Abl gene

C-abl oncogene 1, non-receptor tyrosine kinase

PDB rendering based on 1ab2.
Identifiers
Symbols ABL1; ABL; JTK7; bcr/abl; c-ABL; p150; v-abl
External IDs OMIM: 189980 MGI: 87859 HomoloGene: 3783 GeneCards: ABL1 Gene
EC number 2.7.10.2
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 25 11350
Ensembl ENSG00000097007 ENSMUSG00000026842
UniProt P00519 Q3SYK5
RefSeq (mRNA) NM_005157.4 NM_009594
RefSeq (protein) NP_005148.2 NP_033724
Location (UCSC) Chr 9:
133.59 – 133.76 Mb		 Chr 2:
31.54 – 31.66 Mb
PubMed search [1] [2]

V-abl Abelson murine leukemia viral oncogene homolog 1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene located on chromosome 9.[1]

Contents

Function

The ABL1 proto-oncogene encodes a cytoplasmic and nuclear protein tyrosine kinase that has been implicated in processes of cell differentiation, cell division, cell adhesion, and stress response. Activity of ABL1 protein is negatively regulated by its SH3 domain, and deletion of the SH3 domain turns ABL1 into an oncogene. The t(9;22) translocation results in the head-to-tail fusion of the BCR and ABL1 genes, leading to a fusion gene present in many cases of chronic myelogenous leukemia. The DNA-binding activity of the ubiquitously expressed ABL1 tyrosine kinase is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function for ABL1. The ABL1 gene is expressed as either a 6- or a 7-kb mRNA transcript, with alternatively spliced first exons spliced to the common exons 2-11.[2]

Clinical significance

Mutations in the ABL1 gene are associated with chronic myelogenous leukemia (CML). In CML, the gene is activated by being translocated within the BCR (breakpoint cluster region) gene on chromosome 22. This new fusion gene, BCR-ABL, encodes an unregulated, cytoplasm-targeted tyrosine kinase that allows the cells to proliferate without being regulated by cytokines. This, in turn, allows the cell to become cancerous.

This gene is a partner in a fusion gene with the BCR gene in the Philadelphia chromosome, a characteristic abnormality in chronic myelogenous leukemia (CML) and rarely in some other leukemia forms. The BCR-ABL transcript encodes a tyrosine kinase, which activates mediators of the cell cycle regulation system, leading to a clonal myeloproliferative disorder. The BCR-ABL protein can be inhibited by various small molecules. One such inhibitor is imatinib mesylate, which occupies the tyrosine kinase domain and inhibits BCR-ABL's influence on the cell cycle. Second generation BCR-ABL tyrosine-kinase inhibitors are also under development to inhibit BCR-ABL mutants resistant to imatinib.

Interactions

Abl gene has been shown to interact with RAD9A,[3] YTHDC1,[4] TrkA,[5][6] NCK1,[7][8] Retinoblastoma protein,[9][10] RAD51,[11] Catalase,[12] PSTPIP1,[13] ABI2,[14][15] DOK1,[16][17] ABL2,[14] PAG1,[18] BRCA1,[19] BCAR1,[20][21] NEDD9,[22][23] CRKL,[8][24][25] PAK2,[26] SORBS2,[27][28] Mdm2,[29] SHC1,[30][31] Ataxia telangiectasia mutated,[11][32][33] EPH receptor B2,[34] GRB10,[35][36] Spectrin, alpha 1,[37] SPTAN1,[37] Grb2,[8][38] TERF1,[33] VAV1,[39] RYBP,[40] Mammalian target of rapamycin,[41] BCR gene,[31][42][43] Cbl gene,[7][28] P73,[44][45] GPX1,[46] RFX1[47] and ABI1.[48][49][50]

Regulation

There is some evidence that the expression of Abl is regulated by the microRNA miR-203.[51]

