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2. An expanded evaluation of protein function prediction methods shows an improvement in accuracy

Author

Jiang, Yuxiang, Oron, Tal Ronnen, Clark, Wyatt T, Bankapur, Asma R, D'Andrea, Daniel, Lepore, Rosalba, Funk, Christopher S, Kahanda, Indika, Verspoor, Karin M, Ben-Hur, Asa, Koo, Emily, Penfold-Brown, Duncan, Shasha, Dennis, Youngs, Noah, Bonneau, Richard, Lin, Alexandra, Sahraeian, Sayed ME, Martelli, Pier Luigi, Profiti, Giuseppe, Casadio, Rita, Cao, Renzhi, Zhong, Zhaolong, Cheng, Jianlin, Altenhoff, Adrian, Skunca, Nives, Dessimoz, Christophe, Dogan, Tunca, Hakala, Kai, Kaewphan, Suwisa, Mehryary, Farrokh, Salakoski, Tapio, Ginter, Filip, Fang, Hai, Smithers, Ben, Oates, Matt, Gough, Julian, Törönen, Petri, Koskinen, Patrik, Holm, Liisa, Chen, Ching-Tai, Hsu, Wen-Lian, Bryson, Kevin, Cozzetto, Domenico, Minneci, Federico, Jones, David T, Chapman, Samuel, C., Dukka B K., Khan, Ishita K, Kihara, Daisuke, Ofer, Dan, Rappoport, Nadav, Stern, Amos, Cibrian-Uhalte, Elena, Denny, Paul, Foulger, Rebecca E, Hieta, Reija, Legge, Duncan, Lovering, Ruth C, Magrane, Michele, Melidoni, Anna N, Mutowo-Meullenet, Prudence, Pichler, Klemens, Shypitsyna, Aleksandra, Li, Biao, Zakeri, Pooya, ElShal, Sarah, Tranchevent, Léon-Charles, Das, Sayoni, Dawson, Natalie L, Lee, David, Lees, Jonathan G, Sillitoe, Ian, Bhat, Prajwal, Nepusz, Tamás, Romero, Alfonso E, Sasidharan, Rajkumar, Yang, Haixuan, Paccanaro, Alberto, Gillis, Jesse, Sedeño-Cortés, Adriana E, Pavlidis, Paul, Feng, Shou, Cejuela, Juan M, Goldberg, Tatyana, Hamp, Tobias, Richter, Lothar, Salamov, Asaf, Gabaldon, Toni, Marcet-Houben, Marina, Supek, Fran, Gong, Qingtian, Ning, Wei, Zhou, Yuanpeng, Tian, Weidong, Falda, Marco, Fontana, Paolo, Lavezzo, Enrico, Toppo, Stefano, Ferrari, Carlo, Giollo, Manuel, Piovesan, Damiano, Tosatto, Silvio, del Pozo, Angela, Fernández, José M, Maietta, Paolo, Valencia, Alfonso, Tress, Michael L, Benso, Alfredo, Di Carlo, Stefano, Politano, Gianfranco, Savino, Alessandro, Rehman, Hafeez Ur, Re, Matteo, Mesiti, Marco, Valentini, Giorgio, Bargsten, Joachim W, van Dijk, Aalt DJ, Gemovic, Branislava, Glisic, Sanja, Perovic, Vladmir, Veljkovic, Veljko, Veljkovic, Nevena, Almeida-e-Silva, Danillo C, Vencio, Ricardo ZN, Sharan, Malvika, Vogel, Jörg, Kansakar, Lakesh, Zhang, Shanshan, Vucetic, Slobodan, Wang, Zheng, Sternberg, Michael JE, Wass, Mark N, Huntley, Rachael P, Martin, Maria J, O'Donovan, Claire, Robinson, Peter N, Moreau, Yves, Tramontano, Anna, Babbitt, Patricia C, Brenner, Steven E, Linial, Michal, Orengo, Christine A, Rost, Burkhard, Greene, Casey S, Mooney, Sean D, Friedberg, Iddo, and Radivojac, Predrag

Subjects
Quantitative Biology - Quantitative Methods
Abstract

Background: The increasing volume and variety of genotypic and phenotypic data is a major defining characteristic of modern biomedical sciences. At the same time, the limitations in technology for generating data and the inherently stochastic nature of biomolecular events have led to the discrepancy between the volume of data and the amount of knowledge gleaned from it. A major bottleneck in our ability to understand the molecular underpinnings of life is the assignment of function to biological macromolecules, especially proteins. While molecular experiments provide the most reliable annotation of proteins, their relatively low throughput and restricted purview have led to an increasing role for computational function prediction. However, accurately assessing methods for protein function prediction and tracking progress in the field remain challenging. Methodology: We have conducted the second Critical Assessment of Functional Annotation (CAFA), a timed challenge to assess computational methods that automatically assign protein function. One hundred twenty-six methods from 56 research groups were evaluated for their ability to predict biological functions using the Gene Ontology and gene-disease associations using the Human Phenotype Ontology on a set of 3,681 proteins from 18 species. CAFA2 featured significantly expanded analysis compared with CAFA1, with regards to data set size, variety, and assessment metrics. To review progress in the field, the analysis also compared the best methods participating in CAFA1 to those of CAFA2. Conclusions: The top performing methods in CAFA2 outperformed the best methods from CAFA1, demonstrating that computational function prediction is improving. This increased accuracy can be attributed to the combined effect of the growing number of experimental annotations and improved methods for function prediction., Comment: Submitted to Genome Biology

Published
2016
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3. Domains and disorder towards a sufficient evolutionary description of protein structure

Author

Oates, Matt E.

