Evidence map›Paper›PMID 26224631›Full record

ArticleThe Journal of biological chemistry2015

Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1.

Alexandra K Pozhidaeva, Kareem N Mohni, Sirano Dhe-Paganon, Cheryl H Arrowsmith, Sandra K Weller, Dmitry M Korzhnev, Irina Bezsonova

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. HSV-1 ICP0 Dimer Domain Adopts a Novel β-barrel Fold.bioRxiv : the preprint server for biology · 2024
    Article
  6. Review
  7. Next-Generation Phage Display to Identify Peptide Ligands of Deubiquitinases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Molecular Mechanisms of DUBs Regulation in Signaling and Disease.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

7 authors.

Alexandra K PozhidaevaFrom the Department of Molecular Biology and Biophysics, University of Connecticut Health, Farmington, Connecticut 06030.
Kareem N Mohnithe Department of Biochemistry, Vanderbilt University Medical Center, Nashville, Tennessee 37232.
Sirano Dhe-Paganonthe Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215, and.
Cheryl H Arrowsmiththe Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
Sandra K WellerFrom the Department of Molecular Biology and Biophysics, University of Connecticut Health, Farmington, Connecticut 06030.
Dmitry M KorzhnevFrom the Department of Molecular Biology and Biophysics, University of Connecticut Health, Farmington, Connecticut 06030.
Irina BezsonovaFrom the Department of Molecular Biology and Biophysics, University of Connecticut Health, Farmington, Connecticut 06030, bezsonova@uchc.edu.

Funding

GENETICS OF HSV DNA REPLICATIONR01AI021747 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI WELLER, SANDRA K, WRIGHT, DENNIS L. · 1985 to 2024
$9.9M
NIAID NIH HHS R01 AI021747
6 · The paper itself

Abstract

Human ubiquitin-specific protease 7 (USP7) is a deubiquitinating enzyme that prevents protein degradation by removing polyubiquitin chains from its substrates. It regulates the stability of a number of human transcription factors and tumor suppressors and plays a critical role in the development of several types of cancer, including prostate and small cell lung cancer. In addition, human USP7 is targeted by several viruses of the Herpesviridae family and is required for effective herpesvirus infection. The USP7 C-terminal region (C-USP7) contains five ubiquitin-like domains (UBL1-5) that interact with several USP7 substrates. Although structures of the USP7 C terminus bound to its substrates could provide vital information for understanding USP7 substrate specificity, no such data has been available to date. In this work we have demonstrated that the USP7 ubiquitin-like domains can be studied in isolation by solution NMR spectroscopy, and we have determined the structure of the UBL1 domain. Furthermore, we have employed NMR and viral plaque assays to probe the interaction between the C-USP7 and HSV-1 immediate-early protein ICP0 (infected cell protein 0), which is essential for efficient lytic infection and virus reactivation from latency. We have shown that depletion of the USP7 in HFF-1 cells negatively affects the efficiency of HSV-1 lytic infection. We have also found that USP7 directly binds ICP0 via its C-terminal UBL1-2 domains and mapped the USP7-binding site for ICP0. Therefore, this study represents a first step toward understanding the molecular mechanism of C-USP7 specificity toward its substrates and may provide the basis for future development of novel antiviral and anticancer therapies.

Indexed as

Cell LineHerpes SimplexHerpesvirus 1, HumanHumansImmediate-Early ProteinsProtein BindingProtein Structure, TertiaryUbiquitin-Protein LigasesUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseImmediate-Early ProteinsUbiquitin-Protein LigasesUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseUSP7 protein, humanVmw110 protein, Human herpesvirus 1

Identifiers

PMID26224631
PMCPMC4645603

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.