Evidence map›Paper›PMID 26077900›Full record

ArticleMolecular & cellular proteomics : MCP2015

Comprehensive Temporal Protein Dynamics during the Diauxic Shift in Saccharomyces cerevisiae.

J Patrick Murphy, Ekaterina Stepanova, Robert A Everley, Joao A Paulo, Steven P Gygi

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 98 citations in OpenAlex.

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  20. Quiescence inAnnual review of genetics · 2022
    Review

3 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

5 authors at 1 institution in 1 country.

J Patrick MurphyFrom the ‡Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115.
Ekaterina StepanovaFrom the ‡Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115.
Robert A EverleyFrom the ‡Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115.
Joao A PauloFrom the ‡Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115.
Steven P GygiFrom the ‡Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115 sgygi@hms.harvard.edu.
Harvard University · US

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
Resolving the role of nicotine-mediated phosphorylation on pancreatic fibrosisK01DK098285 · NIDDK · HARVARD MEDICAL SCHOOL · PI PAULO, JOAO A · 2013 to 2017
$638k
NIDDK NIH HHS K01 DK098285NIGMS NIH HHS R01 GM067945
6 · The paper itself

Abstract

Yeast (Saccharomyces cerevisiae) has served as a key model system in biology and as a benchmark for "omics" technology. Although near-complete proteomes of log phase yeast have been measured, protein abundance in yeast is dynamic, particularly during the transition from log to stationary phase. Defining the dynamics of proteomic changes during this transition, termed the diauxic shift, is important to understand the basic biology of proliferative versus quiescent cells. Here, we perform temporal quantitative proteomics to fully capture protein induction and repression during the diauxic shift. Accurate and sensitive quantitation at a high temporal resolution and depth of proteome coverage was achieved using TMT10 reagents and LC-MS3 analysis on an Orbitrap Fusion tribrid mass spectrometer deploying synchronous precursor selection. Triplicate experiments were analyzed using the time-course R package and a simple template matching strategy was used to reveal groups of proteins with similar temporal patterns of protein induction and repression. Within these groups are functionally distinct types of proteins such as those of glyoxylate metabolism and many proteins of unknown function not previously associated with the diauxic shift (e.g. YNR034W-A and FMP16). We also perform a dual time-course experiment to determine Hap2-dependent proteins during the diauxic shift. These data serve as an important basic model for fermentative versus respiratory growth of yeast and other eukaryotes and are a benchmark for temporal quantitative proteomics.

Indexed as

Chromatography, LiquidGene Expression Regulation, FungalMass SpectrometryProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID26077900
PMCPMC4563728
OpenAlexW2212431290

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.