Subjects
572
Abstract

The general title given to this thesis represents the underlying ethos of my work that links most parts together, as well as being the motivation I now have for future work. The main scientific concern I present within is a more specific evolutionary theory on what has happened in land plants to a well known Calcium cell-signalling pathway found in mammals. Namely the Inositol triphosphate mediated Calcium release of ITPR channels in mammalian neural and muscle cells. This is discussed at length in Part ii, Chapters 2-3 of this thesis. Chapter 3 contains a detailed discussion surrounding an already known and characterised Calcium channel (TPC1) in Arabidopsis thaliana that was found to be related albeit very distantly to ITPR channels. Additional partner regulatory proteins are introduced and some justification is made that they interact directly with TPCl providing it with regulated gated activity specifically in guard cells. During the development of the theory presented in Part ii it became essential to understand the location and function of disordered protein regions in sequences over many species and genes, This lead to the production of a Database of Disordered Protein Predictions (D2P2 described in Part iii, as well as methods for visualizing multiple classes of protein annotations such as structural domains, post- translational modification sites, and regions of protein disorder that fold on contact, In Chapter 5 discussion surrounding major results from producing D2P2 and its implications on the evolution of disordered protein state are presented. Finally in Part iv I introduce some relatively unrelated work investigating the domain content of a new genome being sequenced at the King Abdullha University of Science and Technology for the Dinoflagellate species Symbiodinium microadriaticum. One of my main tasks in this collaboration was to identify proteins that mediate many endosymbiotic relationships carried out by Symbiodinium. Finding an example of a superfamily only found in a single clade of bacteria I identify a plausible target protein and mechanism for eluding Toll-like Receptors of host species. In the concluding Part v I summarise pieces of work that I have yet to finish, but include here to give some impression of the sorts of work I have been thinking about and hope to one day complete.

Published
2014

6. Hypothesis-free phenotype prediction within a genetics-first framework

Author

Lu, Chang, primary, Zaucha, Jan, additional, Gam, Rihab, additional, Fang, Hai, additional, Smithers, Ben, additional, Oates, Matt E., additional, Bernabe-Rubio, Miguel, additional, Williams, James, additional, Thurlby, Natalie, additional, Pandurangan, Arun Prasad, additional, Tandon, Himani, additional, Shihab, Hashem, additional, Kalaivani, Raju, additional, Sung, Minkyung, additional, Sardar, Adam, additional, Tzovoras, Bastian Greshake, additional, Danovi, Davide, additional, and Gough, Julian, additional

Published
2023
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8. The genome of Aiptasia , a sea anemone model for coral symbiosis

Author

Baumgarten, Sebastian, Simakov, Oleg, Esherick, Lisl Y., Liew, Yi Jin, Lehnert, Erik M., Michell, Craig T., Li, Yong, Hambleton, Elizabeth A., Guse, Annika, Oates, Matt E., Gough, Julian, Weis, Virginia M., Aranda, Manuel, Pringle, John R., and Voolstra, Christian R.

Published
2015

11. Genome3D: exploiting structure to help users understand their sequences

Author

Lewis, Tony E., Sillitoe, Ian, Andreeva, Antonina, Blundell, Tom L., Buchan, Daniel W.A., Chothia, Cyrus, Cozzetto, Domenico, Dana, José M., Filippis, Ioannis, Gough, Julian, Jones, David T., Kelley, Lawrence A., Kleywegt, Gerard J., Minneci, Federico, Mistry, Jaina, Murzin, Alexey G., Ochoa-Montaño, Bernardo, Oates, Matt E., Punta, Marco, Rackham, Owen J.L., Stahlhacke, Jonathan, Sternberg, Michael J.E., Velankar, Sameer, and Orengo, Christine

Published
2015
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12. The InterPro protein families database: the classification resource after 15 years

Author

Mitchell, Alex, Chang, Hsin-Yu, Daugherty, Louise, Fraser, Matthew, Hunter, Sarah, Lopez, Rodrigo, McAnulla, Craig, McMenamin, Conor, Nuka, Gift, Pesseat, Sebastien, Sangrador-Vegas, Amaia, Scheremetjew, Maxim, Rato, Claudia, Yong, Siew-Yit, Bateman, Alex, Punta, Marco, Attwood, Teresa K., Sigrist, Christian J.A., Redaschi, Nicole, Rivoire, Catherine, Xenarios, Ioannis, Kahn, Daniel, Guyot, Dominique, Bork, Peer, Letunic, Ivica, Gough, Julian, Oates, Matt, Haft, Daniel, Huang, Hongzhan, Natale, Darren A., Wu, Cathy H., Orengo, Christine, Sillitoe, Ian, Mi, Huaiyu, Thomas, Paul D., and Finn, Robert D.

Published
2015
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14. A Proteome Quality Index

Author

Zaucha, Jan, Stahlhacke, Jonathan, Oates, Matt E., Thurlby, Natalie, Rackham, Owen J. L., Fang, Hai, Smithers, Ben, and Gough, Julian

Published
2015
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18. Splice junctions are constrained by protein disorder

Author

Smithers, Ben, Oates, Matt E., and Gough, Julian

Subjects
Intrinsically Disordered Proteins, Nucleotides, Computational Biology, Animals, Eukaryota, Exons, RNA Splice Sites, Amino Acids, Nucleotide Motifs
Abstract

We have discovered that positions of splice junctions in genes are constrained by the tolerance for disorder-promoting amino acids in the translated protein region. It is known that efficient splicing requires nucleotide bias at the splice junction; the preferred usage produces a distribution of amino acids that is disorder-promoting. We observe that efficiency of splicing, as seen in the amino-acid distribution, is not compromised to accommodate globular structure. Thus we infer that it is the positions of splice junctions in the gene that must be under constraint by the local protein environment. Examining exonic splicing enhancers found near the splice junction in the gene, reveals that these (short DNA motifs) are more prevalent in exons that encode disordered protein regions than exons encoding structured regions. Thus we also conclude that local protein features constrain efficient splicing more in structure than in disorder.

