Current Work

I am currently working on stastistical methods for analysis high-throughput data of genomics.

You could contact me at arnaud.droit@ircm.qc.ca

Past work

I completed my PhD in 2007 in the laboratories of Guy Poirier and Jean Morissette at the Laval University in Quebec city where I studied the algorithms of proteins identification in mass spectrometry. After, I started a post-doc in mass spectrometry to study the identification of phospho peptides by mass spectrometry. After that, I was an bioinformatics develloper in a pharma company (Genizon Bioscience) before joining Raphael Gottardo’s lab. I am working on statistical methods for high-throughput data of genomics.

Publications Work

This is my bibliography maintained at citeulike.org

• [2008,article] bibtex
  F. X. Wu, P. Gagné, A. Droit, and G. G. Poirier, "Quality assessment of peptide tandem mass spectra.," BMC bioinformatics, vol. 9 Suppl 6, 2008.
  @article{Article, abstract = {BACKGROUND: Tandem mass spectrometry has emerged as a cornerstone of high throughput proteomic studies owing in part to various high throughput search engines which are used to interpret these tandem mass spectra. However, majority of experimental tandem mass spectra cannot be interpreted by any existing methods. There are many reasons why this happens. However, one of the most important reasons is that majority of experimental spectra are of too poor quality to be interpretable. It wastes time to interpret these "uninterpretable" spectra by any methods. On the other hand, some spectra of high quality are not able to get a score high enough to be interpreted by existing search engines because there are many similar peptides in the searched database. However, such spectra may be good enough to be interpreted by de novo methods or manually verifying methods. Therefore, it is worth in developing a method for assessing spectral quality, which can used for filtering the spectra of poor quality before any interpretation attempts or for finding the most potential candidates for de novo methods or manually verifying methods. RESULTS: This paper develops a novel method to assess the quality of tandem mass spectra, which can eliminate majority of poor quality spectra while losing very minority of high quality spectra. First, a number of features are proposed to describe the quality of tandem mass spectra. The proposed method maps each tandem spectrum into a feature vector. Then Fisher linear discriminant analysis (FLDA) is employed to construct the classifier (the filter) which discriminates the high quality spectra from the poor quality ones. The proposed method has been tested on two tandem mass spectra datasets acquired by ion trap mass spectrometers. CONCLUSION: Computational experiments illustrate that the proposed method outperforms the existing ones. The proposed method is generic, and is expected to be applicable to assessing the quality of spectra acquired by instruments other than ion trap mass spectrometers.},
  author = {Wu, F. X. and Gagn\'{e},
  P. and Droit, A. and Poirier, G. G.},
  citeulike-article-id = {3575659},
  citeulike-linkout-0 = {http://dx.doi.org/10.1186/1471-2105-9-S6-S13},
  citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18541048},
  citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18541048},
  doi = {10.1186/1471-2105-9-S6-S13},
  issn = {1471-2105},
  journal = {BMC bioinformatics},
  keywords = {proteomics},
  posted-at = {2008-11-18 19:14:44},
  priority = {2},
  title = {Quality assessment of peptide tandem mass spectra.},
  url = {http://dx.doi.org/10.1186/1471-2105-9-S6-S13},
  volume = {9 Suppl 6},
  year = {2008}
}
• [2007,article] bibtex
  J. Gagne, C. Ethier, P. Gagne, G. Mercier, M. Bonicalzi, A. Mes-Masson, A. Droit, E. Winstall, M. Isabelle, and G. G. Poirier, "Comparative proteome analysis of human epithelial ovarian cancer," Proteome Science, vol. 5, p. 16, 2007.
  @article{Article,
  author = {Gagne, Jean-Philippe and Ethier, Chantal and Gagne, Pierre and Mercier, Genevieve and Bonicalzi, Marie-Eve and Mes-Masson, Anne-Marie and Droit, Arnaud and Winstall, Eric and Isabelle, Maxim and Poirier, Guy G.},
  citeulike-article-id = {1691712},
  citeulike-linkout-0 = {http://dx.doi.org/10.1186/1477-5956-5-16},
  citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17892554},
  citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17892554},
  day = {24},
  doi = {10.1186/1477-5956-5-16},
  issn = {1477-5956},
  journal = {Proteome Science},
  keywords = {bioinformatics, proteomics},
  month = {September},
  pages = {16+},
  posted-at = {2008-11-18 19:24:04},
  priority = {2},
  title = {Comparative proteome analysis of human epithelial ovarian cancer},
  url = {http://dx.doi.org/10.1186/1477-5956-5-16},
  volume = {5},
  year = {2007}
}
• [2007,article] bibtex
  A. Droit, J. Hunter, M. Rouleau, C. Ethier, A. P. Cloutier, D. Bourgais, and G. Poirier, "PARPs Database: A LIMS systems for protein-protein interaction data mining or Laboratory Information management system," BMC Bioinformatics, vol. 8, iss. 1, 2007.
