Janus kinase deregulation in leukemia and lymphoma

Lanthanum Chloride Inhibits LPS Mediated Expressions of Pro-Inflammatory Cytokines and Adhesion Molecules in HUVECs: Involvement of NF-κB-Jmjd3 Signaling

Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,759 · see citing works

Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders

Baxter, E. J., Scott, L. M., Campbell, P. J., East, C., Fourouclas, N., Swanton, S., Vassiliou, G. S., Bench, A. J., Boyd, E. M., Curtin, N., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)71142-9 · Cited by 3,548 · see citing works

A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera

James, C., Ugo, V., Couedic, J. P. L., Staerk, J., Delhommeau, F., Lacout, C., Garçon, L., Raslová, H., Berger, R., Griscelli, A. B., et al. (2005) · Nature · doi:10.1038/nature03546 · Cited by 3,542 · see citing works

A Gain-of-Function Mutation of <i>JAK2</i> in Myeloproliferative Disorders

Kralovics, R., Passamonti, F., Buser, A. S., Teo, S.-S., Tiedt, R., Passweg, J. R., Tichelli, A., Cazzola, M., & Skoda, R. C. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa051113 · Cited by 3,470 · see citing works

Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis

Levine, R. L., Wadleigh, M., Cools, J., Ebert, B. L., Wernig, G., Huntly, B. J. P., Boggon, T. J., Wlodarska, I., Clark, J. J., Moore, S., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.03.023 · Cited by 2,993 · see citing works

Mutation in <i>TET2</i> in Myeloid Cancers

Delhommeau, F., Dupont, S., Valle, V. D., James, C., Trannoy, S., Massé, A., Kosmider, O., Le Couedic, J.-P., Robert, F., Alberdi, A., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0810069 · Cited by 1,776 · see citing works

Oncogenically active MYD88 mutations in human lymphoma

Ngo, V. N., Young, R. M., Schmitz, R., Jhavar, S. G., Xiao, W., Lim, K., Kohlhammer, H., Xu, W., Yang, Y., Zhao, H., et al. (2010) · Nature · doi:10.1038/nature09671 · Cited by 1,514 · see citing works

JAK2 Exon 12 Mutations in Polycythemia Vera and Idiopathic Erythrocytosis

Scott, L. M., Tong, W., Levine, R. L., Scott, M., Beer, P., Stratton, M. R., Futreal, P., Erber, W., McMullin, M., Harrison, C. N., et al. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa065202 · Cited by 1,346 · see citing works

Safety and Efficacy of INCB018424, a JAK1 and JAK2 Inhibitor, in Myelofibrosis

Verstovšek, S., Kantarjian, H. M., Mesa, R. A., Pardanani, A. D., Cortes, J. E., Thomas, D. A., Estrov, Z. E., Fridman, J. S., Bradley, E. C., Erickson‐Viitanen, S., et al. (2010) · New England Journal of Medicine · doi:10.1056/nejmoa1002028 · Cited by 1,165 · see citing works

Molecular Diagnosis of Primary Mediastinal B Cell Lymphoma Identifies a Clinically Favorable Subgroup of Diffuse Large B Cell Lymphoma Related to Hodgkin Lymphoma

Rosenwald, A., Wright, G. W., Leroy, K., Yu, X., Gaulard, P., Gascoyne, R. D., Chan, W. C., Zhao, T., Haïoun, C., Greiner, T. C., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031074 · Cited by 1,095 · see citing works

Classification and diagnosis of myeloproliferative neoplasms: The 2008 World Health Organization criteria and point-of-care diagnostic algorithms

Tefferi, A., & Vardiman, J. (2008) · Leukemia · doi:10.1038/sj.leu.2404955 · Cited by 1,053 · see citing works

Reversal of Histone Lysine Trimethylation by the JMJD2 Family of Histone Demethylases

Whetstine, J. R., Nottke, A. C., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiácovo, M. P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.028 · Cited by 1,046 · see citing works

Molecular subtypes of diffuse large B-cell lymphoma arise by distinct genetic pathways

Lenz, G., Wright, G. W., Emre, N. C. T., Kohlhammer, H., Davé, S. S., Davis, R. E., Carty, S. A., Lam, L. T., Shaffer, A. L., Xiao, W., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804295105 · Cited by 997 · see citing works

The molecular signature of mediastinal large B-cell lymphoma differs from that of other diffuse large B-cell lymphomas and shares features with classical Hodgkin lymphoma

