(en) Taiga Tamiya, Ikko Kashiwagi, Reiko Takahashi et Hideo Yasukawa, « Suppressors of Cytokine Signaling (SOCS) Proteins and JAK/STAT Pathways: Regulation of T-Cell Inflammation by SOCS1 and SOCS3 », Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 31, no 5, , p. 980–985 (ISSN1079-5642 et 1524-4636, DOI10.1161/ATVBAHA.110.207464, lire en ligne, consulté le )
annualreviews.org
(en) Warren S. Alexander et Douglas J. Hilton, « T he R ole of S uppressors of C ytokine S ignaling (SOCS) P roteins in R egulation of the I mmune R esponse », Annual Review of Immunology, vol. 22, no 1, , p. 503–529 (ISSN0732-0582 et 1545-3278, DOI10.1146/annurev.immunol.22.091003.090312, lire en ligne, consulté le )
asm.org
mcb.asm.org
(en) T L Yi, J L Cleveland et J N Ihle, « Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. », Molecular and Cellular Biology, vol. 12, no 2, , p. 836–846 (ISSN0270-7306 et 1098-5549, PMID1732748, PMCIDPMC364317, DOI10.1128/MCB.12.2.836, lire en ligne, consulté le )
biologists.com
journals.biologists.com
(en) Jason S. Rawlings, Kristin M. Rosler et Douglas A. Harrison, « The JAK/STAT signaling pathway », Journal of Cell Science, (ISSN0021-9533, DOI10.1242/jcs.00963, lire en ligne, consulté le )
Christian Schindler, David E. Levy et Thomas Decker, « JAK-STAT Signaling: From Interferons to Cytokines », Journal of Biological Chemistry, vol. 282, no 28, , p. 20059–20063 (ISSN0021-9258, DOI10.1074/jbc.r700016200, lire en ligne, consulté le )
Ling Liu, Kevin M. McBride et Nancy C. Reich, « STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3 », Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no 23, , p. 8150–8155 (ISSN0027-8424, PMID15919823, PMCID1149424, DOI10.1073/pnas.0501643102, lire en ligne, consulté le )
Jinbo Yang, Jing Huang, Maupali Dasgupta et Nathan Sears, « Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 50, , p. 21499–21504 (ISSN0027-8424, PMID21098664, PMCID3003019, DOI10.1073/pnas.1016147107, lire en ligne, consulté le )
Li Ma, Jin-song Gao, Yingjie Guan et Xiaoyan Shi, « Acetylation modulates prolactin receptor dimerization », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 45, , p. 19314–19319 (ISSN0027-8424, PMID20962278, PMCID2984224, DOI10.1073/pnas.1010253107, lire en ligne, consulté le )
Yuhong Shen, Karni Schlessinger, Xuejun Zhu et Eric Meffre, « Essential Role of STAT3 in Postnatal Survival and Growth Revealed by Mice Lacking STAT3 Serine 727 Phosphorylation », Molecular and Cellular Biology, vol. 24, no 1, , p. 407–419 (ISSN0270-7306, PMID14673173, DOI10.1128/MCB.24.1.407-419.2004, lire en ligne, consulté le )
(en) Matthew Paulson, Carolyn Press, Eric Smith et Naoko Tanese, « IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff », Nature Cell Biology, vol. 4, no 2, , p. 140–147 (ISSN1476-4679, DOI10.1038/ncb747, lire en ligne, consulté le )
(en) Jason S. Rawlings, Kristin M. Rosler et Douglas A. Harrison, « The JAK/STAT signaling pathway », Journal of Cell Science, (ISSN0021-9533, DOI10.1242/jcs.00963, lire en ligne, consulté le )
(en) Neeraj Jain, Tong Zhang, Siok Lyn Fong et Cheh Peng Lim, « Repression of Stat3 activity by activation of mitogen-activated protein kinase (MAPK) », Oncogene, vol. 17, no 24, , p. 3157–3167 (ISSN1476-5594, DOI10.1038/sj.onc.1202238, lire en ligne, consulté le )
(en) Satoshi Yamada, Satoru Shiono, Akiko Joo et Akihiko Yoshimura, « Control mechanism of JAK/STAT signal transduction pathway », FEBS Letters, vol. 534, nos 1-3, , p. 190–196 (ISSN0014-5793 et 1873-3468, DOI10.1016/S0014-5793(02)03842-5, lire en ligne, consulté le )
(en) Abhay Singh, Arul Jayaraman et Juergen Hahn, « Modeling regulatory mechanisms in IL-6 signal transduction in hepatocytes », Biotechnology and Bioengineering, vol. 95, no 5, , p. 850–862 (DOI10.1002/bit.21026, lire en ligne, consulté le )
(en) Ryland D. Mortlock, Senta K. Georgia et Stacey D. Finley, « Dynamic Regulation of JAK-STAT Signaling Through the Prolactin Receptor Predicted by Computational Modeling », Cellular and Molecular Bioengineering, vol. 14, no 1, , p. 15–30 (ISSN1865-5033, PMID33633812, PMCIDPMC7878662, DOI10.1007/s12195-020-00647-8, lire en ligne, consulté le )
(en) Ke Shuai et Bin Liu, « Regulation of gene-activation pathways by PIAS proteins in the immune system », Nature Reviews Immunology, vol. 5, no 8, , p. 593–605 (ISSN1474-1741, DOI10.1038/nri1667, lire en ligne, consulté le )
Daniela Ungureanu, Sari Vanhatupa, Juha Grönholm et Jorma J. Palvimo, « SUMO-1 conjugation selectively modulates STAT1-mediated gene responses », Blood, vol. 106, no 1, , p. 224–226 (ISSN0006-4971 et 1528-0020, DOI10.1182/blood-2004-11-4514, lire en ligne, consulté le )
Mathias Droescher, Andreas Begitt, Andreas Marg et Martin Zacharias, « Cytokine-induced Paracrystals Prolong the Activity of Signal Transducers and Activators of Transcription (STAT) and Provide a Model for the Regulation of Protein Solubility by Small Ubiquitin-like Modifier (SUMO) », Journal of Biological Chemistry, vol. 286, no 21, , p. 18731–18746 (ISSN0021-9258, PMID21460228, PMCIDPMC3099690, DOI10.1074/jbc.m111.235978, lire en ligne, consulté le )
(en) T L Yi, J L Cleveland et J N Ihle, « Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. », Molecular and Cellular Biology, vol. 12, no 2, , p. 836–846 (ISSN0270-7306 et 1098-5549, PMID1732748, PMCIDPMC364317, DOI10.1128/MCB.12.2.836, lire en ligne, consulté le )
(en) Latanya M. Scott, Harshani R. Lawrence, Said M. Sebti et Nicholas J. Lawrence, « Targeting Protein Tyrosine Phosphatases for Anticancer Drug Discovery », Current Pharmaceutical Design, vol. 16, no 16, , p. 1843–1862 (PMID20337577, PMCIDPMC3076191, DOI10.2174/138161210791209027, lire en ligne, consulté le ).