  @article{Article, abstract = {BACKGROUND:In the apost-genomea era, mass spectrometry (MS) has become an important method for the analysis of proteins and the rapid advancement of this technique, in combination with other proteomics methods, results in an increasing amount of proteome data. This data must be archived and analysed using specialized bioinformatics tools. Description: We herein describe aPARPs database,a a data analysis and management pipeline for liquid chromatography tandem mass spectrometry (LC-MS/MS) proteomics. PARPs database is a web-based tool whose features include experiment annotation, protein database searching, protein sequence management, as well as data-mining of the peptides and proteins identified.CONCLUSIONS:Using this pipeline, we have successfully identified several interactions of biological significance between PARP-1 and other proteins, namely RFC-1, 2, 3, 4 and 5.},
  author = {Droit, Arnaud and Hunter, Joanna and Rouleau, Michele and Ethier, Chantal and Cloutier, Aude P. and Bourgais, David and Poirier, Guy},
  citeulike-article-id = {2149519},
  citeulike-linkout-0 = {http://dx.doi.org/10.1186/1471-2105-8-483},
  citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18093328},
  citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18093328},
  doi = {10.1186/1471-2105-8-483},
  journal = {BMC Bioinformatics},
  keywords = {bioinformatics, proteomics},
  number = {1},
  posted-at = {2008-11-18 19:17:01},
  priority = {2},
  title = {PARPs Database: A LIMS systems for protein-protein interaction data mining or Laboratory Information management system},
  url = {http://dx.doi.org/10.1186/1471-2105-8-483},
  volume = {8},
  year = {2007}
}
• [2007,article] bibtex
  M. Rouleau, D. McDonald, P. Gagné, M. E. Ouellet, A. Droit, J. M. Hunter, S. Dutertre, C. Prigent, M. J. Hendzel, and G. G. Poirier, "PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery.," Journal of cellular biochemistry, vol. 100, iss. 2, pp. 385-401, 2007.
  @article{Article, abstract = {Poly(ADP-ribose) polymerase 3 (PARP-3) is a novel member of the PARP family of enzymes that synthesize poly(ADP-ribose) on themselves and other acceptor proteins. Very little is known about this PARP, which is closely related to PARP-1 and PARP-2. By sequence analysis, we find that PARP-3 may be expressed in two isoforms which we studied in more detail to gain insight into their possible functions. We find that both PARP-3 isoforms, transiently expressed as GFP or FLAG fusions, are nuclear. Detection of endogenous PARP-3 with a specific antibody also shows a widespread nuclear distribution, appearing in numerous small foci and a small number of larger foci. Through co-localization experiments and immunoprecipitations, the larger nuclear foci were identified as Polycomb group bodies (PcG bodies) and we found that PARP-3 is part of Polycomb group protein complexes. Furthermore, using a proteomics approach, we determined that both PARP-3 isoforms are part of complexes comprising DNA-PKcs, PARP-1, DNA ligase III, DNA ligase IV, Ku70, and Ku80. Our findings suggest that PARP-3 is a nuclear protein involved in transcriptional silencing and in the cellular response to DNA damage.},
  author = {Rouleau, M. and McDonald, D. and Gagn\'{e},
  P. and Ouellet, M. E. and Droit, A. and Hunter, J. M. and Dutertre, S. and Prigent, C. and Hendzel, M. J. and Poirier, G. G.},
  citeulike-article-id = {3575673},
  citeulike-linkout-0 = {http://dx.doi.org/10.1002/jcb.21051},
  citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16924674},
  citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16924674},
  day = {1},
  doi = {10.1002/jcb.21051},
  issn = {0730-2312},
  journal = {Journal of cellular biochemistry},
  keywords = {parps, proteomics},
  month = {February},
  number = {2},
  pages = {385--401},
  posted-at = {2008-11-18 19:24:51},
  priority = {2},
  title = {PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery.},
  url = {http://dx.doi.org/10.1002/jcb.21051},
  volume = {100},
  year = {2007}
}
• [2006,article] bibtex
  F. X. Wu, P. Gagné, A. Droit, and G. G. Poirier, "RT-PSM, a real-time program for peptide-spectrum matching with statistical significance.," Rapid communications in mass spectrometry : RCM, vol. 20, iss. 8, pp. 1199-1208, 2006.
