RELA

RELA
Factor de transcripción p65
Protein RELA PDB 1bft.png
Estructura tridimensional de la proteína RELA.
HUGO 9955
Símbolo RELA
Símbolos alt. MGC131774; NFKB3
Datos genéticos
Locus Cr. 11 q13.1
Bases de datos
Entrez 5970
OMIM 164014
PDB 1bft
RefSeq NP_068810
UniProt Q04206

El factor de transcripción p65 (RELA) es una proteína codificada en humanos por el gen RELA.[1]

NFKB1 o NFKB2 se unen a REL, RELA o RELB para formar el complejo NFKB. El heterodímero p50/p65 (NFKB1/RELA) es la forma más abundante de complejo NFKB. Este complejo es inhibido por proteínas IκB (NFKBIA o NFKBIB), que inactivan a NFKB secuestrándolo y reteniéndolo en el citoplasma. La fosforilación de los residuos de serina de las proteínas IκB mediante la acción de quinasas como IKBKA o IKBKB, las marca para ser degradadas por una ruta de ubiquitinación, permitiendo la activación del complejo NFKB. El complejo NFKB activado se trasloca al núcleo celular y se une al ADN en motivos de unión kappa-B, tales como las secuencias de nucleótidos 5'-GGGRNNYYCC-3' ó 5'-HGGARNYYCC-3' (donde H es A, C o T; R es una purina, A o G; Y es una pirimidina, C o T).[2]

Interacciones

La proteína RELA ha demostrado ser capaz de interaccionar con:

Referencias

  1. ↑ Nolan GP, Ghosh S, Liou HC, Tempst P, Baltimore D (Apr 1991). «DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-kappa B, a rel-related polypeptide». Cell 64 (5):  pp. 961–9. PMID 2001591. 
  2. ↑ «Entrez Gene: RELA v-rel reticuloendotheliosis viral oncogene homolog A, nuclear factor of kappa light polypeptide gene enhancer in B-cells 3, p65 (avian)».
  3. ↑ Chen, Yi; Wu Joann, Ghosh Gourisankar (Jun. 2003). «KappaB-Ras binds to the unique insert within the ankyrin repeat domain of IkappaBbeta and regulates cytoplasmic retention of IkappaBbeta x NF-kappaB complexes». J. Biol. Chem. (United States) 278 (25):  pp. 23101–6. doi:10.1074/jbc.M301021200. ISSN 0021-9258. PMID 12672800. 
  4. ↑ Suyang, H; Phillips R, Douglas I, Ghosh S (Oct. 1996). «Role of unphosphorylated, newly synthesized I kappa B beta in persistent activation of NF-kappa B». Mol. Cell. Biol. (UNITED STATES) 16 (10):  pp. 5444–9. ISSN 0270-7306. PMID 8816457. 
  5. ↑ Higashitsuji, Hisako; Higashitsuji Hiroaki, Nagao Toshikazu, Nonoguchi Kohsuke, Fujii Shingo, Itoh Katsuhiko, Fujita Jun (Oct. 2002). «A novel protein overexpressed in hepatoma accelerates export of NF-kappa B from the nucleus and inhibits p53-dependent apoptosis». Cancer Cell (United States) 2 (4):  pp. 335–46. ISSN 1535-6108. PMID 12398897. 
  6. ↑ Li, Z; Nabel G J (Oct. 1997). «A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription». Mol. Cell. Biol. (UNITED STATES) 17 (10):  pp. 6184–90. ISSN 0270-7306. PMID 9315679. 
  7. ↑ Anderson, Lisa A; Perkins Neil D (Jan. 2003). «Regulation of RelA (p65) function by the large subunit of replication factor C». Mol. Cell. Biol. (United States) 23 (2):  pp. 721–32. ISSN 0270-7306. PMID 12509469. 
