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BioMed Research International
Volume 2015 (2015), Article ID 124082, 18 pages
http://dx.doi.org/10.1155/2015/124082
Research Article

Proteomic Study to Survey the CIGB-552 Antitumor Effect

Arielis Rodríguez-Ulloa,1 Jeovanis Gil,1 Yassel Ramos,1 Lilian Hernández-Álvarez,2 Lisandra Flores,1 Brizaida Oliva,3 Dayana García,1 Aniel Sánchez-Puente,1 Alexis Musacchio-Lasa,2 Jorge Fernández-de-Cossio,2 Gabriel Padrón,1 Luis J. González López,1 Vladimir Besada,1 and Maribel Guerra-Vallespí3

1Department of Proteomics, Center for Genetic Engineering and Biotechnology, 10600 Havana, Cuba
2Department of Bioinformatics, Center for Genetic Engineering and Biotechnology, 10600 Havana, Cuba
3Pharmaceutical Department, Center for Genetic Engineering and Biotechnology, 10600 Havana, Cuba

Received 11 March 2015; Accepted 26 August 2015

Academic Editor: Zheng Li

Copyright © 2015 Arielis Rodríguez-Ulloa et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. F. Albericio and H. G. Kruger, “Therapeutic peptides,” Future Medicinal Chemistry, vol. 4, no. 12, pp. 1527–1531, 2012. View at Publisher · View at Google Scholar · View at Scopus
  2. D. Wu, Y. Gao, Y. Qi, L. Chen, Y. Ma, and Y. Li, “Peptide-based cancer therapy: opportunity and challenge,” Cancer Letters, vol. 351, no. 1, pp. 13–22, 2014. View at Publisher · View at Google Scholar · View at Scopus
  3. J. Thundimadathil, “Cancer treatment using peptides: current therapies and future prospects,” Journal of Amino Acids, vol. 2012, Article ID 967347, 13 pages, 2012. View at Publisher · View at Google Scholar
  4. M. G. Vallespi, J. R. Fernandez, I. Torrens et al., “Identification of a novel antitumor peptide based on the screening of an Ala-library derived from the LALF32-51 region,” Journal of Peptide Science, vol. 16, no. 1, pp. 40–47, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. J. R. F. Massó, B. P. Argüelles, Y. Tejeda et al., “The antitumor peptide CIGB-552 increases COMMD1 and inhibits growth of human lung cancer cells,” Journal of Amino Acids, vol. 2013, Article ID 251398, 13 pages, 2013. View at Publisher · View at Google Scholar
  6. M. G. Vallespí, G. Pimentel, A. Cabrales-Rico et al., “Antitumor efficacy, pharmacokinetic and biodistribution studies of the anticancer peptide CIGB-552 in mouse models,” Journal of Peptide Science, vol. 20, no. 11, pp. 850–859, 2014. View at Publisher · View at Google Scholar · View at Scopus
  7. G. B. Fields and R. L. Noble, “Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids,” International Journal of Peptide and Protein Research, vol. 35, no. 3, pp. 161–214, 1990. View at Google Scholar · View at Scopus
  8. J. Heukeshoven and R. Dernick, “Characterization of a solvent system for separation of water-insoluble poliovirus proteins by reversed-phase high-performance liquid chromatography,” Journal of Chromatography A, vol. 326, pp. 91–101, 1985. View at Publisher · View at Google Scholar · View at Scopus
  9. D. N. Perkins, D. J. C. Pappin, D. M. Creasy, and J. S. Cottrell, “Probability-based protein identification by searching sequence databases using mass spectrometry data,” Electrophoresis, vol. 20, no. 18, pp. 3551–3567, 1999. View at Publisher · View at Google Scholar · View at Scopus
  10. D. Tabas-Madrid, R. Nogales-Cadenas, and A. Pascual-Montano, “GeneCodis3: a non-redundant and modular enrichment analysis tool for functional genomics,” Nucleic Acids Research, vol. 40, no. 1, pp. W478–W483, 2012. View at Publisher · View at Google Scholar · View at Scopus
