Evidence map›Paper›PMID 28393136›Full record

ArticleACS omega2017

Development of β-Hairpin Peptides for the Measurement of SCF-Family E3 Ligase Activity in Vitro via Ornithine Ubiquitination.

Kaiulani M Houston, Adam T Melvin, Gregery S Woss, Effrat L Fayer, Marcey L Waters, Nancy L Allbritton

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

4 citing papers in PubMed, 6 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

6 authors at 2 institutions in 1 country.

Kaiulani M HoustonDepartment of Chemistry, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Adam T MelvinCain Department of Chemical Engineering, Louisiana State University , Baton Rouge, Louisiana 70803, United States.
Gregery S WossDepartment of Chemistry, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Effrat L FayerDepartment of Chemistry, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Marcey L WatersDepartment of Chemistry, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Nancy L AllbrittonDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, United States; Joint Department of Biomedical Engineering, University of North Carolina, Chapel Hill, North Carolina 27599, United States.
University of North Carolina at Chapel Hill · USLouisiana State University · US

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI David Darr · 1985 to 2026
$201.5M
Single-Cell Measurement of Lipid Signaling in Colorectal CancerR01CA177993 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ALLBRITTON, NANCY L. · 2014 to 2018
$3.0M
Design of Degron-based Substrates Capable of E3 Ligase-mediated UbiquitinationF32CA162574 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MELVIN, ADAM THOMAS · 2011 to 2013
$110k
Development and Optimization of an Analytical Chemical Separations Technique to Analyze E3 Ligase Activity in Single CellsF31CA192529 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WOSS, GREGERY SCOTT · 2015 to 2016
$66k
NCI NIH HHS F31 CA192529NCI NIH HHS F32 CA162574NCI NIH HHS P30 CA016086NCI NIH HHS R01 CA177993
6 · The paper itself

Abstract

Regulation of the ubiquitin-proteasome system (UPS) to treat select types of cancer has become a popular area of drug discovery research. The FDA approval of proteasome inhibitors Bortezomib and Carfilzomib in the treatment of multiple myeloma has led to an increased need for chemical reporters capable of detecting and quantifying protein ubiquitination and the activity of members of the UPS including E3 ubiquitin ligases and the proteasome in the tumor cells of the patients. One limitation of peptide-based reporters is their rapid degradation in the cellular environment by cytosolic peptidases. Conversely, β-hairpin "protectides" exhibit a pronounced secondary structure that significantly increases their lifetime under cellular conditions. The goal of this work was to develop a family of novel, ornithine-rich protectides that could act as primary degrons serving as substrates for in vitro ubiquitination. The fluorescent peptide-based reporters were demonstrated to be highly resistant to degradation in multiple myeloma cell lysates. The most stable β-hairpin primary degron, containing a single ornithine residue at the N-terminus, OWRWR [Ac-OWVRVpGO(FAM)WIRQ-NH

Identifiers

PMID28393136
PMCPMC5377275
OpenAlexW2601299567

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.