Registro:

Referencias:

• Davey, N.E., Van Roey, K., Weatheritt, R.J., Toedt, G., Uyar, B., Altenberg, B., Budd, A., Gibson, T.J., Attributes of short linear motifs (2012) Mol. Biosyst., 8, pp. 268-281
• Van Roey, K., Uyar, B., Weatheritt, R.J., Dinkel, H., Seiler, M., Budd, A., Gibson, T.J., Davey, N.E., Short linear motifs: Ubiquitous and functionally diverse protein interaction modules directing cell regulation (2014) Chem. Rev., 114, pp. 6733-6778
• Diella, F., Understanding eukaryotic linear motifs and their role in cell signaling and regulation (2008) Front. Biosci., 13, pp. 6580-6603
• Van Roey, K., Gibson, T.J., Davey, N.E., Motif switches: Decision-making in cell regulation (2012) Curr. Opin. Struct. Biol., 22, pp. 378-385
• Van Roey, K., Dinkel, H., Weatheritt, R.J., Gibson, T.J., Davey, N.E., The switches ELM resource: A compendium of conditional regulatory interaction interfaces (2013) Sci. Signal., 6, p. rs7
• Davey, N.E., Travé, G., Gibson, T.J., How viruses hijack cell regulation (2011) Trends Biochem. Sci., 36, pp. 159-169
• Uyar, B., Weatheritt, R.J., Dinkel, H., Davey, N.E., Gibson, T.J., Proteome-wide analysis of human disease mutations in short linear motifs: Neglected players in cancer? Mol (2014) Biosyst., 10, pp. 2626-2642
• Mészáros, B., Kumar, M., Gibson, T.J., Uyar, B., Dosztányi, Z., Degrons in cancer (2017) Sci. Signal., 10, p. eaak9982
• Tompa, P., Davey, N.E., Gibson, T.J., Babu, M.M., A million peptide motifs for the molecular biologist (2014) Mol. Cell, 55, pp. 161-169
• Puntervoll, P., ELM server: A new resource for investigating short functional sites in modular eukaryotic proteins (2003) Nucleic Acids Res., 31, pp. 3625-3630
• Dinkel, H., Michael, S., Weatheritt, R.J., Davey, N.E., Van Roey, K., Altenberg, B., Toedt, G., Budd, A., ELM-the database of eukaryotic linear motifs (2012) Nucleic Acids Res., 40, pp. D242-D251
• Dinkel, H., Van Roey, K., Michael, S., Davey, N.E., Weatheritt, R.J., Born, D., Speck, T., Kubán, M., The eukaryotic linear motif resource ELM: 10 years and counting (2014) Nucleic Acids Res., 42, pp. D259-D266
• Dinkel, H., Van Roey, K., Michael, S., Kumar, M., Uyar, B., Altenberg, B., Milchevskaya, V., Behrendt, A., ELM 2016'data update and new functionality of the eukaryotic linear motif resource (2016) Nucleic Acids Res., 44, pp. D294-D300
• Expansion of the gene ontology knowledgebase and resources (2017) Nucleic Acids Res., 45, pp. D331-D338. , The Gene Ontology Consortium
• Kerrien, S., Orchard, S., Montecchi-Palazzi, L., Aranda, B., Quinn, A.F., Vinod, N., Bader, G.D., Sherman, D., Broadening the horizon-level 2 5 of the HUPO-PSI format for molecular interactions (2007) BMC Biol., 5, pp. 44-55
• Sayers, E.W., Barrett, T., Benson, D.A., Bryant, S.H., Canese, K., Chetvernin, V., Church, D.M., Federhen, S., Database resources of the National Center for Biotechnology Information (2009) Nucleic Acids Res, 37, pp. 5-15
• Benson, D.A., Karsch-Mizrachi, I., Lipman, D.J., Ostell, J., Sayers, E.W., Gen bank (2009) Nucleic Acids Res., 37, pp. D26-D31
• Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., The protein data bank (2000) Nucleic Acids Res., 28, pp. 235-242
• Linding, R., Russell, R.B., Neduva, V., Gibson, T.J., GlobPlot: Exploring protein sequences for globularity and disorder (2003) Nucleic Acids Res., 31, pp. 3701-3708
• Dosztányi, Z., Csizmok, V., Tompa, P., Simon, I., IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content (2005) Bioinformatics, 21, pp. 3433-3434
• Via, A., Gould, C.M., Gemünd, C., Gibson, T.J., Helmer-Citterich, M., A structure filter for the eukaryotic linear motif resource (2009) BMC Bioinformatics, 10, pp. 351-369
• Letunic, I., Doerks, T., Bork, P., SMART: Recent updates, new developments and status in 2015 (2015) Nucleic Acids Res., 43, pp. D257-D260
• Finn, R.D., Coggill, P., Eberhardt, R.Y., Eddy, S.R., Mistry, J., Mitchell, A.L., Potter, S.C., Sangrador-Vegas, A., The Pfam protein families database: Towards a more sustainable future (2016) Nucleic Acids Res, 44, pp. D279-D285
• Jehl, P., Manguy, J., Shields, D.C., Higgins, D.G., Davey, N.E., ProViz-a web-based visualization tool to investigate the functional and evolutionary features of protein sequences (2016) Nucleic Acids Res., 44, pp. W11-W15
• Krystkowiak, I., Davey, N.E., SLiMSearch: A framework for proteome-wide discovery and annotation of functional modules in intrinsically disordered regions (2017) Nucleic Acids Res., 45, pp. W464-W469
• Zhao, B., Shu, C., Gao, X., Sankaran, B., Du, F., Shelton, C.L., Herr, A.B., Li, P., Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins (2016) Proc. Natl. Acad. Sci. U. S. A., 113, pp. E3403-E3412
