Evidence map›Paper›PMID 21472564›Full record

ArticleJournal of the American Society for Mass Spectrometry2011

Label-free proteomic identification of endogenous, insulin-stimulated interaction partners of insulin receptor substrate-1.

Thangiah Geetha, Paul Langlais, Moulun Luo, Rebekka Mapes, Natalie Lefort, Shu-Chuan Chen, Lawrence J Mandarino, Zhengping Yi

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

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  7. Skeletal muscle DNA methylation modifications and psychopharmacologic treatment in bipolar disorder.European neuropsychopharmacology : the journal of the European College of Neuropsychopharmacology · 2019
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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

8 authors at 1 institution in 1 country.

Thangiah GeethaCenter for Metabolic and Vascular Biology, Arizona State University, Tempe, AZ, USA.
Paul Langlais
Moulun Luo
Rebekka Mapes
Natalie Lefort
Shu-Chuan Chen
Lawrence J Mandarino
Zhengping Yi
Arizona State University · US

Funding

MOLECULAR REGULATION OF MUSCLE GLUCOSE METABOLISM IN MANR01DK047936 · NIDDK · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI MANDARINO, LAWRENCE J · 1994 to 2022
$10.7M
Human Skeletal Muscle Proteome and Phosphoproteome in Obesity and Type 2 DiabetesR01DK081750 · NIDDK · WAYNE STATE UNIVERSITY · PI YI, ZHENGPING · 2009 to 2017
$3.0M
NIDDK NIH HHS R01 DK047936NIDDK NIH HHS R01 DK081750NIDDK NIH HHS R01DK081750NIDDK NIH HHS R01DK47936
6 · The paper itself

Abstract

Protein-protein interactions are key to most cellular processes. Tandem mass spectrometry (MS/MS)-based proteomics combined with co-immunoprecipitation (CO-IP) has emerged as a powerful approach for studying protein complexes. However, a majority of systematic proteomics studies on protein-protein interactions involve the use of protein overexpression and/or epitope-tagged bait proteins, which might affect binding stoichiometry and lead to higher false positives. Here, we report an application of a straightforward, label-free CO-IP-MS/MS method, without the use of protein overexpression or protein tags, to the investigation of changes in the abundance of endogenous proteins associated with a bait protein, which is in this case insulin receptor substrate-1 (IRS-1), under basal and insulin stimulated conditions. IRS-1 plays a central role in the insulin signaling cascade. Defects in the protein-protein interactions involving IRS-1 may lead to the development of insulin resistance and type 2 diabetes. HPLC-ESI-MS/MS analyses identified eleven novel endogenous insulin-stimulated IRS-1 interaction partners in L6 myotubes reproducibly, including proteins play an important role in protein dephosphorylation [protein phosphatase 1 regulatory subunit 12A, (PPP1R12A)], muscle contraction and actin cytoskeleton rearrangement, endoplasmic reticulum stress, and protein folding, as well as protein synthesis. This novel application of label-free CO-IP-MS/MS quantification to assess endogenous interaction partners of a specific protein will prove useful for understanding how various cell stimuli regulate insulin signal transduction.

Indexed as

AnimalsCells, CulturedChromatography, High Pressure LiquidInsulin Receptor Substrate ProteinsPeptide FragmentsPhosphorylationProtein Interaction MappingProteomicsRatsSpectrometry, Mass, Electrospray IonizationStatistics, NonparametricTandem Mass SpectrometryInsulin Receptor Substrate ProteinsPeptide Fragments

Identifiers

PMID21472564
PMCPMC3072570
OpenAlexW2082944928

What OpenQuestion holds

Textmetadata
LicenceTDM
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.