Savage, K. J. J. (2003) · Blood · doi:10.1182/blood-2003-06-1841 · Cited by 865 · see citing works

Widespread occurrence of the JAK2 V617F mutation in chronic myeloproliferative disorders

Jones, A. V. (2005) · Blood · doi:10.1182/blood-2005-03-1320 · Cited by 843 · cited 2× · see citing works

A TEL-JAK2 Fusion Protein with Constitutive Kinase Activity in Human Leukemia

Penard‐Lacronique, V., Boureux, A., Della-Valle, V., Poirel, H. A., Quang, C. T., Mauchauffé, M., Berthou, C., Lessard, M., Berger, R., Ghysdael, J., et al. (1997) · Science · doi:10.1126/science.278.5341.1309 · Cited by 790 · see citing works

MOZ-TIF2, but not BCR-ABL, confers properties of leukemic stem cells to committed murine hematopoietic progenitors

Huntly, B. J. P., Shigematsu, H., Deguchi, K., Lee, B. H., Mizuno, S., Duclos, N., Rowan, R., Amaral, S., Curley, D., Williams, I. R., et al. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.10.015 · Cited by 697 · see citing works

JAK2 phosphorylates histone H3Y41 and excludes HP1α from chromatin

Dawson, M. A., Bannister, A. J., Göttgens, B., Foster, S. D., Bartke, T., Green, A. R., & Kouzarides, T. (2009) · Nature · doi:10.1038/nature08448 · Cited by 624 · see citing works

Rearrangement of CRLF2 in B-progenitor– and Down syndrome–associated acute lymphoblastic leukemia

Mullighan, C. G., Collins-Underwood, J. R., Phillips, L. A., Loudin, M. G., Liu, W., Zhang, J., Ma, J., Coustan‐Smith, E., Harvey, R. C., Willman, C. L., et al. (2009) · Nature Genetics · doi:10.1038/ng.469 · Cited by 621 · see citing works

Unphosphorylated STAT3 accumulates in response to IL-6 and activates transcription by binding to NFκB

Yang, J., Liao, X., Agarwal, M. K., Barnes, L., Auron, P. E., & Stark, G. R. (2007) · Genes &amp; Development · doi:10.1101/gad.1553707 · Cited by 611 · see citing works

Rearrangement of CRLF2 is associated with mutation of JAK kinases, alteration of IKZF1, Hispanic/Latino ethnicity, and a poor outcome in pediatric B-progenitor acute lymphoblastic leukemia

Harvey, R. C., Mullighan, C. G., Chen, I., Wharton, W., Mikhail, F. M., Carroll, A. J., Kang, H., Liu, W., Dobbin, K. K., Smith, M. A., et al. (2010) · Blood · doi:10.1182/blood-2009-09-245944 · Cited by 568 · see citing works

JAK mutations in high-risk childhood acute lymphoblastic leukemia

Mullighan, C. G., Zhang, J., Harvey, R. C., Collins-Underwood, J. R., Schulman, B. A., Phillips, L. A., Tasian, S. K., Loh, M. L., Su, X., Liu, W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811761106 · Cited by 558 · see citing works

Molecular and Structural Basis of Cytokine Receptor Pleiotropy in the Interleukin-4/13 System

LaPorte, S. L., Juo, Z. S., Václavíková, J., Colf, L. A., Qi, X., Heller, N. M., Keegan, A. D., & García, K. C. (2008) · Cell · doi:10.1016/j.cell.2007.12.030 · Cited by 519 · see citing works

Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cellsPreprint

Loh, Y., Zhang, W., Chen, X., George, J., & Ng, H. (2007) · Genes & Development · doi:10.1101/gad.1588207 · Cited by 507 · see citing works

Deregulated expression of cytokine receptor gene, CRLF2, is involved in lymphoid transformation in B-cell precursor acute lymphoblastic leukemia

Russell, L. J., Capasso, M., Vater, I., Akasaka, T., Bernard, O., Calasanz, M. J., Chandrasekaran, T., Chapiro, É., Gesk, S., Griffiths, M., et al. (2009) · Blood · doi:10.1182/blood-2009-03-208397 · Cited by 498 · see citing works

The JAK2 V617F activating tyrosine kinase mutation is an infrequent event in both “atypical” myeloproliferative disorders and myelodysplastic syndromes

Steensma, D. P., Dewald, G. W., Lasho, T. L., Powell, H. L., McClure, R. F., Levine, R. L., Gilliland, D. G., & Tefferi, A. (2005) · Blood · doi:10.1182/blood-2005-03-1183 · Cited by 466 · see citing works

JAK2 mutation 1849G>T is rare in acute leukemias but can be found in CMML, Philadelphia chromosome-negative CML, and megakaryocytic leukemia.

