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1. Annotation of biologically relevant ligands in UniProtKB using ChEBI.

Author

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, Jun Fan, 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, Jie Luo, 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, Rafael Santos, 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 Ross, C. R. Vinayaka, Qinghua Wang 0003, and Yuqi Wang

Published
2023
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2. UniProt: the universal protein knowledgebase in 2021.

Author

Alex Bateman, Maria Jesus Martin, Sandra E. Orchard, Michele Magrane, Rahat Agivetova, Shadab Ahmad, Emanuele Alpi, Emily H. Bowler-Barnett, Ramona Britto, Borisas Bursteinas, Hema Bye-A-Jee, Ray Coetzee, Austra Cukura, Alan W. Sousa da Silva, Paul Denny 0002, Tunca Dogan, Thankgod Ebenezer, Jun Fan, Leyla Jael García Castro, Penelope Garmiri, George E. Georghiou, Leonardo Gonzales, Emma Hatton-Ellis, Abdulrahman Hussein, Alexandr Ignatchenko, Giuseppe Insana, Rizwan Ishtiaq, Petteri Jokinen, Vishal Joshi, Dushyanth Jyothi, Antonia Lock, Rodrigo Lopez, Aurelien Luciani, Jie Luo, Yvonne Lussi, Alistair MacDougall, Fábio Madeira, Mahdi Mahmoudy, Manuela Menchi, Alok Mishra 0004, Katie Moulang, Andrew Nightingale, Carla Susana Oliveira, Sangya Pundir, Guoying Qi, Shriya Raj, Daniel Rice, Milagros Rodríguez-López, Rabie Saidi, Joseph Sampson, Tony Sawford, Elena Speretta, Edward Turner, Nidhi Tyagi, Preethi Vasudev, Vladimir Volynkin, Kate Warner, Xavier Watkins, Rossana Zaru, Hermann Zellner, Alan J. Bridge, Sylvain Poux, Nicole Redaschi, Lucila Aimo, Ghislaine Argoud-Puy, Andrea H. Auchincloss, Kristian B. Axelsen, Parit Bansal, Delphine Baratin, Marie-Claude Blatter, Jerven T. Bolleman, Emmanuel Boutet, Lionel Breuza, Cristina Casals-Casas, Edouard De Castro, Kamal Chikh Echioukh, Elisabeth Coudert, Béatrice A. Cuche, Mikael Doche, Dolnide Dornevil, Anne Estreicher, Maria Livia Famiglietti, Marc Feuermann, Elisabeth Gasteiger, Sebastien Gehant, Vivienne Baillie Gerritsen, Arnaud Gos, Nadine Gruaz-Gumowski, Ursula Hinz, Chantal Hulo, Nevila Hyka-Nouspikel, Florence Jungo, Guillaume Keller, Arnaud Kerhornou, Vicente Lara, Philippe Le Mercier, Damien Lieberherr, Thierry Lombardot, Xavier Martin, Patrick Masson, Anne Morgat, Teresa Batista Neto, Salvo Paesano, Ivo Pedruzzi, Sandrine Pilbout, Lucille Pourcel, Monica Pozzato, Manuela Pruess, Catherine Rivoire, Christian J. A. Sigrist, Karin Sonesson, Andre Stutz, Shyamala Sundaram, Michael Tognolli, Laure Verbregue, Cathy H. Wu, Cecilia N. Arighi, Leslie Arminski, Chuming Chen, Yongxing Chen, John S. Garavelli, Hongzhan Huang, Kati Laiho, Peter B. McGarvey, Darren A. Natale, Karen Ross, C. R. Vinayaka, Qinghua Wang 0003, Yuqi Wang, Lai-Su Yeh, Jian Zhang 0051, Patrick Ruch, and Douglas Teodoro

Published
2021
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3. UniProt: the universal protein knowledgebase in 2021

