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Publications

Publications by Pedro Gabriel Ferreira

2007

Evaluating deterministic motif significance measures in protein databases

Authors
Ferreira, PG; Azevedo, PJ;

Publication
ALGORITHMS FOR MOLECULAR BIOLOGY

Abstract
Background: Assessing the outcome of motif mining algorithms is an essential task, as the number of reported motifs can be very large. Significance measures play a central role in automatically ranking those motifs, and therefore alleviating the analysis work. Spotting the most interesting and relevant motifs is then dependent on the choice of the right measures. The combined use of several measures may provide more robust results. However caution has to be taken in order to avoid spurious evaluations. Results: From the set of conducted experiments, it was verified that several of the selected significance measures show a very similar behavior in a wide range of situations therefore providing redundant information. Some measures have proved to be more appropriate to rank highly conserved motifs, while others are more appropriate for weakly conserved ones. Support appears as a very important feature to be considered for correct motif ranking. We observed that not all the measures are suitable for situations with poorly balanced class information, like for instance, when positive data is significantly less than negative data. Finally, a visualization scheme was proposed that, when several measures are applied, enables an easy identification of high scoring motifs. Conclusion: In this work we have surveyed and categorized 14 significance measures for pattern evaluation. Their ability to rank three types of deterministic motifs was evaluated. Measures were applied in different testing conditions, where relations were identified. This study provides some pertinent insights on the choice of the right set of significance measures for the evaluation of deterministic motifs extracted from protein databases.

2007

Deterministic motif mining in protein databases

Authors
Ferreira, PG; Azevedo, PJ;

Publication
Successes and New Directions in Data Mining

Abstract
Protein sequence motifs describe, through means of enhanced regular expression syntax, regions of amino acids that have been conserved across several functionally related proteins. These regions may have an implication at the structural and functional level of the proteins. Sequence motif analysis can bring significant improvements towards a better understanding of the protein sequence-structure-function relation. In this chapter, we review the subject of mining deterministic motifs from protein sequence databases. We start by giving a formal definition of the different types of motifs and the respective specificities. Then, we explore the methods available to evaluate the quality and interest of such patterns. Examples of applications and motif repositories are described. We discuss the algorithmic aspects and different methodologies for motif extraction. A brief description on how sequence motifs can be used to extract structural level information patterns is also provided. © 2008, IGI Global.

2009

Deterministic pattern mining on genetic sequences

Authors
Ferreira, PG; Azevedo, PJ;

Publication
Handbook of Research on Machine Learning Applications and Trends: Algorithms, Methods, and Techniques

Abstract
The recent increase in the number of complete genetic sequences freely available through specialized Internet databases presents big challenges for the research community. One such challenge is the efficient and effective search of sequence patterns, also known as motifs, among a set of related genetic sequences. Such patterns describe regions that may provide important insights about the structural and functional role of DNA and proteins. Two main classes can be considered: probabilistic patterns represent a model that simulates the sequences or part of the sequences under consideration and deterministic patterns that either match or not the input sequences. In this chapter a general overview of deterministic sequence mining over sets of genetic sequences is proposed. The authors formulate an architecture that divides the mining process workflow into a set of blocks. Each of these blocks is discussed individually. © 2010, IGI Global.

2006

Mining approximate motifs in time series

Authors
Ferreira, PG; Azevedo, PJ; Silva, CG; Brito, RMM;

Publication
DISCOVERY SCIENCE, PROCEEDINGS

Abstract
The problem of discovering previously unknown frequent patterns in time series, also called motifs, has been recently introduced. A motif is a subseries pattern that appears a significant number of times. Results demonstrate that motifs may provide valuable insights about the data and have a wide range of applications in data mining tasks. The main motivation for this study was the need to mine time series data from protein folding/unfolding simulations. We propose an algorithm that extracts approximate motifs, i.e. motifs that capture portions of time series with a similar and eventually symmetric behavior. Preliminary results on the analysis of protein unfolding data support this proposal as a valuable tool. A.dditional experiments demonstrate that the application of utility of our algorithm is not limited to this particular problem. Rather it can be an interesting tool to be applied in many real world problems.

2009

Using data mining techniques to probe the role of hydrophobic residues in protein folding and unfolding simulations

Authors
Silva, CG; Ferreira, PG; Azevedo, PJ; Brito, RMM;

Publication
Evolving Application Domains of Data Warehousing and Mining: Trends and Solutions

Abstract
The protein folding problem, i.e. the identification of the rules that determine the acquisition of the native, functional, three-dimensional structure of a protein from its linear sequence of amino-acids, still is a major challenge in structural molecular biology. Moreover, the identification of a series of neurodegenerative diseases as protein unfolding/misfolding disorders highlights the importance of a detailed characterisation of the molecular events driving the unfolding and misfolding processes in proteins. One way of exploring these processes is through the use of molecular dynamics simulations. The analysis and comparison of the enormous amount of data generated by multiple protein folding or unfolding simulations is not a trivial task, presenting many interesting challenges to the data mining community. Considering the central role of the hydrophobic effect in protein folding, we show here the application of two data mining methods - hierarchical clustering and association rules - for the analysis and comparison of the solvent accessible surface area (SASA) variation profiles of each one of the 127 amino-acid residues in the amyloidogenic protein Transthyretin, across multiple molecular dynamics protein unfolding simulations. © 2010, IGI Global.

2007

Evaluating protein motif significance measures: A case study on prosite patterns

Authors
Ferreira, PG; Azevedo, PJ;

Publication
2007 IEEE Symposium on Computational Intelligence and Data Mining, Vols 1 and 2

Abstract
The existence of preserved subsequences in a set of related protein sequences suggests that they might play a structural and functional role in protein's mechanisms. Due to its exploratory approach, the mining process tends to deliver a large number of motifs. Therefore it is critical to release methods that identify relevant significant motifs. Many measures of interest and significance have been proposed. However, since motifs have a wide range or applications, how to choose the appropriate significance measures is application dependent. Some measures show consistent results being highly correlated, while others show disagreements. In this paper we review existent measures and study their behavior in order to assist the selection of the most appropriate set of measures. An experimental evaluation of the measures for high quality patterns from the Prosite database is presented.

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