  11. A. Ruepp, B. Brauner, I. Dunger-Kaltenbach et al., “CORUM: the comprehensive resource of mammalian protein complexes,” Nucleic Acids Research, vol. 36, no. 1, pp. D646–D650, 2008. View at Publisher · View at Google Scholar · View at Scopus
  12. T. R. Burkard, M. Planyavsky, I. Kaupe et al., “Initial characterization of the human central proteome,” BMC Systems Biology, vol. 5, article 17, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. D. Mellacheruvu, Z. Wright, A. L. Couzens et al., “The CRAPome: a contaminant repository for affinity purification-mass spectrometry data,” Nature Methods, vol. 10, no. 8, pp. 730–736, 2013. View at Publisher · View at Google Scholar · View at Scopus
  14. T. R. Burkard, U. Rix, F. P. Breitwieser, G. Superti-Furga, and J. Colinge, “A computational approach to analyze the mechanism of action of the kinase inhibitor bafetinib,” PLoS Computational Biology, vol. 6, no. 11, Article ID e1001001, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. Ishihama, Y. Oda, T. Tabata et al., “Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein,” Molecular and Cellular Proteomics, vol. 4, no. 9, pp. 1265–1272, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. C. S. Spahr, M. T. Davis, M. D. McGinley et al., “Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest,” Proteomics, vol. 1, no. 1, pp. 93–107, 2001. View at Publisher · View at Google Scholar
  17. J. E. Elias and S. P. Gygi, “Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry,” Nature Methods, vol. 4, no. 3, pp. 207–214, 2007. View at Publisher · View at Google Scholar · View at Scopus
  18. J. Fernandez-de-Cossio, L. J. Gonzalez, Y. Satomi et al., “Isotopica: a tool for the calculation and viewing of complex isotopic envelopes,” Nucleic Acids Research, vol. 32, supplement 2, pp. W674–W678, 2004. View at Publisher · View at Google Scholar
  19. J. Fernández-de-Cossio, L. J. Gonzalez, Y. Satomi et al., “Automated interpretation of mass spectra of complex mixtures by matching of isotope peak distributions,” Rapid Communications in Mass Spectrometry, vol. 18, no. 20, pp. 2465–2472, 2004. View at Publisher · View at Google Scholar · View at Scopus
  20. P. Shannon, A. Markiel, O. Ozier et al., “Cytoscape: a software environment for integrated models of biomolecular interaction networks,” Genome Research, vol. 13, no. 11, pp. 2498–2504, 2003. View at Publisher · View at Google Scholar · View at Scopus
  21. A. Martin, M. E. Ochagavia, L. C. Rabasa, J. Miranda, J. Fernandez-de-Cossio, and R. Bringas, “BisoGenet: a new tool for gene network building, visualization and analysis,” BMC Bioinformatics, vol. 11, article 91, 2010. View at Publisher · View at Google Scholar · View at Scopus
  22. G. Warsow, B. Greber, S. S. I. Falk et al., “ExprEssence—revealing the essence of differential experimental data in the context of an interaction/regulation net-work,” BMC Systems Biology, vol. 4, article 164, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. P. Chatrath, I. S. Scott, L. S. Morris et al., “Aberrant expression of minichromosome maintenance protein-2 and Ki67 in laryngeal squamous epithelial lesions,” British Journal of Cancer, vol. 89, no. 6, pp. 1048–1054, 2003. View at Publisher · View at Google Scholar · View at Scopus
