A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1

Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

Darnell, J. E., Kerr, L. M., & Stark, G. R. (1994) · Science · doi:10.1126/science.8197455 · Cited by 6,080

STATs and Gene Regulation

Darnell, J. E. (1997) · Science · doi:10.1126/science.277.5332.1630 · Cited by 3,979

Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis

Fried, M. G., & Crothers, D. M. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.23.6505 · Cited by 2,658

A family of cytokine-inducible inhibitors of signalling

Starr, R., Willson, T. A., Viney, E. M., Murray, L. J. L., Rayner, J. R., Jenkins, B. J., Gonda, T. J., Alexander, W. S., Metcalf, D., Nicola, N. A., et al. (1997) · Nature · doi:10.1038/43206 · Cited by 2,066

JAKS AND STATS: Biological Implications

Leonard, W. J., & O’Shea, J. J. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.293 · Cited by 1,826

TRANSCRIPTIONAL RESPONSES TO POLYPEPTIDE LIGANDS: The JAK-STAT Pathway

Schindler, C., & Darnell, J. E. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.003201 · Cited by 1,808

Targeted Disruption of the Stat1 Gene in Mice Reveals Unexpected Physiologic Specificity in the JAK–STAT Signaling Pathway

Meraz, M. A., White, J. M., Sheehan, K. C. F., Bach, E. A., Rodig, S. J., Dighe, A. S., Kaplan, D. H., Riley, J. K., Greenlund, A. C., Campbell, D., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81288-x · Cited by 1,656

A new protein containing an SH2 domain that inhibits JAK kinases

Endo, T. A., Masuhara, M., Yokouchi, M., Suzuki, R., Sakamoto, H., Mitsui, K., Matsumoto, A., Tanimura, S., Ohtsubo, M., Misawa, H., et al. (1997) · Nature · doi:10.1038/43213 · Cited by 1,408

Endocytosis

Mukherjee, S., Ghosh, R. K., & Maxfield, F. R. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.3.759 · Cited by 1,299

Structure and function of a new STAT-induced STAT inhibitor

Naka, T., Narazaki, M., Hirata, M., Matsumoto, T., Minamoto, S., Aono, A., Nishimoto, N., Kajita, T., Taga, T., Yoshizaki, K., et al. (1997) · Nature · doi:10.1038/43219 · Cited by 1,040

Identification of CXCL11 as a STAT3-Dependent Gene Induced by IFN

Yang, C. H., Wei, L., Pfeffer, S. R., Du, Z., Murti, A., Valentine, W. J., Zheng, Y., & Pfeffer, L. M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.2.986 · Cited by 46

Growth hormone signalling: sprouting links between pathways, human genetics and therapeutic options

Pilecka, I., Whatmore, A. J., van Huijsduijnen, R. H., Destenaves, B., & Clayton, P. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.11.004 · Cited by 46

Negative regulation of STAT92E by an N-terminally truncated STAT protein derived from an alternative promoter sitePreprint

Henriksen, M. A., Betz, A., Fuccillo, M. V., & Darnell, J. E., Jr. (2002) · Genes & Development · doi:10.1101/gad.1020702 · Cited by 45

EnterohemorrhagicEscherichia coliO157:H7 Disrupts Stat1-Mediated Gamma Interferon Signal Transduction in Epithelial Cells

Ceponis, P. J. M., McKay, D. M., Ching, J. C. Y., Pereira, P., & Sherman, P. M. (2003) · Infection and Immunity · doi:10.1128/iai.71.3.1396-1404.2003 · Cited by 42

Modulation of Host Cell Gene Expression through Activation of STAT Transcription Factors by Pasteurella multocida Toxin

Orth, J. H. C., Aktories, K., & Kubatzky, K. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609018200 · Cited by 38

Specific down-regulation of interleukin-12 signaling through induction of phospho-STAT4 protein degradation

