Тема: Анализ изменений в протеасомо-ассоциированном протеоме клеток множественной миеломы человека при сочетанной обработке специфическими препаратами-ингибиторами

1. Adams, J., Kauffman, M. (2004). Development of the proteasome inhibitor Velcade
(Bortezomib). Cancer Investigation, 22(2), 304–311.
2. Akinwumi, B. C., Bordun, K.-A. M., Anderson, H. D. (2018). Biological Activities of
Stilbenoids. International Journal of Molecular Sciences, 19(3).
https://doi.org/10.3390/ijms19030792
3. Al-Nedawi, K., Meehan, B., Micallef, J., Lhotak, V., May, L., Guha, A., Rak, J. (2008).
Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from
tumour cells. Nature Cell Biology, 10(5), 619–624. https://doi.org/10.1038/ncb1725
4. Attal, M., Lauwers-Cances, V., Hulin, C., Leleu, X., Caillot, D., Escoffre, M., Moreau, P.
(2017). Lenalidomide, Bortezomib, and Dexamethasone with Transplantation for Myeloma.
New England Journal of Medicine, 376(14), 1311–1320.
https://doi.org/10.1056/NEJMoa1611750
5. Babu, M. M., Lee, R. Van Der, Groot, N. S. De. (2011). Intrinsically disordered proteins :
regulation and disease, 432–440. https://doi.org/10.1016/j.sbi.2011.03.011
6. Barrott, J. J., Haystead, T. A. J. (2013). Hsp90, an unlikely ally in the war on cancer. The
FEBS Journal, 280(6), 1381–1396. https://doi.org/10.1111/febs.12147
7. Ben-Saadon, R., Fajerman, I., Ziv, T., Hellman, U., Schwartz, A. L., Ciechanover, A. (2004).
The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7
are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct
evidence for ubiquitination at the N-terminal residue. The Journal of Biological Chemistry,
279(40), 41414–41421. https://doi.org/10.1074/jbc.M407201200
8. Bernardoni, P., Fazi, B., Costanzi, A., Nardacci, R., Montagna, C., Filomeni, G., Di Sano, F.
(2013). Reticulon1-C modulates protein disulphide isomerase function. Cell Death &
Disease, 4, e581. https://doi.org/10.1038/cddis.2013.1139. Bi, H., Yang, X., Yuan, J., Yang, F., Xu, D., Guo, Y., Sun, S. (2013). H19 inhibits RNA
polymerase II-mediated transcription by disrupting the hnRNP U-actin complex. Biochimica
et Biophysica Acta, 1830(10), 4899–4906. https://doi.org/10.1016/j.bbagen.2013.06.026
10. Bochtler, M., Ditzel, L., Groll, M., Hartmann, C., Huber, R. (1999). The proteasome. Annual
Review of Biophysics and Biomolecular Structure, 28, 295–317.
https://doi.org/10.1146/annurev.biophys.28.1.295
11. Brymora, A., Valova, V. A., Robinson, P. J. (2004). Protein-protein interactions identified by
pull-down experiments and mass spectrometry. Current Protocols in Cell Biology, Chapter
17, Unit 17.5. https://doi.org/10.1002/0471143030.cb1705s22
12. Budenholzer, L., Cheng, C. L., Li, Y., Hochstrasser, M. (2017). Proteasome Structure and
Assembly. Journal of Molecular Biology, 429(22), 3500–3524.
https://doi.org/10.1016/j.jmb.2017.05.027
13. Chen, D., Zhang, Z., Li, M., Wang, W., Li, Y., Rayburn, E. R., Zhang, R. (2007). Ribosomal
protein S7 as a novel modulator of p53-MDM2 interaction: binding to MDM2, stabilization of
p53 protein, and activation of p53 function. Oncogene, 26(35), 5029–5037.
https://doi.org/10.1038/sj.onc.1210327
14. Chen, X., Barton, L. F., Chi, Y., Clurman, B. E., Roberts, J. M. (2007). Ubiquitin-independent
degradation of cell-cycle inhibitors by the REGgamma proteasome. Molecular Cell, 26(6),
843–852. https://doi.org/10.1016/j.molcel.2007.05.022
15. Chen, Z.-Y., Cai, L., Zhu, J., Chen, M., Chen, J., Li, Z.-H., Li, X.-W. (2011). Fyn requires
HnRNPA2B1 and Sam68 to synergistically regulate apoptosis in pancreatic cancer.