  8. ↑ Wu, Min; Xu Liang-Guo, Zhai Zhonghe, Shu Hong-Bing (Jul. 2003). «SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription». J. Biol. Chem. (United States) 278 (29):  pp. 27072–9. doi:10.1074/jbc.M209814200. ISSN 0021-9258. PMID 12736262. 
  9. ↑ a b Jang, Hyun Duk; Yoon Kwiyeom, Shin Young Joo, Kim Jaesang, Lee Soo Young (Jun. 2004). «PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit». J. Biol. Chem. (United States) 279 (23):  pp. 24873–80. doi:10.1074/jbc.M313018200. ISSN 0021-9258. PMID 15140884. 
  10. ↑ a b Zhong, Haihong; May Michael J, Jimi Eijiro, Ghosh Sankar (Mar. 2002). «The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1». Mol. Cell (United States) 9 (3):  pp. 625–36. ISSN 1097-2765. PMID 11931769. 
  11. ↑ Parry, G C; Mackman N (Dec. 1997). «Role of cyclic AMP response element-binding protein in cyclic AMP inhibition of NF-kappaB-mediated transcription». J. Immunol. (UNITED STATES) 159 (11):  pp. 5450–6. ISSN 0022-1767. PMID 9548485. 
  12. ↑ Aarnisalo, P; Palvimo J J, Jänne O A (Mar. 1998). «CREB-binding protein in androgen receptor-mediated signaling». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (5):  pp. 2122–7. ISSN 0027-8424. PMID 9482849. 
  13. ↑ a b Gerritsen, M E; Williams A J, Neish A S, Moore S, Shi Y, Collins T (Apr. 1997). «CREB-binding protein/p300 are transcriptional coactivators of p65». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (7):  pp. 2927–32. ISSN 0027-8424. PMID 9096323. 
  14. ↑ Gu, Ying; Xu You Cheng, Wu Ru Feng, Nwariaku Fiemu E, Souza Rhonda F, Flores Sonia C, Terada Lance S (May. 2003). «p47phox participates in activation of RelA in endothelial cells». J. Biol. Chem. (United States) 278 (19):  pp. 17210–7. doi:10.1074/jbc.M210314200. ISSN 0021-9258. PMID 12618429. 
  15. ↑ Ray, A; Prefontaine K E (Jan. 1994). «Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 91 (2):  pp. 752–6. ISSN 0027-8424. PMID 8290595. 
  16. ↑ Nissen, R M; Yamamoto K R (Sep. 2000). «The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain». Genes Dev. (UNITED STATES) 14 (18):  pp. 2314–29. ISSN 0890-9369. PMID 10995388. 
  17. ↑ Caldenhoven, E; Liden J, Wissink S, Van de Stolpe A, Raaijmakers J, Koenderman L, Okret S, Gustafsson J A, Van der Saag P T (Apr. 1995). «Negative cross-talk between RelA and the glucocorticoid receptor: a possible mechanism for the antiinflammatory action of glucocorticoids». Mol. Endocrinol. (UNITED STATES) 9 (4):  pp. 401–12. ISSN 0888-8809. PMID 7659084. 
  18. ↑ Knuefermann, Pascal; Chen Peter, Misra Arunima, Shi Shu-Ping, Abdellatif Maha, Sivasubramanian Natarajan (Jun. 2002). «Myotrophin/V-1, a protein up-regulated in the failing human heart and in postnatal cerebellum, converts NFkappa B p50-p65 heterodimers to p50-p50 and p65-p65 homodimers». J. Biol. Chem. (United States) 277 (26):  pp. 23888–97. doi:10.1074/jbc.M202937200. ISSN 0021-9258. PMID 11971907. 
  19. ↑ Benezra, Miriam; Chevallier Nathalie, Morrison Debra J, MacLachlan Timothy K, El-Deiry Wafik S, Licht Jonathan D (Jul. 2003). «BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit». J. Biol. Chem. (United States) 278 (29):  pp. 26333–41. doi:10.1074/jbc.M303076200. ISSN 0021-9258. PMID 12700228. 