Wang, K. S., Zorn, E., & Ritz, J. (2001) · Blood · doi:10.1182/blood.v97.12.3860 · Cited by 38

Cross-talk between interleukin 1β (IL-1β) and IL-6 signalling pathways: IL-1β selectively inhibits IL-6-activated signal transducer and activator of transcription factor 1 (STAT1) by a proteasome-dependent mechanism

Shen, X., Tian, Z., Holtzman, M. J., & Gao, B. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3520913 · Cited by 36

Interferonα Activates NF-κB in JAK1-deficient Cells through aTYK2-dependentPathway

Yang, C. H., Murti, A., Valentine, W. J., Du, Z., & Pfeffer, L. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413721200 · Cited by 35

PAD4 controls tumor immunity via restraining the MHC class II machinery in macrophages

Pitter, M. R., Kryczek, I., Zhang, H., Nagarsheth, N., Xia, H., Wu, Z., Tian, Y., Okła, K., Liao, P., Wang, W., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113942 · Cited by 34

Mathematical modelling of interferon-γ signalling in pancreatic stellate cells reflects and predicts the dynamics of STAT1 pathway activity

Rateitschak, K., Karger, A., Fitzner, B., Lange, F., Olaf Wolkenhauer, A., & Jaster, R. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.09.019 · Cited by 34

Tests for cycling in a signalling pathway

Müller, T. G., Faller, D., Timmer, J., Swameye, I., Sandra, O., & Klingmüller, U. (2004) · Journal of the Royal Statistical Society Series C: Applied Statistics · doi:10.1111/j.1467-9876.2004.05148.x · Cited by 33

Conditioned Medium from EnterohemorrhagicEscherichia coli-Infected T84 Cells Inhibits Signal Transducer and Activator of Transcription 1 Activation by Gamma Interferon

Jandu, N., Ceponis, P. J. M., Kato, S. X., Riff, J. D., McKay, D. M., & Sherman, P. M. (2006) · Infection and Immunity · doi:10.1128/iai.74.3.1809-1818.2006 · Cited by 33

Transcriptional Regulation in Neutrophils: Teaching Old Cells New Tricks

McDonald, P. P. (2004) · Advances in immunology · doi:10.1016/s0065-2776(04)82001-7 · Cited by 32

The Receptor Interaction Region of Tyk2 Contains a Motif Required for Its Nuclear Localization

Ragimbeau, J., Dondi, E., Vasserot, A., Romero, P., Uzé, G., & Pellegrini, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103559200 · Cited by 32

Computational models of the JAK1/2-STAT1 signaling

Gambin, A., Charzyńska, A., Ellert‐Miklaszewska, A., & Rybiński, M. (2013) · JAK-STAT · doi:10.4161/jkst.24672 · Cited by 31

STAT nuclear translocation: potential for pharmacological intervention

Meyer, T., & Vinkemeier, U. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.10.1355 · Cited by 31

A Conserved Motif in the Linker Domain of STAT1 Transcription Factor Is Required for Both Recognition and Release from High-Affinity DNA-Binding Sites

Hüntelmann, B., Staab, J., Herrmann‐Lingen, C., & Meyer, T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097633 · Cited by 31

FER Kinase Activation of Stat3 Is Determined by the N-terminal Sequence

Priel-Halachmi, S., Ben‐Dor, I., Shpungin, S., Tennenbaum, T., Molavani, H., Bachrach, M., Salzberg, S., & Nir, U. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003402200 · Cited by 28

Phospho-Ser727 triggers a multistep inactivation of STAT3 by rapid dissociation of pY705–SH2 through C-terminal tail modulation

Yang, J., Kunimoto, H., Katayama, B., Zhao, H., Shiromizu, T., Wang, L., Ozawa, T., Tomonaga, T., Tsuruta, D., & Nakajima, K. (2019) · International Immunology · doi:10.1093/intimm/dxz061 · Cited by 26

Phenotypic variability, not noise, accounts for most of the cell-to-cell heterogeneity in IFN-γ and oncostatin M signaling responses

