Evidence map›Paper›PMID 33950494›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Quantification and Identification of Post-Translational Modifications Using Modern Proteomics Approaches.

Anja Holtz, Nathan Basisty, Birgit Schilling

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

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  5. The α-Synuclein Seeding Amplification Assay for Parkinson's Disease.International journal of molecular sciences · 2025
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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

3 authors.

Anja HoltzBuck Institute for Research on Aging, Novato, CA, USA.
Nathan BasistyBuck Institute for Research on Aging, Novato, CA, USA.
Birgit SchillingBuck Institute for Research on Aging, Novato, CA, USA. bschilling@buckinstitute.org.

Funding

REVERSIBLE MITOCHONDRIAL PROTEIN ACETYLATION AND METABOLIC REGULATIONR24DK085610 · NIDDK · J. DAVID GLADSTONE INSTITUTES · PI VERDIN, ERIC M. · 2010 to 2019
$16.0M
Regulation of Peroxisomal Metabolism by Lysine AcylationR01DK090242 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GOETZMAN, ERIC S · 2011 to 2024
$5.4M
Lysine Acetylation in N. gonorrhoeae Quorum Sensing and Biofilm FormationR01AI108255 · NIAID · UNIVERSITY OF IOWA · PI KIRBY, JOHN R, SCHILLING, BIRGIT · 2014 to 2018
$4.1M
TripleTOF 5600 High Resolution Mass SpectrometerS10OD016281 · OD · BUCK INSTITUTE FOR RESEARCH ON AGING · PI GIBSON, BRADFORD WAYNE · 2013 to 2013
$597k
NIAID NIH HHS R01 AI108255NIDDK NIH HHS R01 DK090242NIDDK NIH HHS R24 DK085610NIH HHS S10 OD016281
6 · The paper itself

Abstract

Post-translational modifications (PTMs) occur dynamically, allowing cells to quickly respond to changes in the environment. Lysine residues can be targeted by several modifications including acylations (acetylation, succinylation, malonylation, glutarylation, and others), methylation, ubiquitination, and other modifications. One of the most efficient methods for the identification of post-translational modifications is utilizing immunoaffinity enrichment followed by high-resolution mass spectrometry. This workflow can be coupled with comprehensive data-independent acquisition (DIA) mass spectrometry to be a high-throughput, label-free PTM quantification approach. Below we describe a detailed protocol to process tissue by homogenization and proteolytically digest proteins, followed by immunoaffinity enrichment of lysine-acetylated peptides to identify and quantify relative changes of acetylation comparing different conditions.

Indexed as

Protein Processing, Post-TranslationalProteomicsSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryAcetylationAnimalsChromatography, High Pressure LiquidChromatography, Reverse-PhaseHigh-Throughput Screening AssaysLiverMiceProteinsResearch DesignProteinsAcetylationData-independent acquisitionMass spectrometryPost-translational modificationsQuantification

Identifiers

PMID33950494
PMCPMC8710235

What OpenQuestion holds

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LicenceCC BY
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.