  20. ↑ a b Yang, X; Chen Y, Gabuzda D (Sep. 1999). «ERK MAP kinase links cytokine signals to activation of latent HIV-1 infection by stimulating a cooperative interaction of AP-1 and NF-kappaB». J. Biol. Chem. (UNITED STATES) 274 (39):  pp. 27981–8. ISSN 0021-9258. PMID 10488148. 
  21. ↑ van Heel, David A; Udalova Irina A, De Silva Arjuna P, McGovern Dermot P, Kinouchi Yoshitaka, Hull Jeremy, Lench Nicholas J, Cardon Lon R, Carey Alisoun H, Jewell Derek P, Kwiatkowski Dominic (May. 2002). «Inflammatory bowel disease is associated with a TNF polymorphism that affects an interaction between the OCT1 and NF(-kappa)B transcription factors». Hum. Mol. Genet. (England) 11 (11):  pp. 1281–9. ISSN 0964-6906. PMID 12019209. 
  22. ↑ a b Spencer, E; Jiang J, Chen Z J (Feb. 1999). «Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP». Genes Dev. (UNITED STATES) 13 (3):  pp. 284–94. ISSN 0890-9369. PMID 9990853. 
  23. ↑ Guermah, M; Malik S, Roeder R G (Jun. 1998). «Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1». Mol. Cell. Biol. (UNITED STATES) 18 (6):  pp. 3234–44. ISSN 0270-7306. PMID 9584164. 
  24. ↑ Schmitz, M L; Stelzer G, Altmann H, Meisterernst M, Baeuerle P A (Mar. 1995). «Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators». J. Biol. Chem. (UNITED STATES) 270 (13):  pp. 7219–26. ISSN 0021-9258. PMID 7706261. 
  25. ↑ a b Chen Lf; Fischle W, Verdin E, Greene W C (Aug. 2001). «Duration of nuclear NF-kappaB action regulated by reversible acetylation». Science (United States) 293 (5535):  pp. 1653–7. doi:10.1126/science.1062374. ISSN 0036-8075. PMID 11533489. 
  26. ↑ a b c d Kiernan, Rosemary; Brès Vanessa, Ng Raymond W M, Coudart Marie-Pierre, El Messaoudi Selma, Sardet Claude, Jin Dong-Yan, Emiliani Stephane, Benkirane Monsef (Jan. 2003). «Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65». J. Biol. Chem. (United States) 278 (4):  pp. 2758–66. doi:10.1074/jbc.M209572200. ISSN 0021-9258. PMID 12419806. 
  27. ↑ Hay, D C; Kemp G D, Dargemont C, Hay R T (May. 2001). «Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription». Mol. Cell. Biol. (United States) 21 (10):  pp. 3482–90. doi:10.1128/MCB.21.10.3482-3490.2001. ISSN 0270-7306. PMID 11313474. 
  28. ↑ a b Hansen, S K; Baeuerle P A, Blasi F (Apr. 1994). «Purification, reconstitution, and I kappa B association of the c-Rel-p65 (RelA) complex, a strong activator of transcription». Mol. Cell. Biol. (UNITED STATES) 14 (4):  pp. 2593–603. ISSN 0270-7306. PMID 8139561. 
  29. ↑ Malek, S; Huxford T, Ghosh G (Sep. 1998). «Ikappa Balpha functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-kappaB». J. Biol. Chem. (UNITED STATES) 273 (39):  pp. 25427–35. ISSN 0021-9258. PMID 9738011. 
  30. ↑ Cohen, L; Henzel W J, Baeuerle P A (Sep. 1998). «IKAP is a scaffold protein of the IkappaB kinase complex». Nature (ENGLAND) 395 (6699):  pp. 292–6. doi:10.1038/26254. ISSN 0028-0836. PMID 9751044. 