H. Bone, U. Dechert, F. Jirik et J. W. Schrader, « SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates », The Journal of Biological Chemistry, vol. 272, no 22, , p. 14470–14476 (ISSN0021-9258, PMID9162089, DOI10.1074/jbc.272.22.14470, lire en ligne, consulté le )
Bonnie L. Lyons, Michael A. Lynes, Lisa Burzenski et Melissa J. Joliat, « Mechanisms of anemia in SHP-1 protein tyrosine phosphatase-deficient "viable motheaten" mice », Experimental Hematology, vol. 31, no 3, , p. 234–243 (ISSN0301-472X, PMID12644021, DOI10.1016/s0301-472x(02)01031-7, lire en ligne, consulté le )
(en) M. F. Johan, D. T. Bowen, M. E. Frew et A. C. Goodeve, « Aberrant methylation of the negative regulators RASSFIA , SHP‐1 and SOCS‐1 in myelodysplastic syndromes and acute myeloid leukaemia », British Journal of Haematology, vol. 129, no 1, , p. 60–65 (ISSN0007-1048 et 1365-2141, DOI10.1111/j.1365-2141.2005.05412.x, lire en ligne, consulté le )
Min You et Zhizhuang Zhao, « Positive Effects of SH2 Domain-containing Tyrosine Phosphatase SHP-1 on Epidermal Growth Factor- and Interferon-γ-stimulated Activation of STAT Transcription Factors in HeLa Cells », Journal of Biological Chemistry, vol. 272, no 37, , p. 23376–23381 (ISSN0021-9258, DOI10.1074/jbc.272.37.23376, lire en ligne, consulté le )
Benjamin G. Neel, Haihua Gu et Lily Pao, « The ‘Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling », Trends in Biochemical Sciences, vol. 28, no 6, , p. 284–293 (ISSN0968-0004, DOI10.1016/s0968-0004(03)00091-4, lire en ligne, consulté le )
Tong R. Wu, Y. Kate Hong, Xu-Dong Wang et Mike Y. Ling, « SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei », Journal of Biological Chemistry, vol. 277, no 49, , p. 47572–47580 (ISSN0021-9258, DOI10.1074/jbc.m207536200, lire en ligne, consulté le )
Yuhong Chen, Renren Wen, Shoua Yang et James Schuman, « Identification of Shp-2 as a Stat5A Phosphatase », Journal of Biological Chemistry, vol. 278, no 19, , p. 16520–16527 (ISSN0021-9258, DOI10.1074/jbc.m210572200, lire en ligne, consulté le )
(en) Eric E. Zhang, Emilie Chapeau, Kazuki Hagihara et Gen-Sheng Feng, « Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism », Proceedings of the National Academy of Sciences, vol. 101, no 45, , p. 16064–16069 (ISSN0027-8424 et 1091-6490, PMID15520383, PMCIDPMC528739, DOI10.1073/pnas.0405041101, lire en ligne, consulté le )
Yuehai Ke, Jacqueline Lesperance, Eric E. Zhang et Emilie A. Bard-Chapeau, « Conditional Deletion of Shp2 in the Mammary Gland Leads to Impaired Lobulo-alveolar Outgrowth and Attenuated Stat5 Activation », Journal of Biological Chemistry, vol. 281, no 45, , p. 34374–34380 (ISSN0021-9258, PMID16959766, PMCIDPMC1761121, DOI10.1074/jbc.m607325200, lire en ligne, consulté le )
(en) Wen-Mei Yu, Teresa S. Hawley, Robert G. Hawley et Cheng-Kui Qu, « Catalytic-dependent and -independent roles of SHP-2 tyrosine phosphatase in interleukin-3 signaling », Oncogene, vol. 22, no 38, , p. 5995–6004 (ISSN1476-5594, DOI10.1038/sj.onc.1206846, lire en ligne, consulté le )
Takechiyo Yamada, Daocheng Zhu, Andrew Saxon et Ke Zhang, « CD45 Controls Interleukin-4-mediated IgE Class Switch Recombination in Human B Cells through Its Function as a Janus Kinase Phosphatase », Journal of Biological Chemistry, vol. 277, no 32, , p. 28830–28835 (ISSN0021-9258, DOI10.1074/jbc.m201781200, lire en ligne, consulté le )
(en) Junko Irie-Sasaki, Takehiko Sasaki, Wataru Matsumoto et Anne Opavsky, « CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling », Nature, vol. 409, no 6818, , p. 349–354 (ISSN1476-4687, DOI10.1038/35053086, lire en ligne, consulté le )
(en) Warren S. Alexander et Douglas J. Hilton, « T he R ole of S uppressors of C ytokine S ignaling (SOCS) P roteins in R egulation of the I mmune R esponse », Annual Review of Immunology, vol. 22, no 1, , p. 503–529 (ISSN0732-0582 et 1545-3278, DOI10.1146/annurev.immunol.22.091003.090312, lire en ligne, consulté le )
(en) Taiga Tamiya, Ikko Kashiwagi, Reiko Takahashi et Hideo Yasukawa, « Suppressors of Cytokine Signaling (SOCS) Proteins and JAK/STAT Pathways: Regulation of T-Cell Inflammation by SOCS1 and SOCS3 », Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 31, no 5, , p. 980–985 (ISSN1079-5642 et 1524-4636, DOI10.1161/ATVBAHA.110.207464, lire en ligne, consulté le )
