Evidence map›Paper›PMID 37740002›Full record

ArticleCommunications biology2023

Structural and functional characterization of USP47 reveals a hot spot for inhibitor design.

Sang Chul Shin, Jinyoung Park, Kyung Hee Kim, Jung Min Yoon, Jinhong Cho, Byung Hak Ha, Yeonji Oh, Hyunah Choo, Eun Joo Song, Eunice EunKyeong Kim

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
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

10 authors at 5 institutions in 2 countries.

Sang Chul ShinBiomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Jinyoung ParkBiomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Kyung Hee KimBiomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Jung Min YoonBiomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Jinhong ChoBiomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Byung Hak HaBiomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Yeonji OhBrain Science Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea.
Hyunah ChooDivision of Bio‑Medical Science and Technology, KIST‑School, University of Science and Technology (UST), Seoul, 02792, Korea.
Eun Joo SongGraduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul, 03760, Republic of Korea. esong@ewha.ac.kr.ORCID http://orcid.org/0000-0002-2420-6666
Eunice EunKyeong KimBiomedical Research Institute, Korea Institute of Science and Technology, Seoul, 02792, Republic of Korea. eunice@kist.re.kr.ORCID http://orcid.org/0000-0002-7707-8055
Korea Institute of Science and Technology · KREwha Womans University · KRKorea Institute of Brain Science · KRBio-Medical Science (South Korea) · KRDana-Farber Cancer Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

USP47 is widely involved in tumor development, metastasis, and other processes while performing a more regulatory role in inflammatory responses, myocardial infarction, and neuronal development. In this study, we investigate the functional and biochemical properties of USP47, whereby depleting USP47 inhibited cancer cell growth in a p53-dependent manner-a phenomenon that enhances during the simultaneous knockdown of USP7. Full-length USP47 shows higher deubiquitinase activity than the catalytic domain. The crystal structures of the catalytic domain, in its free and ubiquitin-bound states, reveal that the misaligned catalytic triads, ultimately, become aligned upon ubiquitin-binding, similar to USP7, thereby becoming ready for catalysis. Yet, the composition and lengths of BL1, BL2, and BL3 of USP47 differ from those for USP7, and they contribute to the observed selectivity. Our study provides molecular details of USP47 regulation, substrate recognition, and the hotspots for drug discovery by targeting USP47.

Indexed as

Cell Transformation, NeoplasticUbiquitinCatalysisCatalytic DomainHumansUbiquitin-Specific Peptidase 7UbiquitinUbiquitin-Specific Peptidase 7USP7 protein, human

Identifiers

PMID37740002
PMCPMC10516900
OpenAlexW4386954462

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.