Topolewski, P., Zakrzewska, K. E., Walczak, J., Nienałtowski, K., Müller‐Newen, G., Singh, A., & Komorowski, M. (2022) · Science Signaling · doi:10.1126/scisignal.abd9303 · Cited by 26

Orf virus inhibits interferon stimulated gene expression and modulates the JAK/STAT signalling pathway

Harvey, R. P., McCaughan, C. A., Wise, L. M., Mercer, A. A., & Fleming, S. B. (2015) · Virus Research · doi:10.1016/j.virusres.2015.06.014 · Cited by 26

Termination of IL‐6‐induced STAT activation is independent of receptor internalization but requires de novo protein synthesis

Thiel, S., Sommer, U., Kortylewski, M., Haan, C., Behrmann, I., Heinrich, P. C., & Graeve, L. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01276-x · Cited by 29

Association of 2',5'-Oligoadenylate Synthetase with the Prolactin (PRL) Receptor: Alteration in PRL-Inducible Stat1 (Signal Transducer and Activator of Transcription 1) Signaling to the IRF-1 (Interferon-Regulatory Factor 1) Promoter

McAveney, K. M., Book, M. L., Ling, P., Chebath, J., & Yu‐Lee, L. (2000) · Molecular Endocrinology · doi:10.1210/me.14.2.295 · Cited by 25

Elucidating the crosstalk mechanism between IFN-gamma and IL-6 via mathematical modelling

Qi, Y.-F., Huang, Y., Wang, H., Zhang, Y., Bao, Y., Sun, L., Wu, Y., Yu, C., Song, Z., Zheng, L., et al. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-41 · Cited by 27

Genetic Interactions of STAT3 and Anticancer Drug Development

Fang, B. (2014) · Cancers · doi:10.3390/cancers6010494 · Cited by 25

A Novel Disrupter of Telomere Silencing 1-like (DOT1L) Interaction Is Required for Signal Transducer and Activator of Transcription 1 (STAT1)-activated Gene Expression

Shah, S., & Henriksen, M. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284190 · Cited by 23

Role of the JAK/STAT Signal Transduction Pathway in the Regulation of Gene Expression in CNS

Dell’Albani, P., Santangelo, R., Torrisi, L. L., Nicoletti, V. G., & Stella, A. M. G. (2003) · Neurochemical Research · doi:10.1023/a:1021644027850 · Cited by 23

Interleukin-6 inhibition of peroxisome proliferator-activated receptor alpha expression is mediated by JAK2- and PI3K-induced STAT1/3 in HepG2 hepatocyte cells

Chew, G.-S., Myers, S., Shu‐Chien, A. C., & Muhammad, T. S. T. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1896-z · Cited by 22

The C-terminal half-fragment of the Sendai virus C protein prevents the gamma-activated factor from binding to a gamma-activated sequence site

Gotoh, B., Komatsu, T., Takeuchi, K., & Yokoo, J. (2003) · Virology · doi:10.1016/s0042-6822(03)00590-7 · Cited by 22

Nuclear phosphatases and the proteasome in suppression of STAT1 activity in hepatocytes

Liu, D., Scafidi, J., Prada, A. E., Zahedi, K. A., & Davis, A. E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02694-3 · Cited by 21

Nucleocytoplasmic Shuttling of STATs. A Target for Intervention?

