Evidence map›Paper›PMID 29441057›Full record

ArticleFrontiers in microbiology2018

Stability of the HTLV-1 Antisense-Derived Protein, HBZ, Is Regulated by the E3 Ubiquitin-Protein Ligase, UBR5.

Amanda R Panfil, Jacob Al-Saleem, Cory M Howard, Nikoloz Shkriabai, Mamuka Kvaratskhelia, Patrick L Green

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. The Pleiotropic Effects of YBX1 on HTLV-1 Transcription.International journal of molecular sciences · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
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 3 institutions in 1 country.

Amanda R PanfilDepartment of Veterinary Biosciences, Center for Retrovirus Research, The Ohio State University, Columbus, OH, United States.
Jacob Al-SaleemDepartment of Veterinary Biosciences, Center for Retrovirus Research, The Ohio State University, Columbus, OH, United States.
Cory M HowardDepartment of Veterinary Biosciences, Center for Retrovirus Research, The Ohio State University, Columbus, OH, United States.
Nikoloz ShkriabaiDivision of Infectious Diseases, School of Medicine, University of Colorado Denver, Aurora, CO, United States.
Mamuka KvaratskheliaDivision of Infectious Diseases, School of Medicine, University of Colorado Denver, Aurora, CO, United States.
Patrick L GreenDepartment of Veterinary Biosciences, Center for Retrovirus Research, The Ohio State University, Columbus, OH, United States.
The Ohio State University · USUniversity of Colorado Denver · USThe Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute · US

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Tasleem J Padamsee · 1985 to 2026
$132.3M
Role of Inflammation in Tax-mediated TumorigenesisP01CA100730 · NCI · WASHINGTON UNIVERSITY · PI Malachi Griffith · 2003 to 2026
$44.8M
NCI NIH HHS P01 CA100730NCI NIH HHS P30 CA016058
6 · The paper itself

Abstract

Human T-cell leukemia virus type 1 (HTLV-1) encodes a protein derived from the antisense strand of the proviral genome designated HBZ (HTLV-1 basic leucine zipper factor). HBZ is the only viral gene consistently expressed in infected patients and adult T-cell leukemia/lymphoma (ATL) tumor cell lines. It functions to antagonize many activities of the Tax viral transcriptional activator, suppresses apoptosis, and supports proliferation of ATL cells. Factors that regulate the stability of HBZ are thus important to the pathophysiology of ATL development. Using affinity-tagged protein and shotgun proteomics, we identified UBR5 as a novel HBZ-binding partner. UBR5 is an E3 ubiquitin-protein ligase that functions as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. Herein, we investigated the role of UBR5 in HTLV-1-mediated T-cell transformation and leukemia/lymphoma development. The UBR5/HBZ interaction was verified

Indexed as

HBZHTLV-1proliferationT-cellubiquitinUBR5

Identifiers

PMID29441057
PMCPMC5797633
OpenAlexW2792225607

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.