlexW2170036464

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.