Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Protein Interaction Mapping/methods"'
Publikováno v:
Bioinformatics, 33(10), 1479-1487. Oxford University Press
Hou, Q, De Geest, P F G, Vranken, W F, Heringa, J & Feenstra, K A 2017, ' Seeing the trees through the forest : sequence-based homo-and heteromeric protein-protein interaction sites prediction using random forest ', Bioinformatics, vol. 33, no. 10, pp. 1479-1487 . https://doi.org/10.1093/bioinformatics/btx005, https://doi.org/10.1093/bioinformatics/btx005
Hou, Q, De Geest, P F G, Vranken, W F, Heringa, J & Feenstra, K A 2017, ' Seeing the trees through the forest : sequence-based homo-and heteromeric protein-protein interaction sites prediction using random forest ', Bioinformatics, vol. 33, no. 10, pp. 1479-1487 . https://doi.org/10.1093/bioinformatics/btx005, https://doi.org/10.1093/bioinformatics/btx005
Motivation Genome sequencing is producing an ever-increasing amount of associated protein sequences. Few of these sequences have experimentally validated annotations, however, and computational predictions are becoming increasingly successful in prod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::868a1d8a0f6f009771cef882a6b4e8ad
https://research.vu.nl/en/publications/e1c176c8-e75e-46da-aee7-815a8d481259
https://research.vu.nl/en/publications/e1c176c8-e75e-46da-aee7-815a8d481259
Publikováno v:
Current protocols in molecular biology
Current protocols in molecular biology, Wiley, 2017, 118, pp.20.12.1-20.12.24. ⟨10.1002/cpmb.36⟩
Current Protocols in Molecular Biology
Current Protocols in Molecular Biology, 2017, 118, pp.20.12.1-20.12.24. ⟨10.1002/cpmb.36⟩
Current protocols in molecular biology, Wiley, 2017, 118, pp.20.12.1-20.12.24. ⟨10.1002/cpmb.36⟩
Current Protocols in Molecular Biology
Current Protocols in Molecular Biology, 2017, 118, pp.20.12.1-20.12.24. ⟨10.1002/cpmb.36⟩
The bacterial two-hybrid (BACTH, for "Bacterial Adenylate Cyclase-based Two-Hybrid") technique is a simple and fast genetic approach to analyze protein-protein interactions in vivo. In this system, the proteins of interest are genetically fused to tw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27c585240cadd70c79abdbcc7c66e044
https://hal-pasteur.archives-ouvertes.fr/pasteur-02879386
https://hal-pasteur.archives-ouvertes.fr/pasteur-02879386
Autor:
Patrick Ruch, Amos Marc Bairoch, Anne Gleizes, Pierre-André Michel, Pascale Gaudet, Emilie Pasche, Julien Gobeill, Luc Mottin, Valentine Rech de Laval
Publikováno v:
Database: The Journal of Biological Databases and Curation
Database, Vol. 2017 (2017) P. bax040
Database
Database, Vol. 2017 (2017) P. bax040
Database
Today, molecular biology databases are the cornerstone of knowledge sharing for life and health sciences. The curation and maintenance of these resources are labour intensive. Although text mining is gaining impetus among curators, its integration in
Publikováno v:
Methods in Molecular Biology ISBN: 9781493970315
Bacterial Protein Secretion Systems
Laure Journet; Eric Cascales. Bacterial Protein Secretion Systems, 1615, Humana Press; Springer Science, pp.159-176, 2017, Methods in Molecular Biology, 978-1-4939-7033-9. ⟨10.1007/978-1-4939-7033-9_13⟩
Bacterial Protein Secretion Systems
Laure Journet; Eric Cascales. Bacterial Protein Secretion Systems, 1615, Humana Press; Springer Science, pp.159-176, 2017, Methods in Molecular Biology, 978-1-4939-7033-9. ⟨10.1007/978-1-4939-7033-9_13⟩
International audience; The bacterial two-hybrid (BACTH, for "Bacterial Adenylate Cyclase-Based Two-Hybrid") system is a simple and fast genetic approach to detecting and characterizing protein-protein interactions in vivo. This system is based on th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26205e8fe843d6ae2d4fb2532a16152d
https://doi.org/10.1007/978-1-4939-7033-9_13
https://doi.org/10.1007/978-1-4939-7033-9_13
Autor:
Peter Gregor, Céline Verheggen, Laura Trinkle-Mulcahy, Yasmeen Ahmad, Andy Cobley, Edouard Bertrand, Mark Whitehorn, Angus I. Lamond, Séverine Boulon
Publikováno v:
Molecular & Cellular Proteomics
Molecular & Cellular Proteomics; Vol 9
Molecular and Cellular Proteomics
Molecular and Cellular Proteomics, American Society for Biochemistry and Molecular Biology, 2010, 9 (5), pp.861--79. ⟨10.1074/mcp.M900517-MCP200⟩
Molecular & Cellular Proteomics : MCP
Molecular & Cellular Proteomics; Vol 9
Molecular and Cellular Proteomics
Molecular and Cellular Proteomics, American Society for Biochemistry and Molecular Biology, 2010, 9 (5), pp.861--79. ⟨10.1074/mcp.M900517-MCP200⟩