Ernst, S., & Müller‐Newen, G. (2019) · Cancers · doi:10.3390/cancers11111815 · Cited by 20

SOCS3 Attenuates GM-CSF/IFN-γ-Mediated Inflammation During Spontaneous Spinal Cord Regeneration

Zhang, X., He, B., Li, H., Wang, Y., Zhou, Y., Wang, W., Song, T., Gu, X., Gu, X., Luo, Y., et al. (2020) · Neuroscience Bulletin · doi:10.1007/s12264-020-00493-8 · Cited by 20

Interferon-γ

Schreiber, G., & Schreiber, R. D. (2003) · Elsevier eBooks · doi:10.1016/b978-012689663-3/50028-4 · Cited by 19

Identification of a distinct subset of disease-associated gain-of-function missense mutations in the STAT1 coiled-coil domain as system mutants

Petersen, J., Staab, J., Bader, O., Buhl, T., Ívetic, A., & Meyer, T. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.07.008 · Cited by 17

Disruption of canonical TGFβ-signaling in murine coronary progenitor cells by low level arsenic

Allison, P. B., Huang, T., Broka, D. M., Parker, P., Barnett, J. V., & Camenisch, T. D. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.04.035 · Cited by 17

Mechanisms of Signal Transduction from Receptors of Type I and Type II Cytokines

Fujii, H. (2007) · Journal of Immunotoxicology · doi:10.1080/15476910601154779 · Cited by 17

T Lymphocyte Activation – An Inside Overview

Aringer, M. (2002) · Acta Medica Austriaca · doi:10.1046/j.1563-2571.2002.01044.x · Cited by 16

Promoter Occupancy of STAT1 in Interferon Responses Is Regulated by Processive Transcription

Wiesauer, I., Gaumannmüller, C., Steinparzer, I., Strobl, B., & Kovarik, P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01097-14 · Cited by 16

Interferon Research: Impact on Understanding Transcriptional Control

Darnell, J. E., Jr. (2007) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-71329-6_8 · Cited by 16

Human Gene Control by Vital Oncogenes: Revisiting a Theoretical Model and Its Implications for Targeted Cancer Therapy

Willis, R. E. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms13010316 · Cited by 15

Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA

Koch, V., Staab, J., Ruppert, V., & Meyer, T. (2012) · BMC Cell Biology · doi:10.1186/1471-2121-13-22 · Cited by 15

Signal Transducer and Activator of Transcription Proteins at the Nexus of Immunodeficiency, Autoimmunity and Cancer

Liongue, C., Sobah, M. L., & Ward, A. C. (2023) · Biomedicines · doi:10.3390/biomedicines12010045 · Cited by 15

Protein Tyrosine Phosphatase PTP1 Negatively Regulates Dictyostelium STATa and Is Required for Proper Cell-Type Proportioning

Early, A. E., Gamper, M., Moniakis, J., Kim, E., Hunter, T. R., Williams, J. G., & Firtel, R. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0171 · Cited by 14

Prolactin activation of IRF‐1 transcription involves changes in histone acetylation

McAlexander, M. B., & Yu‐Lee, L. (2001) · FEBS Letters · doi:10.1016/s0014-5793(00)02385-1 · Cited by 12

IFN-αβ Secreted during Infection Is Necessary but Not Sufficient for Negative Feedback Regulation of IFN-αβ Signaling by Mycobacterium tuberculosis

Prabhakar, S., Qiao, Y., Canova, A., Tse, D. B., & Pine, R. I. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.2.1003 · Cited by 11

STAT module can function as a biphasic amplitude filter

Mayya, V., & Loew, L. M. (2005) · Systems Biology · doi:10.1049/sb:20045037 · Cited by 11

Stimulation of the ICAM‐1 gene transcription by the peroxovanadium compound [bpV(Pic)] involves STAT‐1 but not NF‐κB activation in 293 cells

Audette, M., Larouche, L., Lussier, I., & Fugère, N. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02054.x · Cited by 11

Requirement for multiple activation signals by anti-inflammatory feedback in macrophages

Ray, J. C. J., & Kirschner, D. E. (2006) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2005.11.037 · Cited by 11

The PIAS Protein Family and TC-PTP

Liu, B., & Shuai, K. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_6 · Cited by 10

Different patterns of regulation of Tyr-phosphorylated STAT1 and STAT3 in human hepatoma Hep3B cells by the phosphatase inhibitor orthovanadate

