Evidence map›Paper›PMID 21081186›Full record

ArticleJournal of proteomics2011

The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

Jun Zhong, Raghothama Chaerkady, Kumaran Kandasamy, Marjan Gucek, Robert N Cole, Akhilesh Pandey

Open access · greenAbstract read
In one paragraph

Article in Journal of proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

  1. A Scalable Design for Proximity-Inducing Molecules.bioRxiv : the preprint server for biology · 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

6 authors at 2 institutions in 2 countries.

Jun ZhongMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University, Baltimore, Maryland 21205, USA.
Raghothama Chaerkady
Kumaran Kandasamy
Marjan Gucek
Robert N Cole
Akhilesh Pandey
Johns Hopkins University · USInstitute of Bioinformatics · IN

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Proteomics CoreZICHL005903 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI GUCEK, MARJAN · 2009 to 2022
$23.3M
Networks, Pathways and Dynamics of Lysine ModificationU54GM103520 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BADER, JOEL S. · 2012 to 2013
$7.0M
Purchase of a Linear Ion Trap/Fourier Transform Mass SpectrometerS10RR023025 · NCRR · JOHNS HOPKINS UNIVERSITY · PI COTTER, ROBERT JAMES · 2007 to 2007
$928k
NHLBI PROTEOMICS INITIATIVE-N01HV28180-268028180-268028180N01HV028180 · HV · JOHNS HOPKINS UNIVERSITY · PI VAN EYK, JENNIFER E · 2002 to 2006
–
NCRR NIH HHS S10 RR023025NCRR NIH HHS S10RR023025NCRR NIH HHS U54 RR 020839NCRR NIH HHS U54 RR020839NHLBI NIH HHS N01 HV028180NHLBI NIH HHS N01-HV-28180NIGMS NIH HHS U54 GM103520
6 · The paper itself

Abstract

Signal transduction pathways are tightly controlled by positive and negative regulators. We have previously identified Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; gene symbol ANKS1A) as a negative regulator of growth factor signaling; however, the mechanisms through which Odin regulates these pathways remain to be elucidated. To determine how Odin negatively regulates growth factor signaling, we undertook a proteomic approach to systematically identify proteins that interact with Odin using the SILAC strategy. In this study, we identified 18 molecules that were specifically associated in a protein complex with Odin. Our study established that the complete family of 14-3-3 proteins occur in a protein complex with Odin, which is also supported by earlier reports that identified a few members of the 14-3-3 family as Odin interactors. Among the novel protein interactors of Odin were CD2-associated protein, SH3 domain kinase binding protein 1 and DAB2 interacting protein. We confirmed 8 of the eighteen interactions identified in the Odin protein complex by co-immunoprecipitation experiments. Finally, a literature-based network analysis revealed that Odin interacting partners are involved in various cellular processes, some of which are key molecules in regulating receptor endocytosis.

Indexed as

Protein Structure, TertiaryAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCell LineCytoskeletonEndocytosisHumansImmunoprecipitationMass SpectrometryMicePhosphorylationProtein Interaction MappingReceptor Protein-Tyrosine KinasesSwineAdaptor Proteins, Signal TransducingANKS1A protein, humanCarrier ProteinsOdin protein, mouseReceptor Protein-Tyrosine Kinases

Identifiers

PMID21081186
PMCPMC3205450
OpenAlexW1995742979

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.