Published
2015

20. Additional file 1 of An expanded evaluation of protein function prediction methods shows an improvement in accuracy

Author

Yuxiang Jiang, Oron, Tal Ronnen, Clark, Wyatt T., Bankapur, Asma R., D’Andrea, Daniel, Lepore, Rosalba, Funk, Christopher S., Indika Kahanda, Verspoor, Karin M., Ben-Hur, Asa, Koo, Da Chen Emily, Penfold-Brown, Duncan, Shasha, Dennis, Youngs, Noah, Bonneau, Richard, Lin, Alexandra, Sahraeian, Sayed M. E., Martelli, Pier Luigi, Profiti, Giuseppe, Casadio, Rita, Renzhi Cao, Zhaolong Zhong, Jianlin Cheng, Altenhoff, Adrian, Skunca, Nives, Dessimoz, Christophe, Tunca Dogan, Hakala, Kai, Suwisa Kaewphan, Mehryary, Farrokh, Salakoski, Tapio, Ginter, Filip, Fang, Hai, Smithers, Ben, Oates, Matt, Gough, Julian, Törönen, Petri, Koskinen, Patrik, Holm, Liisa, Ching-Tai Chen, Hsu, Wen-Lian, Bryson, Kevin, Cozzetto, Domenico, Minneci, Federico, Jones, David T., Chapman, Samuel, Dukka BKC, Ishita K. Khan, Kihara, Daisuke, Ofer, Dan, Rappoport, Nadav, Stern, Amos, Cibrian-Uhalte, Elena, Denny, Paul, Foulger, Rebecca E., Hieta, Reija, Legge, Duncan, Lovering, Ruth C., Magrane, Michele, Melidoni, Anna N., Mutowo-Meullenet, Prudence, Pichler, Klemens, Shypitsyna, Aleksandra, Li, Biao, Pooya Zakeri, ElShal, Sarah, Léon-Charles Tranchevent, Sayoni Das, Dawson, Natalie L., Lee, David, Lees, Jonathan G., Sillitoe, Ian, Prajwal Bhat, Nepusz, Tamás, Romero, Alfonso E., Sasidharan, Rajkumar, Haixuan Yang, Paccanaro, Alberto, Gillis, Jesse, Sedeño-Cortés, Adriana E., Pavlidis, Paul, Feng, Shou, Cejuela, Juan M., Goldberg, Tatyana, Hamp, Tobias, Richter, Lothar, Salamov, Asaf, Gabaldon, Toni, Marcet-Houben, Marina, Supek, Fran, Qingtian Gong, Ning, Wei, Yuanpeng Zhou, Weidong Tian, Falda, Marco, Fontana, Paolo, Lavezzo, Enrico, Toppo, Stefano, Ferrari, Carlo, Giollo, Manuel, Piovesan, Damiano, Tosatto, Silvio C.E., Pozo, Angela Del, Fernández, José M., Maietta, Paolo, Valencia, Alfonso, Tress, Michael L., Benso, Alfredo, Carlo, Stefano Di, Politano, Gianfranco, Savino, Alessandro, Hafeez Ur Rehman, Re, Matteo, Mesiti, Marco, Valentini, Giorgio, Bargsten, Joachim W., Dijk, Aalt D. J. Van, Gemovic, Branislava, Glisic, Sanja, Vladmir Perovic, Veljkovic, Veljko, Veljkovic, Nevena, Danillo C. Almeida-E-Silva, Vencio, Ricardo Z. N., Malvika Sharan, Vogel, Jörg, Lakesh Kansakar, Shanshan Zhang, Vucetic, Slobodan, Wang, Zheng, Sternberg, Michael J. E., Wass, Mark N., Huntley, Rachael P., Martin, Maria J., O’Donovan, Claire, Robinson, Peter N., Moreau, Yves, Tramontano, Anna, Babbitt, Patricia C., Brenner, Steven E., Linial, Michal, Orengo, Christine A., Rost, Burkhard, Greene, Casey S., Mooney, Sean D., Friedberg, Iddo, and Radivojac, Predrag

Abstract

A document containing a subset of CAFA2 analyses that are equivalent to those provided about the CAFA1 experiment in the CAFA1 supplement. (PDF 11100 kb)

Published
2016
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21. The InterPro protein families database: the classification resource after 15 years

Author

Mitchell, Alex, Chang, Hsin-Yu, Daugherty, Louise, Fraser, Matthew, Hunter, Sarah, Lopez, Rodrigo, McAnulla, Craig, McMenamin, Conor, Nuka, Gift, Pesseat, Sebastien, Sangrador-Vegas, Amaia, Scheremetjew, Maxim, Rato, Claudia, Yong, Siew-Yit, Bateman, Alex, Punta, Marco, Attwood, Teresa K., Sigrist, Christian J.A., Redaschi, Nicole, Rivoire, Catherine, Xenarios, Ioannis, Kahn, Daniel, Guyot, Dominique, Bork, Peer, Letunic, Ivica, Gough, Julian, Oates, Matt, Haft, Daniel, Huang, Hongzhan, Natale, Darren A., Wu, Cathy H., Orengo, Christine, Sillitoe, Ian, Mi, Huaiyu, Thomas, Paul D., Finn, Robert D., Mitchell, Alex, Chang, Hsin-Yu, Daugherty, Louise, Fraser, Matthew, Hunter, Sarah, Lopez, Rodrigo, McAnulla, Craig, McMenamin, Conor, Nuka, Gift, Pesseat, Sebastien, Sangrador-Vegas, Amaia, Scheremetjew, Maxim, Rato, Claudia, Yong, Siew-Yit, Bateman, Alex, Punta, Marco, Attwood, Teresa K., Sigrist, Christian J.A., Redaschi, Nicole, Rivoire, Catherine, Xenarios, Ioannis, Kahn, Daniel, Guyot, Dominique, Bork, Peer, Letunic, Ivica, Gough, Julian, Oates, Matt, Haft, Daniel, Huang, Hongzhan, Natale, Darren A., Wu, Cathy H., Orengo, Christine, Sillitoe, Ian, Mi, Huaiyu, Thomas, Paul D., and Finn, Robert D.