  24. J. Kikuchi, I. Kinoshita, Y. Shimizu et al., “Minichromosome maintenance (MCM) protein 4 as a marker for proliferation and its clinical and clinicopathological significance in non-small cell lung cancer,” Lung Cancer, vol. 72, no. 2, pp. 229–237, 2011. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Lei, “The MCM complex: its role in DNA replication and implications for cancer therapy,” Current Cancer Drug Targets, vol. 5, no. 5, pp. 365–380, 2005. View at Publisher · View at Google Scholar · View at Scopus
  26. O. Saydam, O. Senol, T. B. M. Schaaij-Visser et al., “Comparative protein profiling reveals minichromosome maintenance (MCM) proteins as novel potential tumor markers for meningiomas,” Journal of Proteome Research, vol. 9, no. 1, pp. 485–494, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. U. Rix and G. Superti-Furga, “Target profiling of small molecules by chemical proteomics,” Nature Chemical Biology, vol. 5, no. 9, pp. 616–624, 2009. View at Publisher · View at Google Scholar · View at Scopus
  28. M. Raida, “Drug target deconvolution by chemical proteomics,” Current Opinion in Chemical Biology, vol. 15, no. 4, pp. 570–575, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. B. van de Sluis, X. Mao, Y. Zhai et al., “COMMD1 disrupts HIF-1α/β dimerization and inhibits human tumor cell invasion,” Journal of Clinical Investigation, vol. 120, no. 6, pp. 2119–2130, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. U. Rix, L. L. R. Rix, A. S. Terker et al., “A comprehensive target selectivity survey of the BCR-ABL kinase inhibitor INNO-406 by kinase profiling and chemical proteomics in chronic myeloid leukemia cells,” Leukemia, vol. 24, no. 1, pp. 44–50, 2010. View at Publisher · View at Google Scholar · View at Scopus
  31. D. M. Gilkes, G. L. Semenza, and D. Wirtz, “Hypoxia and the extracellular matrix: drivers of tumour metastasis,” Nature Reviews Cancer, vol. 14, no. 6, pp. 430–439, 2014. View at Publisher · View at Google Scholar · View at Scopus
  32. N. D. Perkins and T. D. Gilmore, “Good cop, bad cop: the different faces of NF-κB,” Cell Death and Differentiation, vol. 13, no. 5, pp. 759–772, 2006. View at Publisher · View at Google Scholar · View at Scopus
  33. A. S. Baldwin, “Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB,” The Journal of Clinical Investigation, vol. 107, no. 3, pp. 241–246, 2001. View at Publisher · View at Google Scholar · View at Scopus
  34. B. Rayet and C. Gélinas, “Aberrant rel/nfkb genes and activity in human cancer,” Oncogene, vol. 18, no. 49, pp. 6938–6947, 1999. View at Publisher · View at Google Scholar · View at Scopus
  35. S. Liptay, C. K. Weber, L. Ludwig, M. Wagner, G. Adler, and R. M. Schmid, “Mitogenic and antiapoptotic role of constitutive NF-κB/Rel activity in pancreatic cancer,” International Journal of Cancer, vol. 105, no. 6, pp. 735–746, 2003. View at Publisher · View at Google Scholar · View at Scopus
  36. C. Huang, K. Huang, C. Wang et al., “Overexpression of mitogen-activated protein kinase kinase 4 and nuclear factor-kappaB in laryngeal squamous cell carcinoma: a potential indicator for poor prognosis,” Oncology Reports, vol. 22, no. 1, pp. 89–95, 2009. View at Publisher · View at Google Scholar · View at Scopus
  37. B. Lamothe, A. Besse, A. D. Campos, W. K. Webster, H. Wu, and B. G. Darnay, “Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of IκB kinase activation,” The Journal of Biological Chemistry, vol. 282, no. 6, pp. 4102–4112, 2007. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Windheim, M. Stafford, M. Peggie, and P. Cohen, “Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IκBα kinase,” Molecular and Cellular Biology, vol. 28, no. 5, pp. 1783–1791, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. L. Vermeulen, G. De Wilde, P. Van Damme, W. V. Berghe, and G. Haegeman, “Transcriptional activation of the NF-κB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1),” The EMBO Journal, vol. 22, no. 6, pp. 1313–1324, 2003. View at Publisher · View at Google Scholar · View at Scopus