Author

Fábio Madeira, Emmanuel Boutet, Ursula Hinz, Teresa Batista Neto, Parit Bansal, Manuela Pruess, Kristian B. Axelsen, Arnaud Kerhornou, Cecilia N. Arighi, Lai-Su L. Yeh, Shadab Ahmad, John S. Garavelli, Cathy H. Wu, Florence Jungo, Alan Bridge, Leonardo Gonzales, Sandra Orchard, Patrick Masson, Douglas Teodoro, Maria Jesus Martin, Anne Estreicher, Kamal Chikh Echioukh, Hongzhan Huang, Patrick Ruch, Christian J. A. Sigrist, C. R. Vinayaka, Yvonne Lussi, Anne Morgat, Yongxing Chen, Austra Cukura, Emanuele Alpi, Ramona Britto, Alexandr Ignatchenko, Sylvain Poux, Rizwan Ishtiaq, Lionel Breuza, Jun Fan, Edouard de Castro, Petteri Jokinen, Nicole Redaschi, Darren A. Natale, Daniel Rice, Giuseppe Insana, George Georghiou, Nevila Hyka-Nouspikel, Karen E. Ross, Katie Moulang, Vicente Lara, Arnaud Gos, Michael Tognolli, Alok Mishra, Ivo Pedruzzi, Nidhi Tyagi, Leyla Jael Garcia Castro, Edward Turner, Cristina Casals-Casas, Tunca Doğan, Nadine Gruaz-Gumowski, Chantal Hulo, Maria Livia Famiglietti, Andrew Nightingale, Paul Denny, Lucila Aimo, Rossana Zaru, Vishal Joshi, Alistair MacDougall, Andre Stutz, Penelope Garmiri, Carla Susana Oliveira, Hermann Zellner, Marie-Claude Blatter, Emily H Bowler-Barnett, Philippe Le Mercier, Abdulrahman Hussein, Catherine Rivoire, Tony Sawford, Milagros Rodriguez Lopez, Salvo Paesano, Vladimir Volynkin, Manuela Menchi, Hema Bye-A-Jee, Monica Pozzato, Kati Laiho, Delphine Baratin, Qinghua Wang, Leslie Arminski, Preethi Vasudev, Sangya Pundir, Jian Zhang, Emma Hatton-Ellis, Kate Warner, Lucille Pourcel, Elisabeth Gasteiger, Marc Feuermann, Thierry Lombardot, Jerven Bolleman, Mahdi Mahmoudy, Shyamala Sundaram, Alex Bateman, Xavier Watkins, Rahat Agivetova, Guoying Qi, Peter B. McGarvey, Xavier D. Martin, Chuming Chen, Jie Luo, Ray Coetzee, K Sonesson, Alan Wilter Sousa da Silva, ThankGod Ebenezer, Elena Speretta, Rodrigo Lopez, Elisabeth Coudert, Aurelien Luciani, Vivienne Baillie Gerritsen, Yuqi Wang, M Doche, Michele Magrane, Antonia Lock, Dolnide Dornevil, Sandrine Pilbout, Borisas Bursteinas, Andrea H. Auchincloss, Béatrice A. Cuche, Dushyanth Jyothi, Rabie Saidi, Joseph Sampson, Laure Verbregue, Sebastien Gehant, Guillaume Keller, Shriya Raj, Damien Lieberherr, Ghislaine Argoud-Puy, and Teodoro, Douglas

Subjects
Proteomics, COVID-19 / virology, Computational Biology / methods, Molecular Sequence Annotation / methods, Proteome, AcademicSubjects/SCI00010, Knowledge Bases, Computational biology, Proteomics / methods, Biology, ddc:616.0757, SARS-CoV-2 / physiology, COVID-19 / epidemiology, User-Computer Interface, Viral Proteins, 03 medical and health sciences, 0302 clinical medicine, SARS-CoV-2 / genetics, Data Curation / methods, Genetics, Redundancy (engineering), Viral Proteins / genetics, Humans, Database Issue, SARS-CoV-2 / metabolism, Databases, Protein, Pandemics, Data Curation, Proteome / metabolism, 030304 developmental biology, Proteome / genetics, Internet, 0303 health sciences, SARS-CoV-2, COVID-19 / prevention & control, COVID-19, Computational Biology, Molecular Sequence Annotation, Viral Proteins / metabolism, UniProt Knowledgebase, UniProt, 030217 neurology & neurosurgery
Abstract