Abstract

The InterPro database (http://www.ebi.ac.uk/interpro/) is a freely available resource that can be used to classify sequences into protein families and to predict the presence of important domains and sites. Central to the InterPro database are predictive models, known as signatures, from a range of different protein family databases that have different biological focuses and use different methodological approaches to classify protein families and domains. InterPro integrates these signatures, capitalizing on the respective strengths of the individual databases, to produce a powerful protein classification resource. Here, we report on the status of InterPro as it enters its 15th year of operation, and give an overview of new developments with the database and its associated Web interfaces and software. In particular, the new domain architecture search tool is described and the process of mapping of Gene Ontology terms to InterPro is outlined. We also discuss the challenges faced by the resource given the explosive growth in sequence data in recent years. InterPro (version 48.0) contains 36 766 member database signatures integrated into 26 238 InterPro entries, an increase of over 3993 entries (5081 signatures), since 2012

Published
2017

23. An expanded evaluation of protein function prediction methods shows an improvement in accuracy

Author

Jiang, Yuxiang, primary, Oron, Tal Ronnen, additional, Clark, Wyatt T., additional, Bankapur, Asma R., additional, D’Andrea, Daniel, additional, Lepore, Rosalba, additional, Funk, Christopher S., additional, Kahanda, Indika, additional, Verspoor, Karin M., additional, Ben-Hur, Asa, additional, Koo, Da Chen Emily, additional, Penfold-Brown, Duncan, additional, Shasha, Dennis, additional, Youngs, Noah, additional, Bonneau, Richard, additional, Lin, Alexandra, additional, Sahraeian, Sayed M. E., additional, Martelli, Pier Luigi, additional, Profiti, Giuseppe, additional, Casadio, Rita, additional, Cao, Renzhi, additional, Zhong, Zhaolong, additional, Cheng, Jianlin, additional, Altenhoff, Adrian, additional, Skunca, Nives, additional, Dessimoz, Christophe, additional, Dogan, Tunca, additional, Hakala, Kai, additional, Kaewphan, Suwisa, additional, Mehryary, Farrokh, additional, Salakoski, Tapio, additional, Ginter, Filip, additional, Fang, Hai, additional, Smithers, Ben, additional, Oates, Matt, additional, Gough, Julian, additional, Törönen, Petri, additional, Koskinen, Patrik, additional, Holm, Liisa, additional, Chen, Ching-Tai, additional, Hsu, Wen-Lian, additional, Bryson, Kevin, additional, Cozzetto, Domenico, additional, Minneci, Federico, additional, Jones, David T., additional, Chapman, Samuel, additional, BKC, Dukka, additional, Khan, Ishita K., additional, Kihara, Daisuke, additional, Ofer, Dan, additional, Rappoport, Nadav, additional, Stern, Amos, additional, Cibrian-Uhalte, Elena, additional, Denny, Paul, additional, Foulger, Rebecca E., additional, Hieta, Reija, additional, Legge, Duncan, additional, Lovering, Ruth C., additional, Magrane, Michele, additional, Melidoni, Anna N., additional, Mutowo-Meullenet, Prudence, additional, Pichler, Klemens, additional, Shypitsyna, Aleksandra, additional, Li, Biao, additional, Zakeri, Pooya, additional, ElShal, Sarah, additional, Tranchevent, Léon-Charles, additional, Das, Sayoni, additional, Dawson, Natalie L., additional, Lee, David, additional, Lees, Jonathan G., additional, Sillitoe, Ian, additional, Bhat, Prajwal, additional, Nepusz, Tamás, additional, Romero, Alfonso E., additional, Sasidharan, Rajkumar, additional, Yang, Haixuan, additional, Paccanaro, Alberto, additional, Gillis, Jesse, additional, Sedeño-Cortés, Adriana E., additional, Pavlidis, Paul, additional, Feng, Shou, additional, Cejuela, Juan M., additional, Goldberg, Tatyana, additional, Hamp, Tobias, additional, Richter, Lothar, additional, Salamov, Asaf, additional, Gabaldon, Toni, additional, Marcet-Houben, Marina, additional, Supek, Fran, additional, Gong, Qingtian, additional, Ning, Wei, additional, Zhou, Yuanpeng, additional, Tian, Weidong, additional, Falda, Marco, additional, Fontana, Paolo, additional, Lavezzo, Enrico, additional, Toppo, Stefano, additional, Ferrari, Carlo, additional, Giollo, Manuel, additional, Piovesan, Damiano, additional, Tosatto, Silvio C.E., additional, del Pozo, Angela, additional, Fernández, José M., additional, Maietta, Paolo, additional, Valencia, Alfonso, additional, Tress, Michael L., additional, Benso, Alfredo, additional, Di Carlo, Stefano, additional, Politano, Gianfranco, additional, Savino, Alessandro, additional, Rehman, Hafeez Ur, additional, Re, Matteo, additional, Mesiti, Marco, additional, Valentini, Giorgio, additional, Bargsten, Joachim W., additional, van Dijk, Aalt D. J., additional, Gemovic, Branislava, additional, Glisic, Sanja, additional, Perovic, Vladmir, additional, Veljkovic, Veljko, additional, Veljkovic, Nevena, additional, Almeida-e-Silva, Danillo C., additional, Vencio, Ricardo Z. N., additional, Sharan, Malvika, additional, Vogel, Jörg, additional, Kansakar, Lakesh, additional, Zhang, Shanshan, additional, Vucetic, Slobodan, additional, Wang, Zheng, additional, Sternberg, Michael J. E., additional, Wass, Mark N., additional, Huntley, Rachael P., additional, Martin, Maria J., additional, O’Donovan, Claire, additional, Robinson, Peter N., additional, Moreau, Yves, additional, Tramontano, Anna, additional, Babbitt, Patricia C., additional, Brenner, Steven E., additional, Linial, Michal, additional, Orengo, Christine A., additional, Rost, Burkhard, additional, Greene, Casey S., additional, Mooney, Sean D., additional, Friedberg, Iddo, additional, and Radivojac, Predrag, additional