Carcinogenesis, 32(10), 1419–1426. https://doi.org/10.1093/carcin/bgr088
16. Close, P., East, P., Dirac-Svejstrup, A. B., Hartmann, H., Heron, M., Maslen, S., Svejstrup, J.
Q. (2012). DBIRD complex integrates alternative mRNA splicing with RNA polymerase II
transcript elongation. Nature, 484(7394), 386–389. https://doi.org/10.1038/nature10925
17. Collins, G. A., Goldberg, A. L. (2017). The Logic of the 26S Proteasome. Cell, 169(5), 792–
806. https://doi.org/10.1016/j.cell.2017.04.023
18. Cosemans, C., Oben, B., Arijs, I., Daniels, A., Declercq, J., Vanhees, K., Rummens, J.-L.
(2018). Prognostic Biomarkers in the Progression From MGUS to Multiple Myeloma: A
Systematic Review. Clinical Lymphoma, Myeloma & Leukemia, 18(4), 235–248.
https://doi.org/10.1016/j.clml.2018.02.011
19. Dahlmann, B. (2016). Mammalian proteasome subtypes: Their diversity in structure and
function. Archives of Biochemistry and Biophysics, 591, 132–140.
https://doi.org/10.1016/j.abb.2015.12.012
20. Dardenne, E., Polay Espinoza, M., Fattet, L., Germann, S., Lambert, M.-P., Neil, H.,Auboeuf, D. (2014). RNA helicases DDX5 and DDX17 dynamically orchestrate transcription,
miRNA, and splicing programs in cell differentiation. Cell Reports, 7(6), 1900–1913.
https://doi.org/10.1016/j.celrep.2014.05.010
21. de Las Heras-Rubio, A., Perucho, L., Paciucci, R., Vilardell, J., LLeonart, M. E. (2014).
Ribosomal proteins as novel players in tumorigenesis. Cancer Metastasis Reviews, 33(1),
115–141. https://doi.org/10.1007/s10555-013-9460-6
22. Deshaies, R. J., Joazeiro, C. A. P. (2009). RING domain E3 ubiquitin ligases. Annual Review
of Biochemistry, 78, 399–434. https://doi.org/10.1146/annurev.biochem.78.101807.093809
23. Dimopoulos, M. A., Goldschmidt, H., Niesvizky, R., Joshua, D., Chng, W.-J., Oriol, A.,
Moreau, P. (2017). Carfilzomib or bortezomib in relapsed or refractory multiple myeloma
(ENDEAVOR): an interim overall survival analysis of an open-label, randomised, phase 3
trial. The Lancet. Oncology, 18(10), 1327–1337. https://doi.org/10.1016/S1470-
2045(17)30578-8
24. Eckschlager, T., Plch, J., Stiborova, M., Hrabeta, J. (2017). Histone Deacetylase Inhibitors as
Anticancer Drugs. International Journal of Molecular Sciences, 18(7), 1414.
https://doi.org/10.3390/ijms18071414
25. Elsasser, S., Chandler-Militello, D., Muller, B., Hanna, J., Finley, D. (2004). Rad23 and
Rpn10 serve as alternative ubiquitin receptors for the proteasome. The Journal of Biological
Chemistry, 279(26), 26817–26822. https://doi.org/10.1074/jbc.M404020200
26. Elsasser, S., Finley, D. (2005). Delivery of ubiquitinated substrates to protein-unfolding
machines. Nature Cell Biology, 7(8), 742–749. https://doi.org/10.1038/ncb0805-742
27. Enenkel, C., Lehmann, A., Kloetzel, P. M. (1998). Subcellular distribution of proteasomes
implicates a major location of protein degradation in the nuclear envelope-ER network in
yeast. The EMBO Journal, 17(21), 6144–6154. https://doi.org/10.1093/emboj/17.21.6144
28. Erales, J., Coffino, P. (2014). Ubiquitin-independent proteasomal degradation. Biochimica et
Biophysica Acta, 1843(1), 216–221. https://doi.org/10.1016/j.bbamcr.2013.05.008
29. Etlinger, J. D., Goldberg, A. L. (1977). A soluble ATP-dependent proteolytic system
responsible for the degradation of abnormal proteins in reticulocytes. Proceedings of the
National Academy of Sciences of the United States of America, 74(1), 54–58.
30. Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., & Whitehouse, C. M. (1989). Electrospray
ionization for mass spectrometry of large biomolecules. Science (New York, N.Y.), 246(4926),
64–71.
31. Fort, P., Kajava, A. V, Delsuc, F., Coux, O. (2015). Evolution of proteasome regulators in
eukaryotes. Genome Biology and Evolution, 7(5), 1363–1379.
https://doi.org/10.1093/gbe/evv06832. Gao, H., Sun, B., Fu, H., Chi, X., Wang, F., Qi, X., Shao, S. (2016). PDIA6 promotes the
proliferation of HeLa cells through activating the Wnt/beta-catenin signaling pathway.
Oncotarget, 7(33), 53289–53298. https://doi.org/10.18632/oncotarget.10795
33. Garcia-Carbonero, R., Carnero, A., Paz-Ares, L. (2013). Inhibition of HSP90 molecular
chaperones: Moving into the clinic. The Lancet Oncology, 14(9), e358–e369.
https://doi.org/10.1016/S1470-2045(13)70169-4
34. Geng, F., Wenzel, S., Tansey, W. P. (2012). Ubiquitin and Proteasomes in Transcription,
177–204. https://doi.org/10.1146/annurev-biochem-052110-120012
35. Giguere, S. S. B., Guise, A. J., Jean Beltran, P. M., Joshi, P. M., Greco, T. M., Quach, O. L.,
Cristea, I. M. (2016). The Proteomic Profile of Deleted in Breast Cancer 1 (DBC1)
Interactions Points to a Multifaceted Regulation of Gene Expression. Molecular & Cellular
Proteomics : MCP, 15(3), 791–809. https://doi.org/10.1074/mcp.M115.054619
36. Gokduman, K. (2016). Strategies Targeting DNA Topoisomerase I in Cancer Chemotherapy:
Camptothecins, Nanocarriers for Camptothecins, Organic Non-Camptothecin Compounds and
Metal Complexes. Current Drug Targets, 17(16), 1928–1939.
37. Graifer, D., Malygin, A., Zharkov, D. O., Karpova, G. (2014). Biochimie Eukaryotic
ribosomal protein S3 : A constituent of translational machinery and an extraribosomal player
in various cellular processes. Biochimie, 99, 8–18.
https://doi.org/10.1016/j.biochi.2013.11.001
38. Groll, M., Bajorek, M., Kohler, A., Moroder, L., Rubin, D. M., Huber, R., Finley, D. (2000).
A gated channel into the proteasome core particle. Nature Structural Biology, 7(11), 1062–
1067. https://doi.org/10.1038/80992
39. Groll, M., Huber, R. (2003). Substrate access and processing by the 20S proteasome core
particle, 35, 606–616. https://doi.org/10.1016/S1357-2725(02)00390-4
40. Gu, Z. C., Enenkel, C. (2014). Proteasome assembly. Cellular and Molecular Life Sciences,
71(24), 4729–4745. https://doi.org/10.1007/s00018-014-1699-8
41. Guthrie, A. R., Chow, H.-H. S., Martinez, J. A. (2017). Effects of resveratrol on drug- and
carcinogen-metabolizing enzymes, implications for cancer prevention. Pharmacology
Research & Perspectives, 5(1), e00294. https://doi.org/10.1002/prp2.294
42. Han, N., Li, W., Zhang, M. (2013). The function of the RNA-binding protein hnRNP in
cancer metastasis. Journal of Cancer Research and Therapeutics, 9 Suppl, S129-34.
