Evidence map›Paper›PMID 32631902›Full record

ArticleMolecular and cellular biology2020

Impact of Losing hRpn13 Pru or UCHL5 on Proteasome Clearance of Ubiquitinated Proteins and RA190 Cytotoxicity.

Vasty Osei-Amponsa, Vinidhra Sridharan, Mayank Tandon, Christine N Evans, Kimberly Klarmann, Kwong Tai Cheng, Justin Lack, Raj Chari, Kylie J Walters

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

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  18. Dienone Compounds: Targets and Pharmacological Responses.Journal of medicinal chemistry · 2020
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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

9 authors at 4 institutions in 1 country.

Vasty Osei-AmponsaProtein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.
Vinidhra SridharanProtein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.
Mayank TandonCollaborative Bioinformatics Resource, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.
Christine N EvansGenome Modification Core, Frederick National Laboratory for Cancer Research, Frederick, Maryland, USA.
Kimberly KlarmannCCR-Frederick Flow Cytometry Core, Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, Maryland, USA.
Kwong Tai ChengCancer Research Technology Program, Frederick National Laboratory for Cancer Research, Leidos Biomedical Research, Inc., Frederick, Maryland, USA.
Justin LackAdvanced Biomedical Computational Science, Frederick National Laboratory for Cancer Research, Frederick, Maryland, USA.
Raj ChariGenome Modification Core, Frederick National Laboratory for Cancer Research, Frederick, Maryland, USA.
Kylie J WaltersProtein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA kylie.walters@nih.gov.ORCID 0000-0001-7590-2891
Frederick National Laboratory for Cancer Research · USNational Cancer Institute · USLeidos (United States) · USNational Institutes of Health · US

Funding

CCR Collaborative Bioinformatics ResourceZICBC011532 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MALIK, MARIAM · 2013 to 2025
$33.7M
Ubiquitin signaling for protein degradationZIABC011490 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WALTERS, KYLIE · 2013 to 2025
$21.1M
Intramural NIH HHS ZIA BC011490
6 · The paper itself

Abstract

hRpn13/ADRM1 links substrate recruitment with deubiquitination at the proteasome through its proteasome- and ubiquitin-binding Pru domain and DEUBAD domain, which binds and activates deubiquitinating enzyme (DUB) UCHL5/Uch37. Here, we edit the HCT116 colorectal cancer cell line to delete part of the hRpn13 Pru, producing cells that express truncated hRpn13 (trRpn13), which is competent for UCHL5 binding but defective for proteasome interaction.

Indexed as

Amino Acid SequenceBinding SitesCytoplasmHCT116 CellsHumansIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMolecular ChaperonesProteasome Endopeptidase ComplexProtein BindingUbiquitinUbiquitinated ProteinsUbiquitin ThiolesteraseADRM1 protein, humanIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMolecular ChaperonesProteasome Endopeptidase ComplexproteassemblinUbiquitinUbiquitinated ProteinsUbiquitin ThiolesteraseUCHL5 protein, humanAdrm1ADRM1apoptosiscell cycle progressioncell viabilityproteasomeRA190Rpn13ubiquitinUch37UCHL5

Identifiers

PMID32631902
PMCPMC7459265
OpenAlexW3040463543

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.