The aim of the UniProt Knowledgebase is to provide users with a comprehensive, high-quality and freely accessible set of protein sequences annotated with functional information. In this article, we describe significant updates that we have made over the last two years to the resource. The number of sequences in UniProtKB has risen to approximately 190 million, despite continued work to reduce sequence redundancy at the proteome level. We have adopted new methods of assessing proteome completeness and quality. We continue to extract detailed annotations from the literature to add to reviewed entries and supplement these in unreviewed entries with annotations provided by automated systems such as the newly implemented Association-Rule-Based Annotator (ARBA). We have developed a credit-based publication submission interface to allow the community to contribute publications and annotations to UniProt entries. We describe how UniProtKB responded to the COVID-19 pandemic through expert curation of relevant entries that were rapidly made available to the research community through a dedicated portal. UniProt resources are available under a CC-BY (4.0) license via the web at https://www.uniprot.org/.

Published
2020

4. Activities at the Universal Protein Resource (UniProt)

Author

Borisas Bursteinas, L-S Yeh, Klemens Pichler, Guillaume Keller, C Casal-Casas, Gerritsen, A Da Silva, Prudence Mutowo, Xavier D. Martin, Peter B. McGarvey, Volynkin, J Lew, K Sonesson, M. C. Blatter, L Pureza, Rodrigo Lopez, Anne Estreicher, Alex Bateman, Ramona Britto, A-L Veuthey, Penelope Garmiri, Patrick Masson, Baris E. Suzek, Cathy H. Wu, Paul Gane, Maria Jesus Martin, Shyamala Sundaram, Yasmin Alam-Faruque, Ioannis Xenarios, Alan Bridge, WM Chan, Guoying Qi, L Famiglietti, Christian J. A. Sigrist, Nadine Gruaz-Gumowski, Chantal Hulo, Hermann Zellner, Matthew Corbett, Monica Pozzato, Thierry Lombardot, S Staehli, Jerven Bolleman, Sylvain Poux, Séverine Duvaud, Tony Sawford, Chuming Chen, Xavier Watkins, Yuqi Wang, Elisabeth Gasteiger, Kati Laiho, Qinghua Wang, M Bingley, Lydie Bougueleret, Kristian B. Axelsen, Yongxing Chen, Salvo Paesano, Andrew Nightingale, Nicole Redaschi, Emma Hatton-Ellis, John S. Garavelli, Delphine Baratin, Darren A. Natale, Gayatri Chavali, E de Castro, Leslie Arminski, Damien Lieberherr, Elena Cibrian-Uhalte, Catherine Rivoire, Bernd Roechert, Yerramalla, Hongzhan Huang, Alistair MacDougall, Edd Turner, Maria Victoria Schneider, Aleksandra Shypitsyna, Jie Zhang, Michele Magrane, Dolnide Dornevil, Lara, M Donnelly, F. Fazzini, Andrea H. Auchincloss, Emanuele Alpi, Benoit Bely, Brigitte Boeckmann, Rolf Apweiler, Rachael P. Huntley, Lionel Breuza, Sangya Pundir, Lorenzo Cerutti, Tunca Doğan, EB Casanova, P van Rensburg, Rabie Saidi, Jie Luo, Mickael Goujon, Laure Verbregue, Tony Wardell, W Liu, Andre Stutz, P Lemercier, Hamish McWilliam, Ivo Pedruzzi, P-A Binz, Sebastien Gehant, Béatrice A. Cuche, Carlos Bonilla, Duncan Legge, C. R. Vinayaka, Anne Morgat, Diego Poggioli, J Arganiska, Teresa Batista Neto, Emmanuel Boutet, Florence Jungo, Ursula Hinz, Parit Bansal, Sandra Orchard, Ricardo Antunes, Manuela Pruess, M Feuermann, S. Rosanoff, Claire O'Donovan, Cecilia N. Arighi, J. James, M Doche, Elisabeth Coudert, M De Giorgi, Reija Hieta, Sandrine Pilbout, Arnaud Gos, Michael Tognolli, Leyla Jael Garcia Castro, and Lucila Aimo

Subjects
Proteomics, 0303 health sciences, Internet, Representation (systemics), Genome database, Proteins, Molecular Sequence Annotation, Computational biology, Genomics, Biology, Ontology (information science), Universal Protein Resource, II. Protein sequence and structure, motifs and domains, 03 medical and health sciences, Annotation, 0302 clinical medicine, Gene Ontology, Sequence Analysis, Protein, 030220 oncology & carcinogenesis, Genetics, UniProt, Databases, Protein, 030304 developmental biology
Abstract