  @article{Article, abstract = {The analysis of complex biological peptide mixtures by tandem mass spectrometry (MS/MS) produces a huge body of collision-induced dissociation (CID) MS/MS spectra. Several methods have been developed for identifying peptide-spectrum matches (PSMs) by assigning MS/MS spectra to peptides in a database. However, most of these methods either do not give the statistical significance of PSMs (e.g., SEQUEST) or employ time-consuming computational methods to estimate the statistical significance (e.g., PeptideProphet). In this paper, we describe a new algorithm, RT-PSM, which can be used to identify PSMs and estimate their accuracy statistically in real time. RT-PSM first computes PSM scores between an MS/MS spectrum and a set of candidate peptides whose masses are within a preset tolerance of the MS/MS precursor ion mass. Then the computed PSM scores of all candidate peptides are employed to fit the expectation value distribution of the scores into a second-degree polynomial function in PSM score. The statistical significance of the best PSM is estimated by extrapolating the fitting polynomial function to the best PSM score. RT-PSM was tested on two pairs of MS/MS spectrum datasets and protein databases to investigate its performance. The MS/MS spectra were acquired using an ion trap mass spectrometer equipped with a nano-electrospray ionization source. The results show that RT-PSM has good sensitivity and specificity. Using a 55,577-entry protein database and running on a standard Pentium-4, 2.8-GHz CPU personal computer, RT-PSM can process peptide spectra on a sequential, one-by-one basis in 0.047 s on average, compared to more than 7 s per spectrum on average for Sequest and X!Tandem, in their current batch-mode processing implementations. RT-PSM is clearly shown to be fast enough for real-time PSM assignment of MS/MS spectra generated every 3 s or so by a 3D ion trap or by a QqTOF instrument.},
  author = {Wu, F. X. and Gagn\'{e},
  P. and Droit, A. and Poirier, G. G.},
  citeulike-article-id = {3575674},
  citeulike-linkout-0 = {http://dx.doi.org/10.1002/rcm.2435},
  citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16541396},
  citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16541396},
  doi = {10.1002/rcm.2435},
  issn = {0951-4198},
  journal = {Rapid communications in mass spectrometry : RCM},
  keywords = {bioinformatics, proteomics},
  number = {8},
  pages = {1199--1208},
  posted-at = {2008-11-18 19:25:47},
  priority = {2},
  title = {RT-PSM, a real-time program for peptide-spectrum matching with statistical significance.},
  url = {http://dx.doi.org/10.1002/rcm.2435},
  volume = {20},
  year = {2006}
}
• [2006,article] bibtex
  J. P. Gagné, M. J. Hendzel, A. Droit, and G. G. Poirier, "The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives.," Current opinion in cell biology, vol. 18, iss. 2, pp. 145-151, 2006.