  40. H. Higashitsuji, H. Higashitsuji, T. Nagao et al., “A novel protein overexpressed in hepatoma accelerates export of NF-kappa B from the nucleus and inhibits p53-dependent apoptosis,” Cancer Cell, vol. 2, no. 4, pp. 335–346, 2002. View at Publisher · View at Google Scholar · View at Scopus
  41. Y. Li, M. A. Reddy, F. Miao et al., “Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-κB-dependent inflammatory genes. Relevance to diabetes and inflammation,” Journal of Biological Chemistry, vol. 283, no. 39, pp. 26771–26781, 2008. View at Publisher · View at Google Scholar · View at Scopus
  42. X.-D. Yang, B. Huang, M. Li, A. Lamb, N. L. Kelleher, and L.-F. Chen, “Negative regulation of NF-κB action by Set9-mediated lysine methylation of the relA subunit,” The EMBO Journal, vol. 28, no. 8, pp. 1055–1066, 2009. View at Publisher · View at Google Scholar · View at Scopus
  43. T. A. Libermann and D. Baltimore, “Activation of interleukin-6 gene expression through the NF-κB transcription factor,” Molecular and Cellular Biology, vol. 10, no. 5, pp. 2327–2334, 1990. View at Publisher · View at Google Scholar · View at Scopus
  44. B. Hoesel and J. A. Schmid, “The complexity of NF-kappaB signaling in inflammation and cancer,” Molecular Cancer, vol. 12, article 86, 2013. View at Publisher · View at Google Scholar · View at Scopus
  45. M. E. Tanenbaum, T. Vallenius, E. F. Geers, L. Greene, T. P. Mäkelä, and R. H. Medema, “Cyclin G-associated kinase promotes microtubule outgrowth from chromosomes during spindle assembly,” Chromosoma, vol. 119, no. 4, pp. 415–424, 2010. View at Publisher · View at Google Scholar · View at Scopus
  46. D. Frescas and M. Pagano, “Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: tipping the scales of cancer,” Nature Reviews Cancer, vol. 8, no. 6, pp. 438–449, 2008. View at Publisher · View at Google Scholar · View at Scopus
  47. S. Shimizu, M. Narita, and Y. Tsujimoto, “Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC,” Nature, vol. 399, no. 6735, pp. 483–487, 1999. View at Publisher · View at Google Scholar · View at Scopus
  48. Y. Tsujimoto and S. Shimizu, “The voltage-dependent anion channel: an essential player in apoptosis,” Biochimie, vol. 84, no. 2-3, pp. 187–193, 2002. View at Publisher · View at Google Scholar · View at Scopus
  49. G. M. Kasof, L. Goyal, and E. White, “Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins,” Molecular and Cellular Biology, vol. 19, no. 6, pp. 4390–4404, 1999. View at Google Scholar · View at Scopus
  50. H. Liu, Z.-G. Lu, Y. Miki, and K. Yoshida, “Protein kinase C delta induces transcription of the TP53 tumor suppressor gene by controlling death-promoting factor Btf in the apoptotic response to DNA damage,” Molecular and Cellular Biology, vol. 27, no. 24, pp. 8480–8491, 2007. View at Publisher · View at Google Scholar · View at Scopus
  51. C. M. Laurençot, G. L. Scheffer, R. J. Scheper, and R. H. Shoemaker, “Increased LRP mRNA expression is associated with the MDR phenotype in intrinsically resistant human cancer cell lines,” International Journal of Cancer, vol. 72, no. 6, pp. 1021–1026, 1997. View at Publisher · View at Google Scholar · View at Scopus
