Demonstration venue · read-only. Every page can be browsed; the buttons that would change it are switched off. Create an account to run TaxoReview on your own data. A simulation from public publication records: the people listed were not invited and did not agree to review.
? Tutorial for this page

Rabie Saidi

dblp:75/830 · DBLP profile ↗
← Back
7ranked-venue papers
1as first author
3since 2021 · last 2023
0000-0002-0449-5253ORCID · verified

Domains — the database's venue-derived domains; a paper can count in several

Applied, interdisciplinary, general and emerging computing · 6 · 1 first-author · 3 since 2021Artificial intelligence and machine learning · 1

Expertise — from the expertise taxonomy: the topics of the expert's papers under the CCF categories. A weight counts papers with recency: 1 for a paper about the topic, 0.3 when the topic is its context, halved every five years.

Interdisciplinary, comprehensive, and emerging computing
5 papers
Bioinformatics and computational biology · 100%

Topics — the 7 heaviest of 8, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology
protein function prediction
1.842022
Hierarchical deep learning for predicting GO annotations by integrating protein knowledge · Bioinform. 2022
UniRule: a unified rule resource for automatic annotation in the UniProt Knowledgebase · Bioinform. 2021
UniRule: a unified rule resource for automatic annotation in the UniProt Knowledgebase · Bioinform. 2020
Bioinformatics and computational biology › genome annotation
automatic annotation
0.922021
UniRule: a unified rule resource for automatic annotation in the UniProt Knowledgebase · Bioinform. 2021
UniRule: a unified rule resource for automatic annotation in the UniProt Knowledgebase · Bioinform. 2020
Bioinformatics and computational biology › protein analysis › protein bioinformatics
protein annotation
0.712023
Annotation of biologically relevant ligands in UniProtKB using ChEBI · Bioinform. 2023
Bioinformatics and computational biology › protein function prediction
gene ontology annotation
0.612022
Hierarchical deep learning for predicting GO annotations by integrating protein knowledge · Bioinform. 2022
Bioinformatics and computational biology › genome annotation
functional annotation
0.212016
UniProt-DAAC: domain architecture alignment and classification, a new method for automatic functional annotation in UniProtKB · Bioinform. 2016
Bioinformatics and computational biology › protein analysis
protein bioinformatics
0.212022
Hierarchical deep learning for predicting GO annotations by integrating protein knowledge · Bioinform. 2022
Bioinformatics and computational biology
protein domain
0.112016
UniProt-DAAC: domain architecture alignment and classification, a new method for automatic functional annotation in UniProtKB · Bioinform. 2016