Sehgal, P. B., Kumar, V., Guo, G. G., & Murray, W. C. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(03)00050-x · Cited by 10

Review: Dynamic Stability of the Interphase Nucleus in Health and Disease

Tartakoff, A. M., Lichtenstein, M., Nanduri, J., & Tsao, H.-M. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4225 · Cited by 9

MBD5 regulates NMDA receptor expression and seizures by inhibiting Stat1 transcription

Tang, F.-L., Zhang, X., Ke, P., Liu, J., Zhang, Z., Hu, D., Gu, J., Zhang, H., Guo, H., Zang, Q.-W., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106103 · Cited by 8

Transcription Factor Activation in Human Neutrophils

Cloutier, A., & McDonald, P. P. (2003) · KARGER eBooks · doi:10.1159/000071553 · Cited by 11

Proinflammatory Stem Cell Signaling in Cardiac Ischemia

Herrmann, J. L., Markel, T. A., Abarbanell, A. M., Weil, B. R., Wang, M., Wang, Y., Tan, J., & Meldrum, D. R. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2434 · Cited by 8

La vía JAK-STAT de señalización intracelular y su repercusión en oncogénesis, inmunomodulación y desarrollo

Duarte, R., & Frank, D. (2000) · Medicina Clínica · doi:10.1016/s0025-7753(00)71252-8 · Cited by 7

Arsenite Disrupts Zinc-Dependent TGFβ2-SMAD Activity During Murine Cardiac Progenitor Cell Differentiation

Huang, T., Ditzel, E. J., Perrera, A. B., Broka, D. M., & Camenisch, T. D. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv191 · Cited by 7

Identification of the JAK-STAT pathway in canine splenic hemangiosarcoma, thyroid carcinoma, mast cell tumor, and anal sac adenocarcinoma

Cletzer, E., Klahn, S. L., Dervisis, N. G., & LeRoith, T. (2019) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2019.109996 · Cited by 7

Characterization of Japanese flounder (Paralichthys olivaceus) STAT members: An immune-related gene family involved in Edwardsiella tarda and temperature stress

Chen, J., Han, P., Liu, X., & Wang, X. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.108818 · Cited by 7

Cardiac Epithelial-Mesenchymal Transition Is Blocked by Monomethylarsonous Acid (III)

Huang, T., Barnett, J. V., & Camenisch, T. D. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu170 · Cited by 7

Signal transduction by prolactin receptors

Yu‐Lee, L. (2002) · Neuroimmune biology · doi:10.1016/s1567-7443(02)80011-4 · Cited by 7

DNA binding reduces the dissociation rate of STAT1 dimers and impairs the interdimeric exchange of protomers

Riebeling, T., Staab, J., Herrmann‐Lingen, C., & Meyer, T. (2014) · BMC Biochemistry · doi:10.1186/s12858-014-0028-z · Cited by 5

JAK and STAT gene mutations and JAK-STAT pathway activation in lympho- and myeloproliferative neoplasms

Łączak, M., Kuczyńska, M., Grygier, J., Andrzejewska, D., Grochowska, W., Gulaczyk, H., & Lewandowski, K. C. (2022) · Hematology in Clinical Practice · doi:10.5603/hcp.a2021.0013 · Cited by 5

Inhibition of the gamma interferon response by a Sendai virus C protein mutant with no STAT1‐binding ability

Gotoh, B., Takeuchi, K., & Komatsu, T. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.05.001 · Cited by 5

Prolactin and Growth Hormone Receptors

Yu‐Lee, L., & Jeay, S. (2002) · Endocrine updates · doi:10.1007/978-1-4757-3600-7_7 · Cited by 6

Transcriptional synergy in human aortic endothelial cells is vulnerable to combination p300/CBP and BET bromodomain inhibition

Bracken, R. C., Davison, L. M., Buehler, D. P., Fulton, M. E., Carson, E. E., Sheng, Q., Stolze, L. K., Guillermier, C., Steinhauser, M. L., & Brown, J. D. (2024) · iScience · doi:10.1016/j.isci.2024.110011 · Cited by 4