  @article{Article, abstract = {Recent discoveries have resulted in significant breakthroughs in the understanding of PARPs and PARG functions within a broad range of cellular processes. The novel and sometimes unexpected pathways that are regulated by poly(ADP-ribosylation) bring new questions and hypotheses, some of them being contentious. In this review, we highlight current areas of investigation such as the clinical potential of PARP and PARG inhibitors and the important mitotic regulatory functions of poly(ADP-ribose) in cell-cycle progression, a recent discovery that has broadened our knowledge regarding poly(ADP-ribose) functions. A special emphasis is placed on recent advances in relation to PARG that are stimulating new directions in future research. Noticeably, the existence of various PARG isoforms characterized by distinct cellular localizations and nucleocytoplasmic shuttling properties challenges our current comprehension of pADPr metabolism. Observations and suppositions towards functionally important regulatory elements in the N-terminal portion of PARG are also discussed.},
  author = {Gagn\'{e},
  J. P. and Hendzel, M. J. and Droit, A. and Poirier, G. G.},
  citeulike-article-id = {3575676},
  citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.ceb.2006.02.013},
  citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16516457},
  citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16516457},
  doi = {10.1016/j.ceb.2006.02.013},
  issn = {0955-0674},
  journal = {Current opinion in cell biology},
  keywords = {parps, proteomics},
  month = {April},
  number = {2},
  pages = {145--151},
  posted-at = {2008-11-18 19:26:38},
  priority = {2},
  title = {The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives.},
  url = {http://dx.doi.org/10.1016/j.ceb.2006.02.013},
  volume = {18},
  year = {2006}
}
• [2005,article] bibtex
  A. Droit, G. G. Poirier, and J. M. Hunter, "Experimental and bioinformatic approaches for interrogating protein-protein interactions to determine protein function," J Mol Endocrinol, vol. 34, iss. 2, pp. 263-280, 2005.
  @article{Article, abstract = {An ambitious goal of proteomics is to elucidate the structure, interactions and functions of all proteins within cells and organisms. One strategy to determine protein function is to identify the protein-protein interactions. The increasing use of high-throughput and large-scale bioinformatics-based studies has generated a massive amount of data stored in a number of different databases. A challenge for bioinformatics is to explore this disparate data and to uncover biologically relevant interactions and pathways. In parallel, there is clearly a need for the development of approaches that can predict novel protein-protein interaction networks in silico. Here, we present an overview of different experimental and bioinformatic methods to elucidate protein-protein interactions. 10.1677/jme.1.01693},
  author = {Droit, Arnaud and Poirier, Guy G. and Hunter, Joanna M.},
  citeulike-article-id = {2911266},
  citeulike-linkout-0 = {http://dx.doi.org/10.1677/jme.1.01693},
  citeulike-linkout-1 = {http://jme.endocrinology-journals.org/cgi/content/abstract/34/2/263},
  citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/15821096},
  citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=15821096},
  day = {1},
  doi = {10.1677/jme.1.01693},
  journal = {J Mol Endocrinol},
  keywords = {interaction, protein},
  month = {April},
  number = {2},
  pages = {263--280},
  posted-at = {2008-11-18 19:28:49},
  priority = {2},
  title = {Experimental and bioinformatic approaches for interrogating protein-protein interactions to determine protein function},
  url = {http://dx.doi.org/10.1677/jme.1.01693},
  volume = {34},
  year = {2005}
}
• [2005,article] bibtex
  M. E. Bonicalzi, J. F. Haince, A. Droit, and G. G. Poirier, "Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when?," Cell Mol Life Sci, vol. 62, iss. 7-8, pp. 739-750, 2005.
  @article{citeulike:238911, abstract = {Poly(ADP-ribose) glycohydrolase (PARG) is a catabolic enzyme that cleaves ADP-ribose polymers formed by members of the PARP family of enzymes. Despite its discovery and subsequent partial purification in the 1970s and the cloning of its single gene in the late 1990s, little is known about the role of PARG in cell function. Because of its low abundance within cells and its extreme sensitivity to proteases, PARG has been difficult to study. The existence of several PARG isoforms with different subcellular localizations is still debated today after more than 30 years of intensive research. In this article, we want to summarize and discuss the current knowledge related to PARG, its different forms and subcellular distribution. We also examine the possible biological roles of PARG in modulating chromatin structure, transcription, DNA repair and apoptosis.},
  address = {CHUL Research Centre Room RC-9700, Faculty of Medicine, Laval University, 2705, Laurier blvd, Ste-Foy, Qu\'{e}bec G1V 4G2, Canada.},
  author = {Bonicalzi, M. E. and Haince, J. F. and Droit, A. and Poirier, G. G.},
  citeulike-article-id = {238911},
  citeulike-linkout-0 = {http://dx.doi.org/10.1007/s00018-004-4505-1},
  citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15868399},
  citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15868399},
  doi = {10.1007/s00018-004-4505-1},
  issn = {1420-682X},
  journal = {Cell Mol Life Sci},
  keywords = {parps},
  month = {April},
  number = {7-8},
  pages = {739--750},
  posted-at = {2008-11-18 19:28:02},
  priority = {2},
  title = {Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when?},
  url = {http://dx.doi.org/10.1007/s00018-004-4505-1},
  volume = {62},
  year = {2005}
}
• [2005,article] bibtex
  J. P. Gagné, P. Gagné, J. M. Hunter, M. E. Bonicalzi, J. F. Lemay, I. Kelly, C. Le Page, D. Provencher, A. M. Mes-Masson, A. Droit, D. Bourgais, and G. G. Poirier, "Proteome profiling of human epithelial ovarian cancer cell line TOV-112D.," Molecular and cellular biochemistry, vol. 275, iss. 1-2, pp. 25-55, 2005.
