Evidence map›Paper›PMID 30897496›Full record

ReviewCurrent opinion in cell biology2019

Nuclear deubiquitination in the spotlight: the multifaceted nature of USP7 biology in disease.

Radhika Rawat, Daniel T Starczynowski, Panagiotis Ntziachristos

Abstract readReview
In one paragraph

Review in Current opinion in cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The deubiquitinase Usp7 inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Organ defects of the Usp7Biomedical journal · 2023
    Article
  14. ATXN3 deubiquitinates YAP1 to promote tumor growth.American journal of cancer research · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

3 authors.

Radhika RawatDepartment of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Northwestern University, 303 E. Superior Street, Chicago, IL 60611, USA.
Daniel T StarczynowskiExperimental Hematology and Cancer Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH; Department of Cancer Biology, University of Cincinnati, Cincinnati, OH.
Panagiotis NtziachristosSimpson Querrey Center for Epigenetics; Robert H. Lurie Comprehensive Cancer Center, Feinberg School of Medicine, Northwestern University, Chicago, IL. Electronic address: Panos.ntz@northwestern.edu.

Funding

CARCINOGENESIS TRAINING PROGRAMT32CA009560 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Kathleen Janee Green · 1986 to 2026
$8.4M
Decoding innate immune signaling in normal and myelodysplastic hematopoiesisR35HL135787 · NHLBI · CINCINNATI CHILDRENS HOSP MED CTR · PI STARCZYNOWSKI, DANIEL · 2017 to 2022
$4.6M
Targeting IRAK1/4 in Myelodysplastic SyndromesR01DK113639 · NIDDK · CINCINNATI CHILDRENS HOSP MED CTR · PI STARCZYNOWSKI, DANIEL · 2017 to 2020
$1.9M
Exploring a new therapeutic approach through targeting epigenetic enzymes in ALLR00CA188293 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI NTZIACHRISTOS, PANAGIOTIS · 2015 to 2017
$747k
Therapeutic targeting of demethylation-deubiquitination axis in acute leukemiaR01CA248770 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI NTZIACHRISTOS, PANAGIOTIS · 2020 to 2021
$726k
NCI NIH HHS R00 CA188293NCI NIH HHS R01 CA248770NCI NIH HHS T32 CA009560NHLBI NIH HHS R35 HL135787NIDDK NIH HHS R01 DK113639
6 · The paper itself

Abstract

Ubiquitination is a versatile and tightly regulated post-translational protein modification with many distinct outcomes affecting protein stability, localization, interactions, and activity. Ubiquitin chain linkages anchored on substrates can be further modified by additional post-translational modifications, including phosphorylation and SUMOylation. Deubiquitinases (DUBs) reverse these ubiquitin marks with matched levels of precision. Over hundred known DUBs regulate a wide variety of cellular events. In this review, we focus on ubiquitin-specific protease 7 (USP7, also known as herpesvirus-associated ubiquitin-specific protease, or HAUSP) as one of the best studied, disease-associated DUBs. By highlighting the functions of USP7, particularly in the nucleus, and the emergence of the newest generation of USP7 inhibitors, we illustrate the importance of individual DUBs in the nucleus, and the therapeutic prospects of DUB targeting in human disease.

Indexed as

AnimalsApoptosisHumansNeoplasmsPhosphorylationProteolysisUbiquitinationUbiquitin-Specific Peptidase 7Ubiquitin-Specific Peptidase 7USP7 protein, human

Identifiers

PMID30897496
PMCPMC6986459

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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.