The mission of the Universal Protein Resource (UniProt) (http://www.uniprot.org) is to provide the scientific community with a comprehensive, high-quality and freely accessible resource of protein sequences and functional annotation. It integrates, interprets and standardizes data from literature and numerous resources to achieve the most comprehensive catalog possible of protein information. The central activities are the biocuration of the UniProt Knowledgebase and the dissemination of these data through our Web site and web services. UniProt is produced by the UniProt Consortium, which consists of groups from the European Bioinformatics Institute (EBI), the SIB Swiss Institute of Bioinformatics (SIB) and the Protein Information Resource (PIR). UniProt is updated and distributed every 4 weeks and can be accessed online for searches or downloads.

Published
2013

5. [Untitled]

Author

Denis F. Hochstrasser, Jean-Charles Sanchez, M. G. Perari, Paola Rottoli, Barbara Magi, Annalisa Santucci, Antonella Fossi, Vitaliano Pallini, R. Raggiaschi, Luca Bini, and Salvo Paesano

Subjects
medicine.diagnostic_test, biology, business.industry, Clinical Biochemistry, Interstitial lung disease, respiratory system, medicine.disease, Biochemistry, Blood proteins, respiratory tract diseases, Analytical Chemistry, Pathogenesis, Idiopathic pulmonary fibrosis, Bronchoalveolar lavage, Pulmonary fibrosis, Immunology, biology.protein, Medicine, Calgranulin, Sarcoidosis, business
Abstract

We used two-dimensional (2-D) electrophoresis to analyze the protein composition of fluid recovered by bronchoalveolar lavage (BALF) from patients with sarcoidosis and idiopathic pulmonary fibrosis, two forms of interstitial lung disease with different cellular composition and cytokine profile in BALF. They are also characterized by different pathogenesis and clinical evolution, idiopathic pulmonary fibrosis being less favorable than sarcoidosis due to rapidly progressive pulmonary fibrosis. Thirty-eight proteins or protein fragments, never previously assigned in BALF samples, were identified by various methods including mass fingerprinting of tryptic digests. Comparison of the BALF protein maps of the two groups of patients showed 32 spots with statistically significant disease-related variations in relative abundance. In sarcoidosis we found an increase in the amount of several plasma proteins, while in idiopathic pulmonary fibrosis we observed a statistically significant increase in low-molecular-weight proteins, many of which are involved in inflammatory processes (such as MIF and calgranulin) or antioxidant response (such as antioxidant peroxysomal enzyme and thioredoxin peroxidase 2). 2-D electrophoresis allowed us to identify new BALF proteins and to characterize protein composition in patients with sarcoidosis and idiophatic pulmonary fibrosis. Comparison of the gels of the two diseases showed that they differ in BALF protein profiles as they do in type of immune response.

Published
2002
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6. UniProt: a hub for protein information