  52. S. Tang, C. Bai, P. Yang, and X. Chen, “14-3-3ε boosts bleomycin-induced DNA damage response by inhibiting the drug-resistant activity of MVP,” Journal of Proteome Research, vol. 12, no. 6, pp. 2511–2524, 2013. View at Publisher · View at Google Scholar · View at Scopus
  53. A. Losert, D. Lötsch, A. Lackner et al., “The major vault protein mediates resistance to epidermal growth factor receptor inhibition in human hepatoma cells,” Cancer Letters, vol. 319, no. 2, pp. 164–172, 2012. View at Publisher · View at Google Scholar · View at Scopus
  54. K. Kanda, H. Komekado, T. Sawabu et al., “Nardilysin and ADAM proteases promote gastric cancer cell growth by activating intrinsic cytokine signalling via enhanced ectodomain shedding of TNF-α,” EMBO Molecular Medicine, vol. 4, no. 5, pp. 396–411, 2012. View at Publisher · View at Google Scholar · View at Scopus
  55. N. Uraoka, N. Oue, N. Sakamoto et al., “NRD1, which encodes nardilysin protein, promotes esophageal cancer cell invasion through induction of MMP2 and MMP3 expression,” Cancer Science, vol. 105, no. 1, pp. 134–140, 2014. View at Publisher · View at Google Scholar · View at Scopus
  56. H. Roumes, L. Leloup, E. Dargelos, J.-J. Brustis, L. Daury, and P. Cottin, “Calpains: markers of tumor aggressiveness?” Experimental Cell Research, vol. 316, no. 9, pp. 1587–1599, 2010. View at Publisher · View at Google Scholar · View at Scopus
  57. H. S. Jang, S. Lal, and J. A. Greenwood, “Calpain 2 is required for glioblastoma cell invasion: rRegulation of matrix metalloproteinase 2,” Neurochemical Research, vol. 35, no. 11, pp. 1796–1804, 2010. View at Publisher · View at Google Scholar · View at Scopus
  58. B. Chen, J. Tang, Y.-S. Guo, Y. Li, Z.-N. Chen, and J.-L. Jiang, “Calpains are required for invasive and metastatic potentials of human HCC cells,” Cell Biology International, vol. 37, no. 7, pp. 643–652, 2013. View at Publisher · View at Google Scholar · View at Scopus
  59. Y. Su, Z. Cui, Z. Li, and E. R. Block, “Calpain-2 regulation of VEGF-mediated angiogenesis,” The FASEB Journal, vol. 20, no. 9, pp. 1443–1451, 2006. View at Publisher · View at Google Scholar · View at Scopus
  60. D. E. Bassi, J. Fu, R. L. de Cicco, and A. J. P. Klein-Szanto, “Proprotein convertases: “Master switches” in the regulation of tumor growth and progression,” Molecular Carcinogenesis, vol. 44, no. 3, pp. 151–161, 2005. View at Publisher · View at Google Scholar · View at Scopus
  61. M. Lapierre, G. Siegfried, N. Scamuffa et al., “Opposing function of the proprotein convertases furin and PACE4 on breast cancer cells' malignant phenotypes: role of tissue inhibitors of metalloproteinase-1,” Cancer Research, vol. 67, no. 19, pp. 9030–9034, 2007. View at Publisher · View at Google Scholar · View at Scopus
  62. S. Delic, N. Lottmann, K. Jetschke, G. Reifenberger, and M. J. Riemenschneider, “Identification and functional validation of CDH11, PCSK6 and SH3GL3 as novel glioma invasion-associated candidate genes,” Neuropathology and Applied Neurobiology, vol. 38, no. 2, pp. 201–212, 2012. View at Publisher · View at Google Scholar · View at Scopus
  63. D. E. Bassi, J. Cenna, J. Zhang, E. Cukierman, and A. J. Klein-Szanto, “Enhanced aggressiveness of benzopyrene-induced squamous carcinomas in transgenic mice overexpressing the proprotein convertase PACE4 (PCSK6),” Molecular Carcinogenesis, vol. 54, no. 10, pp. 1122–1131, 2015. View at Publisher · View at Google Scholar