Published
2016
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27. The InterPro protein families database: the classification resource after 15 years

Author

Mitchell, Alex, primary, Chang, Hsin-Yu, additional, Daugherty, Louise, additional, Fraser, Matthew, additional, Hunter, Sarah, additional, Lopez, Rodrigo, additional, McAnulla, Craig, additional, McMenamin, Conor, additional, Nuka, Gift, additional, Pesseat, Sebastien, additional, Sangrador-Vegas, Amaia, additional, Scheremetjew, Maxim, additional, Rato, Claudia, additional, Yong, Siew-Yit, additional, Bateman, Alex, additional, Punta, Marco, additional, Attwood, Teresa K., additional, Sigrist, Christian J.A., additional, Redaschi, Nicole, additional, Rivoire, Catherine, additional, Xenarios, Ioannis, additional, Kahn, Daniel, additional, Guyot, Dominique, additional, Bork, Peer, additional, Letunic, Ivica, additional, Gough, Julian, additional, Oates, Matt, additional, Haft, Daniel, additional, Huang, Hongzhan, additional, Natale, Darren A., additional, Wu, Cathy H., additional, Orengo, Christine, additional, Sillitoe, Ian, additional, Mi, Huaiyu, additional, Thomas, Paul D., additional, and Finn, Robert D., additional

Published
2014
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28. The SUPERFAMILY 1.75 database in 2014: a doubling of data

Author

Oates, Matt E., primary, Stahlhacke, Jonathan, additional, Vavoulis, Dimitrios V., additional, Smithers, Ben, additional, Rackham, Owen J.L., additional, Sardar, Adam J., additional, Zaucha, Jan, additional, Thurlby, Natalie, additional, Fang, Hai, additional, and Gough, Julian, additional

Published
2014
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29. Genome3D: exploiting structure to help users understand their sequences

Author

Lewis, Tony E., primary, Sillitoe, Ian, additional, Andreeva, Antonina, additional, Blundell, Tom L., additional, Buchan, Daniel W.A., additional, Chothia, Cyrus, additional, Cozzetto, Domenico, additional, Dana, José M., additional, Filippis, Ioannis, additional, Gough, Julian, additional, Jones, David T., additional, Kelley, Lawrence A., additional, Kleywegt, Gerard J., additional, Minneci, Federico, additional, Mistry, Jaina, additional, Murzin, Alexey G., additional, Ochoa-Montaño, Bernardo, additional, Oates, Matt E., additional, Punta, Marco, additional, Rackham, Owen J.L., additional, Stahlhacke, Jonathan, additional, Sternberg, Michael J.E., additional, Velankar, Sameer, additional, and Orengo, Christine, additional

Published
2014
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30. A Proteome Quality Index

Author

Zaucha, Jan, primary, Stahlhacke, Jonathan, additional, Oates, Matt E., additional, Thurlby, Natalie, additional, Rackham, Owen J. L., additional, Fang, Hai, additional, Smithers, Ben, additional, and Gough, Julian, additional

Published
2014
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32. D2P2: database of disordered protein predictions

Author

Oates, Matt E., primary, Romero, Pedro, additional, Ishida, Takashi, additional, Ghalwash, Mohamed, additional, Mizianty, Marcin J., additional, Xue, Bin, additional, Dosztányi, Zsuzsanna, additional, Uversky, Vladimir N., additional, Obradovic, Zoran, additional, Kurgan, Lukasz, additional, Dunker, A. Keith, additional, and Gough, Julian, additional

Published
2012
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33. A predictive computational framework for direct reprogramming between human cell types

Author

Rackham, Owen J L, Firas, Jaber, Fang, Hai, Oates, Matt E, Holmes, Melissa L, Knaupp, Anja S, Suzuki, Harukazu, Nefzger, Christian M, Daub, Carsten O, Shin, Jay W, Petretto, Enrico, Forrest, Alistair R R, Hayashizaki, Yoshihide, Polo, Jose M, and Gough, Julian

Abstract

Transdifferentiation, the process of converting from one cell type to another without going through a pluripotent state, has great promise for regenerative medicine. The identification of key transcription factors for reprogramming is currently limited by the cost of exhaustive experimental testing of plausible sets of factors, an approach that is inefficient and unscalable. Here we present a predictive system (Mogrify) that combines gene expression data with regulatory network information to predict the reprogramming factors necessary to induce cell conversion. We have applied Mogrify to 173 human cell types and 134 tissues, defining an atlas of cellular reprogramming. Mogrify correctly predicts the transcription factors used in known transdifferentiations. Furthermore, we validated two new transdifferentiations predicted by Mogrify. We provide a practical and efficient mechanism for systematically implementing novel cell conversions, facilitating the generalization of reprogramming of human cells. Predictions are made available to help rapidly further the field of cell conversion.

Published
2016
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34. A daily-updated tree of (sequenced) life as a reference for genome research.

Author

Hai Fang, Oates, Matt E., Pethica, Ralph B., Greenwood, Jenny M., Sardar, Adam J., Rackham, Owen J. L., Donoghue, Philip C. J., Stamatakis, Alexandros, de Lima Morais, David A., and Gough, Julian

Subjects
*GENOMES, *HAPLOIDY, *CELL receptors, *STEM cells, *PARASITIC plants
Abstract

We report a daily-updated sequenced/species Tree Of Life (sTOL) as a reference for the increasing number of cellular organisms with their genomes sequenced. The sTOL builds on a likelihood-based weight calibration algorithm to consolidate NCBI taxonomy information in concert with unbiased sampling of molecular characters from whole genomes of all sequenced organisms. Via quantifying the extent of agreement between taxonomic and molecular data, we observe there are many potential improvements that can be made to the status quo classification, particularly in the Fungi kingdom; we also see that the current state of many animal genomes is rather poor. To augment the use of sTOL in providing evolutionary contexts, we integrate an ontology infrastructure and demonstrate its utility for evolutionary understanding on: nuclear receptors, stem cells and eukaryotic genomes. The sTOL (http://supfam.org/SUPERFAMILY/ sTOL) provides a binary tree of (sequenced) life, and contributes to an analytical platform linking genome evolution, function and phenotype. [ABSTRACT FROM AUTHOR]