• Bateman, A., Martin, M.J., O'donovan, C., Magrane, M., Alpi, E., Antunes, R., Bely, B., Britto, R., UniProt: The universal protein knowledgebase (2017) Nucleic Acids Res, 45, pp. D158-D169
• Fabregat, A., Sidiropoulos, K., Garapati, P., Gillespie, M., Hausmann, K., Haw, R., Jassal, B., McKay, S., The reactome pathway knowledgebase (2016) Nucleic Acids Res., 44, pp. D481-D487
• Kanehisa, M., Furumichi, M., Tanabe, M., Sato, Y., Morishima, K., KEGG: New perspectives on genomes, pathways, diseases and drugs (2017) Nucleic Acids Res, 45, pp. D353-D361
• Gouw, M., Sámano-Sánchez, H., Van Roey, K., Diella, F., Gibson, T.J., Dinkel, H., Exploring short linear motifs using the ELM database and tools (2017) Current Protocols in Bioinformatics, pp. 8221-82235. , In: Bateman, A, Draghici, S, Khurana, E, Orchard, S and Pearson, WR (eds). John Wiley & Sons, Inc., Hoboken
• Via, A., Uyar, B., Brun, C., Zanzoni, A., How pathogens use linear motifs to perturb host cell networks (2015) Trends Biochem. Sci., 40, pp. 36-48
• Ruhanen, H., Hurley, D., Ghosh, A., O'brien, K.T., Johnston, C.R., Shields, D.C., Potential of known and short prokaryotic protein motifs as a basis for novel peptide-based antibacterial therapeutics: A computational survey (2014) Front. Microbiol., 5, pp. 1-18
• Zhu, Y., Li, H., Long, C., Hu, L., Xu, H., Liu, L., Chen, S., Shao, F., Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase (2007) Mol. Cell, 28, pp. 899-913
• Li, H., Xu, H., Zhou, Y., Zhang, J., Long, C., Li, S., Chen, S., Shao, F., The phosphothreonine lyase activity of a bacterial type III effector family (2007) Science, 315, pp. 1000-1003
• Aitio, O., Hellman, M., Kazlauskas, A., Vingadassalom, D.F., Leong, J.M., Saksela, K., Permi, P., Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly (2010) Proc. Natl. Acad. Sci. U. S. A., 107, pp. 21743-21748
• Aitio, O., Hellman, M., Skehan, B., Kesti, T., Leong, J.M., Saksela, K., Permi, P., Enterohaemorrhagic escherichia coli exploits a tryptophan switch to hijack host F-Actin assembly (2012) Structure, 20, pp. 1692-1703
• Tsutsumi, R., Higashi, H., Higuchi, M., Okada, M., Hatakeyama, M., Attenuation of Helicobacter pylori CagA?SHP-2 Signaling by Interaction between CagA and C-terminal Src Kinase (2003) J. Biol. Chem., 278, pp. 3664-3670
• Dodd, D.A., Worth, R.G., Rosen, M.K., Grinstein, S., Van Oers, N.S.C., Hansen, E.J., The Haemophilus ducreyi LspA1 protein inhibits phagocytosis by using a new mechanism involving activation of C-terminal Src kinase (2014) Mbio, 5
• Tauzin, S., Starnes, T.W., Becker, F.B., Ying Lam, P., Huttenlocher, A., Redox and Src family kinase signaling control leukocyte wound attraction and neutrophil reverse migration (2014) J. Cell Biol., 207, pp. 589-598
• Berton, G., Mocsai, A., Lowell, C.A., Src and Syk kinases: Key regulators of phagocytic cell activation (2005) Trends Immunol., 26, pp. 208-214
• Jones, K.R., Joo, Y.M., Jang, S., Yoo, Y.J., Lee, H.S., Chung, I.S., Olsen, C.H., Cha, J.H., Polymorphism in the cagA EPIYA motif impacts development of gastric cancer (2009) J. Clin. Microbiol., 47, pp. 959-968
• Shannon, P., Cytoscape: A software environment for integrated models of biomolecular interaction networks (2003) Genome Res., 13, pp. 2498-2504
• Garai, A., Zeke, A., Gogl, G., Toro, I., Fordos, F., Blankenburg, H., Barkai, T., Emig, D., Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove (2012) Sci. Signal, 5, p. ra74
• Zeke, A., Bastys, T., Alexa, A., Garai, A., Mészáros, B., Kirsch, K., Dosztányi, Z., Reményi, A., Systematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases (2015) Mol. Syst. Biol., 11, pp. 837-858
• Zeke, A., Misheva, M., Remenyi, A., Bogoyevitch, M.A., JNK Signaling: Regulation and functions based on complex proteinprotein partnerships (2016) Microbiol. Mol. Biol. Rev., 80, pp. 793-835
• Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., Ferrin, T.E., UCSF Chimera-a visualization system for exploratory research and analysis (2004) J. Comput. Chem., 25, pp. 1605-1612
• Barr, F.A., Silljé, H.H.W., Nigg, E.A., Polo-like kinases and the orchestration of cell division (2004) Nat. Rev. Mol. Cell Biol., 5, pp. 429-441
• Park, J.E., Soung, N.K., Johmura, Y., Kang, Y.H., Liao, C., Lee, K.H., Park, C.H., Lee, K.S., Polo-box domain: A versatile mediator of polo-like kinase function (2010) Cell. Mol. Life Sci., 67, pp. 1957-1970
• Lowery, D.M., Lim, D., Yaffe, M.B., Structure and function of Polo-like kinases (2005) Oncogene, 24, pp. 248-259
• Palopoli, N., Lythgow, K.T., Edwards, R.J., QSLiMFinder: Improved short linear motif prediction using specific query protein data (2015) Bioinformatics, 31, pp. 2284-2293

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------