Evidence map›Paper›PMID 33681193›Full record

ReviewFrontiers in cell and developmental biology2021

Spotlight on USP4: Structure, Function, and Regulation.

Binbin Hu, Dingyue Zhang, Kejia Zhao, Yang Wang, Lijiao Pei, Qianmei Fu, Xuelei Ma

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2021. 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
2.4field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 44 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

7 authors at 1 institution in 1 country.

Binbin HuDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Dingyue ZhangDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Kejia ZhaoDepartment of Thoracic Surgery, West China Hospital, Sichuan University, Chengdu, China.
Yang WangDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Lijiao PeiDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Qianmei FuDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Xuelei MaDepartment of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Sichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The deubiquitinating enzyme (DUB)-mediated cleavage of ubiquitin plays a critical role in balancing protein synthesis and degradation. Ubiquitin-specific protease 4 (USP4), a member of the largest subfamily of cysteine protease DUBs, removes monoubiquitinated and polyubiquitinated chains from its target proteins. USP4 contains a DUSP (domain in USP)-UBL (ubiquitin-like) domain and a UBL-insert catalytic domain, sharing a common domain organization with its paralogs USP11 and USP15. USP4 plays a critical role in multiple cellular and biological processes and is tightly regulated under normal physiological conditions. When its expression or activity is aberrant, USP4 is implicated in the progression of a wide range of pathologies, especially cancers. In this review, we comprehensively summarize the current knowledge of USP4 structure, biological functions, pathological roles, and cellular regulation, highlighting the importance of exploring effective therapeutic interventions to target USP4.

Indexed as

cancerdeubiquitinaseinflammationNF-κBUSP4

Identifiers

PMID33681193
PMCPMC7935551
OpenAlexW3132248145

What Socratic 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 Socratic graph.