Structure and function of the T-cell protein tyrosine phosphatase

Bourdeau, A., Heinonen, K. M., Brunet, D. V., Tailor, P., Lapp, W. S., & Tremblay, M. L. (2003) · Topics in current genetics · doi:10.1007/978-3-540-40035-6_10 · Cited by 4

Off-target effects of protein tyrosine phosphatase inhibitors on oncostatin M-treated human epidermal keratinocytes: the phosphatase targeting STAT1 remains unknown

Hong, B. V., Lee, J. H., & Rice, R. H. (2020) · PeerJ · doi:10.7717/peerj.9504 · Cited by 3

DUOX expression in human keratinocytes and bronchial epithelial cells: Influence of vanadate

Hill, T., & Rice, R. H. (2017) · Toxicology in Vitro · doi:10.1016/j.tiv.2017.10.010 · Cited by 5

Activation of the JAK/STAT pathway in human neutrophils by NDMA

Ratajczak–Wrona, W., Jabłońska, E., Garley, M., Jablonski, J., Radziwon, P., & Iwaniuk, A. (2013) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1302-60 · Cited by 3

Assessing Sequence-Specific DNA Binding and Transcriptional Activity of STAT1 Transcription Factor

Meyer, T., & Vinkemeier, U. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-738-9_8 · Cited by 3

Mechanisms and Biological Consequences of STAT Signaling by Cytokines that Share the Common Cytokine Receptor γ Chain, γc

Lin, J., & Leonard, W. J. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_29 · Cited by 3

STAT Proteins as Molecular Targets for Cancer Therapy

Buettner, R., Kortylewski, M., Pardoll, D. M., Yu, H., & Jove, R. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_41 · Cited by 3

STAT Pathway of Intracellular Signaling (Review)

Никольский, Н. Н., & Vasilenko, K. P. (2000) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1023/a:1017514502690 · Cited by 2

Self-association of STAT Proteins from Monomers to Paracrystals

Droescher, M., & Vinkemeier, U. (2012) · Springer eBooks · doi:10.1007/978-3-7091-0891-8_4 · Cited by 2

Tyrosine Protein Kinases and Adaptive Immunity: TCR, BCR, Soluble Tyrosine Kinases and NFAT

Gomperts, B. D., Kramer, I. M., & Tatham, P. E. R. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-369441-6.00017-9 · Cited by 1

The pathogenic T387A missense mutation in the gene encoding signal transducer and activator of transcription 1 exhibits a differential gene expression profile

Staab, J., Schwämmle, T., & Meyer, T. (2020) · Molecular Immunology · doi:10.1016/j.molimm.2020.10.005 · Cited by 1

Constitutively Active STATs and Cellular Transformation

Dechow, T. N., & Bromberg, J. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_40 · Cited by 1

Molekulare Determinanten zur sequenzspezifischen DNA-Bindung des Transkriptionsfaktors STAT1

Hüntelmann, B. (2018) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6655 · Cited by 1

Bystander IFN-y activity promotes widespread and sustained cytokine signaling altering the tumor microenvironment

Thibaut, R. (2019) · theses.fr (ABES) · doi:10.70675/ac790b4cz9f35z418cz89f3zeb164a5bcb06 · Cited by 1

Immunoediting and angiogenesis in ovarian cancer

Duncan, T. J. (2010) · Nottingham ePrints (University of Nottingham)

The Data-Based Mathematical Modeling and Parameter Identification in JAK-STAT Signaling Pathway by Using a Hybrid Evolutionary Algorithm

Zhang, W., & Zou, X. (2010) · Lecture notes in computer science · doi:10.1007/978-3-642-16493-4_52

Efeito dos ácidos graxos sobre a via de sinalização da interleucina-2 em linfócitos humanos.