See also

References

  1. ^ Szczylik C, Skorski T, Nicolaides NC, Manzella L, Malaguarnera L, Venturelli D, Gewirtz AM, Calabretta B (August 1991). "Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides". Science 253 (5019): 562–5. doi:10.1126/science.1857987. PMID 1857987. 
  2. ^ "Entrez Gene: ABL1 v-abl Abelson murine leukemia viral oncogene homolog 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25. 
  3. ^ Yoshida, Kiyotsugu; Komatsu Kiyoshi, Wang Hong-Gang, Kufe Donald (May. 2002). "c-Abl Tyrosine Kinase Regulates the Human Rad9 Checkpoint Protein in Response to DNA Damage". Mol. Cell. Biol. (United States) 22 (10): 3292–300. doi:10.1128/MCB.22.10.3292-3300.2002. ISSN 0270-7306. PMC 133797. PMID 11971963. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133797. 
  4. ^ Rafalska, Ilona; Zhang Zhaiyi, Benderska Natalya, Wolff Horst, Hartmann Annette M, Brack-Werner Ruth, Stamm Stefan (Aug. 2004). "The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation". Hum. Mol. Genet. (England) 13 (15): 1535–49. doi:10.1093/hmg/ddh167. ISSN 0964-6906. PMID 15175272. 
  5. ^ Koch, A; Mancini A, Stefan M, Niedenthal R, Niemann H, Tamura T (Mar. 2000). "Direct interaction of nerve growth factor receptor, TrkA, with non-receptor tyrosine kinase, c-Abl, through the activation loop". FEBS Lett. (NETHERLANDS) 469 (1): 72–6. doi:10.1016/S0014-5793(00)01242-4. ISSN 0014-5793. PMID 10708759. 
  6. ^ Yano, H; Cong F, Birge R B, Goff S P, Chao M V (Feb. 2000). "Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor". J. Neurosci. Res. (UNITED STATES) 59 (3): 356–64. doi:10.1002/(SICI)1097-4547(20000201)59:3<356::AID-JNR9>3.0.CO;2-G. ISSN 0360-4012. PMID 10679771. 
  7. ^ a b Miyoshi-Akiyama, T; Aleman L M, Smith J M, Adler C E, Mayer B J (Jul. 2001). "Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor". Oncogene (England) 20 (30): 4058–69. doi:10.1038/sj.onc.1204528. ISSN 0950-9232. PMID 11494134. 
  8. ^ a b c Ren, R; Ye Z S, Baltimore D (Apr. 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes Dev. (UNITED STATES) 8 (7): 783–95. doi:10.1101/gad.8.7.783. ISSN 0890-9369. PMID 7926767. 
  9. ^ Miyamura, T; Nishimura J, Yufu Y, Nawata H (Feb. 1997). "Interaction of BCR-ABL with the retinoblastoma protein in Philadelphia chromosome-positive cell lines". Int. J. Hematol. (IRELAND) 65 (2): 115–21. doi:10.1016/S0925-5710(96)00539-7. ISSN 0925-5710. PMID 9071815. 
  10. ^ Welch, P J; Wang J Y (Nov. 1993). "A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle". Cell (UNITED STATES) 75 (4): 779–90. doi:10.1016/0092-8674(93)90497-E. ISSN 0092-8674. PMID 8242749. 
  11. ^ a b Chen, G; Yuan S S, Liu W, Xu Y, Trujillo K, Song B, Cong F, Goff S P, Wu Y, Arlinghaus R, Baltimore D, Gasser P J, Park M S, Sung P, Lee E Y (Apr. 1999). "Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl". J. Biol. Chem. (UNITED STATES) 274 (18): 12748–52. doi:10.1074/jbc.274.18.12748. ISSN 0021-9258. PMID 10212258. 
  12. ^ Cao, Cheng; Leng Yumei, Kufe Donald (Aug. 2003). "Catalase activity is regulated by c-Abl and Arg in the oxidative stress response". J. Biol. Chem. (United States) 278 (32): 29667–75. doi:10.1074/jbc.M301292200. ISSN 0021-9258. PMID 12777400. 
  13. ^ Cong, F; Spencer S, Côté J F, Wu Y, Tremblay M L, Lasky L A, Goff S P (Dec. 2000). "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation". Mol. Cell (United States) 6 (6): 1413–23. doi:10.1016/S1097-2765(00)00138-6. ISSN 1097-2765. PMID 11163214. 