  31. ↑ a b c Bouwmeester, Tewis; Bauch Angela, Ruffner Heinz, Angrand Pierre-Olivier, Bergamini Giovanna, Croughton Karen, Cruciat Cristina, Eberhard Dirk, Gagneur Julien, Ghidelli Sonja, Hopf Carsten, Huhse Bettina, Mangano Raffaella, Michon Anne-Marie, Schirle Markus, Schlegl Judith, Schwab Markus, Stein Martin A, Bauer Andreas, Casari Georg, Drewes Gerard, Gavin Anne-Claude, Jackson David B, Joberty Gerard, Neubauer Gitte, Rick Jens, Kuster Bernhard, Superti-Furga Giulio (Feb. 2004). «A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway». Nat. Cell Biol. (England) 6 (2):  pp. 97–105. doi:10.1038/ncb1086. ISSN 1465-7392. PMID 14755267. 
  32. ↑ Scheinman, R I; Beg A A, Baldwin A S (Oct. 1993). «NF-kappa B p100 (Lyt-10) is a component of H2TF1 and can function as an I kappa B-like molecule». Mol. Cell. Biol. (UNITED STATES) 13 (10):  pp. 6089–101. ISSN 0270-7306. PMID 8413211. 
  33. ↑ Palvimo, J J; Reinikainen P, Ikonen T, Kallio P J, Moilanen A, Jänne O A (Sep. 1996). «Mutual transcriptional interference between RelA and androgen receptor». J. Biol. Chem. (UNITED STATES) 271 (39):  pp. 24151–6. ISSN 0021-9258. PMID 8798655. 
  34. ↑ Espinosa, Lluís; Inglés-Esteve Julia, Robert-Moreno Alex, Bigas Anna (Feb. 2003). «IkappaBalpha and p65 regulate the cytoplasmic shuttling of nuclear corepressors: cross-talk between Notch and NFkappaB pathways». Mol. Biol. Cell (United States) 14 (2):  pp. 491–502. doi:10.1091/mbc.E02-07-0404. ISSN 1059-1524. PMID 12589049. 
  35. ↑ Lee, S K; Kim J H, Lee Y C, Cheong J, Lee J W (Apr. 2000). «Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor». J. Biol. Chem. (UNITED STATES) 275 (17):  pp. 12470–4. ISSN 0021-9258. PMID 10777532. 
  36. ↑ Kim, D W; Gazourian L, Quadri S A, Romieu-Mourez R, Sherr D H, Sonenshein G E (Nov. 2000). «The RelA NF-kappaB subunit and the aryl hydrocarbon receptor (AhR) cooperate to transactivate the c-myc promoter in mammary cells». Oncogene (England) 19 (48):  pp. 5498–506. doi:10.1038/sj.onc.1203945. ISSN 0950-9232. PMID 11114727. 
  37. ↑ Ruby, Carl E; Leid Mark, Kerkvliet Nancy I (Sep. 2002). «2,3,7,8-Tetrachlorodibenzo-p-dioxin suppresses tumor necrosis factor-alpha and anti-CD40-induced activation of NF-kappaB/Rel in dendritic cells: p50 homodimer activation is not affected». Mol. Pharmacol. (United States) 62 (3):  pp. 722–8. ISSN 0026-895X. PMID 12181450. 
  38. ↑ Weber, Marion; Sydlik Carmen, Quirling Martina, Nothdurfter Caroline, Zwergal Andreas, Heiss Peter, Bell Susanne, Neumeier Dieter, Ziegler-Heitbrock H W Loms, Brand Korbinian (Jun. 2003). «Transcriptional inhibition of interleukin-8 expression in tumor necrosis factor-tolerant cells: evidence for involvement of C/EBP beta». J. Biol. Chem. (United States) 278 (26):  pp. 23586–93. doi:10.1074/jbc.M211646200. ISSN 0021-9258. PMID 12707271. 
  39. ↑ Xia, C; Cheshire J K, Patel H, Woo P (Dec. 1997). «Cross-talk between transcription factors NF-kappa B and C/EBP in the transcriptional regulation of genes». Int. J. Biochem. Cell Biol. (ENGLAND) 29 (12):  pp. 1525–39. ISSN 1357-2725. PMID 9570146. 
