Related Experiment Video
Updated: Jun 23, 2026

07:11
CorrelationCalculator and Filigree: Tools for Data-Driven Network Analysis of Metabolomics Data
Published on: November 10, 2023
Studying the effects of correlation on protein selection in proteomics data
Savita Venkataramani1, Dayanand N Naik
1Department of Mathematics, Hampton University, Hampton, VA, USA.
Proteomics
|May 1, 2009
Summary
Correlation significantly impacts false discovery rate (FDR) assessments in large-scale biological data. This study applies Efron
Area of Science:
- Statistical genomics and proteomics
- Bioinformatics and computational biology
Background:
- Efron's (2007) methods assess correlation's effect on false discovery rate (FDR) in large-scale testing, particularly for microarray data.
- While FDR procedures don't mandate test independence, correlation can lead to inaccurate estimations of significant findings.
- Accurate FDR assessment is crucial for identifying true discoveries in high-throughput biological experiments.
Purpose of the Study:
- To review Efron's (2007) FDR assessment methods.
- To apply these methods to smaller-scale spectrometry proteomics data.
- To investigate the impact of correlation on FDR and the identification of critical proteins in proteomics.
Main Methods:
- Review of statistical methodologies for FDR assessment.
- Application of Efron's correlation-adjusted FDR methods.
- Analysis of spectrometry proteomics data to evaluate FDR under correlated test statistics.
Main Results:
- Correlation was found to affect FDR values in the analyzed proteomics dataset.
- The number of proteins identified as statistically significant was influenced by the presence of correlation.
- The findings demonstrate the relevance of accounting for correlation even in smaller-scale proteomics studies.
Conclusions:
- Correlation significantly impacts the accuracy of false discovery rate calculations in biological data analysis.
- Efron's methods are applicable and necessary for reliable FDR assessment in proteomics.
- Ignoring correlation can lead to misinterpretation of results, over- or underestimating the number of significant proteins.
Related Concept Videos
Proteomics
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Conservation of Protein Domains Over Different Proteins
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