Scott J Rodig, Marco A Meraz, J.Michael White et Pat A Lampe, « Disruption of the Jak1 Gene Demonstrates Obligatory and Nonredundant Roles of the Jaks in Cytokine-Induced Biologic Responses », Cell, vol. 93, no 3, , p. 373–383 (ISSN0092-8674, DOI10.1016/s0092-8674(00)81166-6, lire en ligne, consulté le )
(en) Hong Luo, Paul Rose, Dwayne Barber et William P. Hanratty, « Mutation in the Jak Kinase JH2 Domain Hyperactivates Drosophila and Mammalian Jak-Stat Pathways », Molecular and Cellular Biology, vol. 17, no 3, , p. 1562–1571 (ISSN1098-5549, PMID9032284, PMCIDPMC231882, DOI10.1128/MCB.17.3.1562, lire en ligne, consulté le )
Riqiang Yan, Stephen Small, Claude Desplan et Charles R Dearolf, « Identification of a Stat Gene That Functions in Drosophila Development », Cell, vol. 84, no 3, , p. 421–430 (ISSN0092-8674, DOI10.1016/s0092-8674(00)81287-8, lire en ligne, consulté le )
(en) Marko Pesu, Fabio Candotti, Matthew Husa et Sigrun R. Hofmann, « Jak3, severe combined immunodeficiency, and a new class of immunosuppressive drugs », Immunological Reviews, vol. 203, no 1, , p. 127–142 (ISSN0105-2896 et 1600-065X, DOI10.1111/j.0105-2896.2005.00220.x, lire en ligne, consulté le )
(en) Katharina Welsch, Julia Holstein, Arian Laurence et Kamran Ghoreschi, « Targeting JAK/STAT signalling in inflammatory skin diseases with small molecule inhibitors », European Journal of Immunology, vol. 47, no 7, , p. 1096–1107 (ISSN0014-2980 et 1521-4141, DOI10.1002/eji.201646680, lire en ligne, consulté le )
(en) Donata Vercelli, « Discovering susceptibility genes for asthma and allergy », Nature Reviews Immunology, vol. 8, no 3, , p. 169–182 (ISSN1474-1741, DOI10.1038/nri2257, lire en ligne, consulté le )
(en) S. J. Thomas, J. A. Snowden, M. P. Zeidler et S. J. Danson, « The role of JAK/STAT signalling in the pathogenesis, prognosis and treatment of solid tumours », British Journal of Cancer, vol. 113, no 3, , p. 365–371 (ISSN1532-1827, PMID26151455, PMCIDPMC4522639, DOI10.1038/bjc.2015.233, lire en ligne, consulté le )
Bernd Groner et Viktoria von Manstein, « Jak Stat signaling and cancer: Opportunities, benefits and side effects of targeted inhibition », Molecular and Cellular Endocrinology, jak-Stat signaling and cancer, vol. 451, , p. 1–14 (ISSN0303-7207, DOI10.1016/j.mce.2017.05.033, lire en ligne, consulté le )
Christian Schindler, David E. Levy et Thomas Decker, « JAK-STAT Signaling: From Interferons to Cytokines », Journal of Biological Chemistry, vol. 282, no 28, , p. 20059–20063 (ISSN0021-9258, DOI10.1074/jbc.r700016200, lire en ligne, consulté le )
(en) Ryland D. Mortlock, Senta K. Georgia et Stacey D. Finley, « Dynamic Regulation of JAK-STAT Signaling Through the Prolactin Receptor Predicted by Computational Modeling », Cellular and Molecular Bioengineering, vol. 14, no 1, , p. 15–30 (ISSN1865-5033, PMID33633812, PMCIDPMC7878662, DOI10.1007/s12195-020-00647-8, lire en ligne, consulté le )
Daniela Ungureanu, Sari Vanhatupa, Juha Grönholm et Jorma J. Palvimo, « SUMO-1 conjugation selectively modulates STAT1-mediated gene responses », Blood, vol. 106, no 1, , p. 224–226 (ISSN0006-4971 et 1528-0020, DOI10.1182/blood-2004-11-4514, lire en ligne, consulté le )
Mathias Droescher, Andreas Begitt, Andreas Marg et Martin Zacharias, « Cytokine-induced Paracrystals Prolong the Activity of Signal Transducers and Activators of Transcription (STAT) and Provide a Model for the Regulation of Protein Solubility by Small Ubiquitin-like Modifier (SUMO) », Journal of Biological Chemistry, vol. 286, no 21, , p. 18731–18746 (ISSN0021-9258, PMID21460228, PMCIDPMC3099690, DOI10.1074/jbc.m111.235978, lire en ligne, consulté le )
Min You et Zhizhuang Zhao, « Positive Effects of SH2 Domain-containing Tyrosine Phosphatase SHP-1 on Epidermal Growth Factor- and Interferon-γ-stimulated Activation of STAT Transcription Factors in HeLa Cells », Journal of Biological Chemistry, vol. 272, no 37, , p. 23376–23381 (ISSN0021-9258, DOI10.1074/jbc.272.37.23376, lire en ligne, consulté le )
Benjamin G. Neel, Haihua Gu et Lily Pao, « The ‘Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling », Trends in Biochemical Sciences, vol. 28, no 6, , p. 284–293 (ISSN0968-0004, DOI10.1016/s0968-0004(03)00091-4, lire en ligne, consulté le )