  40. ↑ Tetsuka, Toshifumi; Uranishi Hiroaki, Sanda Takaomi, Asamitsu Kaori, Yang Jiang-Ping, Wong-Staal Flossie, Okamoto Takashi (Sep. 2004). «RNA helicase A interacts with nuclear factor kappaB p65 and functions as a transcriptional coactivator». Eur. J. Biochem. (Germany) 271 (18):  pp. 3741–51. doi:10.1111/j.1432-1033.2004.04314.x. ISSN 0014-2956. PMID 15355351. 
  41. ↑ Hassa, P O; Covic M, Hasan S, Imhof R, Hottiger M O (Dec. 2001). «The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function». J. Biol. Chem. (United States) 276 (49):  pp. 45588–97. doi:10.1074/jbc.M106528200. ISSN 0021-9258. PMID 11590148. 
  42. ↑ Jung, Dong-Ju; Sung Hee-Sook, Goo Young-Wha, Lee Hyun Mi, Park Ok Ku, Jung Sung-Yun, Lim Janghoo, Kim Han-Jong, Lee Soo-Kyung, Kim Tae Sung, Lee Jae Woon, Lee Young Chul (Jul. 2002). «Novel transcription coactivator complex containing activating signal cointegrator 1». Mol. Cell. Biol. (United States) 22 (14):  pp. 5203–11. ISSN 0270-7306. PMID 12077347. 
  43. ↑ Ashburner, B P; Westerheide S D, Baldwin A S (Oct. 2001). «The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression». Mol. Cell. Biol. (United States) 21 (20):  pp. 7065–77. doi:10.1128/MCB.21.20.7065-7077.2001. ISSN 0270-7306. PMID 11564889. 
  44. ↑ a b Wang, D; Westerheide S D, Hanson J L, Baldwin A S (Oct. 2000). «Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II». J. Biol. Chem. (UNITED STATES) 275 (42):  pp. 32592–7. doi:10.1074/jbc.M001358200. ISSN 0021-9258. PMID 10938077. 
  45. ↑ Yu, Zhiyuan; Zhang Wenzheng, Kone Bruce C (Aug. 2002). «Histone deacetylases augment cytokine induction of the iNOS gene». J. Am. Soc. Nephrol. (United States) 13 (8):  pp. 2009–17. ISSN 1046-6673. PMID 12138131. 
  46. ↑ Leitges, M; Sanz L, Martin P, Duran A, Braun U, García J F, Camacho F, Diaz-Meco M T, Rennert P D, Moscat J (Oct. 2001). «Targeted disruption of the zetaPKC gene results in the impairment of the NF-kappaB pathway». Mol. Cell (United States) 8 (4):  pp. 771–80. ISSN 1097-2765. PMID 11684013. 
  47. ↑ Yu, Zhiyuan; Zhang Wenzheng, Kone Bruce C (Oct. 2002). «Signal transducers and activators of transcription 3 (STAT3) inhibits transcription of the inducible nitric oxide synthase gene by interacting with nuclear factor kappaB». Biochem. J. (England) 367 (Pt 1):  pp. 97–105. doi:10.1042/BJ20020588. ISSN 0264-6021. PMID 12057007. 
  48. ↑ Asamitsu, Kaori; Tetsuka Toshifumi, Kanazawa Satoshi, Okamoto Takashi (Jul. 2003). «RING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunit». J. Biol. Chem. (United States) 278 (29):  pp. 26879–87. doi:10.1074/jbc.M211831200. ISSN 0021-9258. PMID 12748188. 
  49. ↑ Kuang, Ping-Ping; Berk John L, Rishikof David C, Foster Judith A, Humphries Donald E, Ricupero Dennis A, Goldstein Ronald H (Jul. 2002). «NF-kappaB induced by IL-1beta inhibits elastin transcription and myofibroblast phenotype». Am. J. Physiol., Cell Physiol. (United States) 283 (1):  pp. C58-65. doi:10.1152/ajpcell.00314.2001. ISSN 0363-6143. PMID 12055073. 