Jelinek, J., Oki, Y., Gharibyan, V., Bueso-Ramos, C., Prchal, J., Verstovsek, S., Beran, M., Estey, E., Kantarjian, H., & Issa, J. (2005) · Blood · doi:10.1182/blood-2005-05-1800 · Cited by 418 · see citing works

Oncogenic IL7R gain-of-function mutations in childhood T-cell acute lymphoblastic leukemia

Zenatti, P. P., Ribeiro, D., Li, W., Zuurbier, L. C., da Silva, M. C., Paganin, M., Tritapoe, J. M., Hixon, J. A., Silveira, A. B., Cardoso, B. A., et al. (2011) · Nature Genetics · doi:10.1038/ng.924 · Cited by 414 · see citing works

JAK2 haplotype is a major risk factor for the development of myeloproliferative neoplasms

Jones, A., Chase, A., Silver, R., Oscier, D., Zoi, K., Wang, Y. L., Cario, H., Pahl, H., Collins, A., Reiter, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.334 · Cited by 407 · see citing works

Identification of novel cluster groups in pediatric high-risk B-precursor acute lymphoblastic leukemia with gene expression profiling: correlation with genome-wide DNA copy number alterations, clinical characteristics, and outcome

Harvey, R. C., Mullighan, C. G., Wang, X., Dobbin, K. K., Davidson, G. S., Bedrick, E. J., Chen, I., Atlas, S. R., Kang, H., Kerem, A. R., et al. (2010) · Blood · doi:10.1182/blood-2009-08-239681 · Cited by 402 · see citing works

The JAK2V617F activating mutation occurs in chronic myelomonocytic leukemia and acute myeloid leukemia, but not in acute lymphoblastic leukemia or chronic lymphocytic leukemia.

Levine, R., Loriaux, M., Huntly, B. J. P., Loh, M., Beran, M., Stoffregen, E. P., Berger, R., Clark, J. J., Willis, S., Nguyen, K. T., et al. (2005) · Blood · doi:10.1182/blood-2005-05-1898 · Cited by 400 · see citing works

Physiological Jak2V617F expression causes a lethal myeloproliferative neoplasm with differential effects on hematopoietic stem and progenitor cells

Mullally, A., Lane, S. W., Ball, B., Megerdichian, C., Okabe, R., Al-Shahrour, F., Paktinat, M., Haydu, J. E., Housman, E., Lord, A. M., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.05.015 · Cited by 386 · see citing works

A common JAK2 haplotype confers susceptibility to myeloproliferative neoplasms

Olcaydu, D., Harutyunyan, A. S., Jäger, R., Berg, T., Gisslinger, B., Pabinger, I., Gisslinger, H., & Královics, R. (2009) · Nature Genetics · doi:10.1038/ng.341 · Cited by 361 · see citing works

Cooperative signaling through the signal transducer and activator of transcription 3 and nuclear factor-κB pathways in subtypes of diffuse large B-cell lymphoma

Lam, L. T., Wright, G. W., Davis, R. E., Lenz, G., Farinha, P., Dang, L., Chan, J. W., Rosenwald, A., Gascoyne, R. D., & Staudt, L. M. (2007) · Blood · doi:10.1182/blood-2007-09-111948 · Cited by 355 · see citing works

A germline JAK2 SNP is associated with predisposition to the development of JAK2V617F-positive myeloproliferative neoplasms

Kilpivaara, O., Mukherjee, S., Schram, A. M., Wadleigh, M., Mullally, A., Ebert, B. L., Bass, A. J., Marubayashi, S., Heguy, A., Garcia‐Manero, G., et al. (2009) · Nature Genetics · doi:10.1038/ng.342 · Cited by 349 · see citing works

Gain-of-function mutations in interleukin-7 receptor-α ( IL7R ) in childhood acute lymphoblastic leukemias

Shochat, C., Tal, N., Bandapalli, O. R., Palmi, C., Ganmore, I., Kronnie, G. T., Cario, G., Cazzaniga, G., Kulozik, A. E., Stanulla, M., et al. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20110580 · Cited by 348 · see citing works

Activating alleles of JAK3 in acute megakaryoblastic leukemia.

