References analysis of the Wikipedia article "ABL1" in the Japanese version

doi.org (Global: 2^nd place; Japanese: 6^th place)

“Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides”. Science 253 (5019): 562–5. (August 1991). Bibcode: 1991Sci...253..562S. doi:10.1126/science.1857987. PMID 1857987.

“Mutational analyses of the human Rad51-Tyr315 residue, a site for phosphorylation in leukaemia cells”. Genes to Cells 9 (9): 781–90. (September 2004). doi:10.1111/j.1365-2443.2004.00772.x. PMID 15330855.

“BCR-ABL stimulates mutagenic homologous DNA double-strand break repair via the DNA-end-processing factor CtIP”. Carcinogenesis 32 (1): 27–34. (January 2011). doi:10.1093/carcin/bgq216. PMID 20974687.

“Targeting DNA Homologous Repair Proficiency With Concomitant Topoisomerase II and c-Abl Inhibition”. Frontiers in Oncology 11: 3666. (2021). doi:10.3389/fonc.2021.733700. PMC 8488401. PMID 34616682.

“Overriding imatinib resistance with a novel ABL kinase inhibitor”. Science 305 (5682): 399–401. (July 2004). Bibcode: 2004Sci...305..399S. doi:10.1126/science.1099480. PMID 15256671.

“Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase”. J. Biol. Chem. 278 (24): 21685–92. (June 2003). doi:10.1074/jbc.M301447200. PMID 12672821.

“Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth”. Oncogene 14 (2): 233–41. (January 1997). doi:10.1038/sj.onc.1200822. PMID 9010225.

“Isolation of hNap1BP which interacts with human Nap1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease”. Gene 271 (2): 159–69. (June 2001). doi:10.1016/S0378-1119(01)00521-2. PMID 11418237.

“Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response”. J. Biol. Chem. 278 (15): 12961–7. (April 2003). doi:10.1074/jbc.M300058200. PMID 12569093.

“Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity”. Genes Dev. 9 (21): 2569–82. (November 1995). doi:10.1101/gad.9.21.2569. PMID 7590236.

“Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl”. J. Biol. Chem. 274 (18): 12748–52. (April 1999). doi:10.1074/jbc.274.18.12748. PMID 10212258.

“Interaction between ATM protein and c-Abl in response to DNA damage”. Nature 387 (6632): 520–3. (May 1997). Bibcode: 1997Natur.387R.520S. doi:10.1038/387520a0. PMID 9168117.

“Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks”. J. Biol. Chem. 276 (31): 29282–91. (August 2001). doi:10.1074/jbc.M011534200. PMID 11375976.

“p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene”. J. Biol. Chem. 271 (41): 25198–203. (October 1996). doi:10.1074/jbc.271.41.25198. PMID 8810278.

“Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases”. Curr. Biol. 5 (3): 296–305. (March 1995). doi:10.1016/S0960-9822(95)00060-1. PMID 7780740.

“Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway”. EMBO J. 13 (4): 764–73. (February 1994). doi:10.1002/j.1460-2075.1994.tb06319.x. PMC 394874. PMID 8112292.

“BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner”. Cell 66 (1): 161–71. (July 1991). doi:10.1016/0092-8674(91)90148-R. PMID 1712671.

“Constitutive association of BRCA1 and c-Abl and its ATM-dependent disruption after irradiation”. Mol. Cell. Biol. 22 (12): 4020–32. (June 2002). doi:10.1128/MCB.22.12.4020-4032.2002. PMC 133860. PMID 12024016.

“Catalase activity is regulated by c-Abl and Arg in the oxidative stress response”. J. Biol. Chem. 278 (32): 29667–75. (August 2003). doi:10.1074/jbc.M301292200. PMID 12777400.

“Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor”. Oncogene 20 (30): 4058–69. (July 2001). doi:10.1038/sj.onc.1204528. PMID 11494134.

“Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl”. Biochem. J. 370 (Pt 1): 29–34. (February 2003). doi:10.1042/BJ20021539. PMC 1223168. PMID 12475393.

“Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites”. Genes Dev. 8 (7): 783–95. (April 1994). doi:10.1101/gad.8.7.783. PMID 7926767.

“Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation”. Blood 89 (1): 297–306. (January 1997). doi:10.1182/blood.V89.1.297. PMID 8978305.

“Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells”. Blood 96 (10): 3406–13. (November 2000). doi:10.1182/blood.V96.10.3406. PMID 11071635.

“Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok”. Cell 88 (2): 205–11. (January 1997). doi:10.1016/S0092-8674(00)81841-3. PMID 9008161.

“Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor”. Oncogene 20 (30): 3995–4006. (July 2001). doi:10.1038/sj.onc.1204524. PMID 11494128.

“Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases”. J. Biol. Chem. 278 (41): 39609–14. (October 2003). doi:10.1074/jbc.M305770200. PMID 12893824.