  14. ^ a b Cao, Cheng; Leng Yumei, Li Chufang, Kufe Donald (Apr. 2003). "Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response". J. Biol. Chem. (United States) 278 (15): 12961–7. doi:10.1074/jbc.M300058200. ISSN 0021-9258. PMID 12569093. 
  15. ^ Dai, Z; Pendergast A M (Nov. 1995). "Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity". Genes Dev. (UNITED STATES) 9 (21): 2569–82. doi:10.1101/gad.9.21.2569. ISSN 0890-9369. PMID 7590236. 
  16. ^ van Dijk, T B; van Den Akker E, Amelsvoort M P, Mano H, Löwenberg B, von Lindern M (Nov. 2000). "Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells". Blood (UNITED STATES) 96 (10): 3406–13. ISSN 0006-4971. PMID 11071635. 
  17. ^ Yamanashi, Y; Baltimore D (Jan. 1997). "Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok". Cell (UNITED STATES) 88 (2): 205–11. doi:10.1016/S0092-8674(00)81841-3. ISSN 0092-8674. PMID 9008161. 
  18. ^ Wen, S T; Van Etten R A (Oct. 1997). "The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity". Genes Dev. (UNITED STATES) 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. ISSN 0890-9369. PMC 316562. PMID 9334312. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316562. 
  19. ^ Foray, Nicolas; Marot Didier, Randrianarison Voahangy, Venezia Nicole Dalla, Picard Didier, Perricaudet Michel, Favaudon Vincent, Jeggo Penny (Jun. 2002). "Constitutive Association of BRCA1 and c-Abl and Its ATM-Dependent Disruption after Irradiation". Mol. Cell. Biol. (United States) 22 (12): 4020–32. doi:10.1128/MCB.22.12.4020-4032.2002. ISSN 0270-7306. PMC 133860. PMID 12024016. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133860. 
  20. ^ Salgia, R; Pisick E, Sattler M, Li J L, Uemura N, Wong W K, Burky S A, Hirai H, Chen L B, Griffin J D (Oct. 1996). "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". J. Biol. Chem. (UNITED STATES) 271 (41): 25198–203. doi:10.1074/jbc.271.41.25198. ISSN 0021-9258. PMID 8810278. 
  21. ^ Mayer, B J; Hirai H, Sakai R (Mar. 1995). "Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases". Curr. Biol. (ENGLAND) 5 (3): 296–305. doi:10.1016/S0960-9822(95)00060-1. ISSN 0960-9822. PMID 7780740. 
  22. ^ Minegishi, M; Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (Oct. 1996). "Structure and function of Cas-L, a 105-kD Crk-associated substrate- related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes". J. Exp. Med. (UNITED STATES) 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. ISSN 0022-1007. PMC 2192828. PMID 8879209. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2192828. 
  23. ^ Law, S F; Estojak J, Wang B, Mysliwiec T, Kruh G, Golemis E A (Jul. 1996). "Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae". Mol. Cell. Biol. (UNITED STATES) 16 (7): 3327–37. ISSN 0270-7306. PMC 231327. PMID 8668148. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231327. 
  24. ^ Heaney, C; Kolibaba K, Bhat A, Oda T, Ohno S, Fanning S, Druker B J (Jan. 1997). "Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation". Blood (UNITED STATES) 89 (1): 297–306. ISSN 0006-4971. PMID 8978305. 
  25. ^ Kyono, W T; de Jong R, Park R K, Liu Y, Heisterkamp N, Groffen J, Durden D L (Nov. 1998). "Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI)". J. Immunol. (UNITED STATES) 161 (10): 5555–63. ISSN 0022-1767. PMID 9820532. 
  26. ^ Roig, J; Tuazon P T, Zipfel P A, Pendergast A M, Traugh J A (Dec. 2000). "Functional interaction between c-Abl and the p21-activated protein kinase γ-PAK". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (26): 14346–51. doi:10.1073/pnas.97.26.14346. ISSN 0027-8424. PMC 18921. PMID 11121037. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18921. 