Walters, D. K., Mercher, T., Gu, T., O'Hare, T., Tyner, J., Loriaux, M., Goss, V., Lee, K. A., Eide, C., Wong, M., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.06.002 · Cited by 347 · see citing works

Functional screening identifies CRLF2 in precursor B-cell acute lymphoblastic leukemia

Yoda, A., Yoda, Y., Chiaretti, S., Bar‐Natan, M., Mani, K. M., Rodig, S. J., West, N. H., Xiao, Y., Brown, J. R., Mitsiades, C. S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911726107 · Cited by 336 · see citing works

Small Molecule Inhibitors of IκB Kinase Are Selectively Toxic for Subgroups of Diffuse Large B-Cell Lymphoma Defined by Gene Expression Profiling

Lam, L. T., Davis, R. E., Pierce, J., Hepperle, M. E., Xu, Y., Foley, M. H., Nong, Y., Wen, D., Adams, J., Dang, L., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.28.11.1 · Cited by 336 · see citing works

Mutations of JAK2 in acute lymphoblastic leukaemias associated with Down's syndrome

Bercovich, D., Ganmore, I., Scott, L. M., Wainreb, G., Birger, Y., Elimelech, A., Shochat, C., Cazzaniga, G., Biondi, A., Basso, G., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61341-0 · Cited by 335 · see citing works

Transcriptional regulation of the cyclin D1 promoter by STAT5: its involvement in cytokine‐dependent growth of hematopoietic cells

Matsumura, I., Kitamura, T., Wakao, H., Tanaka, H., Hashimoto, K., Albanese, C., Downward, J., Pestell, R. G., & Kanakura, Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1367 · Cited by 332 · see citing works

Mutation of JAK2 in the myeloproliferative disorders: timing, clonality studies, cytogenetic associations, and role in leukemic transformation.

Campbell, P., Baxter, E. J., Beer, P., Scott, L. M., Bench, A., Huntly, B. J. P., Erber, W., Kušec, R., Larsen, T., Giraudier, S., et al. (2006) · Blood · doi:10.1182/blood-2005-12-013748 · Cited by 332 · see citing works

Somatically acquired JAK1 mutations in adult acute lymphoblastic leukemia

Flex, E., Petrangeli, V., Stella, L., Chiaretti, S., Hornakova, T., Knoops, L., Ariola, C., Fodale, V., Clappier, E., Paoloni, F. P., et al. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20072182 · Cited by 331 · see citing works

Leukemic blasts in transformed JAK2-V617F–positive myeloproliferative disorders are frequently negative for the JAK2-V617F mutation.

Theocharides, A. P. A., Boissinot, M., Girodon, F., Garand, R., Teo, S.-S., Lippert, É., Talmant, P., Tichelli, A., Hermouet, S., & Skoda, R. C. (2007) · Blood · doi:10.1182/blood-2006-12-062125 · Cited by 324 · see citing works

Guideline for investigation and management of adults and children presenting with a thrombocytosis

Harrison, C. N., Bareford, D., Butt, N. M., Campbell, P. J., Conneally, E., Drummond, M. W., Erber, W. N., Everington, T., Green, A. R., Hall, G. W., et al. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08122.x · Cited by 317 · see citing works

Expression of a homodimeric type I cytokine receptor is required for JAK2V617F-mediated transformation

Lu, X., Levine, R. L., Tong, W., Wernig, G., Pikman, Y., Zarnegar, S., Gilliland, D. G., & Lodish, H. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509714102 · Cited by 316 · see citing works

Small molecule inhibitors of IkappaB kinase are selectively toxic for subgroups of diffuse large B-cell lymphoma defined by gene expression profiling.

Lam, L. T., Davis, R. E., Pierce, J., Hepperle, M. E., Xu, Y., Foley, M. H., Nong, Y., Wen, D., Adams, J., Dang, L., et al. (2005) · PubMed · Cited by 312 · see citing works

Two routes to leukemic transformation after a JAK2 mutation–positive myeloproliferative neoplasm

Beer, P. A., Delhommeau, F., Couedic, J. P. L., Dawson, M. A., Chen, E., Bareford, D., Kušec, R., McMullin, M. F., Harrison, C. N., Vannucchi, A. M., et al. (2009) · Blood · doi:10.1182/blood-2009-08-236596 · Cited by 306 · see citing works

Stat5 Is Essential for the Myelo- and Lymphoproliferative Disease Induced by TEL/JAK2

Schwaller, J., Parganas, E., Wang, D., Cain, D., Aster, J. C., Williams, I. R., Lee, C., Gerthner, R., Kitamura, T., Frantsve‐Hawley, J., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00067-8 · Cited by 303 · see citing works