Molecular & Cellular Proteomics : MCP
International audience; The reliable identification of protein interaction partners and how such interactions change in response to physiological or pathological perturbations is a key goal in most areas of cell biology. Stable isotope labeling with
Autor:
Tomoko Hirozane-Kishikawa, Alex Smolyar, Nono Ayivi-Guedehoussou, Irma Lemmens, Fana Gebreab, Sebiha Cevik, Pascal Braun, Jin Sook Ahn, Michael E. Cusick, Haiyuan Yu, Christophe Simon, Huey Ling Kao, Niels Klitgord, Matija Dreze, David Szeto, Amélie Dricot, Marc Vidal, Jean Vandenhaute, Nicolas Simonis, Elizabeth Dann, Jean François Rual, Anne-Ruxandra Carvunis, Kristin C. Gunsalus, Mike Boxem, Chenwei Lin, Murat Tasan, Jan Tavernier, Changyu Fan, Anne Sophie de Smet, Frederick P. Roth, Tong Hao, David E. Hill, Kavitha Venkatesan, Muhammed A. Yildirim, Muneesh Tewari, Ning Li, Julie M. Sahalie, Stuart Milstein, Nicolas Bertin
Publikováno v:
Nature methods, 6 (1
To provide accurate biological hypotheses and elucidate global properties of cellular networks, systematic identification of protein-protein interactions must meet high quality standards.We present an expanded C. elegans protein-protein interaction n
Autor:
Xiaofeng Xin, Julie M. Sahalie, Haiyuan Yu, Christophe Simon, David E. Hill, Nicolas Simonis, Amélie Dricot, Marc Vidal, Michael Snyder, Juyong Park, Michael E. Cusick, Irma Lemmens, Jean François Rual, Pascal Braun, Frederick P. Roth, Changyu Fan, Stanley Tam, Troy Moore, Leah Tardivo, Nenad Svrzikapa, Albert-László Barabási, Ryan R. Murray, Tong Hao, Adriana Motyl, Tomoko Hirozane-Kishikawa, Anne-Sophie De Smet, Alexei Vazquez, Kavitha Venkatesan, Muhammed A. Yildirim, Michael E. Hudson, Jan Tavernier, Nan Li, Charles Boone, Fana Gebreab
Publikováno v:
Science, 322 (5898
Current yeast interactome network maps contain several hundred molecular complexes with limited and somewhat controversial representation of direct binary interactions. We carried out a comparative quality assessment of current yeast interactome data
Autor:
Yves Nominé, Sebastian Charbonnier, Patricia Cassonnet, Anne Forster, Julie Abdat, Marilyne Blémont, Nicolas Wolff, Kevin Ricquier, Renaud Vincentelli, Katja Luck, Juline Poirson, Marie-Laure Straub, Jérôme Reboul, Jolanta Polanowska, Jeremy Turchetto, Gilles Travé, Francois, Jean-Paul Borg, Yves Jacob, Murielle Masson
Publikováno v:
Nature Methods
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-U154. ⟨10.1038/NMETH.3438⟩
Nature Methods, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature methods
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature Methods, Nature Publishing Group, 2015, 12 (8), pp.787-U154. ⟨10.1038/NMETH.3438⟩
Nature Methods, 2015, 12 (8), pp.787-793. ⟨10.1038/nmeth.3438⟩
Nature methods
Many protein interactions are mediated by small linear motifs interacting specifically with defined families of globular domains. Quantifying the specificity of a motif requires measuring and comparing its binding affinities to all its putative targe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d23a387bd6b6333f1fd2c0becc6ef51
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883959
https://hal-pasteur.archives-ouvertes.fr/pasteur-02883959
Publikováno v:
Bioinformatics. 19:1901-1908
Motivation: The analysis of protein–protein interactions allows for detailed exploration of the cellular machinery. The biochemical purification of protein complexes followed by identification of components by mass spectrometry is currently the met
Autor:
Thibault Andrieu, Marc Blondel, Yvette Mettey, Hervé Galons, Dominique Dormont, Nicolas Talarek, Laurent Meijer, Stéphane Bach, Jean-Michel Vierfond, Christophe Cullin
Publikováno v:
Nature Biotechnology
Nature Biotechnology, 2003, 21 (9), pp.1075-1081. ⟨10.1038/nbt855⟩
Nature Biotechnology, Nature Publishing Group, 2003, 21, pp.1075-1081
Nature Biotechnology, Nature Publishing Group, 2003, 21 (9), pp.1075-1081. ⟨10.1038/nbt855⟩
Nature Biotechnology, 2003, 21, pp.1075-1081
HAL
Nature Biotechnology, 2003, 21 (9), pp.1075-1081. ⟨10.1038/nbt855⟩
Nature Biotechnology, Nature Publishing Group, 2003, 21, pp.1075-1081
Nature Biotechnology, Nature Publishing Group, 2003, 21 (9), pp.1075-1081. ⟨10.1038/nbt855⟩
Nature Biotechnology, 2003, 21, pp.1075-1081
HAL
International audience; We have developed a rapid, yeast-based, two-step assay to screen for antiprion drugs. The method allowed us to identify several compounds effective against budding yeast prions responsible for the [PSI+] and [URE3] phenotypes.