Evidence map›Paper›PMID 27765818›Full record

ArticleMolecular & cellular proteomics : MCP2016

Time-resolved Analysis of Proteome Dynamics by Tandem Mass Tags and Stable Isotope Labeling in Cell Culture (TMT-SILAC) Hyperplexing.

Kevin A Welle, Tian Zhang, Jennifer R Hryhorenko, Shichen Shen, Jun Qu, Sina Ghaemmaghami

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.9field-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

54 citing papers in PubMed, 102 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Kevin A WelleFrom the ‡University of Rochester Mass Spectrometry Resource Laboratory, Rochester, NY.
Tian Zhang§Department of Biology, University of Rochester, Rochester, NY.
Jennifer R HryhorenkoFrom the ‡University of Rochester Mass Spectrometry Resource Laboratory, Rochester, NY.
Shichen Shen¶Department of Pharmaceutical Sciences, University at Buffalo, Buffalo, NY.
Jun Qu¶Department of Pharmaceutical Sciences, University at Buffalo, Buffalo, NY.
Sina GhaemmaghamiFrom the ‡University of Rochester Mass Spectrometry Resource Laboratory, Rochester, NY; sghaemma@bio.rochester.edu.
University of Rochester · USUniversity at Buffalo, State University of New York · US

Funding

University of Buffalo Clinical and Translational Science Institute - Supplement SchulyerUL1TR001412 · NCATS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI MURPHY, TIMOTHY F · 2015 to 2024
$33.8M
The prevalence and mechanism of selectivity in basal autophagyR35GM119502 · NIGMS · UNIVERSITY OF ROCHESTER · PI SINA GHAEMMAGHAMI · 2016 to 2026
$5.9M
QExactive for UR Proteomics ResearchS10OD021486 · OD · UNIVERSITY OF ROCHESTER · PI GHAEMMAGHAMI, SINA · 2016 to 2016
$309k
NCATS NIH HHS UL1 TR001412NIGMS NIH HHS R35 GM119502NIH HHS S10 OD021486
6 · The paper itself

Abstract

Recent advances in mass spectrometry have enabled system-wide analyses of protein turnover. By globally quantifying the kinetics of protein clearance and synthesis, these methodologies can provide important insights into the regulation of the proteome under varying cellular and environmental conditions. To facilitate such analyses, we have employed a methodology that combines metabolic isotopic labeling (Stable Isotope Labeling in Cell Culture - SILAC) with isobaric tagging (Tandem Mass Tags - TMT) for analysis of multiplexed samples. The fractional labeling of multiple time-points can be measured in a single mass spectrometry run, providing temporally resolved measurements of protein turnover kinetics. To demonstrate the feasibility of the approach, we simultaneously measured the kinetics of protein clearance and accumulation for more than 3000 proteins in dividing and quiescent human fibroblasts and verified the accuracy of the measurements by comparison to established non-multiplexed approaches. The results indicate that upon reaching quiescence, fibroblasts compensate for lack of cellular growth by globally downregulating protein synthesis and upregulating protein degradation. The described methodology significantly reduces the cost and complexity of temporally-resolved dynamic proteomic experiments and improves the precision of proteome-wide turnover data.

Indexed as

Cell Culture TechniquesCell DivisionCells, CulturedFibroblastsHumansIsotope LabelingKineticsProteomeProteomicsTandem Mass SpectrometryProteome

Identifiers

PMID27765818
PMCPMC5141271
OpenAlexW2538451428

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.