Constitutively activated STAT3 promotes cell proliferation and survival in the activated B-cell subtype of diffuse large B-cell lymphomas

Ding, B. B., Yu, J., Yu, R. Y.-L., Mendez, L., Shaknovich, R., Zhang, Y., Cattoretti, G., & Ye, B. H. (2007) · Blood · doi:10.1182/blood-2007-04-087734 · Cited by 298 · see citing works

Clinical correlates of JAK2V617F presence or allele burden in myeloproliferative neoplasms: a critical reappraisal

Vannucchi, A. M., Antonioli, E., Guglielmelli, P., Pardanani, A. D., & Tefferi, A. (2008) · Leukemia · doi:10.1038/leu.2008.113 · Cited by 293 · see citing works

Progenitors homozygous for the V617F mutation occur in most patients with polycythemia vera, but not essential thrombocythemia

Scott, L. M., Scott, M. A., Campbell, P. J., & Green, A. R. (2006) · Blood · doi:10.1182/blood-2006-04-018259 · Cited by 292 · see citing works

The JAK2 V617F mutation occurs in hematopoietic stem cells in polycythemia vera and predisposes toward erythroid differentiation

Jamieson, C. H. M., Gotlib, J. R., Durocher, J. A., Chao, M. P., Mariappan, M. R., Lay, M. J., Jones, C. D., Zehnder, J. L., Lilleberg, S. L., & Weissman, I. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601462103 · Cited by 284 · see citing works

Cooperative Epigenetic Modulation by Cancer Amplicon Genes

Rui, L., Emre, N. C. T., Kruhlak, M. J., Chung, H., Steidl, C., Slack, G. W., Wright, G. W., Lenz, G., Ngo, V. N., Shaffer, A. L., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.11.013 · Cited by 283 · see citing works

The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling

Ungureanu, D., Wu, J., Pekkala, T., Niranjan, Y., Young, C., Jensen, O. N., Xu, C., Neubert, T. A., Skoda, R. C., Hubbard, S. R., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2099 · Cited by 277 · see citing works

Acquisition of the V617F mutation of JAK2 is a late genetic event in a subset of patients with myeloproliferative disorders

Královics, R., Teo, S.-S., Li, S., Theocharides, A. P. A., Buser, A. S., Tichelli, A., & Skoda, R. C. (2006) · Blood · doi:10.1182/blood-2005-11-009605 · Cited by 275 · see citing works

Genomic imbalances including amplification of the tyrosine kinase gene JAK2 in CD30+ Hodgkin cells.

Joos, S., Küpper, M., Ohl, S., von Bonin, F., Mechtersheimer, G., Bentz, M., Marynen, P., Mӧller, P., Pfreundschuh, M. G., Trümper, L. H. P., et al. (2000) · PubMed · Cited by 273 · see citing works

The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor

Lucet, I. S., Fantino, E., Styles, M., Bamert, R. S., Patel, O., Broughton, S. E., Walter, M., Burns, C. J., Treutlein, H., Wilks, A. F., et al. (2005) · Blood · doi:10.1182/blood-2005-06-2413 · Cited by 270 · see citing works

The t(8;9)(p22;p24) Is a Recurrent Abnormality in Chronic and Acute Leukemia that Fuses PCM1 to JAK2

Reiter, A., Walz, C., Watmore, A. E., Schoch, C., Blau, I., Schlegelberger, B., Berger, U., Telford, N., Aruliah, S., Yin, J. A. L., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4263 · Cited by 269 · see citing works

Increased risks of polycythemia vera, essential thrombocythemia, and myelofibrosis among 24 577 first-degree relatives of 11 039 patients with myeloproliferative neoplasms in Sweden

Landgren, O., Goldin, L. R., Kristinsson, S. Y., Helgadottir, E. A., Samuelsson, J., & Björkholm, M. (2008) · Blood · doi:10.1182/blood-2008-03-143602 · Cited by 257 · see citing works

Phase 2 study of CEP-701, an orally available JAK2 inhibitor, in patients with primary or post-polycythemia vera/essential thrombocythemia myelofibrosis

Santos, F. P. D. S., Kantarjian, H. M., Jain, N., Manshouri, T., Thomas, D. A., Garcia‐Manero, G., Kennedy, D., Estrov, Z. E., Cortes, J. E., & Verstovšek, S. (2009) · Blood · doi:10.1182/blood-2009-10-246363 · Cited by 234 · see citing works