Methods — techniques the papers use, named apart from their topics

interpro signatures · 0.9ontology-based annotation · 0.7SPARQL querying · 0.7hierarchical classification · 0.6deep learning · 0.6cross-validation · 0.2
YearPublicationVenuePosition
2023 Annotation of biologically relevant ligands in UniProtKB using ChEBI
abstract
MOTIVATION: To provide high quality, computationally tractable annotation of binding sites for biologically relevant (cognate) ligands in UniProtKB using the chemical ontology ChEBI (Chemical Entities of Biological Interest), to better support efforts to study and predict functionally relevant interactions between protein sequences and structures and small molecule ligands. RESULTS: We structured the data model for cognate ligand binding site annotations in UniProtKB and performed a complete reannotation of all cognate ligand binding sites using stable unique identifiers from ChEBI, which we now use as the reference vocabulary for all such annotations. We developed improved search and query facilities for cognate ligands in the UniProt website, REST API and SPARQL endpoint that leverage the chemical structure data, nomenclature and classification that ChEBI provides. AVAILABILITY AND IMPLEMENTATION: Binding site annotations for cognate ligands described using ChEBI are available for UniProtKB protein sequence records in several formats (text, XML and RDF) and are freely available to query and download through the UniProt website (www.uniprot.org), REST API (www.uniprot.org/help/api), SPARQL endpoint (sparql.uniprot.org/) and FTP site (https://ftp.uniprot.org/pub/databases/uniprot/). SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
Elisabeth Coudert, Sebastien Gehant, Edouard De Castro, Monica Pozzato, Delphine Baratin, Teresa Batista Neto, Christian J. A. Sigrist, Nicole Redaschi, Alan J. Bridge, Lucila Aimo, Ghislaine Argoud-Puy, Andrea H. Auchincloss, Kristian B. Axelsen, Parit Bansal, Marie-Claude Blatter, Jerven T. Bolleman, Emmanuel Boutet, Lionel Breuza, Blanca Cabrera Gil, Cristina Casals-Casas, Kamal Chikh Echioukh, Béatrice A. Cuche, Anne Estreicher, Maria Livia Famiglietti, Marc Feuermann, Elisabeth Gasteiger, Pascale Gaudet, Vivienne Baillie Gerritsen, Arnaud Gos, Nadine Gruaz-Gumowski, Chantal Hulo, Nevila Hyka-Nouspikel, Florence Jungo, Arnaud Kerhornou, Philippe Le Mercier, Damien Lieberherr, Patrick Masson, Anne Morgat, Venkatesh Muthukrishnan, Salvo Paesano, Ivo Pedruzzi, Sandrine Pilbout, Lucille Pourcel, Sylvain Poux, Manuela Pruess, Catherine Rivoire, Karin Sonesson, Shyamala Sundaram, Alex Bateman, Maria Jesus Martin, Sandra E. Orchard, Michele Magrane, Shadab Ahmad, Emanuele Alpi, Emily H. Bowler-Barnett, Ramona Britto, Hema Bye-A-Jee, Austra Cukura, Paul Denny 0002, Tunca Dogan, Thankgod Ebenezer, Penelope Garmiri, Leonardo Jose da Costa Gonzales, Emma Hatton-Ellis, Abdulrahman Hussein, Alexandr Ignatchenko, Giuseppe Insana, Rizwan Ishtiaq, Vishal Joshi, Dushyanth Jyothi, Swaathi Kandasamy, Antonia Lock, Aurelien Luciani, Marija Lugaric, Yvonne Lussi, Alistair MacDougall, Fábio Madeira, Mahdi Mahmoudy, Alok Mishra 0004, Katie Moulang, Andrew Nightingale, Sangya Pundir, Guoying Qi, Shriya Raj, Pedro Raposo, Daniel Rice, Rabie Saidi, Elena Speretta, James D. Stephenson, Prabhat Totoo, Edward Turner, Nidhi Tyagi, Preethi Vasudev, Kate Warner, Xavier Watkins, Rossana Zaru, Hermann Zellner, Cathy H. Wu, Cecilia N. Arighi, Leslie Arminski, Chuming Chen, Yongxing Chen, Hongzhan Huang, Kati Laiho, Peter B. McGarvey, Darren A. Natale, Karen E. Ross, C. R. Vinayaka, Qinghua Wang 0003
Bioinform.89
2022 Hierarchical deep learning for predicting GO annotations by integrating protein knowledge
abstract
MOTIVATION: Experimental testing and manual curation are the most precise ways for assigning Gene Ontology (GO) terms describing protein functions. However, they are expensive, time-consuming and cannot cope with the exponential growth of data generated by high-throughput sequencing methods. Hence, researchers need reliable computational systems to help fill the gap with automatic function prediction. The results of the last Critical Assessment of Function Annotation challenge revealed that GO-terms prediction remains a very challenging task. Recent developments on deep learning are significantly breaking out the frontiers leading to new knowledge in protein research thanks to the integration of data from multiple sources. However, deep models hitherto developed for functional prediction are mainly focused on sequence data and have not achieved breakthrough performances yet. RESULTS: We propose DeeProtGO, a novel deep-learning model for predicting GO annotations by integrating protein knowledge. DeeProtGO was trained for solving 18 different prediction problems, defined by the three GO sub-ontologies, the type of proteins, and the taxonomic kingdom. Our experiments reported higher prediction quality when more protein knowledge is integrated. We also benchmarked DeeProtGO against state-of-the-art methods on public datasets, and showed it can effectively improve the prediction of GO annotations. AVAILABILITY AND IMPLEMENTATION: DeeProtGO and a case of use are available at https://github.com/gamerino/DeeProtGO. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
Gabriela Alejandra Merino, Rabie Saidi, Diego H. Milone, Georgina Stegmayer, Maria Jesus Martin
Bioinform.2
2021 UniRule: a unified rule resource for automatic annotation in the UniProt Knowledgebase
Alistair MacDougall, Vladimir Volynkin, Rabie Saidi, Diego Poggioli, Hermann Zellner, Emma Hatton-Ellis, Vishal Joshi, Claire O'Donovan, Sandra E. Orchard, Andrea H. Auchincloss, Delphine Baratin, Jerven T. Bolleman, Elisabeth Coudert, Edouard De Castro, Chantal Hulo, Patrick Masson, Ivo Pedruzzi, Catherine Rivoire, Cecilia N. Arighi, Qinghua Wang 0003, Chuming Chen, Hongzhan Huang, John S. Garavelli, C. R. Vinayaka, Lai-Su Yeh, Darren A. Natale, Kati Laiho, Maria Jesus Martin, Alexandre Renaux, Klemens Pichler
Bioinform.3
2020 UniRule: a unified rule resource for automatic annotation in the UniProt Knowledgebase
abstract