Author

Ursula Hinz, Prudence Mutowo, Laure Verbregue, Weizhong Li, Nadine Gruaz-Gumowski, Chantal Hulo, Hermann Zellner, Shyamala Sundaram, P Lemercier, Guoying Qi, Parit Bansal, Tony Sawford, Sebastien Gehant, Delphine Baratin, Francesco Fazzini, Monica Pozzato, Séverine Duvaud, Lai-Su L. Yeh, Nicole Redaschi, Emma Hatton-Ellis, Darren A. Natale, Damien Lieberherr, Luis Figueira, Bernd Roechert, Borisas Bursteinas, Gayatri Chavali, Brigitte Boeckmann, Cristina Casal-Casas, Baris E. Suzek, Cathy H. Wu, Paul Gane, Ghislaine Argoud-Puy, Klemens Pichler, Rachael P. Huntley, Sangya Pundir, Alan Bridge, Edouard de Castro, Benoit Bely, Kristian B. Axelsen, Emmanuel Boutet, Andre Stutz, Penelope Garmiri, Christian J. A. Sigrist, John S. Garavelli, Rolf Apweiler, Peter B. McGarvey, Patrick Masson, Maria Jesus Martin, K Sonesson, Xavier Watkins, Ioannis Xenarios, Vladimir Volynkin, Hamish McWilliam, Mark Bingley, Guillaume Keller, Hongzhan Huang, Rabie Saidi, Sylvain Poux, Tunca Doğan, Yuqi Wang, Diego Poggioli, Rodrigo Lopez, Alistair MacDougall, Kati Laiho, Qinghua Wang, W Liu, Carlos Bonilla, Duncan Legge, C. R. Vinayaka, Anne Morgat, Thierry Lombardot, Jerven Bolleman, Nevila Nouspikel, Aleksandra Shypitsyna, Emanuele Alpi, Yongxing Chen, Anne Lise Veuthey, Andrew Nightingale, Béatrice A. Cuche, Alex Bateman, Ramona Britto, Alan Wilter Sousa da Silva, Jie Luo, Lionel Breuza, Marie Claude Blatter, Elena Cibrian-Uhalte, Michel Schneider, Chuming Chen, Michele Magrane, L Famiglietti, Meher Shruti Yerramalla, Lydie Bougueleret, Vivienne Baillie Gerritsen, Anne Estreicher, Dolnide Dornevil, Catherine Rivoire, Jian Zhang, S Staehli, Andrew Peter Cowley, Tony Wardell, Ivo Pedruzzi, Andrea H. Auchincloss, Salvo Paesano, Elisabeth Gasteiger, Luis Pureza, Marc Feuermann, Leslie Arminski, Xavier D. Martin, Teresa Batista Neto, Steven Rosanoff, Florence Jungo, Sandra Orchard, Claire O'Donovan, Elisabeth Coudert, Ricardo Antunes, Sandrine Pilbout, Vicente Lara, Arnaud Gos, Reija Hieta, Manuela Pruess, Joanna Arganiska, Edward Turner, Maurizio De Giorgi, M Doche, Cecilia N. Arighi, Michael Tognolli, Leyla Jael Garcia Castro, and Lucila Aimo

Subjects
Proteome, Computer science, Molecular Sequence Annotation, Computational biology, Accession number (bioinformatics), DNA sequencing, World Wide Web, Identifier, Annotation, Sequence Analysis, Protein, Genetics, Database Issue, natural sciences, UniProt, Databases, Protein
Abstract

UniProt is an important collection of protein sequences and their annotations, which has doubled in size to 80 million sequences during the past year. This growth in sequences has prompted an extension of UniProt accession number space from 6 to 10 characters. An increasing fraction of new sequences are identical to a sequence that already exists in the database with the majority of sequences coming from genome sequencing projects. We have created a new proteome identifier that uniquely identifies a particular assembly of a species and strain or subspecies to help users track the provenance of sequences. We present a new website that has been designed using a user-experience design process. We have introduced an annotation score for all entries in UniProt to represent the relative amount of knowledge known about each protein. These scores will be helpful in identifying which proteins are the best characterized and most informative for comparative analysis. All UniProt data is provided freely and is available on the web at http://www.uniprot.org/.

Published
2014

7. The mouse SWISS-2D PAGE database: a tool for proteomics study of diabetes and obesity

Author

Jean-Charles Sanchez, Anna Nolan, Christine Hoogland, Diego Chiappe, Matthew V. Sennitt, Denis F. Hochstrasser, Michael A. Cawthorne, Salvo Paesano, Véronique Converset, Steven Wang, Pierre-Alain Binz, and Ron D. Appel

Subjects
Database, Pancreatic islets, Network on, Non insulin dependent diabetes mellitus, ExPASy, Adipose tissue, Biology, medicine.disease, Proteomics, computer.software_genre, Biochemistry, medicine.anatomical_structure, Diabetes mellitus, Brown adipose tissue, medicine, Molecular Biology, computer
Abstract

A number of two-dimensional electrophoresis (2-DE) reference maps from mouse samples have been established and could be accessed through the internet. An up-to-date list can be found in WORLD-2D PAGE (http://www.expasy.ch/ch2d/2d- index.html), an index of 2-DE databases and services. None of them were established from mouse white and brown adipose tissues, pancreatic islets, liver nuclei and skeletal muscle. This publication describes the mouse SWISS-2D PAGE database. Proteins present in samples of mouse (C57BI/6J) liver, liver nuclei, muscle, white and brown adipose tissue and pancreatic islets are assembled and described in an accessible uniform format. SWISS-2D PAGE can be accessed through the World Wide Web (WWW) network on the ExPASy molecular biology server (http://www.expasy.ch/ ch2d/).

