Evidence map›Paper›PMID 27756680›Full record

ArticleArchives of biochemistry and biophysics2016

Steady-state kinetic studies reveal that the anti-cancer target Ubiquitin-Specific Protease 17 (USP17) is a highly efficient deubiquitinating enzyme.

Nicole M Hjortland, Andrew D Mesecar

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of biochemistry and biophysics, 2016. 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
0.2field-weighted citation impact, top 35% 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.

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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

2 authors at 1 institution in 1 country.

Nicole M HjortlandDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47906, United States.
Andrew D MesecarDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47906, United States; Department of Biochemistry, Purdue University, West Lafayette, IN 47906, United States; Department of Chemistry, Purdue University, West Lafayette, IN 47906, United States; Purdue Center for Cancer Research, Purdue University, West Lafayette, IN 47906, United States. Electronic address: amesecar@purdue.edu.
Purdue University West Lafayette · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
NCI NIH HHS P30 CA023168
6 · The paper itself

Abstract

USP17 is a deubiquitinating enzyme that is upregulated in numerous cancers and therefore a drug target. We developed a robust expression, purification, and assay system for USP17 enabling its enzymatic and structural characterization. USP17 was expressed in E. coli as inclusion bodies and then solubilized, refolded, and purified using affinity and size-exclusion chromatography. Milligram quantities of pure USP17 can be produced that is catalytically more efficient (k

Indexed as

Gene Expression RegulationCell Line, TumorDeubiquitinating EnzymesEndopeptidasesEscherichia coliHeLa CellsHumansHydrogen-Ion ConcentrationKineticsLightLysineMutagenesis, Site-DirectedNeoplasmsProtein DenaturationProtein FoldingScattering, RadiationDeubiquitinating EnzymesEndopeptidasesLysineUbiquitinUSP17L2 protein, humanDeubiquitinatingDUB3Protein refoldingUbiquitinUbiquitin Specific Protease 17USP17

Identifiers

PMID27756680
PMCPMC5868344
OpenAlexW2534229385

What OpenQuestion holds

Textmetadata
LicenceTDM
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.