Published
2013
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36. The InterPro protein families database: the classification resource after 15 years

Author

Mitchell, Alex, Chang, Hsin-Yu, Daugherty, Louise, Fraser, Matthew, Hunter, Sarah, Lopez, Rodrigo, McAnulla, Craig, McMenamin, Conor, Nuka, Gift, Pesseat, Sebastien, Sangrador-Vegas, Amaia, Scheremetjew, Maxim, Rato, Claudia, Yong, Siew-Yit, Bateman, Alex, Punta, Marco, Attwood, Teresa K., Sigrist, Christian J.A., Redaschi, Nicole, Rivoire, Catherine, Xenarios, Ioannis, Kahn, Daniel, Guyot, Dominique, Bork, Peer, Letunic, Ivica, Gough, Julian, Oates, Matt, Haft, Daniel, Huang, Hongzhan, Natale, Darren A., Wu, Cathy H., Orengo, Christine, Sillitoe, Ian, Mi, Huaiyu, Thomas, Paul D., Finn, Robert D., Mitchell, Alex, Chang, Hsin-Yu, Daugherty, Louise, Fraser, Matthew, Hunter, Sarah, Lopez, Rodrigo, McAnulla, Craig, McMenamin, Conor, Nuka, Gift, Pesseat, Sebastien, Sangrador-Vegas, Amaia, Scheremetjew, Maxim, Rato, Claudia, Yong, Siew-Yit, Bateman, Alex, Punta, Marco, Attwood, Teresa K., Sigrist, Christian J.A., Redaschi, Nicole, Rivoire, Catherine, Xenarios, Ioannis, Kahn, Daniel, Guyot, Dominique, Bork, Peer, Letunic, Ivica, Gough, Julian, Oates, Matt, Haft, Daniel, Huang, Hongzhan, Natale, Darren A., Wu, Cathy H., Orengo, Christine, Sillitoe, Ian, Mi, Huaiyu, Thomas, Paul D., and Finn, Robert D.

Abstract

The InterPro database (http://www.ebi.ac.uk/interpro/) is a freely available resource that can be used to classify sequences into protein families and to predict the presence of important domains and sites. Central to the InterPro database are predictive models, known as signatures, from a range of different protein family databases that have different biological focuses and use different methodological approaches to classify protein families and domains. InterPro integrates these signatures, capitalizing on the respective strengths of the individual databases, to produce a powerful protein classification resource. Here, we report on the status of InterPro as it enters its 15th year of operation, and give an overview of new developments with the database and its associated Web interfaces and software. In particular, the new domain architecture search tool is described and the process of mapping of Gene Ontology terms to InterPro is outlined. We also discuss the challenges faced by the resource given the explosive growth in sequence data in recent years. InterPro (version 48.0) contains 36 766 member database signatures integrated into 26 238 InterPro entries, an increase of over 3993 entries (5081 signatures), since 2012