  @article{citeulike:3575679, abstract = {A proteome profiling of the epithelial ovarian cancer cell line TOV-112D was initiated as a protein expression reference in the study of ovarian cancer. Two complementary proteomic approaches were used in order to maximise protein identification: two-dimensional gel electrophoresis (2DE) protein separation coupled to matrix assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF MS) and one-dimensional gel electrophoresis (1DE) coupled to liquid-chromatography tandem mass spectrometry (LC MS/MS). One hundred and seventy-two proteins have been identified among 288 spots selected on two-dimensional gels and a total of 579 proteins were identified with the 1DE LC MS/MS approach. This proteome profiling covers a wide range of protein expression and identifies several proteins known for their oncogenic properties. Bioinformatics tools were used to mine databases in order to determine whether the identified proteins have previously been implicated in pathways associated with carcinogenesis or cell proliferation. Indeed, several of the proteins have been reported to be specific ovarian cancer markers while others are common to many tumorigenic tissues or proliferating cells. The diversity of proteins found and their association with known oncogenic pathways validate this proteomic approach. The proteome 2D map of the TOV-112D cell line will provide a valuable resource in studies on differential protein expression of human ovarian carcinomas while the 1DE LC MS/MS approach gives a picture of the actual protein profile of the TOV-112D cell line. This work represents one of the most complete ovarian protein expression analysis reports to date and the first comparative study of gene expression profiling and proteomic patterns in ovarian cancer.},
  author = {Gagn\'{e},
  J. P. and Gagn\'{e},
  P. and Hunter, J. M. and Bonicalzi, M. E. and Lemay, J. F. and Kelly, I. and Le Page, C. and Provencher, D. and Mes-Masson, A. M. and Droit, A. and Bourgais, D. and Poirier, G. G.},
  citeulike-article-id = {3575679},
  citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/16335783},
  citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=16335783},
  issn = {0300-8177},
  journal = {Molecular and cellular biochemistry},
  keywords = {proteomics},
  month = {July},
  number = {1-2},
  pages = {25--55},
  posted-at = {2008-11-18 19:27:24},
  priority = {2},
  title = {Proteome profiling of human epithelial ovarian cancer cell line TOV-112D.},
  url = {http://view.ncbi.nlm.nih.gov/pubmed/16335783},
  volume = {275},
  year = {2005}
}
• [1998,article] bibtex
  J. Lugtenburg and H. de Groot, "Characterization of photosynthetic reaction centers with specific isotope labels," Photosynthesis Research, vol. 55, iss. 2, pp. 241-245, 1998.