“The SH2-containing adapter protein GRB10 interacts with BCR-ABL”. Oncogene 17 (8): 941–8. (August 1998). doi:10.1038/sj.onc.1202024. PMID 9747873.

“Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains”. J. Biol. Chem. 272 (5): 2659–67. (January 1997). doi:10.1074/jbc.272.5.2659. PMID 9006901.

“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. 275 (15): 10779–87. (April 2000). doi:10.1074/jbc.275.15.10779. PMID 10753870.

“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. 272 (52): 33260–70. (December 1997). doi:10.1074/jbc.272.52.33260. PMID 9407116.

“Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation”. EMBO J. 21 (14): 3715–27. (July 2002). doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.

“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. 184 (4): 1365–75. (October 1996). doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209.

“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. 16 (7): 3327–37. (July 1996). doi:10.1128/mcb.16.7.3327. PMC 231327. PMID 8668148.

“Direct interaction of nerve growth factor receptor, TrkA, with non-receptor tyrosine kinase, c-Abl, through the activation loop”. FEBS Lett. 469 (1): 72–6. (March 2000). doi:10.1016/S0014-5793(00)01242-4. PMID 10708759.

“Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor”. J. Neurosci. Res. 59 (3): 356–64. (February 2000). doi:10.1002/(SICI)1097-4547(20000201)59:3<356::AID-JNR9>3.0.CO;2-G. PMID 10679771.

“p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage”. Nature 399 (6738): 814–7. (June 1999). Bibcode: 1999Natur.399..814Y. doi:10.1038/21704. PMID 10391251.

“Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis”. Nature 399 (6738): 809–13. (June 1999). Bibcode: 1999Natur.399..809A. doi:10.1038/21697. PMID 10391250.

“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. 11 (19): 2456–67. (October 1997). doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.

“Functional interaction between c-Abl and the p21-activated protein kinase gamma-PAK”. Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14346–51. (December 2000). Bibcode: 2000PNAS...9714346R. doi:10.1073/pnas.97.26.14346. PMC 18921. PMID 11121037.

“Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation”. Mol. Cell 6 (6): 1413–23. (December 2000). doi:10.1016/S1097-2765(00)00138-6. PMID 11163214.

“c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage”. Mol. Cell. Biol. 22 (10): 3292–300. (May 2002). doi:10.1128/MCB.22.10.3292-3300.2002. PMC 133797. PMID 11971963.

“Interaction of BCR-ABL with the retinoblastoma protein in Philadelphia chromosome-positive cell lines”. Int. J. Hematol. 65 (2): 115–21. (February 1997). doi:10.1016/S0925-5710(96)00539-7. PMID 9071815.

“A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle”. Cell 75 (4): 779–90. (November 1993). doi:10.1016/0092-8674(93)90497-E. PMID 8242749.

“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 16 (14): 1779–88. (April 1998). doi:10.1038/sj.onc.1201708. PMID 9583676.

“c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein”. Mol. Cell. Biol. 16 (12): 7054–62. (December 1996). doi:10.1128/mcb.16.12.7054. PMC 231708. PMID 8943360.

“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 93 (8): 2707–20. (April 1999). doi:10.1182/blood.V93.8.2707. PMID 10194451.

“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. 272 (28): 17542–50. (July 1997). doi:10.1074/jbc.272.28.17542. PMID 9211900.

“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. 273 (22): 13681–92. (May 1998). doi:10.1074/jbc.273.22.13681. PMID 9593709.

“Association of Bcr-Abl with the proto-oncogene Vav is implicated in activation of the Rac-1 pathway”. J. Biol. Chem. 277 (14): 12437–45. (April 2002). doi:10.1074/jbc.M112397200. PMID 11790798.

“The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation”. Hum. Mol. Genet. 13 (15): 1535–49. (August 2004). doi:10.1093/hmg/ddh167. PMID 15175272.

“Genetic and epigenetic silencing of microRNA-203 enhances ABL1 and BCR-ABL1 oncogene expression”. Cancer Cell 13 (6): 496–506. (June 2008). doi:10.1016/j.ccr.2008.04.018. hdl:10261/7369. PMID 18538733.

harvard.edu (Global: 18^th place; Japanese: 107^th place)

ui.adsabs.harvard.edu

“Overriding imatinib resistance with a novel ABL kinase inhibitor”. Science 305 (5682): 399–401. (July 2004). Bibcode: 2004Sci...305..399S. doi:10.1126/science.1099480. PMID 15256671.

“Interaction between ATM protein and c-Abl in response to DNA damage”. Nature 387 (6632): 520–3. (May 1997). Bibcode: 1997Natur.387R.520S. doi:10.1038/387520a0. PMID 9168117.

“p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage”. Nature 399 (6738): 814–7. (June 1999). Bibcode: 1999Natur.399..814Y. doi:10.1038/21704. PMID 10391251.

“Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis”. Nature 399 (6738): 809–13. (June 1999). Bibcode: 1999Natur.399..809A. doi:10.1038/21697. PMID 10391250.

nih.gov (Global: 4^th place; Japanese: 24^th place)

pubmed.ncbi.nlm.nih.gov

“Lymphosarcoma: virus-induced thymic-independent disease in mice”. Cancer Research 30 (8): 2213–22. (August 1970). PMID 4318922.

“Overriding imatinib resistance with a novel ABL kinase inhibitor”. Science 305 (5682): 399–401. (July 2004). Bibcode: 2004Sci...305..399S. doi:10.1126/science.1099480. PMID 15256671.

“Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth”. Oncogene 14 (2): 233–41. (January 1997). doi:10.1038/sj.onc.1200822. PMID 9010225.

“Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl”. J. Biol. Chem. 274 (18): 12748–52. (April 1999). doi:10.1074/jbc.274.18.12748. PMID 10212258.

“Interaction between ATM protein and c-Abl in response to DNA damage”. Nature 387 (6632): 520–3. (May 1997). Bibcode: 1997Natur.387R.520S. doi:10.1038/387520a0. PMID 9168117.

“Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases”. Curr. Biol. 5 (3): 296–305. (March 1995). doi:10.1016/S0960-9822(95)00060-1. PMID 7780740.

“Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway”. EMBO J. 13 (4): 764–73. (February 1994). doi:10.1002/j.1460-2075.1994.tb06319.x. PMC 394874. PMID 8112292.

“Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr”. Cancer Res. 63 (2): 298–303. (January 2003). PMID 12543778.

“Catalase activity is regulated by c-Abl and Arg in the oxidative stress response”. J. Biol. Chem. 278 (32): 29667–75. (August 2003). doi:10.1074/jbc.M301292200. PMID 12777400.

“Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor”. Oncogene 20 (30): 4058–69. (July 2001). doi:10.1038/sj.onc.1204528. PMID 11494134.

“Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl”. Biochem. J. 370 (Pt 1): 29–34. (February 2003). doi:10.1042/BJ20021539. PMC 1223168. PMID 12475393.

“Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites”. Genes Dev. 8 (7): 783–95. (April 1994). doi:10.1101/gad.8.7.783. PMID 7926767.

“Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation”. Blood 89 (1): 297–306. (January 1997). doi:10.1182/blood.V89.1.297. PMID 8978305.

“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. 161 (10): 5555–63. (November 1998). PMID 9820532.

“Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok”. Cell 88 (2): 205–11. (January 1997). doi:10.1016/S0092-8674(00)81841-3. PMID 9008161.

“Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor”. Oncogene 20 (30): 3995–4006. (July 2001). doi:10.1038/sj.onc.1204524. PMID 11494128.

“Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases”. J. Biol. Chem. 278 (41): 39609–14. (October 2003). doi:10.1074/jbc.M305770200. PMID 12893824.

“The SH2-containing adapter protein GRB10 interacts with BCR-ABL”. Oncogene 17 (8): 941–8. (August 1998). doi:10.1038/sj.onc.1202024. PMID 9747873.

“Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation”. EMBO J. 21 (14): 3715–27. (July 2002). doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.

“p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage”. Nature 399 (6738): 814–7. (June 1999). Bibcode: 1999Natur.399..814Y. doi:10.1038/21704. PMID 10391251.

“Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis”. Nature 399 (6738): 809–13. (June 1999). Bibcode: 1999Natur.399..809A. doi:10.1038/21697. PMID 10391250.

“The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation”. Hum. Mol. Genet. 13 (15): 1535–49. (August 2004). doi:10.1093/hmg/ddh167. PMID 15175272.

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ABL1 (Japanese Wikipedia)

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ABL1 (Japanese Wikipedia)

doi.org (Global: 2nd place; Japanese: 6th place)

ensembl.org (Global: 1,626th place; Japanese: 2,625th place)

May2017.archive.ensembl.org

eur.nl (Global: low place; Japanese: low place)

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handle.net (Global: 102nd place; Japanese: 78th place)

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harvard.edu (Global: 18th place; Japanese: 107th place)

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nih.gov (Global: 4th place; Japanese: 24th place)

pubmed.ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

uniprot.org (Global: 5,673rd place; Japanese: low place)

wikipedia.org (Global: low place; Japanese: low place)

en.wikipedia.org

doi.org (Global: 2^nd place; Japanese: 6^th place)

ensembl.org (Global: 1,626^th place; Japanese: 2,625^th place)

handle.net (Global: 102^nd place; Japanese: 78^th place)

harvard.edu (Global: 18^th place; Japanese: 107^th place)

nih.gov (Global: 4^th place; Japanese: 24^th place)

uniprot.org (Global: 5,673^rd place; Japanese: low place)