Evidence map›Paper›PMID 25559986›Full record

ArticleAnalytical chemistry2015

Top-down 193-nm ultraviolet photodissociation mass spectrometry for simultaneous determination of polyubiquitin chain length and topology.

Joe R Cannon, Kirby Martinez-Fonts, Scott A Robotham, Andreas Matouschek, Jennifer S Brodbelt

Abstract read
In one paragraph

Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Mobility-Assisted Pseudo-MSJournal of the American Society for Mass Spectrometry · 2024
    Article
  2. The Ubiquitin Tale: Current Strategies and Future Challenges.ACS pharmacology & translational science · 2024
    Review
  3. Article
  4. Quantitative Analysis of Diubiquitin Isomers Using Ion Mobility Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023
    Article
  5. Review
  6. Article
  7. Article
  8. The ubiquitin proteoform problem.Current opinion in chemical biology · 2021
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Top-Down Analysis of Proteins in Low Charge States.Journal of the American Society for Mass Spectrometry · 2019
    Article
  14. Article
  15. Top-down analysis of novel synthetic branched proteins.Journal of mass spectrometry : JMS · 2019
    Article
  16. Article
  17. Modulation of Protein Fragmentation Through Carbamylation of Primary Amines.Journal of the American Society for Mass Spectrometry · 2017
    Article
  18. SITS Derivatization of Peptides to Enhance 266 nm Ultraviolet Photodissociation (UVPD).Journal of the American Society for Mass Spectrometry · 2017
    Article
  19. Article
  20. Article
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

5 authors.

Joe R CannonDepartment of Chemistry, University of Texas , 105 E. 24th St., Austin, Texas 78712, United States.
Kirby Martinez-Fonts
Scott A Robotham
Andreas Matouschek
Jennifer S Brodbelt

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MARKO, JOHN F · 2009 to 2013
$12.8M
TRAINING PROGRAM IN ONCOGENESIS &DEVELOPMENT BIOLOGYT32CA080621 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI EKLUND, ELIZABETH ANN · 2001 to 2018
$4.1M
Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
IRACDA Postdoctoral Program: Collaborative Opportunities for Research EducatorsK12GM102745 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2013 to 2017
$2.2M
NCI NIH HHS T32 CA080621NCI NIH HHS U54 CA143869NIGMS NIH HHS 1K12GM102745NIGMS NIH HHS K12 GM102745NIGMS NIH HHS R01 GM063004NIGMS NIH HHS U54 GM105816NIGMS NIH HHS U54GM105816
6 · The paper itself

Abstract

Protein ubiquitin modifications present a vexing analytical challenge, because of the dynamic changes in the site of modification on the substrate, the number of ubiquitin moieties attached, and the diversity of linkage patterns in which they are attached. Presented here is a method to confidently assign size and linkage type of polyubiquitin modifications. The method combines intact mass measurement to determine the number of ubiquitin moieties in the chain with backbone fragmentation by 193-nm ultraviolet photodissociation (UVPD) to determine the linkage pattern. UVPD fragmentation of proteins leads to reproducible backbone cleavage at almost every inter-residue position, and in polyubiquitin chains, the N-terminally derived fragments from each constituent monomer are identical, up to the site of conjugation. The N-terminal ubiquitin fragment ions are superimposed to create a diagnostic pattern that allows easy recognition of the dominant chain linkages. The method is demonstrated by achieving almost-complete fragmentation of monoubiquitin and then, subsequently, fragmentation of dimeric, tetrameric, and longer Lys48- and Lys63-linked ubiquitin chains. The utility of the method for the analysis of mixed linkage chains is confirmed for mixtures of Lys48 and Lys63 tetramers with known relative concentrations and for an in vitro-formulated ubiquitin chain attached to a substrate protein.

Indexed as

AnimalsHumansLysineMass SpectrometryMicePhotolysisPolyubiquitinUltraviolet RaysLysinePolyubiquitin

Identifiers

PMID25559986
PMCPMC4318624

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.