Evidence map›Paper›PMID 28887381›Full record

ArticleMolecular & cellular proteomics : MCP2017

Global Analysis of Membrane-associated Protein Oligomerization Using Protein Correlation Profiling.

Zachary McBride, Donglai Chen, Christy Reick, Jun Xie, Daniel B Szymanski

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. PMF proteins mediate mitochondrial fusion in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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 2 institutions in 1 country.

Zachary McBride‡Department of Biological Sciences, Purdue University, West Lafayette, Indiana.
Donglai Chen§Department of Statistics, Purdue University, West Lafayette, Indiana.
Christy Reick¶College of Osteopathic Medicine, Marian University, Indianapolis.
Jun Xie§Department of Statistics, Purdue University, West Lafayette, Indiana.
Daniel B Szymanski‡Department of Biological Sciences, Purdue University, West Lafayette, Indiana; dszyman@purdue.edu.
Purdue University West Lafayette · USMarian University - Indiana · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane-associated proteins are required for essential processes like transport, organelle biogenesis, and signaling. Many are expected to function as part of an oligomeric protein complex. However, membrane-associated proteins are challenging to work with, and large-scale data sets on the oligomerization state of this important class of proteins is missing. Here we combined cell fractionation of Arabidopsis leaves with nondenaturing detergent solubilization and LC/MS-based profiling of size exclusion chromatography fractions to measure the apparent masses of >1350 membrane-associated proteins. Our method identified proteins from all of the major organelles, with more than 50% of them predicted to be part of a stable complex. The plasma membrane was the most highly enriched in large protein complexes compared with other organelles. Hundreds of novel protein complexes were identified. Over 150 proteins had a complicated localization pattern, and were clearly partitioned between cytosolic and membrane-associated pools. A subset of these dual localized proteins had oligomerization states that differed based on localization. Our data set is an important resource for the community that includes new functionally relevant data for membrane-localized protein complexes that could not be predicted based on sequence alone. Our method enables the analysis of protein complex localization and dynamics, and is a first step in the development of a method in which LC/MS profile data can be used to predict the composition of membrane-associated protein complexes.

Indexed as

ArabidopsisArabidopsis ProteinsCell FractionationCytosolGas Chromatography-Mass SpectrometryMembrane ProteinsPlant LeavesProtein MultimerizationProteomicsArabidopsis ProteinsMembrane Proteins

Identifiers

PMID28887381
PMCPMC5672003
OpenAlexW2751684792

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.