  27. ^ Wang, B; Golemis E A, Kruh G D (Jul. 1997). "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks". J. Biol. Chem. (UNITED STATES) 272 (28): 17542–50. doi:10.1074/jbc.272.28.17542. ISSN 0021-9258. PMID 9211900. 
  28. ^ a b Soubeyran, Philippe; Barac Ana, Szymkiewicz Iwona, Dikic Ivan (Feb. 2003). "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl". Biochem. J. (England) 370 (Pt 1): 29–34. doi:10.1042/BJ20021539. ISSN 0264-6021. PMC 1223168. PMID 12475393. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223168. 
  29. ^ Goldberg, Zehavit; Vogt Sionov Ronit, Berger Michael, Zwang Yaara, Perets Ruth, Van Etten Richard A, Oren Moshe, Taya Yoichi, Haupt Ygal (Jul. 2002). "Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation". EMBO J. (England) 21 (14): 3715–27. doi:10.1093/emboj/cdf384. ISSN 0261-4189. PMC 125401. PMID 12110584. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125401. 
  30. ^ Wisniewski, D; Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh W M, Tempst P, Clarkson B (Apr. 1999). "A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells". Blood (UNITED STATES) 93 (8): 2707–20. ISSN 0006-4971. PMID 10194451. 
  31. ^ a b Puil, L; Liu J, Gish G, Mbamalu G, Bowtell D, Pelicci P G, Arlinghaus R, Pawson T (Feb. 1994). "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". EMBO J. (ENGLAND) 13 (4): 764–73. ISSN 0261-4189. PMC 394874. PMID 8112292. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=394874. 
  32. ^ Shafman, T; Khanna K K, Kedar P, Spring K, Kozlov S, Yen T, Hobson K, Gatei M, Zhang N, Watters D, Egerton M, Shiloh Y, Kharbanda S, Kufe D, Lavin M F (May. 1997). "Interaction between ATM protein and c-Abl in response to DNA damage". Nature (ENGLAND) 387 (6632): 520–3. doi:10.1038/387520a0. ISSN 0028-0836. PMID 9168117. 
  33. ^ a b Kishi, S; Zhou X Z, Ziv Y, Khoo C, Hill D E, Shiloh Y, Lu K P (Aug. 2001). "Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks". J. Biol. Chem. (United States) 276 (31): 29282–91. doi:10.1074/jbc.M011534200. ISSN 0021-9258. PMID 11375976. 
  34. ^ Yu, H H; Zisch A H, Dodelet V C, Pasquale E B (Jul. 2001). "Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor". Oncogene (England) 20 (30): 3995–4006. doi:10.1038/sj.onc.1204524. ISSN 0950-9232. PMID 11494128. 
  35. ^ Bai, R Y; Jahn T, Schrem S, Munzert G, Weidner K M, Wang J Y, Duyster J (Aug. 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene (ENGLAND) 17 (8): 941–8. doi:10.1038/sj.onc.1202024. ISSN 0950-9232. PMID 9747873. 
  36. ^ Frantz, J D; Giorgetti-Peraldi S, Ottinger E A, Shoelson S E (Jan. 1997). "Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains". J. Biol. Chem. (UNITED STATES) 272 (5): 2659–67. doi:10.1074/jbc.272.5.2659. ISSN 0021-9258. PMID 9006901. 
  37. ^ a b Ziemnicka-Kotula, D; Xu J, Gu H, Potempska A, Kim K S, Jenkins E C, Trenkner E, Kotula L (May. 1998). "Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton". J. Biol. Chem. (UNITED STATES) 273 (22): 13681–92. doi:10.1074/jbc.273.22.13681. ISSN 0021-9258. PMID 9593709. 
  38. ^ Warmuth, M; Bergmann M, Priess A, Häuslmann K, Emmerich B, Hallek M (Dec. 1997). "The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr". J. Biol. Chem. (UNITED STATES) 272 (52): 33260–70. doi:10.1074/jbc.272.52.33260. ISSN 0021-9258. PMID 9407116. 
