Evidence map›Paper›PMID 34043369›Full record

ArticleJournal of proteome research2021

A Compendium of Murine (Phospho)Peptides Encompassing Different Isobaric Labeling and Data Acquisition Strategies.

Olesja Popow, Xinyue Liu, Kevin M Haigis, Steven P Gygi, Joao A Paulo

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

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  4. FeJournal of proteomics · 2022
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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

5 authors at 1 institution in 1 country.

Olesja PopowDepartment of Cancer Biology, Dana-Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts 02115, United States.
Xinyue LiuDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, United States.
Kevin M HaigisDepartment of Cancer Biology, Dana-Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts 02115, United States.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, United States.ORCID 0000-0001-7626-0034
Joao A PauloDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, United States.ORCID 0000-0002-4291-413X
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
Advancing Multiplexed Isobaric Tag-based Strategies for Proteome ProfilingR01GM132129 · NIGMS · HARVARD MEDICAL SCHOOL · PI PAULO, JOAO A · 2019 to 2023
$1.7M
Cancer Research UK 27144NIGMS NIH HHS R01 GM067945NIGMS NIH HHS R01 GM132129
6 · The paper itself

Abstract

Targeted mass spectrometry-based assays typically rely on previously acquired large data sets for peptide target selection. Such repositories are widely available for unlabeled peptides. However, they are less common for isobaric tagged peptides. Here we have assembled two series of six data sets originating from a mouse embryonic fibroblast cell line (NIH/3T3). One series is of peptides derived from a tryptic digest of a whole cell proteome and a second from enriched phosphopeptides. These data sets encompass three labeling approaches (unlabeled, TMT11-labeled, and TMTpro16-labeled) and two data acquisition strategies (ion trap MS2 with and without FAIMS-based gas phase separation). We identified a total of 1 509 526 peptide-spectrum matches which covered 11 482 proteins from the whole cell proteome tryptic digest, and 188 849 phosphopeptides from the phosphopeptide enrichment. The data sets were of similar depth, and while overlap across data sets was modest, protein overlap was high, thus reinforcing the comprehensiveness of these data sets. The data also supported FAIMS as a means to increase data set depth. These data sets provide a rich resource of peptides that may be used as starting points for targeted assays. Future data sets may be compiled for any genome-sequenced organism using the technologies and strategies highlighted herein. The data have been deposited in the ProteomeXchange Consortium with data set identifier PXD024298.

Indexed as

FibroblastsProteomicsAnimalsApoptosis Regulatory ProteinsMass SpectrometryMicePhosphopeptidesProteomeApoptosis Regulatory ProteinsFaim protein, mousePhosphopeptidesProteome3T3eclipseFAIMStargeted proteomicsTMTTMTpro

Identifiers

PMID34043369
PMCPMC8254770
OpenAlexW3165738623

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.