  @article{citeulike:3561603, abstract = {In this minireview the information at the atomic level that has been obtained by studying photosynthetic reaction centers with site-directed isotope labelling is discussed. The required isotopically labelled RCs are prepared using isotopically labelled amino acids and cofactors that have been prepared via organic total synthetic chemistry. In some cases the results of isotopically labelled RCs that are prepared via other methods are also discussed.},
  author = {Lugtenburg, Johan and de Groot, Huub},
  citeulike-article-id = {3561603},
  citeulike-linkout-0 = {http://dx.doi.org/10.1023/A:1005993115333},
  citeulike-linkout-1 = {http://www.springerlink.com/content/x2108407110kk76g},
  day = {21},
  doi = {10.1023/A:1005993115333},
  journal = {Photosynthesis Research},
  keywords = {test},
  month = {March},
  number = {2},
  pages = {241--245},
  posted-at = {2008-11-17 19:49:56},
  priority = {2},
  title = {Characterization of photosynthetic reaction centers with specific isotope labels},
  url = {http://dx.doi.org/10.1023/A:1005993115333},
  volume = {55},
  year = {1998}
}
• [,article] bibtex
  S. Mathivanan, M. Ahmed, N. G. Ahn, H. Alexandre, R. Amanchy, P. C. Andrews, J. S. Bader, B. M. Balgley, M. Bantscheff, K. L. Bennett, E. Björling, B. Blagoev, R. Bose, S. K. Brahmachari, A. S. Burlingame, X. R. Bustelo, G. Cagney, G. T. Cantin, H. L. Cardasis, J. E. Celis, R. Chaerkady, F. Chu, P. A. Cole, C. E. Costello, R. J. Cotter, D. Crockett, J. P. Delany, A. M. De Marzo, L. V. Desouza, E. W. Deutsch, E. Dransfield, G. Drewes, A. Droit, M. J. Dunn, K. Elenitoba-Johnson, R. M. Ewing, J. Van Eyk, V. Faca, J. Falkner, X. Fang, C. Fenselau, D. Figeys, P. Gagné, C. Gelfi, K. Gevaert, J. M. Gimble, F. Gnad, R. Goel, P. Gromov, S. M. Hanash, W. S. Hancock, H. C. Harsha, G. Hart, F. Hays, F. He, P. Hebbar, K. Helsens, H. Hermeking, W. Hide, K. Hjernø, D. F. Hochstrasser, O. Hofmann, D. M. Horn, R. H. Hruban, N. Ibarrola, P. James, O. N. Jensen, P. H. Jensen, P. Jung, K. Kandasamy, I. Kheterpal, R. F. Kikuno, U. Korf, R. Körner, B. Kuster, M. Kwon, H. Lee, Y. Lee, M. Lefevre, M. Lehvaslaiho, P. Lescuyer, F. Levander, M. S. Lim, C. Löbke, J. A. Loo, M. Mann, L. Martens, J. Martinez-Heredia, M. Mccomb, J. Mcredmond, A. Mehrle, R. Menon, C. A. Miller, H. Mischak, S. S. Mohan, R. Mohmood, H. Molina, M. F. Moran, J. D. Morgan, R. Moritz, M. Morzel, D. C. Muddiman, A. Nalli, D. J. Navarro, T. A. Neubert, O. Ohara, R. Oliva, G. S. Omenn, M. Oyama, Y. Paik, K. Pennington, R. Pepperkok, B. Periaswamy, E. F. Petricoin, G. G. Poirier, K. T. S. Prasad, S. O. Purvine, A. B. Rahiman, P. Ramachandran, Y. L. Ramachandra, R. H. Rice, J. Rick, R. H. Ronnholm, J. Salonen, J. Sanchez, T. Sayd, B. Seshi, K. Shankari, S. J. Sheng, V. Shetty, K. Shivakumar, R. J. Simpson, R. Sirdeshmukh, M. K. W. Siu, J. C. Smith, R. D. Smith, D. J. States, S. Sugano, M. Sullivan, G. Superti-Furga, M. Takatalo, V. Thongboonkerd, J. C. Trinidad, M. Uhlen, J. Vandekerckhove, J. Vasilescu, T. D. Veenstra, J. Vidal-Taboada, M. Vihinen, R. Wait, X. Wang, S. Wiemann, B. Wu, T. Xu, J. R. Yates, J. Zhong, M. Zhou, Y. Zhu, P. Zurbig, and A. Pandey, "Human Proteinpedia enables sharing of human protein data," Nature Biotechnology, vol. 26, iss. 2, pp. 164-167.