https://doi.org/10.4103/0973-1482.122506
43. Hanash, S. M., Pitteri, S. J., Faca, V. M. (2008). Mining the plasma proteome for cancer
biomarkers. Nature, 452(7187), 571–579. https://doi.org/10.1038/nature06916
44. Hashimoto, Y., Kim, D. J., Adams, J. C. (2011). The roles of fascins in health and disease.The Journal of Pathology, 224(3), 289–300. https://doi.org/10.1002/path.2894
45. Hashimoto, Y., Parsons, M., Adams, J. C. (2007). Dual actin-bundling and protein kinase Cbinding activities of fascin regulate carcinoma cell migration downstream of Rac and
contribute to metastasis. Molecular Biology of the Cell, 18(11), 4591–4602.
https://doi.org/10.1091/mbc.E07-02-0157
46. Heinemeyer, W., Ramos, P. C., Dohmen, R. J. (2004). The ultimate nanoscale mincer:
assembly, structure and active sites of the 20S proteasome core. Cellular and Molecular Life
Sciences : CMLS, 61(13), 1562–1578. https://doi.org/10.1007/s00018-004-4130-z
47. Hirano, H., Kimura, Y., Kimura, A. (2016). Biological significance of co- and posttranslational modifications of the yeast 26S proteasome. Journal of Proteomics, 134, 37–46.
https://doi.org/10.1016/j.jprot.2015.11.016
48. Hirano, Y., Hayashi, H., Iemura, S.-I., Hendil, K. B., Niwa, S.-I., Kishimoto, T., Murata, S.
(2006). Cooperation of multiple chaperones required for the assembly of mammalian 20S
proteasomes. Molecular Cell, 24(6), 977–984. https://doi.org/10.1016/j.molcel.2006.11.015
49. Hirano, Y., Hendil, K. B., Yashiroda, H., Iemura, S., Nagane, R., Hioki, Y., Murata, S.
(2005). A heterodimeric complex that promotes the assembly of mammalian 20S
proteasomes. Nature, 437(7063), 1381–1385. https://doi.org/10.1038/nature04106
50. Hofmeister, C. C., Poi, M., Bowers, M. A., Zhao, W., Phelps, M. A., Benson, D. M., Byrd, J.
C. (2014). A phase I trial of flavopiridol in relapsed multiple myeloma. Cancer
Chemotherapy and Pharmacology, 73(2), 249–257. https://doi.org/10.1007/s00280-013-2347-
y
51. Hsieh, F. Y., Tengstrand, E., Pekol, T. M., Guerciolini, R., Miwa, G. (2009). Elucidation of
potential bortezomib response markers in mutliple myeloma patients. Journal of
Pharmaceutical and Biomedical Analysis, 49(1), 115–122.
https://doi.org/10.1016/j.jpba.2008.09.053
52. Hwang, G.-W. (2007). Ubiquitin-proteasome system as a factor that determine the sensitivity
to methylmercury. Yakugaku Zasshi : Journal of the Pharmaceutical Society of Japan, 127(3),
463–468.
53. Inobe, T., Matouschek, A. (2014). ScienceDirect Paradigms of protein degradation by the
proteasome. Current Opinion in Structural Biology, 24, 156–164.
https://doi.org/10.1016/j.sbi.2014.02.002
54. Jagannath, S., Barlogie, B., Berenson, J., Siegel, D., Irwin, D., Richardson, P. G., Anderson,
K. C. (2004). A phase 2 study of two doses of bortezomib in relapsed or refractory myeloma.
British Journal of Haematology, 127(2), 165–172. https://doi.org/10.1111/j.1365-
2141.2004.05188.x55. Jang, C.-Y., Lee, J. Y., Kim, J. (2004). RpS3, a DNA repair endonuclease and ribosomal
protein, is involved in apoptosis. FEBS Letters, 560(1–3), 81–85.
https://doi.org/10.1016/S0014-5793(04)00074-2
56. Jean-Philippe, J., Paz, S., Caputi, M. (2013). hnRNP A1: the Swiss army knife of gene
expression. International Journal of Molecular Sciences, 14(9), 18999–19024.
https://doi.org/10.3390/ijms140918999
57. Jung, T., Catalgol, B., Grune, T. (2009). The proteasomal system. Molecular Aspects of
Medicine, 30(4), 191–296. https://doi.org/10.1016/j.mam.2009.04.001
58. Just, W., Geerkens, C., Held, K. R., Vogel, W. (1992). Expression of RPS4X in fibroblasts
from patients with structural aberrations of the X chromosome. Human Genetics, 89(2), 240–
242.
