Evidence map›Paper›PMID 22190850›Full record

ArticleJournal of biomedicine & biotechnology2011

A high-throughput solid-phase microplate protein-binding assay to investigate interactions between myofilament proteins.

Brandon J Biesiadecki, J-P Jin

Abstract read
In one paragraph

Article in Journal of biomedicine & biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
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  4. X-Ray Exposure Induces Structural Changes in Human Breast Proteins.International journal of molecular sciences · 2025
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  8. Review
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  10. Recombinant actin-depolymerizing factor of the apicomplexanFrontiers in cellular and infection microbiology · 2022
    Article
  11. Article
  12. Article
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  14. Article
  15. Article
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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

2 authors.

Brandon J BiesiadeckiDepartment of Physiology and Cell Biology, The Ohio State University, Columbus, OH 43210, USA. biesiadecki.1@osu.edu
J-P Jin

Funding

Role of Troponin T Isoforms in Nemaline MyopathyR01AR048816 · NIAMS · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING · 2003 to 2014
$3.2M
Proteolytic Regulation of Troponin T & Cardiac FunctionR01HL098945 · NHLBI · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING · 2010 to 2014
$2.0M
Regulation & Function of CalponinR01HL086720 · NHLBI · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING · 2007 to 2010
$1.5M
Troponin structure &function in cardiomyopathyR01HL078773 · NHLBI · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING · 2005 to 2008
$1.3M
Post-translational Modification in Cardiac MuscleR00HL091056 · NHLBI · OHIO STATE UNIVERSITY · PI BIESIADECKI, BRANDON J · 2009 to 2011
$747k
The Role of Tropomyosin Post-translational Modification in Cardiac MuscleK99HL091056 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BIESIADECKI, BRANDON J · 2008 to 2009
$180k
NHLBI NIH HHS HL-078773NHLBI NIH HHS HL-086720NHLBI NIH HHS HL-091056NHLBI NIH HHS HL-098945NHLBI NIH HHS K99 HL091056NHLBI NIH HHS R00 HL091056NHLBI NIH HHS R01 HL078773NHLBI NIH HHS R01 HL086720NHLBI NIH HHS R01 HL098945NIAMS NIH HHS AR048816NIAMS NIH HHS R01 AR048816
6 · The paper itself

Abstract

To understand the structure-function relationship of muscle-regulatory-protein isoforms, mutations, and posttranslational modifications, it is necessary to probe functional effects at the level of the protein-protein interaction. Traditional methodologies assessing such protein-protein interactions are laborious and require significant amounts of purified protein, while many current methodologies require costly and specialized equipment or modification of the proteins, which may affect their interaction. To address these issues, we developed a novel method of microplate-based solid-phase protein-binding assay over the recent years. This method assesses specific protein-protein interactions at physiological conditions, utilizes relatively small amounts of protein, is free of protein modification, and does not require specialized instrumentation. Here we present detailed methodology for the solid-phase protein-binding assay with examples that we have successfully applied to quantify interactions of myofilament-regulatory proteins. We further provide considerations for optimization of the assay conditions and its broader application in studies of other protein-protein interactions.

Indexed as

AnimalsHumansImmunoenzyme TechniquesMuscle ProteinsMyofibrilsProtein IsoformsProtein Processing, Post-TranslationalMuscle ProteinsProtein Isoforms

Identifiers

PMID22190850
PMCPMC3228687

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.