Tong R. Wu, Y. Kate Hong, Xu-Dong Wang et Mike Y. Ling, « SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei », Journal of Biological Chemistry, vol. 277, no 49, , p. 47572–47580 (ISSN0021-9258, DOI10.1074/jbc.m207536200, lire en ligne, consulté le )
Yuhong Chen, Renren Wen, Shoua Yang et James Schuman, « Identification of Shp-2 as a Stat5A Phosphatase », Journal of Biological Chemistry, vol. 278, no 19, , p. 16520–16527 (ISSN0021-9258, DOI10.1074/jbc.m210572200, lire en ligne, consulté le )
Yuehai Ke, Jacqueline Lesperance, Eric E. Zhang et Emilie A. Bard-Chapeau, « Conditional Deletion of Shp2 in the Mammary Gland Leads to Impaired Lobulo-alveolar Outgrowth and Attenuated Stat5 Activation », Journal of Biological Chemistry, vol. 281, no 45, , p. 34374–34380 (ISSN0021-9258, PMID16959766, PMCIDPMC1761121, DOI10.1074/jbc.m607325200, lire en ligne, consulté le )
Takechiyo Yamada, Daocheng Zhu, Andrew Saxon et Ke Zhang, « CD45 Controls Interleukin-4-mediated IgE Class Switch Recombination in Human B Cells through Its Function as a Janus Kinase Phosphatase », Journal of Biological Chemistry, vol. 277, no 32, , p. 28830–28835 (ISSN0021-9258, DOI10.1074/jbc.m201781200, lire en ligne, consulté le )
Scott J Rodig, Marco A Meraz, J.Michael White et Pat A Lampe, « Disruption of the Jak1 Gene Demonstrates Obligatory and Nonredundant Roles of the Jaks in Cytokine-Induced Biologic Responses », Cell, vol. 93, no 3, , p. 373–383 (ISSN0092-8674, DOI10.1016/s0092-8674(00)81166-6, lire en ligne, consulté le )
Riqiang Yan, Stephen Small, Claude Desplan et Charles R Dearolf, « Identification of a Stat Gene That Functions in Drosophila Development », Cell, vol. 84, no 3, , p. 421–430 (ISSN0092-8674, DOI10.1016/s0092-8674(00)81287-8, lire en ligne, consulté le )
(en) Latanya M. Scott, Harshani R. Lawrence, Said M. Sebti et Nicholas J. Lawrence, « Targeting Protein Tyrosine Phosphatases for Anticancer Drug Discovery », Current Pharmaceutical Design, vol. 16, no 16, , p. 1843–1862 (PMID20337577, PMCIDPMC3076191, DOI10.2174/138161210791209027, lire en ligne, consulté le ).
Christian Schindler, David E. Levy et Thomas Decker, « JAK-STAT Signaling: From Interferons to Cytokines », Journal of Biological Chemistry, vol. 282, no 28, , p. 20059–20063 (ISSN0021-9258, DOI10.1074/jbc.r700016200, lire en ligne, consulté le )
Ling Liu, Kevin M. McBride et Nancy C. Reich, « STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3 », Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no 23, , p. 8150–8155 (ISSN0027-8424, PMID15919823, PMCID1149424, DOI10.1073/pnas.0501643102, lire en ligne, consulté le )
Jinbo Yang, Jing Huang, Maupali Dasgupta et Nathan Sears, « Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 50, , p. 21499–21504 (ISSN0027-8424, PMID21098664, PMCID3003019, DOI10.1073/pnas.1016147107, lire en ligne, consulté le )
Li Ma, Jin-song Gao, Yingjie Guan et Xiaoyan Shi, « Acetylation modulates prolactin receptor dimerization », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 45, , p. 19314–19319 (ISSN0027-8424, PMID20962278, PMCID2984224, DOI10.1073/pnas.1010253107, lire en ligne, consulté le )
Yuhong Shen, Karni Schlessinger, Xuejun Zhu et Eric Meffre, « Essential Role of STAT3 in Postnatal Survival and Growth Revealed by Mice Lacking STAT3 Serine 727 Phosphorylation », Molecular and Cellular Biology, vol. 24, no 1, , p. 407–419 (ISSN0270-7306, PMID14673173, DOI10.1128/MCB.24.1.407-419.2004, lire en ligne, consulté le )
(en) Matthew Paulson, Carolyn Press, Eric Smith et Naoko Tanese, « IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff », Nature Cell Biology, vol. 4, no 2, , p. 140–147 (ISSN1476-4679, DOI10.1038/ncb747, lire en ligne, consulté le )
(en) Jason S. Rawlings, Kristin M. Rosler et Douglas A. Harrison, « The JAK/STAT signaling pathway », Journal of Cell Science, (ISSN0021-9533, DOI10.1242/jcs.00963, lire en ligne, consulté le )
(en) Neeraj Jain, Tong Zhang, Siok Lyn Fong et Cheh Peng Lim, « Repression of Stat3 activity by activation of mitogen-activated protein kinase (MAPK) », Oncogene, vol. 17, no 24, , p. 3157–3167 (ISSN1476-5594, DOI10.1038/sj.onc.1202238, lire en ligne, consulté le )