59. Kenney, S. P., Meng, X.-J. (2015). Identification and fine mapping of nuclear and nucleolar
localization signals within the human ribosomal protein S17. PloS One, 10(4), e0124396.
https://doi.org/10.1371/journal.pone.0124396
60. Kim, D., Kim, W., Lee, K., Kim, S., Lee, H., Kim, H., Kim, K. (2012). hnRNP Q regulates
translation of p53 in normal and stress conditions, 20(2), 226–234.
https://doi.org/10.1038/cdd.2012.109
61. Kim, J.-E., Chen, J., Lou, Z. (2009). p30 DBC is a potential regulator of tumorigenesis. Cell
Cycle (Georgetown, Tex.), 8(18), 2932–2935.
62. Kim, Y., Kim, H. D., Youn, B., Park, Y. G., Kim, J. (2013). Ribosomal protein S3 is secreted
as a homodimer in cancer cells. Biochemical and Biophysical Research Communications,
441(4), 805–808. https://doi.org/10.1016/j.bbrc.2013.10.132
63. Kim, Y., Lee, M. S., Kim, H. D., Kim, J. (2016). Ribosomal protein S3 (rpS3) secreted from
various cancer cells is N-linked glycosylated. Oncotarget, 7(49), 80350–80362.
https://doi.org/10.18632/oncotarget.10180
64. Kisselev, A. F., Akopian, T. N., Castillo, V., & Goldberg, A. L. (1999). Proteasome active
sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein
breakdown. Molecular Cell, 4(3), 395–402.
65. Kisselev, A. F., van der Linden, W. A., & Overkleeft, H. S. (2012). Proteasome inhibitors: an
expanding army attacking a unique target. Chemistry & Biology, 19(1), 99–115.
https://doi.org/10.1016/j.chembiol.2012.01.003
66. Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999). A
novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell, 96(5),
635–644.
67. Koomen, J. M., Haura, E. B., Bepler, G., Sutphen, R., Remily-Wood, E. R., Benson, K., …Dalton, W. S. (2008). Proteomic Contributions to Personalized Cancer Care. Molecular &
Cellular Proteomics, 7(10), 1780–1794. https://doi.org/10.1074/mcp.R800002-MCP200
68. Kumar, S. K., & Rajkumar, S. V. (2018). The multiple myelomas — current concepts in
cytogenetic classification and therapy. Nature Reviews Clinical Oncology, 1.
https://doi.org/10.1038/s41571-018-0018-y
69. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of
bacteriophage T4. Nature, 227(5259), 680–685.
70. Lee, B.-H., Lee, M. J., Park, S., Oh, D.-C., Elsasser, S., Chen, P.-C., … Finley, D. (2010).
Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature,
467(7312), 179–184. https://doi.org/10.1038/nature09299
71. Livneh, I., Cohen-Kaplan, V., Cohen-Rosenzweig, C., Avni, N., & Ciechanover, A. (2016).
The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its
death. Cell Research, 26(8), 869–885. https://doi.org/10.1038/cr.2016.86
72. Luria, S. E., Adams, J. N., & Ting, R. C. (1960). Transduction of lactose-utilizing ability
among strains of E. coli and S. dysenteriae and the properties of the transducing phage
particles. Virology, 12, 348–390.
