Evidence map›Paper›PMID 33946350›Full record

ArticleBiomolecules2021

Isopeptidase Kinetics Determination by a Real Time and Sensitive qFRET Approach.

Yan Liu, Yali Shen, Yang Song, Lei Xu, J Jefferson P Perry, Jiayu Liao

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

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 57% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

6 authors at 3 institutions in 2 countries.

Yan LiuDepartment of Bioengineering, Bourns College of Engineering, University of California at Riverside, 900 University Avenue, Riverside, CA 92521, USA.
Yali ShenDepartment of Abdominal Oncology, Cancer Center, West China Hospital, Sichuan University, Chengdu 610041, China.
Yang SongDepartment of Bioengineering, Bourns College of Engineering, University of California at Riverside, 900 University Avenue, Riverside, CA 92521, USA.
Lei XuDepartment of Geography & the Environment, California State University, Fullerton, 800 N State College Blvd, Fullerton, CA 92831, USA.
J Jefferson P PerryDepartment of Biochemistry, University of California at Riverside, 900 University Avenue, Riverside, CA 92521, USA.
Jiayu LiaoDepartment of Bioengineering, Bourns College of Engineering, University of California at Riverside, 900 University Avenue, Riverside, CA 92521, USA.ORCID 0000-0002-2624-5781
University of California, Riverside · USCalifornia State University, Fullerton · USSichuan University · CN

Funding

2/2 Drug Development and Capacity Building: A UCR/CoH-CCC Partnership (Pilot Project 2)P20CA242620 · NCI · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI MARTINEZ, ERNEST, SEEWALDT, VICTORIA L. · 2019 to 2022
$1.2M
NCI NIH HHS P20 CA242620NIH HHS AI076504the Science and Technology Department of Sichuan Province, China 2019YJ0142
6 · The paper itself

Abstract

Isopeptidase activity of proteases plays critical roles in physiological and pathological processes in living organisms, such as protein stability in cancers and protein activity in infectious diseases. However, the kinetics of protease isopeptidase activity has not been explored before due to a lack of methodology. Here, we report the development of novel qFRET-based protease assay for characterizing the isopeptidase kinetics of SENP1. The reversible process of SUMOylation in vivo requires an enzymatic cascade that includes E1, E2, and E3 enzymes and Sentrin/SUMO-specific proteases (SENPs), which can act either as endopeptidases that process the pre-SUMO before its conjugation, or as isopeptidases to deconjugate SUMO from its target substrate. We first produced the isopeptidase substrate of CyPet-SUMO1/YPet-RanGAP1c by SUMOylation reaction in the presence of SUMO E1 and E2 enzymes. Then a qFRET analyses of real-time FRET signal reduction of the conjugated substrate of CyPet-SUMO1/YPet-RanGAP1c to free CyPet-SUMO1 and YPet-RanGAP1c by the SENP1 were able to obtain the kinetic parameters,

Indexed as

Carbon-Nitrogen LyasesCatalytic DomainCysteine EndopeptidasesEnzyme AssaysFluorescence Resonance Energy TransferHumansKineticsPlasmidsRecombinant ProteinsSensitivity and SpecificitySumoylationCarbon-Nitrogen LyasesCysteine EndopeptidasesisopeptidaseRecombinant Proteinsenzyme kineticsisopeptidasequantitative FRET (qFRET) assaySENPSUMOylation

Identifiers

PMID33946350
PMCPMC8145275
OpenAlexW3157895180

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.