(en) Satoshi Yamada, Satoru Shiono, Akiko Joo et Akihiko Yoshimura, « Control mechanism of JAK/STAT signal transduction pathway », FEBS Letters, vol. 534, nos 1-3, , p. 190–196 (ISSN0014-5793 et 1873-3468, DOI10.1016/S0014-5793(02)03842-5, lire en ligne, consulté le )
(en) Ryland D. Mortlock, Senta K. Georgia et Stacey D. Finley, « Dynamic Regulation of JAK-STAT Signaling Through the Prolactin Receptor Predicted by Computational Modeling », Cellular and Molecular Bioengineering, vol. 14, no 1, , p. 15–30 (ISSN1865-5033, PMID33633812, PMCIDPMC7878662, DOI10.1007/s12195-020-00647-8, lire en ligne, consulté le )
(en) Ke Shuai et Bin Liu, « Regulation of gene-activation pathways by PIAS proteins in the immune system », Nature Reviews Immunology, vol. 5, no 8, , p. 593–605 (ISSN1474-1741, DOI10.1038/nri1667, lire en ligne, consulté le )
Daniela Ungureanu, Sari Vanhatupa, Juha Grönholm et Jorma J. Palvimo, « SUMO-1 conjugation selectively modulates STAT1-mediated gene responses », Blood, vol. 106, no 1, , p. 224–226 (ISSN0006-4971 et 1528-0020, DOI10.1182/blood-2004-11-4514, lire en ligne, consulté le )
Mathias Droescher, Andreas Begitt, Andreas Marg et Martin Zacharias, « Cytokine-induced Paracrystals Prolong the Activity of Signal Transducers and Activators of Transcription (STAT) and Provide a Model for the Regulation of Protein Solubility by Small Ubiquitin-like Modifier (SUMO) », Journal of Biological Chemistry, vol. 286, no 21, , p. 18731–18746 (ISSN0021-9258, PMID21460228, PMCIDPMC3099690, DOI10.1074/jbc.m111.235978, lire en ligne, consulté le )
(en) T L Yi, J L Cleveland et J N Ihle, « Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. », Molecular and Cellular Biology, vol. 12, no 2, , p. 836–846 (ISSN0270-7306 et 1098-5549, PMID1732748, PMCIDPMC364317, DOI10.1128/MCB.12.2.836, lire en ligne, consulté le )
H. Bone, U. Dechert, F. Jirik et J. W. Schrader, « SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates », The Journal of Biological Chemistry, vol. 272, no 22, , p. 14470–14476 (ISSN0021-9258, PMID9162089, DOI10.1074/jbc.272.22.14470, lire en ligne, consulté le )
Bonnie L. Lyons, Michael A. Lynes, Lisa Burzenski et Melissa J. Joliat, « Mechanisms of anemia in SHP-1 protein tyrosine phosphatase-deficient "viable motheaten" mice », Experimental Hematology, vol. 31, no 3, , p. 234–243 (ISSN0301-472X, PMID12644021, DOI10.1016/s0301-472x(02)01031-7, lire en ligne, consulté le )
(en) M. F. Johan, D. T. Bowen, M. E. Frew et A. C. Goodeve, « Aberrant methylation of the negative regulators RASSFIA , SHP‐1 and SOCS‐1 in myelodysplastic syndromes and acute myeloid leukaemia », British Journal of Haematology, vol. 129, no 1, , p. 60–65 (ISSN0007-1048 et 1365-2141, DOI10.1111/j.1365-2141.2005.05412.x, lire en ligne, consulté le )
Min You et Zhizhuang Zhao, « Positive Effects of SH2 Domain-containing Tyrosine Phosphatase SHP-1 on Epidermal Growth Factor- and Interferon-γ-stimulated Activation of STAT Transcription Factors in HeLa Cells », Journal of Biological Chemistry, vol. 272, no 37, , p. 23376–23381 (ISSN0021-9258, DOI10.1074/jbc.272.37.23376, lire en ligne, consulté le )
Benjamin G. Neel, Haihua Gu et Lily Pao, « The ‘Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling », Trends in Biochemical Sciences, vol. 28, no 6, , p. 284–293 (ISSN0968-0004, DOI10.1016/s0968-0004(03)00091-4, lire en ligne, consulté le )
Tong R. Wu, Y. Kate Hong, Xu-Dong Wang et Mike Y. Ling, « SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei », Journal of Biological Chemistry, vol. 277, no 49, , p. 47572–47580 (ISSN0021-9258, DOI10.1074/jbc.m207536200, lire en ligne, consulté le )
Yuhong Chen, Renren Wen, Shoua Yang et James Schuman, « Identification of Shp-2 as a Stat5A Phosphatase », Journal of Biological Chemistry, vol. 278, no 19, , p. 16520–16527 (ISSN0021-9258, DOI10.1074/jbc.m210572200, lire en ligne, consulté le )
(en) Eric E. Zhang, Emilie Chapeau, Kazuki Hagihara et Gen-Sheng Feng, « Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism », Proceedings of the National Academy of Sciences, vol. 101, no 45, , p. 16064–16069 (ISSN0027-8424 et 1091-6490, PMID15520383, PMCIDPMC528739, DOI10.1073/pnas.0405041101, lire en ligne, consulté le )