73. Mccann, T. S., & Tansey, W. P. (2014). Functions of the Proteasome on Chromatin, 1026–
1044. https://doi.org/10.3390/biom4041026
74. Micallef, J., Dharsee, M., Chen, J., Ackloo, S., Evans, K., Qiu, L., & Chang, H. (2010).
Applying mass spectrometry based proteomic technology to advance the understanding of
multiple myeloma. Journal of Hematology & Oncology, 3, 13. https://doi.org/10.1186/1756-
8722-3-13
75. Mitsiades, N., Mitsiades, C. S., Richardson, P. G., Poulaki, V., Tai, Y.-T., Chauhan, D., …
Anderson, K. C. (2003). The proteasome inhibitor PS-341 potentiates sensitivity of multiple
myeloma cells to conventional chemotherapeutic agents: therapeutic applications. Blood,
101(6), 2377–2380. https://doi.org/10.1182/blood-2002-06-1768
76. Moreau, P. (2017). How I treat myeloma with new agents. Blood, 130(13), 1507–1513.
https://doi.org/10.1182/blood-2017-05-743203
77. Moreau, P., & de Wit, E. (2017). Recent progress in relapsed multiple myeloma therapy:
implications for treatment decisions. British Journal of Haematology, 179(2), 198–218.
https://doi.org/10.1111/bjh.14780
78. Muguruma, Y., Yahata, T., Warita, T., Hozumi, K., Nakamura, Y., Suzuki, R., … Ando, K.
(2017, December). Jagged1-induced Notch activation contributes to the acquisition of
bortezomib resistance in myeloma cells. Blood Cancer Journal. United States.
https://doi.org/10.1038/s41408-017-0001-379. Nathan, J. A., Kim, H. T., Ting, L., Gygi, S. P., & Goldberg, A. L. (2013). Why do cellular
proteins linked to K63-polyubiquitin chains not associate with proteasomes? The EMBO
Journal, 32(4), 552–565. https://doi.org/10.1038/emboj.2012.354
80. Ogiso, Y., Tomida, A., & Tsuruo, T. (2002). Nuclear localization of proteasomes participates
in stress-inducible resistance of solid tumor cells to topoisomerase II-directed drugs. Cancer
Research, 62(17), 5008–5012.
81. Orlowski, R. Z. (2004). Bortezomib in combination with other therapies for the treatment of
multiple myeloma. Journal of the National Comprehensive Cancer Network : JNCCN, 2
Suppl 4, S16-20.
82. Otero, M. G., Cromberg, L. E., Almenar-queralt, A., Encalada, S. E., Devoto, V. M. P.,
Bruno, L., & Goldstein, L. S. B. (2014). Fast axonal transport of the proteasome complex
depends on membrane interaction and molecular motor function, 1537–1549.
https://doi.org/10.1242/jcs.140780
83. Pao, K.-C., Wood, N. T., Knebel, A., Rafie, K., Stanley, M., Mabbitt, P. D., … Virdee, S.
(2018). Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity.
Nature. https://doi.org/10.1038/s41586-018-0026-1
84. Paquet, E. R., Hovington, H., Brisson, H., Lacombe, C., Larue, H., Tetu, B., … Lebel, M.
(2015). Low level of the X-linked ribosomal protein S4 in human urothelial carcinomas is
associated with a poor prognosis. Biomarkers in Medicine, 9(3), 187–197.
https://doi.org/10.2217/bmm.14.115
85. Parker, C. E., Pearson, T. W., Anderson, N. L., & Borchers, C. H. (2010). Mass-spectrometrybased clinical proteomics--a review and prospective. The Analyst, 135(8), 1830–1838.
https://doi.org/10.1039/c0an00105h
86. Plowman, J. E. (2007). The proteomics of keratin proteins. Journal of Chromatography. B,
Analytical Technologies in the Biomedical and Life Sciences, 849(1–2), 181–189.
https://doi.org/10.1016/j.jchromb.2006.07.055
87. Popat, R., Plesner, T., Davies, F., Cook, G., Cook, M., Elliott, P., … Cavenagh, J. (2013,
March). A phase 2 study of SRT501 (resveratrol) with bortezomib for patients with relapsed
and or refractory multiple myeloma. British Journal of Haematology. England.
