Evidence map›Paper›PMID 27723317›Full record

ArticleJournal of the American Chemical Society2016

Selenocysteine as a Latent Bioorthogonal Electrophilic Probe for Deubiquitylating Enzymes.

Samuel D Whedon, Nagula Markandeya, Ambar S J B Rana, Nicholas A Senger, Caroline E Weller, Frantisek Tureček, Eric R Strieter, Champak Chatterjee

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 42 citations in OpenAlex.

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  13. A Highly Efficient Synthesis of Polyubiquitin Chains.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018
    Article
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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

8 authors at 2 institutions in 1 country.

Samuel D WhedonDepartment of Chemistry, University of Washington , Seattle, Washington 98195, United States.
Nagula MarkandeyaDepartment of Chemistry, University of Washington , Seattle, Washington 98195, United States.
Ambar S J B RanaDepartment of Chemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Nicholas A SengerDepartment of Chemistry, University of Washington , Seattle, Washington 98195, United States.
Caroline E WellerDepartment of Chemistry, University of Washington , Seattle, Washington 98195, United States.
Frantisek TurečekDepartment of Chemistry, University of Washington , Seattle, Washington 98195, United States.
Eric R StrieterDepartment of Chemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Champak ChatterjeeDepartment of Chemistry, University of Washington , Seattle, Washington 98195, United States.
University of Washington · USUniversity of Wisconsin–Madison · US

Funding

Understanding the Function of Deubiquitinases Using Chemical Tools: Administrative SupplementR01GM110543 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI STRIETER, ERIC ROBERT · 2014 to 2022
$2.9M
Chemical Strategies to Investigate Gene Regulation By Histone SumoylationR01GM110430 · NIGMS · UNIVERSITY OF WASHINGTON · PI CHATTERJEE, CHAMPAK · 2014 to 2022
$2.5M
NIGMS NIH HHS R01 GM110430NIGMS NIH HHS R01 GM110543
6 · The paper itself

Abstract

Deubiquitylating enzymes (DUBs) remove ubiquitin (Ub) from various cellular proteins and render eukaryotic ubiquitylation a dynamic process. The misregulation of protein ubiquitylation is associated with many human diseases, and there is an urgent need to identify specific DUBs associated with therapeutically relevant targets of Ub. We report the development of two facile selenocysteine-based strategies to generate the DUB probe dehydroalanine (Dha). Optimized oxidative or alkylative elimination of Se yielded Dha at the C-terminus of Ub. The high utility of alkylative elimination, which is compatible with multiple thiols in Ub targets, was demonstrated by generating a probe derived from the Ub ligase tripartite motif protein 25 (TRIM-25). Successful capture of the TRIM-25-associated DUB, ubiquitin-specific protease 15, demonstrated the versatility of our chemical strategy for identifying target-specific DUBs.

Identifiers

PMID27723317
PMCPMC5550359
OpenAlexW2529962815

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.