Yuehai Ke, Jacqueline Lesperance, Eric E. Zhang et Emilie A. Bard-Chapeau, « Conditional Deletion of Shp2 in the Mammary Gland Leads to Impaired Lobulo-alveolar Outgrowth and Attenuated Stat5 Activation », Journal of Biological Chemistry, vol. 281, no 45, , p. 34374–34380 (ISSN0021-9258, PMID16959766, PMCIDPMC1761121, DOI10.1074/jbc.m607325200, lire en ligne, consulté le )
(en) Wen-Mei Yu, Teresa S. Hawley, Robert G. Hawley et Cheng-Kui Qu, « Catalytic-dependent and -independent roles of SHP-2 tyrosine phosphatase in interleukin-3 signaling », Oncogene, vol. 22, no 38, , p. 5995–6004 (ISSN1476-5594, DOI10.1038/sj.onc.1206846, lire en ligne, consulté le )
Takechiyo Yamada, Daocheng Zhu, Andrew Saxon et Ke Zhang, « CD45 Controls Interleukin-4-mediated IgE Class Switch Recombination in Human B Cells through Its Function as a Janus Kinase Phosphatase », Journal of Biological Chemistry, vol. 277, no 32, , p. 28830–28835 (ISSN0021-9258, DOI10.1074/jbc.m201781200, lire en ligne, consulté le )
(en) Junko Irie-Sasaki, Takehiko Sasaki, Wataru Matsumoto et Anne Opavsky, « CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling », Nature, vol. 409, no 6818, , p. 349–354 (ISSN1476-4687, DOI10.1038/35053086, lire en ligne, consulté le )
(en) Warren S. Alexander et Douglas J. Hilton, « T he R ole of S uppressors of C ytokine S ignaling (SOCS) P roteins in R egulation of the I mmune R esponse », Annual Review of Immunology, vol. 22, no 1, , p. 503–529 (ISSN0732-0582 et 1545-3278, DOI10.1146/annurev.immunol.22.091003.090312, lire en ligne, consulté le )
(en) Taiga Tamiya, Ikko Kashiwagi, Reiko Takahashi et Hideo Yasukawa, « Suppressors of Cytokine Signaling (SOCS) Proteins and JAK/STAT Pathways: Regulation of T-Cell Inflammation by SOCS1 and SOCS3 », Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 31, no 5, , p. 980–985 (ISSN1079-5642 et 1524-4636, DOI10.1161/ATVBAHA.110.207464, lire en ligne, consulté le )
Scott J Rodig, Marco A Meraz, J.Michael White et Pat A Lampe, « Disruption of the Jak1 Gene Demonstrates Obligatory and Nonredundant Roles of the Jaks in Cytokine-Induced Biologic Responses », Cell, vol. 93, no 3, , p. 373–383 (ISSN0092-8674, DOI10.1016/s0092-8674(00)81166-6, lire en ligne, consulté le )
(en) Hong Luo, Paul Rose, Dwayne Barber et William P. Hanratty, « Mutation in the Jak Kinase JH2 Domain Hyperactivates Drosophila and Mammalian Jak-Stat Pathways », Molecular and Cellular Biology, vol. 17, no 3, , p. 1562–1571 (ISSN1098-5549, PMID9032284, PMCIDPMC231882, DOI10.1128/MCB.17.3.1562, lire en ligne, consulté le )
Riqiang Yan, Stephen Small, Claude Desplan et Charles R Dearolf, « Identification of a Stat Gene That Functions in Drosophila Development », Cell, vol. 84, no 3, , p. 421–430 (ISSN0092-8674, DOI10.1016/s0092-8674(00)81287-8, lire en ligne, consulté le )
(en) Marko Pesu, Fabio Candotti, Matthew Husa et Sigrun R. Hofmann, « Jak3, severe combined immunodeficiency, and a new class of immunosuppressive drugs », Immunological Reviews, vol. 203, no 1, , p. 127–142 (ISSN0105-2896 et 1600-065X, DOI10.1111/j.0105-2896.2005.00220.x, lire en ligne, consulté le )
(en) Katharina Welsch, Julia Holstein, Arian Laurence et Kamran Ghoreschi, « Targeting JAK/STAT signalling in inflammatory skin diseases with small molecule inhibitors », European Journal of Immunology, vol. 47, no 7, , p. 1096–1107 (ISSN0014-2980 et 1521-4141, DOI10.1002/eji.201646680, lire en ligne, consulté le )
(en) Donata Vercelli, « Discovering susceptibility genes for asthma and allergy », Nature Reviews Immunology, vol. 8, no 3, , p. 169–182 (ISSN1474-1741, DOI10.1038/nri2257, lire en ligne, consulté le )
(en) S. J. Thomas, J. A. Snowden, M. P. Zeidler et S. J. Danson, « The role of JAK/STAT signalling in the pathogenesis, prognosis and treatment of solid tumours », British Journal of Cancer, vol. 113, no 3, , p. 365–371 (ISSN1532-1827, PMID26151455, PMCIDPMC4522639, DOI10.1038/bjc.2015.233, lire en ligne, consulté le )
Bernd Groner et Viktoria von Manstein, « Jak Stat signaling and cancer: Opportunities, benefits and side effects of targeted inhibition », Molecular and Cellular Endocrinology, jak-Stat signaling and cancer, vol. 451, , p. 1–14 (ISSN0303-7207, DOI10.1016/j.mce.2017.05.033, lire en ligne, consulté le )