https://doi.org/10.1111/bjh.12154
88. Rees-Unwin, K. S., Craven, R. A., Davenport, E., Hanrahan, S., Totty, N. F., Dring, A. M., …
Davies, F. E. (2007). Proteomic evaluation of pathways associated with dexamethasonemediated apoptosis and resistance in multiple myeloma. British Journal of Haematology,
139(4), 559–567. https://doi.org/10.1111/j.1365-2141.2007.06837.x
89. Ross, J. A., Robles-Escajeda, E., Oaxaca, D. M., Padilla, D. L., & Kirken, R. A. (2017). Theprohibitin protein complex promotes mitochondrial stabilization and cell survival in
hematologic malignancies. Oncotarget, 8(39), 65445–65456.
https://doi.org/10.18632/oncotarget.18920
90. Russell, S. J., Reed, S. H., Huang, W., Friedberg, E. C., & Johnston, S. A. (1999). The 19S
regulatory complex of the proteasome functions independently of proteolysis in nucleotide
excision repair. Molecular Cell, 3(6), 687–695.
91. Sauer, R. T., & Baker, T. A. (2011). AAA+ proteases: ATP-fueled machines of protein
destruction. Annual Review of Biochemistry, 80, 587–612. https://doi.org/10.1146/annurevbiochem-060408-172623
92. Sha, Z., & Goldberg, A. L. (2014). Proteasome-mediated processing of Nrf1 is essential for
coordinate induction of all proteasome subunits and p97. Current Biology : CB, 24(14), 1573–
1583. https://doi.org/10.1016/j.cub.2014.06.004
93. Smith, D. B., & Johnson, K. S. (1988). Single-step purification of polypeptides expressed in
Escherichia coli as fusions with glutathione S-transferase. Gene, 67(1), 31–40.
94. Stadtmueller, B. M., Kish-Trier, E., Ferrell, K., Petersen, C. N., Robinson, H., Myszka, D. G.,
… Hill, C. P. (2012). Structure of a proteasome Pba1-Pba2 complex: implications for
proteasome assembly, activation, and biological function. The Journal of Biological
Chemistry, 287(44), 37371–37382. https://doi.org/10.1074/jbc.M112.367003
95. Staley, J. P., Guthrie, C. (1998). Mechanical devices of the spliceosome: motors, clocks,
springs, and things. Cell, 92(3), 315–326.
96. Su, V., Lau, A. F. (2009). Ubiquitin-like and ubiquitin-associated domain proteins:
significance in proteasomal degradation. Cellular and Molecular Life Sciences : CMLS,
66(17), 2819–2833. https://doi.org/10.1007/s00018-009-0048-9
97. Tagami, S., Eguchi, Y., Kinoshita, M., Takeda, M., & Tsujimoto, Y. (2000). A novel protein,
RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their
anti-apoptotic activity. Oncogene, 19(50), 5736–5746. https://doi.org/10.1038/sj.onc.1203948
98. Teicher, B. A., & Tomaszewski, J. E. (2015). Proteasome inhibitors. Biochemical
Pharmacology, 96(1), 1–9. https://doi.org/10.1016/j.bcp.2015.04.008
99. Thrower, J. S. (2000). Recognition of the polyubiquitin proteolytic signal. The EMBO
Journal, 19(1), 94–102. https://doi.org/10.1093/emboj/19.1.94
100. Tomko, R. J. J., Hochstrasser, M. (2013). Molecular architecture and assembly of the
eukaryotic proteasome. Annual Review of Biochemistry, 82, 415–445.
https://doi.org/10.1146/annurev-biochem-060410-150257
101. Tsofack, S. P., Meunier, L., Sanchez, L., Madore, J., Provencher, D., Mes-Masson, A.-
M., Lebel, M. (2013). Low expression of the X-linked ribosomal protein S4 in human serousepithelial ovarian cancer is associated with a poor prognosis. BMC Cancer, 13, 303.
https://doi.org/10.1186/1471-2407-13-303
102. Tsvetkov, P., Reuven, N., Shaul, Y. (2010). Ubiquitin-independent p53 proteasomal
degradation. Cell Death and Differentiation, 17(1), 103–108.
https://doi.org/10.1038/cdd.2009.67
103. Unverdorben, P., Beck, F., Sledz, P., Schweitzer, A., Pfeifer, G., Plitzko, J. M., Forster,
F. (2014). Deep classification of a large cryo-EM dataset defines the conformational
landscape of the 26S proteasome. Proceedings of the National Academy of Sciences of the
United States of America, 111(15), 5544–5549. https://doi.org/10.1073/pnas.1403409111
104. Van Drie, J. H. (2011). Protein folding, protein homeostasis, and cancer. Chinese Journal
of Cancer, 30(2), 124–137.