Gorjão, R. (2008) · doi:10.11606/t.42.2008.tde-15092008-134403

Identification and analysis of JAK/STAT pathway target genes in Drosophila melanogaster

Bina, S. (2009) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3177

Expression des SOCS-1 et SOCS-3 par les lymphocytes T humains en réponse à des cytokines immuno-modulatrices

El‐Khoury, L. (2009) · doi:10.71781/27957

Review Signaling by STATs

Ivashkiv, L. B., & Hu, X. (2013)

Drug Discovery Approaches Targeting the JAK/STAT Pathway

Seidel, H. M., & Rosen, J. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_45

The role of Ken&Barbie in JAK/STAT signalling during development of Drosophila melanogaster

Arbouzova, N. I. (2005)

The role of parallel signaling pathways in maintaining lymphoid cell survival

Nagy, Z. S., & Kirken, R. A. (2002)

Modulation der hepatischen Akut-Phase-Reaktion und der antiviralen Antwort durch pro-apoptotische Stimuli

Mathematisch-naturwissenschaftlichen Fakultät, I. (2009)

Cytokines and Signaling

David, M. (2005) · CRC Press eBooks · doi:10.1201/9781420039849.ch4

Activating the Adaptive Immune System

Kramer, I. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394803-8.00015-2

Contribution of Protein Tyrosine Phosphateses to the Ontogeny and Progression of Chronic Myeloid Leukemia

Tremblay, M. L. (2006) · doi:10.21236/ada462811

Impact of Toxoplasma gondii on STAT1 activity and epigenetic regulation during IFN-γ signaling of its host cell

Nast, R. (2018) · doi:10.53846/goediss-7026

Die Bedeutung der Coiled-coil-Domäne für die Inaktivierung des Transkriptionsfaktors STAT1

Petersen, J. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7960

Identifying Mechanisms Used by Adherent-invasive Escherichia coli Associated with Crohn Disease to Evade the Immune System

Ossa, J. C. (2012) · TSpace (University of Toronto)

The importance of homotypic interactions of unphosphorylated STAT proteins in cytokine-induced signal transduction

Menon, P. R. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8488

Interferon Signaling

Levrero, M. (2005) · Springer eBooks · doi:10.1007/3-540-27194-5_13

Faculty Opinions recommendation of A phosphorylation-acetylation switch regulates STAT1 signaling.

Sharrocks, A. D. (2009) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1147405.604579

Reevaluation der potenziell onkogenen, Lymphom-assoziierten Missense-Mutation D427H im STAT3-Molekül

Behrendsen, L. S. (2023) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9644

Deletion of SH2D5 alleviates epileptic seizures and NMDAR expression via autophagic degradation of STAT1

Guo, H., Zhang, H., Zhang, C., Shen, Y., Jiang, L., Yang, M., Zhang, Y., Zhang, N., Zhang, R., Yu, R., et al. (2025) · JCI Insight · doi:10.1172/jci.insight.191347

Identification of a Nuclear Stat1 Protein Tyrosine Phosphatase

ten Hoeve, J., de Jesus Ibarra-Sanchez, M., Fu, Y., Zhu, W., Tremblay, M., David, M., & Shuai, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5662-5668.2002 · Cited by 507

The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.

Haspel, R. L., Salditt‐Georgieff, M., & Darnell, J. E. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01016.x · Cited by 312

DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1

Meyer, T., Marg, A., Lemke, P., Wiesner, B., & Vinkemeier, U. (2003) · Genes & Development · doi:10.1101/gad.268003 · Cited by 161

SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei

Wu, T., Hong, Y. K., Wang, X., Ling, M. Y., Dragoi, A. M., Chung, A. S., Campbell, A. G., Han, Z.-Y., Feng, G., & Chin, Y. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207536200 · Cited by 170

Nuclear export signal located within the DNA‐binding domain of the STAT1transcription factor

McBride, K. M., McDonald, C., & Reich, N. C. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.6196 · Cited by 196