Evidence map›Paper›PMID 25117199›Full record

ArticleJournal of proteome research2014

Direct detection of biotinylated proteins by mass spectrometry.

Lucio Matias Schiapparelli, Daniel B McClatchy, Han-Hsuan Liu, Pranav Sharma, John R Yates, Hollis T Cline

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
3.6field-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

80 citing papers in PubMed, 132 citations in OpenAlex.

  1. Bioorthogonal Chemistry in Neurobiology: From Imaging to Proteomics.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
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20 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

6 authors at 1 institution in 1 country.

Lucio Matias SchiapparelliThe Dorris Neuroscience Center, Department of Molecular and Cellular Neuroscience, ‡Department of Chemical Physiology, and §Kellogg School of Science and Technology, The Scripps Research Institute , La Jolla, California 92037, United States.
Daniel B McClatchy
Han-Hsuan Liu
Pranav Sharma
John R Yates
Hollis T Cline
Scripps Research Institute · US

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Quantitative Proteome Analysis of Brain DevelopmentR01MH067880 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI YATES III, JOHN R · 2003 to 2017
$7.1M
NIH Director's Pioneer Award (RMI)DP1OD000458 · OD · SCRIPPS RESEARCH INSTITUTE, THE · PI CLINE, HOLLIS T. · 2005 to 2009
$4.4M
Trans-Synaptic Transport of Endogenous Proteins to Label CircuitsR01MH091676 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI CLINE, HOLLIS T. · 2010 to 2013
$1.5M
Analysis of the Dynamic Synaptic ProteomeR21MH099799 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI CLINE, HOLLIS T. · 2012 to 2013
$512k
NHLBI NIH HHS HHSN268201000035CNIGMS NIH HHS P41 GM103533NIH HHS DP1 OD000458NIH HHS OD000458NIMH NIH HHS MH067880NIMH NIH HHS MH091676NIMH NIH HHS MH099799NIMH NIH HHS R01 MH067880NIMH NIH HHS R01 MH091676NIMH NIH HHS R21 MH099799
6 · The paper itself

Abstract

Mass spectrometric strategies to identify protein subpopulations involved in specific biological functions rely on covalently tagging biotin to proteins using various chemical modification methods. The biotin tag is primarily used for enrichment of the targeted subpopulation for subsequent mass spectrometry (MS) analysis. A limitation of these strategies is that MS analysis does not easily discriminate unlabeled contaminants from the labeled protein subpopulation under study. To solve this problem, we developed a flexible method that only relies on direct MS detection of biotin-tagged proteins called "Direct Detection of Biotin-containing Tags" (DiDBiT). Compared with conventional targeted proteomic strategies, DiDBiT improves direct detection of biotinylated proteins ∼200 fold. We show that DiDBiT is applicable to several protein labeling protocols in cell culture and in vivo using cell permeable NHS-biotin and incorporation of the noncanonical amino acid, azidohomoalanine (AHA), into newly synthesized proteins, followed by click chemistry tagging with biotin. We demonstrate that DiDBiT improves the direct detection of biotin-tagged newly synthesized peptides more than 20-fold compared to conventional methods. With the increased sensitivity afforded by DiDBiT, we demonstrate the MS detection of newly synthesized proteins labeled in vivo in the rodent nervous system with unprecedented temporal resolution as short as 3 h.

Indexed as

AnimalsBiotinHEK293 CellsHumansMaleProteinsProteomeProteomicsRatsRats, WistarSuccinimidesTandem Mass SpectrometryBiotinbiotinyl N-hydroxysuccinimide esterProteinsProteomeSuccinimides

Identifiers

PMID25117199
PMCPMC4156236
OpenAlexW1175020023

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.