Evidence map›Paper›PMID 38291002›Full record

ArticleAngewandte Chemie (International ed. in English)2024

A Modular Turn-On Strategy to Profile E2-Specific Ubiquitination Events in Living Cells.

Caitlin J Hill, Suprama Datta, Nicholas P McCurtin, Hannah Z Kimball, Molly C Kingsley, Abraham L Bayer, Alexander C Martin, Qianni Peng, Eranthie Weerapana, Rebecca A Scheck

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

Article in Angewandte Chemie (International ed. in English), 2024. 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
0.7field-weighted citation impact, top 33% 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, 3 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

10 authors at 2 institutions in 1 country.

Caitlin J HillDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0001-8772-5044
Suprama DattaDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0003-1157-0490
Nicholas P McCurtinDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0002-4560-978X
Hannah Z KimballDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0009-0000-0300-9025
Molly C KingsleyDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0002-5921-3743
Abraham L BayerDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0001-7534-6354
Alexander C MartinDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.
Qianni PengDepartment of Chemistry, Boston College, Chestnut Hill, MA 02467, USA.
Eranthie WeerapanaDepartment of Chemistry, Boston College, Chestnut Hill, MA 02467, USA.ORCID 0000-0002-0835-8301
Rebecca A ScheckDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0003-0916-0572
Tufts University · USBoston College · US

Funding

A chemical strategy to unravel tumor suppression through the ubiquitin pathwayR01GM134097 · NIGMS · TUFTS UNIVERSITY MEDFORD · PI SCHECK, REBECCA · 2019 to 2023
$1.5M
NIGMS NIH HHS R01 GM134097NIGMS NIH HHS R01GM134097
6 · The paper itself

Abstract

A cascade of three enzymes, E1-E2-E3, is responsible for transferring ubiquitin to target proteins, which controls many different aspects of cellular signaling. The role of the E2 has been largely overlooked, despite influencing substrate identity, chain multiplicity, and topology. Here we report a method-targeted charging of ubiquitin to E2 (tCUbE)-that can track a tagged ubiquitin through its entire enzymatic cascade in living mammalian cells. We use this approach to reveal new targets whose ubiquitination depends on UbcH5a E2 activity. We demonstrate that tCUbE can be broadly applied to multiple E2s and in different human cell lines. tCUbE is uniquely suited to examine E2-E3-substrate cascades of interest and/or piece together previously unidentified cascades, thereby illuminating entire branches of the UPS and providing critical insight that will be useful for identifying new therapeutic targets in the UPS.

Indexed as

UbiquitinUbiquitin-Conjugating EnzymesAnimalsHumansMammalsUbiquitinationUbiquitin-Protein LigasesUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligaseschemical methodsconditional protein splicingpost-translational modificationsprotein profilingubiquitin proteasome system

Identifiers

PMID38291002
PMCPMC11606432
OpenAlexW4391399877

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.