Evidence map›Paper›PMID 31408259›Full record

ReviewProteomics2020

Accumulation of "Old Proteins" and the Critical Need for MS-based Protein Turnover Measurements in Aging and Longevity.

Nathan Basisty, Anja Holtz, Birgit Schilling

Abstract readReview
In one paragraph

Review in Proteomics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Combined Effect of Silybin and Sodium Acetylated Hyaluronate on UV-Induced Photoaging.Skin research and technology : official journal of International Society for Bioengineering and the Skin (ISBS) [and] International Society for Digital Imaging of Skin (ISDIS) [and] International Society for Skin Imaging (ISSI) · 2026
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  20. The Emerging Role of Senescence in Ocular Disease.Oxidative medicine and cellular longevity · 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

3 authors.

Nathan BasistyThe Buck Institute for Research on Aging, Novato, CA, USA.ORCID 0000-0001-6173-1139
Anja HoltzThe Buck Institute for Research on Aging, Novato, CA, USA.ORCID 0000-0001-9856-002X
Birgit SchillingThe Buck Institute for Research on Aging, Novato, CA, USA.ORCID 0000-0001-9907-2749

Funding

Molecular pathogenesis of skeletal muscle atrophyR01AR071762 · NIAMS · UNIVERSITY OF IOWA · PI ADAMS, CHRISTOPHER M · 2017 to 2021
$2.4M
Molecular Mechanisms of Age-related Muscle LossI01BX000976 · VA · IOWA CITY VA MEDICAL CENTER · PI YOREK, MARK A. · 2012 to 2022
–
BLRD VA I01 BX000976NIAMS NIH HHS R01 AR071762
6 · The paper itself

Abstract

Aging and age-related diseases are accompanied by proteome remodeling and progressive declines in cellular machinery required to maintain protein homeostasis (proteostasis), such as autophagy, ubiquitin-mediated degradation, and protein synthesis. While many studies have focused on capturing changes in proteostasis, the identification of proteins that evade these cellular processes has recently emerged as an approach to studying the aging proteome. With advances in proteomic technology, it is possible to monitor protein half-lives and protein turnover at the level of individual proteins in vivo. For large-scale studies, these technologies typically include the use of stable isotope labeling coupled with MS and comprehensive assessment of protein turnover rates. Protein turnover studies have revealed groups of highly relevant long-lived proteins (LLPs), such as the nuclear pore complexes, extracellular matrix proteins, and protein aggregates. Here, the role of LLPs during aging and age-related diseases and the methods used to identify and quantify their changes are reviewed. The methods available to conduct studies of protein turnover, used in combination with traditional proteomic methods, will enable the field to perform studies in a systems biology context, as changes in proteostasis may not be revealed in studies that solely measure differential protein abundances.

Indexed as

AgingProteostasisAnimalsHumansLongevityMass SpectrometryProtein AggregatesProteinsProteolysisProteomicsProtein AggregatesProteinsaginglong-lived proteinsmass spectrometryprotein turnoverproteostasis

Identifiers

PMID31408259
PMCPMC7015777

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.