Evidence map›Paper›PMID 22729469›Full record

ReviewMolecular & cellular proteomics : MCP2012

Characterizing ubiquitination sites by peptide-based immunoaffinity enrichment.

Daisy Bustos, Corey E Bakalarski, Yanling Yang, Junmin Peng, Donald S Kirkpatrick

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  5. A ubiquitin language communicates ribosomal distress.Seminars in cell & developmental biology · 2024
    Review
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  14. Site-specific ubiquitination of pathogenic huntingtin attenuates its deleterious effects.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

5 authors at 2 institutions in 1 country.

Daisy BustosDepartment of Protein Chemistry, Genentech, Inc., South San Francisco, California 94080, USA.
Corey E Bakalarski
Yanling Yang
Junmin Peng
Donald S Kirkpatrick
St. Jude Children's Research Hospital · USGenentech

Funding

Analysis of Ubiquitinated ProteomeR21RR025822 · NCRR · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI PENG, JUNMIN · 2009 to 2010
$581k
NCRR NIH HHS R21 RR025822NCRR NIH HHS RR025822
6 · The paper itself

Abstract

Advances in high resolution tandem mass spectrometry and peptide enrichment technologies have transformed the field of protein biochemistry by enabling analysis of end points that have traditionally been inaccessible to molecular and biochemical techniques. One field benefitting from this research has been the study of ubiquitin, a 76-amino acid protein that functions as a covalent modifier of other proteins. Seminal work performed decades ago revealed that trypsin digestion of a branched protein structure known as A24 yielded an enigmatic diglycine signature bound to a lysine residue in histone 2A. With the onset of mass spectrometry proteomics, identification of K-GG-modified peptides has emerged as an effective way to map the position of ubiquitin modifications on a protein of interest and to quantify the extent of substrate ubiquitination. The initial identification of K-GG peptides by mass spectrometry initiated a flurry of work aimed at enriching these post-translationally modified peptides for identification and quantification en masse. Recently, immunoaffinity reagents have been reported that are capable of capturing K-GG peptides from ubiquitin and its thousands of cellular substrates. Here we focus on the history of K-GG peptides, their identification by mass spectrometry, and the utility of immunoaffinity reagents for studying the mechanisms of cellular regulation by ubiquitin.

Indexed as

UbiquitinationGlycylglycinePeptidesProteinsProteomicsTandem Mass SpectrometryUbiquitinUbiquitinated ProteinsGlycylglycinePeptidesProteinsUbiquitinUbiquitinated Proteins

Identifiers

PMID22729469
PMCPMC3518114
OpenAlexW2018141733

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.