  @article{Article,
  author = {Mathivanan, Suresh and Ahmed, Mukhtar and Ahn, Natalie G. and Alexandre, Hainard and Amanchy, Ramars and Andrews, Philip C. and Bader, Joel S. and Balgley, Brian M. and Bantscheff, Marcus and Bennett, Keiryn L. and Bj\"{o}rling, Erik and Blagoev, Blagoy and Bose, Ron and Brahmachari, Samir K. and Burlingame, Alma S. and Bustelo, Xos\'{e} R. and Cagney, Gerard and Cantin, Greg T. and Cardasis, Helene L. and Celis, Julio E. and Chaerkady, Raghothama and Chu, Feixia and Cole, Philip A. and Costello, Catherine E. and Cotter, Robert J. and Crockett, David and Delany, James P. and De Marzo, Angelo M. and Desouza, Leroi V. and Deutsch, Eric W. and Dransfield, Eric and Drewes, Gerard and Droit, Arnaud and Dunn, Michael J. and Elenitoba-Johnson, Kojo and Ewing, Rob M. and Van Eyk, Jennifer and Faca, Vitor and Falkner, Jayson and Fang, Xiangming and Fenselau, Catherine and Figeys, Daniel and Gagn\'{e},
  Pierre and Gelfi, Cecilia and Gevaert, Kris and Gimble, Jeffrey M. and Gnad, Florian and Goel, Renu and Gromov, Pavel and Hanash, Samir M. and Hancock, William S. and Harsha, H. C. and Hart, Gerald and Hays, Faith and He, Fuchu and Hebbar, Prashantha and Helsens, Kenny and Hermeking, Heiko and Hide, Winston and Hjern{\o},
  Karin and Hochstrasser, Denis F. and Hofmann, Oliver and Horn, David M. and Hruban, Ralph H. and Ibarrola, Nieves and James, Peter and Jensen, Ole N. and Jensen, Pia H. and Jung, Peter and Kandasamy, Kumaran and Kheterpal, Indu and Kikuno, Reiko F. and Korf, Ulrike and K\"{o}rner, Roman and Kuster, Bernhard and Kwon, Min-Seok and Lee, Hyoung-Joo and Lee, Young-Jin and Lefevre, Michael and Lehvaslaiho, Minna and Lescuyer, Pierre and Levander, Fredrik and Lim, Megan S. and L\"{o}bke, Christian and Loo, Joseph A. and Mann, Matthias and Martens, Lennart and Martinez-Heredia, Juan and Mccomb, Mark and Mcredmond, James and Mehrle, Alexander and Menon, Rajasree and Miller, Christine A. and Mischak, Harald and Mohan, Sujatha S. and Mohmood, Riaz and Molina, Henrik and Moran, Michael F. and Morgan, James D. and Moritz, Robert and Morzel, Martine and Muddiman, David C. and Nalli, Anuradha and Navarro, Daniel J. and Neubert, Thomas A. and Ohara, Osamu and Oliva, Rafael and Omenn, Gilbert S. and Oyama, Masaaki and Paik, Young-Ki and Pennington, Kyla and Pepperkok, Rainer and Periaswamy, Balamurugan and Petricoin, Emanuel F. and Poirier, Guy G. and Prasad, Keshava T. S. and Purvine, Samuel O. and Rahiman, Abdul B. and Ramachandran, Prasanna and Ramachandra, Y. L. and Rice, Robert H. and Rick, Jens and Ronnholm, Ragna H. and Salonen, Johanna and Sanchez, Jean-Charles and Sayd, Thierry and Seshi, Beerelli and Shankari, Kripa and Sheng, Shi J. and Shetty, Vivekananda and Shivakumar, K. and Simpson, Richard J. and Sirdeshmukh, Ravi and Siu, Michael K. W. and Smith, Jeffrey C. and Smith, Richard D. and States, David J. and Sugano, Sumio and Sullivan, Matthew and Superti-Furga, Giulio and Takatalo, Maarit and Thongboonkerd, Visith and Trinidad, Jonathan C. and Uhlen, Mathias and Vandekerckhove, Jo\"{e}l and Vasilescu, Julian and Veenstra, Timothy D. and Vidal-Taboada, Jos\'{e}-Manuel and Vihinen, Mauno and Wait, Robin and Wang, Xiaoyue and Wiemann, Stefan and Wu, Billy and Xu, Tao and Yates, John R. and Zhong, Jun and Zhou, Ming and Zhu, Yunping and Zurbig, Petra and Pandey, Akhilesh},
  citeulike-article-id = {2350768},
  citeulike-linkout-0 = {http://dx.doi.org/10.1038/nbt0208-164},
  citeulike-linkout-1 = {http://dx.doi.org/10.1038/nbt0208-164},
  citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/18259167},
  citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=18259167},
  doi = {10.1038/nbt0208-164},
  issn = {1087-0156},
  journal = {Nature Biotechnology},
  keywords = {bioinformatics, proteomics},
  number = {2},
  pages = {164--167},
  posted-at = {2008-11-18 19:16:06},
  priority = {2},
  publisher = {Nature Publishing Group},
  title = {Human Proteinpedia enables sharing of human protein data},
  url = {http://dx.doi.org/10.1038/nbt0208-164},
  volume = {26}
}