Evidence map›Paper›PMID 31186290›Full record

ArticleMolecular & cellular proteomics : MCP2019

A Label-free Mass Spectrometry Method to Predict Endogenous Protein Complex Composition.

Zachary McBride, Donglai Chen, Youngwoo Lee, Uma K Aryal, Jun Xie, Daniel B Szymanski

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 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 1 institution in 1 country.

Zachary McBride‡Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana.
Donglai Chen§Department of Statistics, Purdue University, West Lafayette, Indiana.
Youngwoo Lee‡Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana.
Uma K Aryal¶Purdue Proteomics Facility, Bindley Biosciences Center, Discovery Park, Purdue University, West Lafayette, Indiana.
Jun Xie§Department of Statistics, Purdue University, West Lafayette, Indiana.
Daniel B Szymanski‡Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana; ‖Department of Biological Sciences,Purdue University, West Lafayette, Indiana. Electronic address: dszyman@purdue.edu.
Purdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Information on the composition of protein complexes can accelerate mechanistic analyses of cellular systems. Protein complex composition identifies genes that function together and provides clues about regulation within and between cellular pathways. Cytosolic protein complexes control metabolic flux, signal transduction, protein abundance, and the activities of cytoskeletal and endomembrane systems. It has been estimated that one third of all cytosolic proteins in leaves exist in an oligomeric state, yet the composition of nearly all remain unknown. Subunits of stable protein complexes copurify, and combinations of mass-spectrometry-based protein correlation profiling and bioinformatic analyses have been used to predict protein complex subunits. Because of uncertainty regarding the power or availability of bioinformatic data to inform protein complex predictions across diverse species, it would be highly advantageous to predict composition based on elution profile data alone. Here we describe a mass spectrometry-based protein correlation profiling approach to predict the composition of hundreds of protein complexes based on biochemical data. Extracts were obtained from an intact organ and separated in parallel by size and charge under nondenaturing conditions. More than 1000 proteins with reproducible elution profiles across all replicates were subjected to clustering analyses. The resulting dendrograms were used to predict the composition of known and novel protein complexes, including many that are likely to assemble through self-interaction. An array of validation experiments demonstrated that this new method can drive protein complex discovery, guide hypothesis testing, and enable systems-level analyses of protein complex dynamics in any organism with a sequenced genome.

Indexed as

ArabidopsisArabidopsis ProteinsMass SpectrometryPlant LeavesProteomicsArabidopsis ProteinsArabidopsisLabel-free quantificationMacromolecular complex analysisPlant Biology*Protein complex analysisProtein correlation profiling

Identifiers

PMID31186290
PMCPMC6683005
OpenAlexW2949606885

What OpenQuestion holds

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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.