(en) Matthew Paulson, Carolyn Press, Eric Smith et Naoko Tanese, « IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff », Nature Cell Biology, vol. 4, no 2, , p. 140–147 (ISSN1476-4679, DOI10.1038/ncb747, lire en ligne, consulté le )
(en) Neeraj Jain, Tong Zhang, Siok Lyn Fong et Cheh Peng Lim, « Repression of Stat3 activity by activation of mitogen-activated protein kinase (MAPK) », Oncogene, vol. 17, no 24, , p. 3157–3167 (ISSN1476-5594, DOI10.1038/sj.onc.1202238, lire en ligne, consulté le )
(en) Ke Shuai et Bin Liu, « Regulation of gene-activation pathways by PIAS proteins in the immune system », Nature Reviews Immunology, vol. 5, no 8, , p. 593–605 (ISSN1474-1741, DOI10.1038/nri1667, lire en ligne, consulté le )
(en) Wen-Mei Yu, Teresa S. Hawley, Robert G. Hawley et Cheng-Kui Qu, « Catalytic-dependent and -independent roles of SHP-2 tyrosine phosphatase in interleukin-3 signaling », Oncogene, vol. 22, no 38, , p. 5995–6004 (ISSN1476-5594, DOI10.1038/sj.onc.1206846, lire en ligne, consulté le )
(en) Junko Irie-Sasaki, Takehiko Sasaki, Wataru Matsumoto et Anne Opavsky, « CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling », Nature, vol. 409, no 6818, , p. 349–354 (ISSN1476-4687, DOI10.1038/35053086, lire en ligne, consulté le )
(en) Donata Vercelli, « Discovering susceptibility genes for asthma and allergy », Nature Reviews Immunology, vol. 8, no 3, , p. 169–182 (ISSN1474-1741, DOI10.1038/nri2257, lire en ligne, consulté le )
(en) S. J. Thomas, J. A. Snowden, M. P. Zeidler et S. J. Danson, « The role of JAK/STAT signalling in the pathogenesis, prognosis and treatment of solid tumours », British Journal of Cancer, vol. 113, no 3, , p. 365–371 (ISSN1532-1827, PMID26151455, PMCIDPMC4522639, DOI10.1038/bjc.2015.233, lire en ligne, consulté le )
Ling Liu, Kevin M. McBride et Nancy C. Reich, « STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3 », Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no 23, , p. 8150–8155 (ISSN0027-8424, PMID15919823, PMCID1149424, DOI10.1073/pnas.0501643102, lire en ligne, consulté le )
Jinbo Yang, Jing Huang, Maupali Dasgupta et Nathan Sears, « Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 50, , p. 21499–21504 (ISSN0027-8424, PMID21098664, PMCID3003019, DOI10.1073/pnas.1016147107, lire en ligne, consulté le )
Li Ma, Jin-song Gao, Yingjie Guan et Xiaoyan Shi, « Acetylation modulates prolactin receptor dimerization », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 45, , p. 19314–19319 (ISSN0027-8424, PMID20962278, PMCID2984224, DOI10.1073/pnas.1010253107, lire en ligne, consulté le )
Yuhong Shen, Karni Schlessinger, Xuejun Zhu et Eric Meffre, « Essential Role of STAT3 in Postnatal Survival and Growth Revealed by Mice Lacking STAT3 Serine 727 Phosphorylation », Molecular and Cellular Biology, vol. 24, no 1, , p. 407–419 (ISSN0270-7306, PMID14673173, DOI10.1128/MCB.24.1.407-419.2004, lire en ligne, consulté le )
(en) Ryland D. Mortlock, Senta K. Georgia et Stacey D. Finley, « Dynamic Regulation of JAK-STAT Signaling Through the Prolactin Receptor Predicted by Computational Modeling », Cellular and Molecular Bioengineering, vol. 14, no 1, , p. 15–30 (ISSN1865-5033, PMID33633812, PMCIDPMC7878662, DOI10.1007/s12195-020-00647-8, lire en ligne, consulté le )
Mathias Droescher, Andreas Begitt, Andreas Marg et Martin Zacharias, « Cytokine-induced Paracrystals Prolong the Activity of Signal Transducers and Activators of Transcription (STAT) and Provide a Model for the Regulation of Protein Solubility by Small Ubiquitin-like Modifier (SUMO) », Journal of Biological Chemistry, vol. 286, no 21, , p. 18731–18746 (ISSN0021-9258, PMID21460228, PMCIDPMC3099690, DOI10.1074/jbc.m111.235978, lire en ligne, consulté le )
(en) T L Yi, J L Cleveland et J N Ihle, « Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. », Molecular and Cellular Biology, vol. 12, no 2, , p. 836–846 (ISSN0270-7306 et 1098-5549, PMID1732748, PMCIDPMC364317, DOI10.1128/MCB.12.2.836, lire en ligne, consulté le )
(en) Latanya M. Scott, Harshani R. Lawrence, Said M. Sebti et Nicholas J. Lawrence, « Targeting Protein Tyrosine Phosphatases for Anticancer Drug Discovery », Current Pharmaceutical Design, vol. 16, no 16, , p. 1843–1862 (PMID20337577, PMCIDPMC3076191, DOI10.2174/138161210791209027, lire en ligne, consulté le ).