JAK2 V617F impairs hematopoietic stem cell function in a conditional knock-in mouse model of JAK2 V617F–positive essential thrombocythemia

Li, J., Spensberger, D., Ahn, J. S., Anand, S., Beer, P. A., Ghevaert, C., Chen, E., Forrai, A., Scott, L. M., Ferreira, R., et al. (2010) · Blood · doi:10.1182/blood-2009-12-259747 · Cited by 206 · see citing works

Fusion Tyrosine Kinases Induce Drug Resistance by Stimulation of Homology-Dependent Recombination Repair, Prolongation of G 2 /M Phase, and Protection from Apoptosis

Słupianek, A., Hoser, G., Majsterek, I., Bronisz, A., Malecki, M. T., Błasiak, J., Fishel, R. A., & Skórski, T. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4189-4201.2002 · Cited by 205 · see citing works

Incidence and diversity of PAX5 fusion genes in childhood acute lymphoblastic leukemia

Nebral, K., Denk, D., Attarbaschi, A., König, M., Mann, G., Haas, O. A., & Strehl, S. (2008) · Leukemia · doi:10.1038/leu.2008.306 · Cited by 204 · see citing works

Polycythemia vera is not initiated by JAK2 mutation

Nussenzveig, R. H., Swierczek, S. I., Jelı́nek, J., Gaikwad, A. S., Liu, E., Verstovšek, S., Prchal, J. F., & Prchal, J. T. (2006) · Experimental Hematology · doi:10.1016/j.exphem.2006.11.012 · Cited by 201 · see citing works

Specific JAK2 mutation (JAK2R683) and multiple gene deletions in Down syndrome acute lymphoblastic leukemia

Kearney, L., de Castro, D. G., Yeung, J., Procter, J., Horsley, S. W., Eguchi‐Ishimae, M., Bateman, C. M., Anderson, K., Chaplin, T., Young, B. D., et al. (2008) · Blood · doi:10.1182/blood-2008-08-170928 · Cited by 187 · see citing works

JAK signaling globally counteracts heterochromatic gene silencing

Shi, S., Calhoun, H. C., Fan, X., Li, J., Le, L. X., & Li, W. X. (2006) · Nature Genetics · doi:10.1038/ng1860 · Cited by 177 · see citing works

JAK2 stimulates homologous recombination and genetic instability: potential implication in the heterogeneity of myeloproliferative disorders

Plo, I., Nakatake, M., Malivert, L., de Villartay, J., Giraudier, S., Villeval, J., Wiesmüller, L., & Vainchenker, W. (2008) · Blood · doi:10.1182/blood-2008-01-134114 · Cited by 176 · see citing works

Distinct Clinical Phenotypes Associated with JAK2V617F Reflect Differential STAT1 Signaling

Chen, E., Beer, P. A., Godfrey, A. L., Ortmann, C. A., Li, J., Costa‐Pereira, A. P., Ingle, C., Dermitzakis, E. T., Campbell, P. J., & Green, A. R. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.013 · Cited by 173 · see citing works

JAK1 and Tyk2 Activation by the Homologous Polycythemia Vera JAK2 V617F Mutation

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Multiple signaling pathways are involved in erythropoietin-independent differentiation of erythroid progenitors in polycythemia vera

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Selective targeting of JAK/STAT signaling is potentiated by Bcl-xL blockade in IL-2–dependent adult T-cell leukemia

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TRIM27 mediates STAT3 activation at retromer-positive structures to promote colitis and colitis-associated carcinogenesis

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STAT3 Activation and Oncogenesis in Lymphoma

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Cytokine receptor signaling is required for the survival of ALK− anaplastic large cell lymphoma, even in the presence of JAK1/STAT3 mutations

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Kinase inhibition, competitive binding and proteasomal degradation: resolving the molecular function of the suppressor of cytokine signaling ( SOCS ) proteins

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Advances in the Discovery of Selective JAK Inhibitors

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Cytokine‐induced megakaryocytic differentiation is regulated by genome‐wide loss of a uSTAT transcriptional program

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Epigenetic gene regulation by Janus kinase 1 in diffuse large B-cell lymphoma

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Pharmacophore and Virtual Screening of JAK3 inhibitors

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O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies

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TYK2: An Upstream Kinase of STATs in Cancer

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Molecular Structure and Function of Janus Kinases: Implications for the Development of Inhibitors