  64. F. Couture, C. Levesque, V. Dumulon-Perreault et al., “PACE4-based molecular targeting of prostate cancer using an engineered 64Cu-radiolabeled peptide inhibitor,” Neoplasia, vol. 16, no. 8, pp. 634–643, 2014. View at Publisher · View at Google Scholar
  65. D. E. Bassi, J. Zhang, J. Cenna, S. Litwin, E. Cukierman, and A. J. P. Klein-Szanto, “Proprotein convertase inhibition results in decreased skin cell proliferation, tumorigenesis, and metastasis,” Neoplasia, vol. 12, no. 7, pp. 516–526, 2010. View at Publisher · View at Google Scholar · View at Scopus
  66. S. Wang, B. Zhang, and D. V. Faller, “Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth,” The EMBO Journal, vol. 21, no. 12, pp. 3019–3028, 2002. View at Publisher · View at Google Scholar · View at Scopus
  67. W. Pan, L. S. de Graca, Y. Shao, Q. Yin, H. Wu, and X. Jiang, “PHAPI/pp32 suppresses tumorigenesis by stimulating apoptosis,” The Journal of Biological Chemistry, vol. 284, no. 11, pp. 6946–6954, 2009. View at Publisher · View at Google Scholar · View at Scopus
  68. H. Tsuchiya, T. Iseda, and O. Hino, “Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product,” Cancer Research, vol. 56, no. 13, pp. 2881–2885, 1996. View at Google Scholar · View at Scopus
  69. C. A. Lancaster, P. M. Taylor-Harris, A. J. Self, S. Brill, H. E. Van Erp, and A. Hall, “Characterization of rhoGAP: a GTPase-activating protein for rho-related small GTPases,” The Journal of Biological Chemistry, vol. 269, no. 2, pp. 1137–1142, 1994. View at Google Scholar · View at Scopus
  70. M. Lazarini, F. Traina, J. A. Machado-Neto et al., “ARHGAP21 is a RhoGAP for RhoA and RhoC with a role in proliferation and migration of prostate adenocarcinoma cells,” Biochimica et Biophysica Acta - Molecular Basis of Disease, vol. 1832, no. 2, pp. 365–374, 2013. View at Publisher · View at Google Scholar · View at Scopus
  71. G. M. Nagaraja and R. P. Kandpal, “Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins,” Biochemical and Biophysical Research Communications, vol. 313, no. 3, pp. 654–665, 2004. View at Publisher · View at Google Scholar · View at Scopus
  72. E. Jacque and S. C. Ley, “RNF11, a new piece in the A20 puzzle,” The EMBO Journal, vol. 28, no. 5, pp. 455–456, 2009. View at Publisher · View at Google Scholar · View at Scopus
  73. N. Shembade, A. Ma, and E. W. Harhaj, “Inhibition of NF-κB signaling by A20 through disruption of ubiquitin enzyme complexes,” Science, vol. 327, no. 5969, pp. 1135–1139, 2010. View at Publisher · View at Google Scholar · View at Scopus
  74. I. E. Wartz, K. M. O'Rourke, H. Zhou et al., “De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling,” Nature, vol. 430, no. 7000, pp. 694–699, 2004. View at Publisher · View at Google Scholar · View at Scopus
  75. Y. Yoshida, A. Murakami, and K. Tanaka, “Skp1 stabilizes the conformation of F-box proteins,” Biochemical and Biophysical Research Communications, vol. 410, no. 1, pp. 24–28, 2011. View at Publisher · View at Google Scholar · View at Scopus
  76. M. Shirane, S. Hatakeyama, K. Hattori, K. Nakayama, and K. Nakayama, “Common pathway for the ubiquitination of IkappaBalpha, IkappaBbeta, and IkappaBepsilon mediated by the F-box protein FWD1,” The Journal of Biological Chemistry, vol. 274, no. 40, pp. 28169–28174, 1999. View at Google Scholar
  77. M.-P. Bousquet-Dubouch, E. Baudelet, F. Guérin et al., “Affinity purification strategy to capture human endogenous proteasome complexes diversity and to identify proteasome-interacting proteins,” Molecular & Cellular Proteomics, vol. 8, no. 5, pp. 1150–1164, 2009. View at Publisher · View at Google Scholar · View at Scopus