Evidence map›Paper›PMID 26235900›Full record

ArticleScientific reports2015

YIP1 family member 4 (YIPF4) is a novel cellular binding partner of the papillomavirus E5 proteins.

Marietta Müller, Christopher W Wasson, Ramya Bhatia, Sally Boxall, David Millan, Grace Y S Goh, Jürgen Haas, Nicola J Stonehouse, Andrew Macdonald

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 20 citations in OpenAlex.

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  10. Papillomaviruses and Endocytic Trafficking.International journal of molecular sciences · 2018
    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

9 authors at 3 institutions in 1 country.

Marietta MüllerUniversity of Leeds, UK.
Christopher W WassonUniversity of Leeds, UK.
Ramya BhatiaDivision of Pathway Medicine, The University of Edinburgh, UK.
Sally BoxallUniversity of Leeds, UK.
David MillanDepartment of Pathology, Southern General Hospital, Glasgow, Scotland, UK.
Grace Y S GohUniversity of Leeds, UK.
Jürgen HaasDivision of Pathway Medicine, The University of Edinburgh, UK.
Nicola J StonehouseUniversity of Leeds, UK.
Andrew MacdonaldUniversity of Leeds, UK.
University of Leeds · GBUniversity of Edinburgh · GBSouthern General Hospital · GB

Funding

Medical Research Council G0501453Medical Research Council MR/K012665/1
6 · The paper itself

Abstract

E5 proteins are amongst the least understood of the Human Papillomavirus (HPV) encoded gene products. They are small, membrane-integrated proteins known to modulate a number of critical host pathways associated with pathogenesis including growth factor receptor signaling and immune evasion. Their role in the virus life cycle is less clear, indicating a role in the productive stages of the life cycle. However, a mechanism for this is currently lacking. Here we describe the identification of a novel binding partner of E5, YIPF4 using yeast two-hybrid analysis. YIPF4 is also a poorly characterized membrane spanning protein. Mutagenesis studies implicated the transmembrane regions of each protein as important for their interaction. Binding to YIPF4 was found for all E5 proteins tested suggesting that this interaction may mediate a conserved E5 function. In normal human keratinocytes YIPF4 expression was down-regulated upon differentiation and this reduction was partially rescued in cells harbouring HPV. Despite the conserved nature of the interaction with E5, siRNA mediated depletion of YIPF4 failed to impede two well-characterized functions of E5, namely EGFR trafficking or HLA class I presentation. Continued studies of YIPF4 are warranted to determine its role in the PV life cycle.

Indexed as

Cell Culture TechniquesCell DifferentiationDNA-Binding ProteinsErbB ReceptorsFemaleHistocompatibility Antigens Class IHumansKeratinocytesMembrane ProteinsOncogene Proteins, ViralProtein Structure, TertiaryTwo-Hybrid System TechniquesUterine Cervical DysplasiaUterine Cervical NeoplasmsViral ProteinsViroporin ProteinsDNA-Binding ProteinsE7 protein, Human papillomavirus type 18EGFR protein, humanErbB ReceptorsHistocompatibility Antigens Class IMembrane Proteinsoncogene protein E5, Human papillomavirus type 16Oncogene Proteins, ViralViral ProteinsViroporin ProteinsYIPF4 protein, human

Identifiers

PMID26235900
PMCPMC4522686
OpenAlexW1833772980

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.