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Inhibition of STAT3 with the Generation 2.5 Antisense Oligonucleotide, AZD9150, Decreases Neuroblastoma Tumorigenicity and Increases Chemosensitivity

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Three Distinct Patterns of Histone H3Y41 Phosphorylation Mark Active Genes

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Cancer gene profiling in non-small cell lung cancers reveals activating mutations in JAK2 and JAK3 with therapeutic implications

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Accumulation of JAK activation loop phosphorylation is linked to type I JAK inhibitor withdrawal syndrome in myelofibrosis

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Structural basis of Janus kinase trans-activation

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SOCS1 is a critical checkpoint in immune homeostasis, inflammation and tumor immunity

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The role of the Janus-faced transcription factor PAX5-JAK2 in acute lymphoblastic leukemia

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Inhibition of protein kinase II (CK2) prevents induced signal transducer and activator of transcription (STAT) 1/3 and constitutive STAT3 activation

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JAK2 Rearrangements Are a Recurrent Alteration in CD30+ Systemic T-Cell Lymphomas With Anaplastic Morphology

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t(8;9)(p22;p24)/PCM1-JAK2 Activates SOCS2 and SOCS3 via STAT5

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Pharmacological Modulation of the Crosstalk between Aberrant Janus Kinase Signaling and Epigenetic Modifiers of the Histone Deacetylase Family to Treat Cancer

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The role of the JAK-STAT pathway and related signal cascades in telomerase activation during the development of hematologic malignancies

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Insights in dynamic kinome reprogramming as a consequence of MEK inhibition in MLL-rearranged AML

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Activating mutations of the gp130/JAK/STAT pathway in human diseases

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Targeting the JAK-STAT pathway in lymphoma: a focus on pacritinib

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The JAK-STAT signaling pathway is differentially activated in CALR-positive compared with JAK2V617F-positive ET patients

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Off-Target V(D)J Recombination Drives Lymphomagenesis and Is Escalated by Loss of the Rag2 C Terminus

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Steering of carcinoma progression by the YIN/YANG interaction of STAT1/STAT3

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Socs36E attenuates STAT signaling to optimize motile cell specification in the Drosophila ovary

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The PAX5‐JAK2 translocation acts as dual‐hit mutation that promotes aggressive B‐cell leukemia via nuclear STAT5 activation

Jurado, S., Fedl, A. S., Jaritz, M., Kostanova‐Poliakova, D., Malin, S., Mullighan, C. G., Strehl, S., Fischer, M., & Busslinger, M. (2022) · The EMBO Journal · doi:10.15252/embj.2021108397 · Cited by 31 · see citing works

Comprehensive Ex Vivo Transposon Mutagenesis Identifies Genes That Promote Growth Factor Independence and Leukemogenesis

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Genomic Profiling of T-Cell Neoplasms Reveals Frequent JAK1 and JAK3 Mutations With Clonal Evasion From Targeted Therapies

Greenplate, A. R., Wang, K., Tripathi, R. M., Palma, N. A., Ali, S. M., Stephens, P. J., Miller, V. A., Shyr, Y., Guo, Y. P., Reddy, N. M., et al. (2018) · JCO Precision Oncology · doi:10.1200/po.17.00019 · Cited by 30 · see citing works

Sex disparities in head & neck cancer driver genes: An analysis of the TCGA dataset

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Untwining Anti-Tumor and Immunosuppressive Effects of JAK Inhibitors—A Strategy for Hematological Malignancies?

Klein, K., Stoiber, D., Sexl, V., & Witalisz‐Siepracka, A. (2021) · Cancers · doi:10.3390/cancers13112611 · Cited by 30 · see citing works

Integrating non-coding RNAs in JAK-STAT regulatory networks

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Inflammatory and tumorigenic effects of environmental pollutants found in particulate matter on lung epithelial cells

Taş, İ., Zhou, R., Park, S., Yang, Y., Gamage, C. D. B., Son, Y., Paik, M., & Kim, H. (2019) · Toxicology in Vitro · doi:10.1016/j.tiv.2019.05.022 · Cited by 29 · see citing works

Emerging therapeutic paradigms to target the dysregulated Janus kinase/signal transducer and activator of transcription pathway in hematological malignancies

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miR-543 regulates the epigenetic landscape of myelofibrosis by targeting TET1 and TET2

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STAT5 inhibition induces TRAIL/DR4 dependent apoptosis in peripheral T-cell lymphoma

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Hypothesis of Opposite Interplay Between the Canonical WNT/beta-catenin Pathway and PPAR Gamma in Primary Central Nervous System Lymphomas