MOTIVATION: The number of protein records in the UniProt Knowledgebase (UniProtKB: https://www.uniprot.org) continues to grow rapidly as a result of genome sequencing and the prediction of protein-coding genes. Providing functional annotation for these proteins presents a significant and continuing challenge. RESULTS: In response to this challenge, UniProt has developed a method of annotation, known as UniRule, based on expertly curated rules, which integrates related systems (RuleBase, HAMAP, PIRSR, PIRNR) developed by the members of the UniProt consortium. UniRule uses protein family signatures from InterPro, combined with taxonomic and other constraints, to select sets of reviewed proteins which have common functional properties supported by experimental evidence. This annotation is propagated to unreviewed records in UniProtKB that meet the same selection criteria, most of which do not have (and are never likely to have) experimentally verified functional annotation. Release 2020_01 of UniProtKB contains 6496 UniRule rules which provide annotation for 53 million proteins, accounting for 30% of the 178 million records in UniProtKB. UniRule provides scalable enrichment of annotation in UniProtKB. AVAILABILITY AND IMPLEMENTATION: UniRule rules are integrated into UniProtKB and can be viewed at https://www.uniprot.org/unirule/. UniRule rules and the code required to run the rules, are publicly available for researchers who wish to annotate their own sequences. The implementation used to run the rules is known as UniFIRE and is available at https://gitlab.ebi.ac.uk/uniprot-public/unifire.
Alistair MacDougall, Vladimir Volynkin, Rabie Saidi, Diego Poggioli, Hermann Zellner, Emma Hatton-Ellis, Vishal Joshi, Claire O'Donovan, Sandra E. Orchard, Andrea H. Auchincloss, Delphine Baratin, Jerven T. Bolleman, Elisabeth Coudert, Edouard De Castro, Chantal Hulo, Patrick Masson, Ivo Pedruzzi, Catherine Rivoire, Cecilia N. Arighi, Qinghua Wang 0003, Chuming Chen, Hongzhan Huang, John S. Garavelli, C. R. Vinayaka, Lai-Su Yeh, Darren A. Natale, Kati Laiho, Maria Jesus Martin, Alexandre Renaux, Klemens Pichler
Bioinform.3
2016 UniProt-DAAC: domain architecture alignment and classification, a new method for automatic functional annotation in UniProtKB
abstract
MOTIVATION: Similarity-based methods have been widely used in order to infer the properties of genes and gene products containing little or no experimental annotation. New approaches that overcome the limitations of methods that rely solely upon sequence similarity are attracting increased attention. One of these novel approaches is to use the organization of the structural domains in proteins. RESULTS: We propose a method for the automatic annotation of protein sequences in the UniProt Knowledgebase (UniProtKB) by comparing their domain architectures, classifying proteins based on the similarities and propagating functional annotation. The performance of this method was measured through a cross-validation analysis using the Gene Ontology (GO) annotation of a sub-set of UniProtKB/Swiss-Prot. The results demonstrate the effectiveness of this approach in detecting functional similarity with an average F-score: 0.85. We applied the method on nearly 55.3 million uncharacterized proteins in UniProtKB/TrEMBL resulted in 44 818 178 GO term predictions for 12 172 114 proteins. 22% of these predictions were for 2 812 016 previously non-annotated protein entries indicating the significance of the value added by this approach. AVAILABILITY AND IMPLEMENTATION: The results of the method are available at: ftp://ftp.ebi.ac.uk/pub/contrib/martin/DAAC/ CONTACT: [email protected] SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
Tunca Dogan, Alistair MacDougall, Rabie Saidi, Diego Poggioli, Alex Bateman, Claire O'Donovan, Maria Jesus Martin
Bioinform.3
2012 Ranking and Selecting Association Rules Based on Dominance Relationship
abstract
The huge number of association rules represent the main hamper that a decision maker faces. In order to bypass this hamper, an efficient selection of rules has to be performed. Since selection is necessarily based on evaluation, many interestingness measures have been proposed. However, the abundance of these measures gave rise to a new problem, namely the heterogeneity of the evaluation results and this created confusion to the decision. In this respect, we propose a novel approach to discover interesting association rules without favoring or excluding any measure by adopting the notion of dominance between association rules. Our approach bypasses the problem of measure heterogeneity and unveils a compromise between their evaluations. Interestingly enough, the proposed approach also avoids another non-trivial problem which is the threshold value specification.
Slim Bouker, Rabie Saidi, Sadok Ben Yahia, Engelbert Mephu Nguifo
ICTAI2
2010 Protein sequences classification by means of feature extraction with substitution matrices
abstract
BACKGROUND: This paper deals with the preprocessing of protein sequences for supervised classification. Motif extraction is one way to address that task. It has been largely used to encode biological sequences into feature vectors to enable using well-known machine-learning classifiers which require this format. However, designing a suitable feature space, for a set of proteins, is not a trivial task. For this purpose, we propose a novel encoding method that uses amino-acid substitution matrices to define similarity between motifs during the extraction step. RESULTS: In order to demonstrate the efficiency of such approach, we compare several encoding methods using some machine learning classifiers. The experimental results showed that our encoding method outperforms other ones in terms of classification accuracy and number of generated attributes. We also compared the classifiers in term of accuracy. Results indicated that SVM generally outperforms the other classifiers with any encoding method. We showed that SVM, coupled with our encoding method, can be an efficient protein classification system. In addition, we studied the effect of the substitution matrices variation on the quality of our method and hence on the classification quality. We noticed that our method enables good classification accuracies with all the substitution matrices and that the variances of the obtained accuracies using various substitution matrices are slight. However, the number of generated features varies from a substitution matrix to another. Furthermore, the use of already published datasets allowed us to carry out a comparison with several related works. CONCLUSIONS: The outcomes of our comparative experiments confirm the efficiency of our encoding method to represent protein sequences in classification tasks.
Rabie Saidi, Mondher Maddouri, Engelbert Mephu Nguifo
BMC Bioinform.1