37. An expanded evaluation of protein function prediction methods shows an improvement in accuracy

Author

Yuxiang Jiang, Tal Ronnen Oron, Wyatt T. Clark, Asma R. Bankapur, Daniel D’Andrea, Rosalba Lepore, Christopher S. Funk, Indika Kahanda, Karin M. Verspoor, Asa Ben-Hur, Da Chen Emily Koo, Duncan Penfold-Brown, Dennis Shasha, Noah Youngs, Richard Bonneau, Alexandra Lin, Sayed M. E. Sahraeian, Pier Luigi Martelli, Giuseppe Profiti, Rita Casadio, Renzhi Cao, Zhaolong Zhong, Jianlin Cheng, Adrian Altenhoff, Nives Skunca, Christophe Dessimoz, Tunca Dogan, Kai Hakala, Suwisa Kaewphan, Farrokh Mehryary, Tapio Salakoski, Filip Ginter, Hai Fang, Ben Smithers, Matt Oates, Julian Gough, Petri Törönen, Patrik Koskinen, Liisa Holm, Ching-Tai Chen, Wen-Lian Hsu, Kevin Bryson, Domenico Cozzetto, Federico Minneci, David T. Jones, Samuel Chapman, Dukka BKC, Ishita K. Khan, Daisuke Kihara, Dan Ofer, Nadav Rappoport, Amos Stern, Elena Cibrian-Uhalte, Paul Denny, Rebecca E. Foulger, Reija Hieta, Duncan Legge, Ruth C. Lovering, Michele Magrane, Anna N. Melidoni, Prudence Mutowo-Meullenet, Klemens Pichler, Aleksandra Shypitsyna, Biao Li, Pooya Zakeri, Sarah ElShal, Léon-Charles Tranchevent, Sayoni Das, Natalie L. Dawson, David Lee, Jonathan G. Lees, Ian Sillitoe, Prajwal Bhat, Tamás Nepusz, Alfonso E. Romero, Rajkumar Sasidharan, Haixuan Yang, Alberto Paccanaro, Jesse Gillis, Adriana E. Sedeño-Cortés, Paul Pavlidis, Shou Feng, Juan M. Cejuela, Tatyana Goldberg, Tobias Hamp, Lothar Richter, Asaf Salamov, Toni Gabaldon, Marina Marcet-Houben, Fran Supek, Qingtian Gong, Wei Ning, Yuanpeng Zhou, Weidong Tian, Marco Falda, Paolo Fontana, Enrico Lavezzo, Stefano Toppo, Carlo Ferrari, Manuel Giollo, Damiano Piovesan, Silvio C.E. Tosatto, Angela del Pozo, José M. Fernández, Paolo Maietta, Alfonso Valencia, Michael L. Tress, Alfredo Benso, Stefano Di Carlo, Gianfranco Politano, Alessandro Savino, Hafeez Ur Rehman, Matteo Re, Marco Mesiti, Giorgio Valentini, Joachim W. Bargsten, Aalt D. J. van Dijk, Branislava Gemovic, Sanja Glisic, Vladmir Perovic, Veljko Veljkovic, Nevena Veljkovic, Danillo C. Almeida-e-Silva, Ricardo Z. N. Vencio, Malvika Sharan, Jörg Vogel, Lakesh Kansakar, Shanshan Zhang, Slobodan Vucetic, Zheng Wang, Michael J. E. Sternberg, Mark N. Wass, Rachael P. Huntley, Maria J. Martin, Claire O’Donovan, Peter N. Robinson, Yves Moreau, Anna Tramontano, Patricia C. Babbitt, Steven E. Brenner, Michal Linial, Christine A. Orengo, Burkhard Rost, Casey S. Greene, Sean D. Mooney, Iddo Friedberg, Predrag Radivojac, Jiang, Yuxiang, Oron, Tal Ronnen, Clark, Wyatt T., Bankapur, Asma R., D’Andrea, Daniel, Lepore, Rosalba, Funk, Christopher S., Kahanda, Indika, Verspoor, Karin M., Ben-Hur, Asa, Koo, Da Chen Emily, Penfold-Brown, Duncan, Shasha, Denni, Youngs, Noah, Bonneau, Richard, Lin, Alexandra, Sahraeian, Sayed M. E., Martelli, Pier Luigi, Profiti, Giuseppe, Casadio, Rita, Cao, Renzhi, Zhong, Zhaolong, Cheng, Jianlin, Altenhoff, Adrian, Skunca, Nive, Dessimoz, Christophe, Dogan, Tunca, Hakala, Kai, Kaewphan, Suwisa, Mehryary, Farrokh, Salakoski, Tapio, Ginter, Filip, Fang, Hai, Smithers, Ben, Oates, Matt, Gough, Julian, Törönen, Petri, Koskinen, Patrik, Holm, Liisa, Chen, Ching-Tai, Hsu, Wen-Lian, Bryson, Kevin, Cozzetto, Domenico, Minneci, Federico, Jones, David T., Chapman, Samuel, Bkc, Dukka, Khan, Ishita K., Kihara, Daisuke, Ofer, Dan, Rappoport, Nadav, Stern, Amo, Cibrian-Uhalte, Elena, Denny, Paul, Foulger, Rebecca E., Hieta, Reija, Legge, Duncan, Lovering, Ruth C., Magrane, Michele, Melidoni, Anna N., Mutowo-Meullenet, Prudence, Pichler, Klemen, Shypitsyna, Aleksandra, Li, Biao, Zakeri, Pooya, Elshal, Sarah, Tranchevent, Léon-Charle, Das, Sayoni, Dawson, Natalie L., Lee, David, Lees, Jonathan G., Sillitoe, Ian, Bhat, Prajwal, Nepusz, Tamá, Romero, Alfonso E., Sasidharan, Rajkumar, Yang, Haixuan, Paccanaro, Alberto, Gillis, Jesse, Sedeño-Cortés, Adriana E., Pavlidis, Paul, Feng, Shou, Cejuela, Juan M., Goldberg, Tatyana, Hamp, Tobia, Richter, Lothar, Salamov, Asaf, Gabaldon, Toni, Marcet-Houben, Marina, Supek, Fran, Gong, Qingtian, Ning, Wei, Zhou, Yuanpeng, Tian, Weidong, Falda, Marco, Fontana, Paolo, Lavezzo, Enrico, Toppo, Stefano, Ferrari, Carlo, Giollo, Manuel, Piovesan, Damiano, Tosatto, Silvio C.E., del Pozo, Angela, Fernández, José M., Maietta, Paolo, Valencia, Alfonso, Tress, Michael L., Benso, Alfredo, Di Carlo, Stefano, Politano, Gianfranco, Savino, Alessandro, Rehman, Hafeez Ur, Re, Matteo, Mesiti, Marco, Valentini, Giorgio, Bargsten, Joachim W., van Dijk, Aalt D. J., Gemovic, Branislava, Glisic, Sanja, Perovic, Vladmir, Veljkovic, Veljko, Veljkovic, Nevena, Almeida-e-Silva, Danillo C., Vencio, Ricardo Z. N., Sharan, Malvika, Vogel, Jörg, Kansakar, Lakesh, Zhang, Shanshan, Vucetic, Slobodan, Wang, Zheng, Sternberg, Michael J. E., Wass, Mark N., Huntley, Rachael P., Martin, Maria J., O’Donovan, Claire, Robinson, Peter N., Moreau, Yve, Tramontano, Anna, Babbitt, Patricia C., Brenner, Steven E., Linial, Michal, Orengo, Christine A., Rost, Burkhard, Greene, Casey S., Mooney, Sean D., Friedberg, Iddo, Radivojac, Predrag, Friedberg, Iddo [0000-0002-1789-8000], Apollo - University of Cambridge Repository, (ukupan broj autora: 147), Biotechnology and Biological Sciences Research Council (BBSRC), National Science Foundation (Estados Unidos), United States of Department of Health & Human Services, National Natural Science Foundation of China, Natural Sciences and Engineering Research Council (Canadá), São Paulo Research Foundation, Ministerio de Economía y Competitividad (España), Biotechnology and Biological Sciences Research Council (Reino Unido), Katholieke Universiteit Leuven (Bélgica), Newton International Fellowship Scheme of the Royal Society grant, British Heart Foundation, Ministry of Education, Science and Technological Development (Serbia), Office of Biological and Environmental Research (Estados Unidos), Australian Research Council, University of Padua (Italia), Swiss National Science Foundation, Institute of Biotechnology, Computational genomics, and Bioinformatics