  50. ↑ Sif, S; Gilmore T D (Nov. 1994). «Interaction of the v-Rel oncoprotein with cellular transcription factor Sp1». J. Virol. (UNITED STATES) 68 (11):  pp. 7131–8. ISSN 0022-538X. PMID 7933095. 
  51. ↑ Amini, Shohreh; Clavo Anaira, Nadraga Yuri, Giordano Antonio, Khalili Kamel, Sawaya Bassel E (Aug. 2002). «Interplay between cdk9 and NF-kappaB factors determines the level of HIV-1 gene transcription in astrocytic cells». Oncogene (England) 21 (37):  pp. 5797–803. doi:10.1038/sj.onc.1205754. ISSN 0950-9232. PMID 12173051. 
  52. ↑ Yamit-Hezi, A; Dikstein R (Sep. 1998). «TAFII105 mediates activation of anti-apoptotic genes by NF-kappaB». EMBO J. (ENGLAND) 17 (17):  pp. 5161–9. doi:10.1093/emboj/17.17.5161. ISSN 0261-4189. PMID 9724652. 
  53. ↑ Heppner, C; Bilimoria K Y, Agarwal S K, Kester M, Whitty L J, Guru S C, Chandrasekharappa S C, Collins F S, Spiegel A M, Marx S J, Burns A L (Aug. 2001). «The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation». Oncogene (England) 20 (36):  pp. 4917–25. doi:10.1038/sj.onc.1204529. ISSN 0950-9232. PMID 11526476. 
  54. ↑ Yang, J P; Hori M, Sanda T, Okamoto T (May. 1999). «Identification of a novel inhibitor of nuclear factor-kappaB, RelA-associated inhibitor». J. Biol. Chem. (UNITED STATES) 274 (22):  pp. 15662–70. ISSN 0021-9258. PMID 10336463. 
  55. ↑ Takada, Norio; Sanda Takaomi, Okamoto Hiroshi, Yang Jian-Ping, Asamitsu Kaori, Sarol Lilen, Kimura Genjiro, Uranishi Hiroaki, Tetsuka Toshifumi, Okamoto Takashi (Aug. 2002). «RelA-associated inhibitor blocks transcription of human immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1 actions». J. Virol. (United States) 76 (16):  pp. 8019–30. ISSN 0022-538X. PMID 12134007. 
  56. ↑ Tomita, S; Fujita T, Kirino Y, Suzuki T (Apr. 2000). «PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein». J. Biol. Chem. (UNITED STATES) 275 (17):  pp. 13056–60. ISSN 0021-9258. PMID 10777610. 
  57. ↑ Liss, Andrew S; Bose Henry R (May. 2002). «Mutational analysis of the v-Rel dimerization interface reveals a critical role for v-Rel homodimers in transformation». J. Virol. (United States) 76 (10):  pp. 4928–39. ISSN 0022-538X. PMID 11967310. 
  58. ↑ Garkavtsev, Igor; Kozin Sergey V, Chernova Olga, Xu Lei, Winkler Frank, Brown Edward, Barnett Gene H, Jain Rakesh K (Mar. 2004). «The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis». Nature (England) 428 (6980):  pp. 328–32. doi:10.1038/nature02329. PMID 15029197. 
  59. ↑ Uranishi, H; Tetsuka T, Yamashita M, Asamitsu K, Shimizu M, Itoh M, Okamoto T (Apr. 2001). «Involvement of the pro-oncoprotein TLS (translocated in liposarcoma) in nuclear factor-kappa B p65-mediated transcription as a coactivator». J. Biol. Chem. (United States) 276 (16):  pp. 13395–401. doi:10.1074/jbc.M011176200. ISSN 0021-9258. PMID 11278855. 

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