Evidence map›Paper›PMID 30005169›Full record

ReviewExpert review of proteomics2018

Proteomics and pulse azidohomoalanine labeling of newly synthesized proteins: what are the potential applications?

Yuanhui Ma, John R Yates

Abstract readReview
In one paragraph

Review in Expert review of proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. An Enigma of N-termini dependent protein degradation.Biochemistry and biophysics reports · 2025
    Article
  4. Article
  5. Review
  6. Proteomics of the heart.Physiological reviews · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
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

2 authors.

Yuanhui Maa Departments of Molecular Medicine and Neurobiology , The Scripps Research Institute , La Jolla , CA , USA.ORCID 0000-0003-0868-3160
John R Yatesa Departments of Molecular Medicine and Neurobiology , The Scripps Research Institute , La Jolla , CA , USA.ORCID 0000-0001-5267-1672

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI YATES III, JOHN R · 2012 to 2021
$20.7M
Proteogenetics of Autism Spectrum DisordersR01MH100175 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI MUOTRI, ALYSSON R., YATES III, JOHN R · 2013 to 2025
$7.4M
Quantitative Proteome Analysis of Brain DevelopmentR01MH067880 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI YATES III, JOHN R · 2003 to 2017
$7.1M
Proteomic Profiling of CFTR Protein InteractionR01HL079442 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI BALCH, WILLIAM EDWARD, YATES III, JOHN R · 2005 to 2014
$4.6M
The CFTR InteractomeR01HL131697 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI YATES III, JOHN R · 2016 to 2019
$1.9M
Pulse-Chase Labeling with 15N and AHA in an Alzheimer's Mouse ModelR03AG047957 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI YATES III, JOHN R · 2014 to 2015
$281k
NHLBI NIH HHS R01 HL079442NHLBI NIH HHS R01 HL131697NIA NIH HHS R03 AG047957NIGMS NIH HHS P41 GM103533NIMH NIH HHS R01 MH067880NIMH NIH HHS R01 MH100175
6 · The paper itself

Abstract

introductionMeasuring the immediate changes in cells that arise from changing environmental conditions is crucial to understanding the underlying mechanisms involved. These changes can be measured with metabolic stable isotope fully labeled proteomes, but requires looking for changes in the midst of a large background. In addition, labeling efficiency can be an issue in primary and fully differentiated cells. Area covered: Azidohomoalanine (AHA), an analog of methionine, can be accepted by cellular translational machinery and incorporated into newly synthesized proteins (NSPs). AHA-NSPs can be coupled to biotin via CuAAC-mediated click-chemistry and enriched using avidin-based affinity purification. Thus, AHA-containing proteins or peptides can be enriched and efficiently separated from the whole proteome. In this review, we describe the development of mass spectrometry (MS) based AHA strategies and discuss their potential to measure proteins involved in immune response, secretome, gut microbiome, and proteostasis as well as their potential for clinical uses. Expert commentary: AHA strategies have been used to identify synthesis activity and to compare two biological conditions in various biological model organisms. In combination with instrument development, improved sample preparation and fractionation strategies, MS-based AHA strategies have the potential for broad application, and the methods should translate into clinical use.

Indexed as

Isotope LabelingProtein BiosynthesisAlanineAnimalsHumansImmunityMicrobiotaProteomicsProteostasisAlanineazidohomoalanineapplicationAzidohomoalanineBiological studiesnewly synthesized proteinProteomics

Identifiers

PMID30005169
PMCPMC6329588

What OpenQuestion holds

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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.