H. Bone, U. Dechert, F. Jirik et J. W. Schrader, « SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates », The Journal of Biological Chemistry, vol. 272, no 22, , p. 14470–14476 (ISSN0021-9258, PMID9162089, DOI10.1074/jbc.272.22.14470, lire en ligne, consulté le )
Bonnie L. Lyons, Michael A. Lynes, Lisa Burzenski et Melissa J. Joliat, « Mechanisms of anemia in SHP-1 protein tyrosine phosphatase-deficient "viable motheaten" mice », Experimental Hematology, vol. 31, no 3, , p. 234–243 (ISSN0301-472X, PMID12644021, DOI10.1016/s0301-472x(02)01031-7, lire en ligne, consulté le )
(en) Eric E. Zhang, Emilie Chapeau, Kazuki Hagihara et Gen-Sheng Feng, « Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism », Proceedings of the National Academy of Sciences, vol. 101, no 45, , p. 16064–16069 (ISSN0027-8424 et 1091-6490, PMID15520383, PMCIDPMC528739, DOI10.1073/pnas.0405041101, lire en ligne, consulté le )
Yuehai Ke, Jacqueline Lesperance, Eric E. Zhang et Emilie A. Bard-Chapeau, « Conditional Deletion of Shp2 in the Mammary Gland Leads to Impaired Lobulo-alveolar Outgrowth and Attenuated Stat5 Activation », Journal of Biological Chemistry, vol. 281, no 45, , p. 34374–34380 (ISSN0021-9258, PMID16959766, PMCIDPMC1761121, DOI10.1074/jbc.m607325200, lire en ligne, consulté le )
(en) Hong Luo, Paul Rose, Dwayne Barber et William P. Hanratty, « Mutation in the Jak Kinase JH2 Domain Hyperactivates Drosophila and Mammalian Jak-Stat Pathways », Molecular and Cellular Biology, vol. 17, no 3, , p. 1562–1571 (ISSN1098-5549, PMID9032284, PMCIDPMC231882, DOI10.1128/MCB.17.3.1562, lire en ligne, consulté le )
(en) S. J. Thomas, J. A. Snowden, M. P. Zeidler et S. J. Danson, « The role of JAK/STAT signalling in the pathogenesis, prognosis and treatment of solid tumours », British Journal of Cancer, vol. 113, no 3, , p. 365–371 (ISSN1532-1827, PMID26151455, PMCIDPMC4522639, DOI10.1038/bjc.2015.233, lire en ligne, consulté le )
H. Bone, U. Dechert, F. Jirik et J. W. Schrader, « SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates », The Journal of Biological Chemistry, vol. 272, no 22, , p. 14470–14476 (ISSN0021-9258, PMID9162089, DOI10.1074/jbc.272.22.14470, lire en ligne, consulté le )
Bonnie L. Lyons, Michael A. Lynes, Lisa Burzenski et Melissa J. Joliat, « Mechanisms of anemia in SHP-1 protein tyrosine phosphatase-deficient "viable motheaten" mice », Experimental Hematology, vol. 31, no 3, , p. 234–243 (ISSN0301-472X, PMID12644021, DOI10.1016/s0301-472x(02)01031-7, lire en ligne, consulté le )
(en) Eric E. Zhang, Emilie Chapeau, Kazuki Hagihara et Gen-Sheng Feng, « Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism », Proceedings of the National Academy of Sciences, vol. 101, no 45, , p. 16064–16069 (ISSN0027-8424 et 1091-6490, PMID15520383, PMCIDPMC528739, DOI10.1073/pnas.0405041101, lire en ligne, consulté le )
Bernd Groner et Viktoria von Manstein, « Jak Stat signaling and cancer: Opportunities, benefits and side effects of targeted inhibition », Molecular and Cellular Endocrinology, jak-Stat signaling and cancer, vol. 451, , p. 1–14 (ISSN0303-7207, DOI10.1016/j.mce.2017.05.033, lire en ligne, consulté le )
(en) Hong Luo, Paul Rose, Dwayne Barber et William P. Hanratty, « Mutation in the Jak Kinase JH2 Domain Hyperactivates Drosophila and Mammalian Jak-Stat Pathways », Molecular and Cellular Biology, vol. 17, no 3, , p. 1562–1571 (ISSN1098-5549, PMID9032284, PMCIDPMC231882, DOI10.1128/MCB.17.3.1562, lire en ligne, consulté le )
(en) Abhay Singh, Arul Jayaraman et Juergen Hahn, « Modeling regulatory mechanisms in IL-6 signal transduction in hepatocytes », Biotechnology and Bioengineering, vol. 95, no 5, , p. 850–862 (DOI10.1002/bit.21026, lire en ligne, consulté le )
(en) M. F. Johan, D. T. Bowen, M. E. Frew et A. C. Goodeve, « Aberrant methylation of the negative regulators RASSFIA , SHP‐1 and SOCS‐1 in myelodysplastic syndromes and acute myeloid leukaemia », British Journal of Haematology, vol. 129, no 1, , p. 60–65 (ISSN0007-1048 et 1365-2141, DOI10.1111/j.1365-2141.2005.05412.x, lire en ligne, consulté le )
(en) Marko Pesu, Fabio Candotti, Matthew Husa et Sigrun R. Hofmann, « Jak3, severe combined immunodeficiency, and a new class of immunosuppressive drugs », Immunological Reviews, vol. 203, no 1, , p. 127–142 (ISSN0105-2896 et 1600-065X, DOI10.1111/j.0105-2896.2005.00220.x, lire en ligne, consulté le )
(en) Katharina Welsch, Julia Holstein, Arian Laurence et Kamran Ghoreschi, « Targeting JAK/STAT signalling in inflammatory skin diseases with small molecule inhibitors », European Journal of Immunology, vol. 47, no 7, , p. 1096–1107 (ISSN0014-2980 et 1521-4141, DOI10.1002/eji.201646680, lire en ligne, consulté le )
(en) Satoshi Yamada, Satoru Shiono, Akiko Joo et Akihiko Yoshimura, « Control mechanism of JAK/STAT signal transduction pathway », FEBS Letters, vol. 534, nos 1-3, , p. 190–196 (ISSN0014-5793 et 1873-3468, DOI10.1016/S0014-5793(02)03842-5, lire en ligne, consulté le )