105. Verma, R., McDonald, H., Yates, J. R. 3rd, Deshaies, R. J. (2001). Selective degradation
of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk. Molecular
Cell, 8(2), 439–448.
106. Verrier, F., Mignotte, B., Jan, G., Brenner, C. (2003). Study of PTPC composition during
apoptosis for identification of viral protein target. Annals of the New York Academy of
Sciences, 1010, 126–142.
107. Vizlin-Hodzic, D., Johansson, H., Ryme, J., Simonsson, T., Simonsson, S. (2011). SAFA has a role in transcriptional regulation of Oct4 in ES cells through promoter binding.
Cellular Reprogramming, 13(1), 13–27. https://doi.org/10.1089/cell.2010.0075
108. Wang, H., Ding, N., Guo, J., Xia, J., Ruan, Y. (2016). Dysregulation of TTP and HuR
plays an important role in cancers. Tumour Biology : The Journal of the International Society
for Oncodevelopmental Biology and Medicine, 37(11), 14451–14461.
https://doi.org/10.1007/s13277-016-5397-z
109. Watanabe, M., Furuno, N., Goebl, M., Go, M., Miyauchi, K., Sekiguchi, T., Nishimito, T.
(1991). Molecular cloning of the human gene, CCG2, that complements the BHK-derived
temperature-sensitive cell cycle mutant tsBN63: identity of CCG2 with the human X
chromosomal SCAR/RPS4X gene. Journal of Cell Science, 100 ( Pt 1, 35–43.
110. Willenbacher, E., Balog, A., Willenbacher, W. (2018). Short overview on the current
standard of treatment in newly diagnosed multiple myeloma. Memo, 11(1), 59–64.
https://doi.org/10.1007/s12254-018-0383-3
111. Yadavilli, S., Mayo, L. D., Higgins, M., Lain, S., Hegde, V., Deutsch, W. A. (2009).
Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2
through its KH domain. DNA Repair, 8(10), 1215–1224.
https://doi.org/10.1016/j.dnarep.2009.07.003112. Yamamoto, T., Kosaka, N., Hattori, Y., Ochiya, T. (2018). A Challenge to Aging Society
by microRNA in Extracellular Vesicles: microRNA in Extracellular Vesicles as Promising
Biomarkers and Novel Therapeutic Targets in Multiple Myeloma. Journal of Clinical
Medicine, 7(3). https://doi.org/10.3390/jcm7030055
113. Zaiss, D. M. W., Standera, S., Kloetzel, P.-M., Sijts, A. J. A. M. (2002). PI31 is a
modulator of proteasome formation and antigen processing. Proceedings of the National
Academy of Sciences of the United States of America, 99(22), 14344–14349.
https://doi.org/10.1073/pnas.212257299
114. Zhou, R., Shanas, R., Nelson, M. A., Bhattacharyya, A., Shi, J. (2010). Increased
expression of the heterogeneous nuclear ribonucleoprotein K in pancreatic cancer and its
association with the mutant p53. International Journal of Cancer, 126(2), 395–404.
https://doi.org/10.1002/ijc.24744
115. Zhou, X., Liao, W.-J., Liao, J.-M., Liao, P., Lu, H. (2015). Ribosomal proteins: functions
beyond the ribosome. Journal of Molecular Cell Biology, 7(2), 92–104.
https://doi.org/10.1093/jmcb/mjv014
116. Zhu, N., Zheng, S., Xu, R., Yu, R. (2003). [Overexpression of S3 ribosomal protein gene
is involved in drug resistance in K562/DOX cells]. Zhonghua xue ye xue za zhi = Zhonghua
xueyexue zazhi, 24(3), 141–143
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