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Important scaffold function of the Janus kinase 2 uncovered by a novel mouse model harboring a Jak2 activation-loop mutation

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Impaired NFAT and NFκB activation are involved in suppression of CD40 ligand expression by Δ9-tetrahydrocannabinol in human CD4+ T cells

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The discovery of 2,5-isomers of triazole-pyrrolopyrimidine as selective Janus kinase 2 (JAK2) inhibitors versus JAK1 and JAK3

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Janus kinase 3 regulates adherens junctions and epithelial mesenchymal transition through β-catenin

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Identification of a novel functional JAK1 S646P mutation in acute lymphoblastic leukemia

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Acute lymphoblastic leukemia secondary to myeloproliferative neoplasms or after lenalidomide exposure

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Understanding the structural features of JAK2 inhibitors: a combined 3D-QSAR, DFT and molecular dynamics study

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A mix of S and ΔS variants of STAT3 enable survival of activated B-cell-like diffuse large B-cell lymphoma cells in culture

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Combining Stochastic Deformation/Relaxation and Intermolecular Contacts Analysis for Extracting Pharmacophores from Ligand–Receptor Complexes

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Histone Modifications and Their Targeting in Lymphoid Malignancies

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Nuclear Import of JAK1 Is Mediated by a Classical NLS and Is Required for Survival of Diffuse Large B-cell Lymphoma

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Characterization of Clozapine-Responsive Human T Cells

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Adapter Protein Shc Regulates Janus Kinase 3 Phosphorylation

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Overexpression of Jak2: A Predictor of Unfavorable Prognosis for Nasopharyngeal Carcinoma

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Icariin ameliorates LPS-induced acute lung injury in mice via complement C5a-C5aR1 and TLR4 signaling pathways

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Systemic ALK-negative anaplastic large cell lymphoma: Insights into morphologic, immunophenotypic, genetic and molecular characteristics

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Malignant hematopoietic cell lines: In vitro models for the study of primary mediastinal B-cell lymphomas

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Conversion of a False Virtual Screen Hit into Selective JAK2 JH2 Domain Binders Using Convergent Design Strategies

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Maintenance of hematopoietic stem cells by tyrosine-unphosphorylated STAT5 and JAK inhibition

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Janus Reveals Another Face: The Biologic Rationale for Targeting Janus Kinase 2 in Lymphoma

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Differential expression analysis of JAK/STAT pathway related genes in breast cancer

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LEE011 and ruxolitinib: a synergistic drug combination for natural killer/T-cell lymphoma (NKTCL)

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Suppression by Δ9-tetrahydrocannabinol of the primary immunoglobulin M response by human peripheral blood B cells is associated with impaired STAT3 activation

Ngaotepprutaram, T., Kaplan, B. L. F., Carney, S., Crawford, R. B., & Kaminski, N. E. (2013) · Toxicology · doi:10.1016/j.tox.2013.05.009 · Cited by 12 · see citing works

Primary Cutaneous CD30-Positive Lymphoproliferative Disorders—Current Therapeutic Approaches with a Focus on Brentuximab Vedotin

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Kinase inactive Tyrosine kinase (Tyk2) Supports Differentiation of Brown fat Cells

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Targeting childhood, adolescent and young adult non‐Hodgkin lymphoma: therapeutic horizons

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Cholinergic and cytoprotective signaling cascades mediate the mitigative effect of erythropoietin on acute radiation syndrome

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JAK2 Mediates the Regulation of Pept1 Expression by Leptin in the Grass Carp (Ctenopharyngodon idella) Intestine

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Mutations and chromosomal rearrangements ofJAK2: not only a myeloid issue

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Acute lymphoblastic leukaemia with T- and B-lineage defining markers

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Chromosome 21 gain is dispensable for transient myeloproliferative disorder driven by a novel GATA1 mutation

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Identification of the Prognostic Value Among Suppressor Of Cytokine Signaling Family Members in Kidney Renal Clear Cell Carcinoma

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Identification of a Novel ZBTB20-JAK2 Fusion by Mate-Pair Sequencing in a Young Adult With B-Lymphoblastic Leukemia/Lymphoma

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Janus Kinase Signaling: Oncogenic Criminal of Lymphoid Cancers

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HiJAKing the epigenome in leukemia and lymphoma

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Janus Kinases in Leukemia

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JAK, an Oncokinase in Hematological Cancer

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JAK Kinases in Leukemias, Lymphomas, and Multiple Myeloma

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