Published
2001
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8. A Molecular Scanner To Automate Proteomic Research and To Display Proteome Images

Author

Pierre-Alain Binz, Markus Müller, Daniel Walther, Willy V. Bienvenut, Robin Gras, Christine Hoogland, Gérard Bouchet, Elisabeth Gasteiger, Roberto Fabbretti, Steven Gay, Patricia Palagi, Marc R. Wilkins, Véronique Rouge, Luisa Tonella, Salvo Paesano, Gérald Rossellat, Abderrahim Karmime, Amos Bairoch, Jean-Charles Sanchez, Ron D. Appel, and Denis F. Hochstrasser

Subjects
Electrophoresis, Gel, Two-Dimensional/methods, Image Processing, Computer-Assisted/instrumentation/methods, Peptide, Computational biology, Mass spectrometry, Proteomics, Peptide Mapping, Trypsin Inhibitor, Kunitz Soybean/analysis/chemistry, Genome, Blood Proteins/analysis/chemistry, Analytical Chemistry, Automation, Peptide mass fingerprinting, Image Processing, Computer-Assisted, Humans, Electrophoresis, Gel, Two-Dimensional, ddc:576, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods, chemistry.chemical_classification, Chromatography, Blood Proteins, Electrophoresis, Polyacrylamide Gel/methods, Identification (information), Peptide Mapping/methods, chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Proteome, Electrophoresis, Polyacrylamide Gel, Bottom-up proteomics, Trypsin Inhibitor, Kunitz Soybean
Abstract

Identification and characterization of all proteins expressed by a genome in biological samples represent major challenges in proteomics. Today's commonly used high-throughput approaches combine two-dimensional electrophoresis (2-DE) with peptide mass fingerprinting (PMF) analysis. Although automation is often possible, a number of limitations still adversely affect the rate of protein identification and annotation in 2-DE databases: the sequential excision process of pieces of gel containing protein; the enzymatic digestion step; the interpretation of mass spectra (reliability of identifications); and the manual updating of 2-DE databases. We present a highly automated method that generates a fully annoated 2-DE map. Using a parallel process, all proteins of a 2-DE are first simultaneously digested proteolytically and electro-transferred onto a poly(vinylidene difluoride) membrane. The membrane is then directly scanned by MALDI-TOF MS. After automated protein identification from the obtained peptide mass fingerprints using PeptIdent software (http://www.expasy.ch/tools/peptident.html + ++), a fully annotated 2-D map is created on-line. It is a multidimensional representation of a proteome that contains interpreted PMF data in addition to protein identification results. This "MS-imaging" method represents a major step toward the development of a clinical molecular scanner.

Published
1999
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9. Ongoing and future developments at the Universal Protein Resource