Subjects
0301 basic medicine, Computer science, Disease gene prioritization, Protein function prediction, Ecology, Evolution, Behavior and Systematics, Genetics, Cell Biology, 05 Environmental Sciences, 600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit, computer.software_genre, Quantitative Biology - Quantitative Methods, Wiskundige en Statistische Methoden - Biometris, Field (computer science), Laboratorium voor Plantenveredeling, Function (engineering), Databases, Protein, 1183 Plant biology, microbiology, virology, Quantitative Methods (q-bio.QM), media_common, Genetics & Heredity, Settore BIO/11 - BIOLOGIA MOLECOLARE, Ecology, SISTA, 1184 Genetics, developmental biology, physiology, Life Sciences & Biomedicine, Algorithms, Bioinformatics, Evolution, media_common.quotation_subject, BIOINFORMÁTICA, Machine learning, Bottleneck, Set (abstract data type), BIOS Applied Bioinformatics, 03 medical and health sciences, Annotation, Structure-Activity Relationship, Behavior and Systematics, Human Phenotype Ontology, Humans, ddc:610, DISINTEGRIN, Mathematical and Statistical Methods - Biometris, BIOINFORMATICS, 08 Information And Computing Sciences, Science & Technology, business.industry, Research, ADAM, Proteins, Computational Biology, Molecular Sequence Annotation, 06 Biological Sciences, Data set, ONTOLOGY, Plant Breeding, 030104 developmental biology, Gene Ontology, Biotechnology & Applied Microbiology, FOS: Biological sciences, Artificial intelligence, business, computer, Software
Abstract

BACKGROUND: A major bottleneck in our understanding of the molecular underpinnings of life is the assignment of function to proteins. While molecular experiments provide the most reliable annotation of proteins, their relatively low throughput and restricted purview have led to an increasing role for computational function prediction. However, assessing methods for protein function prediction and tracking progress in the field remain challenging. RESULTS: We conducted the second critical assessment of functional annotation (CAFA), a timed challenge to assess computational methods that automatically assign protein function. We evaluated 126 methods from 56 research groups for their ability to predict biological functions using Gene Ontology and gene-disease associations using Human Phenotype Ontology on a set of 3681 proteins from 18 species. CAFA2 featured expanded analysis compared with CAFA1, with regards to data set size, variety, and assessment metrics. To review progress in the field, the analysis compared the best methods from CAFA1 to those of CAFA2. CONCLUSIONS: The top-performing methods in CAFA2 outperformed those from CAFA1. This increased accuracy can be attributed to a combination of the growing number of experimental annotations and improved methods for function prediction. The assessment also revealed that the definition of top-performing algorithms is ontology specific, that different performance metrics can be used to probe the nature of accurate predictions, and the relative diversity of predictions in the biological process and human phenotype ontologies. While there was methodological improvement between CAFA1 and CAFA2, the interpretation of results and usefulness of individual methods remain context-dependent., We acknowledge the contributions of Maximilian Hecht, Alexander Grün, Julia Krumhoff, My Nguyen Ly, Jonathan Boidol, Rene Schoeffel, Yann Spöri, Jessika Binder, Christoph Hamm and Karolina Worf. This work was partially supported by the following grants: National Science Foundation grants DBI-1458477 (PR), DBI-1458443 (SDM), DBI-1458390 (CSG), DBI-1458359 (IF), IIS-1319551 (DK), DBI-1262189 (DK), and DBI-1149224 (JC); National Institutes of Health grants R01GM093123 (JC), R01GM097528 (DK), R01GM076990 (PP), R01GM071749 (SEB), R01LM009722 (SDM), and UL1TR000423 (SDM); the National Natural Science Foundation of China grants 3147124 (WT) and 91231116 (WT); the National Basic Research Program of China grant 2012CB316505 (WT); NSERC grant RGPIN 371348-11 (PP); FP7 infrastructure project TransPLANT Award 283496 (ADJvD); Microsoft Research/FAPESP grant 2009/53161-6 and FAPESP fellowship 2010/50491-1 (DCAeS); Biotechnology and Biological Sciences Research Council grants BB/L020505/1 (DTJ), BB/F020481/1 (MJES), BB/K004131/1 (AP), BB/F00964X/1 (AP), and BB/L018241/1 (CD); the Spanish Ministry of Economics and Competitiveness grant BIO2012-40205 (MT); KU Leuven CoE PFV/10/016 SymBioSys (YM); the Newton International Fellowship Scheme of the Royal Society grant NF080750 (TN). CSG was supported in part by the Gordon and Betty Moore Foundation’s Data-Driven Discovery Initiative grant GBMF4552. Computational resources were provided by CSC – IT Center for Science Ltd., Espoo, Finland (TS). This work was supported by the Academy of Finland (TS). RCL and ANM were supported by British Heart Foundation grant RG/13/5/30112. PD, RCL, and REF were supported by Parkinson’s UK grant G-1307, the Alexander von Humboldt Foundation through the German Federal Ministry for Education and Research, Ernst Ludwig Ehrlich Studienwerk, and the Ministry of Education, Science and Technological Development of the Republic of Serbia grant 173001. This work was a Technology Development effort for ENIGMA – Ecosystems and Networks Integrated with Genes and Molecular Assemblies (http://enigma.lbl.gov), a Scientific Focus Area Program at Lawrence Berkeley National Laboratory, which is based upon work supported by the U.S. Department of Energy, Office of Science, Office of Biological & Environmental Research grant DE-AC02-05CH11231. ENIGMA only covers the application of this work to microbial proteins. NSF DBI-0965616 and Australian Research Council grant DP150101550 (KMV). NSF DBI-0965768 (ABH). NIH T15 LM00945102 (training grant for CSF). FP7 FET grant MAESTRA ICT-2013-612944 and FP7 REGPOT grant InnoMol (FS). NIH R01 GM60595 (PCB). University of Padova grants CPDA138081/13 (ST) and GRIC13AAI9 (EL). Swiss National Science Foundation grant 150654 and UK BBSRC grant BB/M015009/1 (COD). PRB2 IPT13/0001 - ISCIII-SGEFI / FEDER (JMF)., This is the final version of the article. It first appeared from BioMed Central at http://dx.doi.org/10.1186/s13059-016-1037-6.

Published
2016

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