Evidence map›Paper›PMID 33556866›Full record

ReviewMolecular & cellular proteomics : MCP2021

Proteome Turnover in the Spotlight: Approaches, Applications, and Perspectives.

Alison Barbara Ross, Julian David Langer, Marko Jovanovic

Abstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing 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

90 citing papers in PubMed.

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  9. Age-based approach to characterize the dynamics of cellular processes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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30 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.

Alison Barbara RossDepartment of Biological Sciences, Columbia University, New York, New York, USA.
Julian David LangerProteomics, Max Planck Institute of Biophysics, Frankfurt am Main, Germany; Proteomics, Max Planck Institute for Brain Research, Frankfurt am Main, Germany. Electronic address: julian.langer@biophys.mpg.de.
Marko JovanovicDepartment of Biological Sciences, Columbia University, New York, New York, USA. Electronic address: mj2794@columbia.edu.

Funding

Regulation of Protein Production Dynamics:RNA Binding Proteins and the Ribosome CodeR35GM128802 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI JOVANOVIC, MARKO · 2018 to 2022
$2.3M
NIGMS NIH HHS R35 GM128802
6 · The paper itself

Abstract

In all cells, proteins are continuously synthesized and degraded to maintain protein homeostasis and modify gene expression levels in response to stimuli. Collectively, the processes of protein synthesis and degradation are referred to as protein turnover. At a steady state, protein turnover is constant to maintain protein homeostasis, but in dynamic responses, proteins change their rates of synthesis and degradation to adjust their proteomes to internal or external stimuli. Thus, probing the kinetics and dynamics of protein turnover lends insight into how cells regulate essential processes such as growth, differentiation, and stress response. Here, we outline historical and current approaches to measuring the kinetics of protein turnover on a proteome-wide scale in both steady-state and dynamic systems, with an emphasis on metabolic tracing using stable isotope-labeled amino acids. We highlight important considerations for designing proteome turnover experiments, key biological findings regarding the conserved principles of proteome turnover regulation, and future perspectives for both technological and biological investigation.

Indexed as

ProteomeAmino AcidsAnimalsHumansIsotope LabelingLightPharmaceutical PreparationsProteomicsRadioisotopesAmino AcidsPharmaceutical PreparationsProteomeRadioisotopesDynamic SILACMass spectrometryProtein degradationProtein synthesisProteome turnoverProteomicspSILAC

Identifiers

PMID33556866
PMCPMC7950106

What OpenQuestion holds

Textmetadata
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.