  39. ^ Bassermann, Florian; Jahn Thomas, Miething Cornelius, Seipel Petra, Bai Ren-Yuan, Coutinho Sunita, Tybulewicz Victor L, Peschel Christian, Duyster Justus (Apr. 2002). "Association of Bcr-Abl with the proto-oncogene Vav is implicated in activation of the Rac-1 pathway". J. Biol. Chem. (United States) 277 (14): 12437–45. doi:10.1074/jbc.M112397200. ISSN 0021-9258. PMID 11790798. 
  40. ^ Zhu, J; Shore S K (Dec. 1996). "c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein". Mol. Cell. Biol. (UNITED STATES) 16 (12): 7054–62. ISSN 0270-7306. PMC 231708. PMID 8943360. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231708. 
  41. ^ Kumar, V; Sabatini D, Pandey P, Gingras A C, Majumder P K, Kumar M, Yuan Z M, Carmichael G, Weichselbaum R, Sonenberg N, Kufe D, Kharbanda S (Apr. 2000). "Regulation of the rapamycin and FKBP-target 1/mammalian target of rapamycin and cap-dependent initiation of translation by the c-Abl protein-tyrosine kinase". J. Biol. Chem. (UNITED STATES) 275 (15): 10779–87. doi:10.1074/jbc.275.15.10779. ISSN 0021-9258. PMID 10753870. 
  42. ^ Ling, Xiaoyang; Ma Guozhen, Sun Tong, Liu Jiaxin, Arlinghaus Ralph B (Jan. 2003). "Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr". Cancer Res. (United States) 63 (2): 298–303. ISSN 0008-5472. PMID 12543778. 
  43. ^ Pendergast, A M; Muller A J, Havlik M H, Maru Y, Witte O N (Jul. 1991). "BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner". Cell (UNITED STATES) 66 (1): 161–71. doi:10.1016/0092-8674(91)90148-R. ISSN 0092-8674. PMID 1712671. 
  44. ^ Yuan, Z M; Shioya H, Ishiko T, Sun X, Gu J, Huang Y Y, Lu H, Kharbanda S, Weichselbaum R, Kufe D (Jun. 1999). "p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage". Nature (ENGLAND) 399 (6738): 814–7. doi:10.1038/21704. ISSN 0028-0836. PMID 10391251. 
  45. ^ Agami, R; Blandino G, Oren M, Shaul Y (Jun. 1999). "Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis". Nature (ENGLAND) 399 (6738): 809–13. doi:10.1038/21697. ISSN 0028-0836. PMID 10391250. 
  46. ^ Cao, Cheng; Leng Yumei, Huang Wei, Liu Xuan, Kufe Donald (Oct. 2003). "Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases". J. Biol. Chem. (United States) 278 (41): 39609–14. doi:10.1074/jbc.M305770200. ISSN 0021-9258. PMID 12893824. 
  47. ^ Agami, R; Shaul Y (Apr. 1998). "The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genes". Oncogene (ENGLAND) 16 (14): 1779–88. doi:10.1038/sj.onc.1201708. ISSN 0950-9232. PMID 9583676. 
  48. ^ Tani, Katsuko; Sato Seiichi, Sukezane Taiko, Kojima Hiroshi, Hirose Hidenori, Hanafusa Hidesaburo, Shishido Tomoyuki (Jun. 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. (United States) 278 (24): 21685–92. doi:10.1074/jbc.M301447200. ISSN 0021-9258. PMID 12672821. 
  49. ^ Biesova, Z; Piccoli C, Wong W T (Jan. 1997). "Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth". Oncogene (ENGLAND) 14 (2): 233–41. doi:10.1038/sj.onc.1200822. ISSN 0950-9232. PMID 9010225. 
  50. ^ Yamamoto, A; Suzuki T, Sakaki Y (Jun. 2001). "Isolation of hNap1BP which interacts with human Nap1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease". Gene (Netherlands) 271 (2): 159–69. doi:10.1016/S0378-1119(01)00521-2. ISSN 0378-1119. PMID 11418237. 
  51. ^ Bueno MJ, Pérez de Castro I, Gómez de Cedrón M, Santos J, Calin GA, Cigudosa JC, Croce CM, Fernández-Piqueras J, Malumbres M (2008). "Genetic and epigenetic silencing of microRNA-203 enhances ABL1 and BCR-ABL1 oncogene expression". Cancer Cell 13 (6): 496–506. doi:10.1016/j.ccr.2008.04.018. PMID 18538733. 

Further reading

External links