Author

Vicente Lara, Arnaud Gos, Nikolas Pontikos, L. Bollondi, L Famiglietti, Barker Wc, Chuming Chen, Michael Tognolli, Patrick Masson, Salvo Paesano, Tony Sawford, Sandrine Pilbout, Jerven Bolleman, Jian Zhang, S Staehli, Elisabeth Gasteiger, David Binns, Ursula Hinz, Nadine Gruaz-Gumowski, Chantal Hulo, Maria Jesus Martin, M. Corbett, Veuthey Al, Paul Browne, Guillaume Keller, S. Jimenez, Roberts Nv, Brigitte Boeckmann, Natale Da, Suzek Be, Edward Turner, T. Kappler, Steven Rosanoff, Leslie Arminski, Florence Jungo, M Donnelly, P. Dubey, Ruth Y. Eberhardt, Lydie Bougueleret, Vivienne Baillie Gerritsen, Maria Victoria Schneider, Lionel Breuza, Isabelle Cusin, Delphine Baratin, E. Dimmer, Rachael P. Huntley, Julius O.B. Jacobsen, Arighi Cn, Quintaje Sb, Alan Bridge, Nicole Redaschi, Shyamala Sundaram, Peter B. McGarvey, Rebecca E. Foulger, Duncan Legge, Andre Stutz, Monica Pozzato, Raja Mazumder, Anne Morgat, M Doche, K Sonesson, Anne Estreicher, Blatter Mc, Manuela Pruess, Serenella Ferro, Séverine Duvaud, F. Fazzini, Rolf Apweiler, Natarajan Tg, E. Stanley, M Feuermann, Claire O'Donovan, J. James, Ivo Pedruzzi, Castro Lg, Wu Ch, M Bingley, W Liu, He Huang, Bernd Roechert, Laure Verbregue, Elisabeth Coudert, Ioannis Xenarios, M. Moinat, Sandra Orchard, P Lemercier, Damien Lieberherr, Ricardo Antunes, Ghislaine Argoud-Puy, Sebastien Gehant, Qiang Wang, Klemens Pichler, S. Patient, Nicolas Hulo, Diego Poggioli, J. Nchoutmboube, Emmanuel Boutet, H. Sehra, Chan Wm, Yasmin Alam-Faruque, M. Kleen, Van Rensburg P, Kati Laiho, Kristian B. Axelsen, John S. Garavelli, Christian J. A. Sigrist, Amos Marc Bairoch, Yongxing Chen, A. Fedotov, Yeh Ls, Sylvain Poux, Lynette Bower, Quan Lin, Daniel Barrell, Benoit Bely, U. Ugochukwu, Xavier D. Martin, Catherine Rivoire, E. Decastro, Jie Luo, Alain Gateau, Michele Magrane, Dolnide Dornevil, Vinayaka Cr, Andrea H. Auchincloss, Yuqi Wang, An algorithmic view on genomes, cells, and environments (BAMBOO), Inria Grenoble - Rhône-Alpes, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Swiss Institute of Bioinformatics [Lausanne] (SIB), Université de Lausanne = University of Lausanne (UNIL), Institut de Microélectronique, Electromagnétisme et Photonique - Laboratoire d'Hyperfréquences et Caractérisation (IMEP-LAHC), Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut National Polytechnique de Grenoble (INPG)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Institut de minéralogie et de physique des milieux condensés (IMPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Institut de Physique du Globe de Paris (IPG Paris)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Inria Grenoble - Rhône-Alpes, Institut National de Recherche en Informatique et en Automatique (Inria), Université de Lausanne (UNIL), Université Pierre et Marie Curie - Paris 6 (UPMC)-IPG PARIS-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), UniProt Consortium, Apweiler, R., Martin, MJ., O'Donovan, C., Magrane, M., Alam-Faruque, Y., Antunes, R., Barrell, D., Bely, B., Bingley, M., Binns, D., Bower, L., Browne, P., Chan, WM., Dimmer, E., Eberhardt, R., Fazzini, F., Fedotov, A., Foulger, R., Garavelli, J., Castro, LG., Huntley, R., Jacobsen, J., Kleen, M., Laiho, K., Legge, D., Lin, Q., Liu, W., Luo, J., Orchard, S., Patient, S., Pichler, K., Poggioli, D., Pontikos, N., Pruess, M., Rosanoff, S., Sawford, T., Sehra, H., Turner, E., Corbett, M., Donnelly, M., van Rensburg, P., Xenarios, I., Bougueleret, L., Auchincloss, A., Argoud-Puy, G., Axelsen, K., Bairoch, A., Baratin, D., Blatter, MC., Boeckmann, B., Bolleman, J., Bollondi, L., Boutet, E., Quintaje, SB., Breuza, L., Bridge, A., deCastro, E., Coudert, E., Cusin, I., Doche, M., Dornevil, D., Duvaud, S., Estreicher, A., Famiglietti, L., Feuermann, M., Gehant, S., Ferro, S., Gasteiger, E., Gateau, A., Gerritsen, V., Gos, A., Gruaz-Gumowski, N., Hinz, U., Hulo, C., Hulo, N., James, J., Jimenez, S., Jungo, F., Kappler, T., Keller, G., Lara, V., Lemercier, P., Lieberherr, D., Martin, X., Masson, P., Moinat, M., Morgat, A., Paesano, S., Pedruzzi, I., Pilbout, S., Poux, S., Pozzato, M., Redaschi, N., Rivoire, C., Roechert, B., Schneider, M., Sigrist, C., Sonesson, K., Staehli, S., Stanley, E., Stutz, A., Sundaram, S., Tognolli, M., Verbregue, L., Veuthey, AL., Wu, CH., Arighi, CN., Arminski, L., Barker, WC., Chen, C., Chen, Y., Dubey, P., Huang, H., Mazumder, R., McGarvey, P., Natale, DA., Natarajan, TG., Nchoutmboube, J., Roberts, NV., Suzek, BE., Ugochukwu, U., Vinayaka, CR., Wang, Q., Wang, Y., Yeh, LS., and Zhang, J.

