Evidence map›Paper›PMID 28737031›Full record

ArticleJournal of proteome research2017

Ubiquitin Chain Enrichment Middle-Down Mass Spectrometry (UbiChEM-MS) Reveals Cell-Cycle Dependent Formation of Lys11/Lys48 Branched Ubiquitin Chains.

Ambar S J B Rana, Ying Ge, Eric R Strieter

Abstract read
In one paragraph

Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Review
  2. Review
  3. Proteomic approaches to study ubiquitinomics.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    Review
  4. Quantitative Analysis of Diubiquitin Isomers Using Ion Mobility Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023
    Article
  5. Review
  6. Review
  7. The ubiquitin proteoform problem.Current opinion in chemical biology · 2021
    Review
  8. Review
  9. Tools for Decoding Ubiquitin Signaling in DNA Repair.Frontiers in cell and developmental biology · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Quantitative Middle-Down MS Analysis of Parkin-Mediated Ubiquitin Chain Assembly.Journal of the American Society for Mass Spectrometry · 2020
    Article
  14. Article
  15. Review
  16. Review
  17. Who guards the guardian? Mechanisms that restrain APC/C during the cell cycle.Biochimica et biophysica acta. Molecular cell research · 2018
    Review
  18. Review
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

3 authors.

Ambar S J B RanaDepartment of Chemistry, University of Massachusetts - Amherst , Amherst, Massachusetts 01003, United States.
Ying GeDepartment of Chemistry, University of Wisconsin - Madison , Madison, Wisconsin 53706, United States.ORCID 0000-0001-5211-6812
Eric R StrieterDepartment of Chemistry, University of Massachusetts - Amherst , Amherst, Massachusetts 01003, United States.ORCID 0000-0003-3447-3669

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
Enabling Top-Down Proteomics through Materials Chemistry and NanotechnologyR01GM117058 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING, JIN, SONG · 2015 to 2023
$2.7M
Ultra High Resolution Mass Spectrometer for Biomedical ResearchS10OD018475 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2015 to 2015
$2.0M
NIGMS NIH HHS R01 GM110543NIGMS NIH HHS R01 GM117058NIH HHS S10 OD018475
6 · The paper itself

Abstract

The dynamics of cellular signaling events are tightly regulated by a diverse set of ubiquitin chains. Recent work has suggested that branched ubiquitin chains composed of Lys11 and Lys48 isopeptide linkages play a critical role in regulating cell cycle progression. Yet, endogenous Lys11/Lys48 branched chains could not be detected. By combining a Lys11 linkage specific antibody with high-resolution middle-down mass spectrometry (an approach termed UbiChEM-MS) we sought to identify endogenous Lys11/Lys48 branched ubiquitin chains in cells. Using asynchronous cells, we find that Lys11-linked branched chains can only be detected upon cotreatment with a proteasome and nonselective deubiquitinase inhibitor. Releasing cells from mitotic arrest results in a marked accumulation of Lys11/Lys48 branched chains in which branch points represent ∼3-4% of the total ubiquitin population. This report highlights the utility of UbiChEM-MS in characterizing the architecture of Lys11 Ub chains under various cellular conditions and corroborates the formation of Lys11/Lys48 branched chains during mitosis.

Indexed as

MitosisAmino Acid SequenceAminopyridinesDeubiquitinating EnzymesHEK293 CellsHumansLeupeptinsLysineMass SpectrometryNocodazolePolyubiquitinProteasome Endopeptidase ComplexProteasome InhibitorsThiocyanatesUbiquitin2,6-diaminopyridine-3,5-bis(thiocyanate)Aminopyridinesbenzyloxycarbonylleucyl-leucyl-leucine aldehydeDeubiquitinating EnzymesLeupeptinsLysineNocodazolePolyubiquitinProteasome Endopeptidase ComplexProteasome InhibitorsThiocyanatesUbiquitinbranched ubiquitin chainsmass spectrometrypolyubiquitin chainsUbiChEM-MS

Identifiers

PMID28737031
PMCPMC6036340

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Registered trials

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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.