Evidence map›Paper›PMID 20639865›Full record

ArticleNature biotechnology2010

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

Guoqiang Xu, Jeremy S Paige, Samie R Jaffrey

Open access · greenAbstract read
In one paragraph

Article in Nature biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 295 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
295citing papers in PubMed, 1 pooled it
14.1field-weighted citation impact, top 1% 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

295 citing papers in PubMed, 1 synthesis or guideline pooled it, 541 citations in OpenAlex.

  1. Pooled it
  2. Review
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  12. Article
  13. Computational Pipelines for Protein Ubiquitylation Analysis and Prediction.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. The functional landscape of the human ubiquitinome.bioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Article

235 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Guoqiang XuDepartment of Pharmacology, Weill Medical College, Cornell University, New York, New York, USA.
Jeremy S Paige
Samie R Jaffrey
Cornell University · US

Funding

CANCER PHARMACOLOGYT32CA062948 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI LORRAINE J GUDAS · 1994 to 2026
$12.1M
QqTOF Hybrid Mass SpectrometerS10RR022615 · NCRR · WEILL MEDICAL COLL OF CORNELL UNIV · PI GROSS, STEVEN S · 2007 to 2007
$470k
MASS SPECTROMETRY SYST: RETINOID &CANCERS10RR019355 · NCRR · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI GROSS, STEVEN S · 2004 to 2004
$452k
Comprehensive profiling of ubiquitination in neuronsR21MH086128 · NIMH · WEILL MEDICAL COLL OF CORNELL UNIV · PI JAFFREY, SAMIE R · 2010 to 2011
$420k
NCI NIH HHS T32 CA062948NCI NIH HHS T32CA062948NCRR NIH HHS RR19355NCRR NIH HHS RR22615NCRR NIH HHS S10 RR019355NCRR NIH HHS S10 RR022615NIMH NIH HHS MH086128NIMH NIH HHS R21 MH086128
6 · The paper itself

Abstract

Protein ubiquitination is a post-translational modification (PTM) that regulates various aspects of protein function by different mechanisms. Characterization of ubiquitination has lagged behind that of smaller PTMs, such as phosphorylation, largely because of the difficulty of isolating and identifying peptides derived from the ubiquitinated portion of proteins. To address this issue, we generated a monoclonal antibody that enriches for peptides containing lysine residues modified by diglycine, an adduct left at sites of ubiquitination after trypsin digestion. We use mass spectrometry to identify 374 diglycine-modified lysines on 236 ubiquitinated proteins from HEK293 cells, including 80 proteins containing multiple sites of ubiquitination. Seventy-two percent of these proteins and 92% of the ubiquitination sites do not appear to have been reported previously. Ubiquitin remnant profiling of the multi-ubiquitinated proteins proliferating cell nuclear antigen (PCNA) and tubulin alpha-1A reveals differential regulation of ubiquitination at specific sites by microtubule inhibitors, demonstrating the effectiveness of our method to characterize the dynamics of lysine ubiquitination.

Indexed as

Amino Acid SequenceChromatography, AffinityHEK293 CellsHumansKidneyLysineMass SpectrometryMolecular Sequence DataProliferating Cell Nuclear AntigenProtein Processing, Post-TranslationalTubulinUbiquitinUbiquitinated ProteinsUbiquitinationLysineProliferating Cell Nuclear AntigenTubulinUbiquitinUbiquitinated Proteins

Identifiers

PMID20639865
PMCPMC2946519
OpenAlexW2061184183

What OpenQuestion holds

Textmetadata
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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.