Subjects
Proteomics, 0303 health sciences, Sequence database, 030302 biochemistry & molecular biology, Proteins, Articles, Computational biology, Biology, Bioinformatics, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Systems Integration, Universal Protein Resource, 03 medical and health sciences, Information resource, Protein sequencing, Sequence Analysis, Protein, Metagenomics, UniProt Knowledgebase, Genetics, Databases, Protein/trends, Proteins/chemistry, Proteins/genetics, UniProt, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Databases, Protein, 030304 developmental biology
Abstract

International audience; The primary mission of Universal Protein Resource (UniProt) is to support biological research by maintaining a stable, comprehensive, fully classified, richly and accurately annotated protein sequence knowledgebase, with extensive cross-references and querying interfaces freely accessible to the scientific community. UniProt is produced by the UniProt Consortium which consists of groups from the European Bioinformatics Institute (EBI), the Swiss Institute of Bioinformatics (SIB) and the Protein Information Resource (PIR). UniProt is comprised of four major components, each optimized for different uses: the UniProt Archive, the UniProt Knowledgebase, the UniProt Reference Clusters and the UniProt Metagenomic and Environmental Sequence Database. UniProt is updated and distributed every 4 weeks and can be accessed online for searches or download at http://www.uniprot.org.

Published
2011
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10. Exploitation of specific properties of trifluoroethanol for extraction and separation of membrane proteins

Author

Véronique Converset, Jacques M. P. Deshusses, Yvan Wenger, Alexander Scherl, Jean-Charles Sanchez, Denis F. Hochstrasser, Salvo Paesano, Garry L. Corthals, Nadia Walter, and Jennifer A. Burgess

Subjects
Chromatography, Chemistry, Isoelectric focusing, Membrane Proteins/isolation & purification, Membrane Proteins, Trifluoroethanol/chemistry, Trifluoroethanol, Tandem mass spectrometry, Biochemistry, Chaotropic agent, Beta barrel, Membrane, Protein structure, Membrane protein, Peptide mass fingerprinting, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Electrophoresis, Gel, Two-Dimensional, ddc:576, Molecular Biology
Abstract

Hydrophobic proteins are difficult to analyze by two-dimensional electrophoresis (2-DE) because of their intrinsic tendency to self-aggregate during the first dimension (isoelectric focusing, IEF) or the equilibration steps. This aggregation renders their redissolution for the second dimension uncertain and results in the reduction of the number and intensity of protein spots, and in undesirable vertical and horizontal streaks across gels. Trifluoroethanol (TFE) is traditionally used at high concentration to solubilize peptides and proteins for NMR studies. Depending upon its concentration, TFE strongly affects the three-dimensional structure of proteins. We report here a phase separation system based on TFE/CHCl(3), which is able to extract a number of intrinsic membrane proteins. The addition of TFE in the in-gel sample rehydration buffer to improve membrane protein IEF separation is also presented. The procedure using urea, thiourea, and sulfobetaine as chaotropic agents was modified by the addition of TFE and removing of sulfobetaine at an optimized concentration in the solubilization medium used for the first dimension. When using membrane fractions isolated from Escherichia coli, the intensity and the number of spots detected from 2-DE gels that used TFE in the solubilization medium were significantly increased. The majority of the proteins identified using peptide mass fingerprinting and tandem mass spectrometry (MS/MS) were intrinsic membrane proteins, proteins of beta barrel structure or transmembrane proteins.

Published
2003

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