Cited by 6,080Cytokine Signaling Pathways and Interactionsinterferon and immune responsesNF-κB Signaling Pathways

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

Darnell, James E., Kerr, lan M., Stark, George R.·1994·Science

DOI 10.1126/science.8197455

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Abstract

Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.

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Zhong, Z., Wen, Z., & Darnell, J. E. (1994) · Science · doi:10.1126/science.8140422 · Cited by 2,070
Interferon-alpha regulates nuclear translocation and DNA-binding affinity of ISGF3, a multimeric transcriptional activator.
Kessler, D. S., Veals, S. A., Fu, X. Y., & Levy, D. E. (1990) · Genes & Development · doi:10.1101/gad.4.10.1753 · Cited by 312
Enhancer‐like interferon responsive sequences of the human and murine (2′‐5′) oligoadenylate synthetase gene promoters.
Cohen, B., Peretz, D., Vaiman, D., Benech, P., & Chebath, J. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02958.x · Cited by 180

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Show all 3 references

Research works printed but not linked: 84

AGUET, M, MOLECULAR-CLONING AND EXPRESSION OF THE HUMAN INTERFERON-GAMMA RECEPTOR, CELL 55: 273 (1988). · DOI
ALMENDRAL, J.M., COMPLEXITY OF THE EARLY GENETIC RESPONSE TO GROWTH-FACTORS IN MOUSE FIBROBLASTS, MOLECULAR AND CELLULAR BIOLOGY 8: 2140 (1988).
10.1016/0092-8674(93)90415-M · DOI
BEADLING, C, ISOLATION OF INTERLEUKIN-2-INDUCED IMMEDIATE-EARLY GENES, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 2719 (1993).
BLANAR, M.A., TRANSCRIPTIONAL ACTIVATION OF HLA-DR-ALPHA BY INTERFERON-GAMMA REQUIRES A TRANS-ACTING PROTEIN, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 85: 4672 (1988).
10.1126/science.7504325 · DOI
COLAMONICI, O.R., MULTICHAIN STRUCTURE OF THE IFN-ALPHA RECEPTOR ON HEMATOPOIETIC-CELLS, JOURNAL OF IMMUNOLOGY 148: 2126 (1992). · DOI
DALE, T.C., OVERLAPPING SITES FOR CONSTITUTIVE AND INDUCED DNA-BINDING FACTORS INVOLVED IN INTERFERON-STIMULATED TRANSCRIPTION, EMBO JOURNAL 8: 831 (1989). · DOI
DALE, T.C., RAPID ACTIVATION BY INTERFERON-ALPHA OF A LATENT DNA-BINDING PROTEIN PRESENT IN THE CYTOPLASM OF UNTREATED CELLS, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 86: 1203 (1989).
10.1126/science.1496402 · DOI
DECKER, T, INTERACTIONS OF ALPHA-INTERFERON AND GAMMA-INTERFERON IN THE TRANSCRIPTIONAL REGULATION OF THE GENE ENCODING A GUANYLATE-BINDING PROTEIN, EMBO JOURNAL 8: 2009 (1989). · DOI
DECKER, T, CYTOPLASMIC ACTIVATION OF GAF, AN IFN-GAMMA-REGULATED DNA-BINDING FACTOR, EMBO JOURNAL 10: 927 (1991). · DOI
FIRMBACHKRAFT, I, TYK2, PROTOTYPE OF A NOVEL CLASS OF NONRECEPTOR TYROSINE KINASE GENES, ONCOGENE 5: 1329 (1990).
10.1126/science.1650499 · DOI
10.1093/nar/9.23.6505 · DOI
FRIEDMAN, R.L., TRANSCRIPTIONAL AND POSTTRANSCRIPTIONAL REGULATION OF INTERFERON-INDUCED GENE-EXPRESSION IN HUMAN-CELLS, CELL 38: 745 (1984). · DOI
10.1016/0092-8674(92)90106-M · DOI
FU, X.Y., ISGF3, THE TRANSCRIPTIONAL ACTIVATOR INDUCED BY INTERFERON-ALPHA, CONSISTS OF MULTIPLE INTERACTING POLYPEPTIDE-CHAINS, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 87: 8555 (1990).
FU, X.Y., THE PROTEINS OF ISGF-3, THE INTERFERON ALPHA-INDUCED TRANSCRIPTIONAL ACTIVATOR, DEFINE A GENE FAMILY INVOLVED IN SIGNAL TRANSDUCTION, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 89: 7840 (1992).
GARRER, M.M., NUCLEIC ACIDS RES 9: 3047 (1981). · DOI
10.1126/science.1898992 · DOI
GREENBERG, M.E., NERVE GROWTH-FACTOR AND EPIDERMAL GROWTH-FACTOR INDUCE RAPID TRANSIENT CHANGES IN PROTO-ONCOGENE TRANSCRIPTION IN PC12 CELLS, JOURNAL OF BIOLOGICAL CHEMISTRY 260: 14101 (1985). · DOI
10.1038/311433a0 · DOI
HARADA, H, STRUCTURALLY SIMILAR BUT FUNCTIONALLY DISTINCT FACTORS, IRF-1 AND IRF-2, BIND TO THE SAME REGULATORY ELEMENTS OF IFN AND IFN-INDUCIBLE GENES, CELL 58: 729 (1989). · DOI
HARPUR, A.G., ONCOGENE 7: 895 (1992).
HEMMI, S, A NOVEL MEMBER OF THE INTERFERON RECEPTOR FAMILY COMPLEMENTS FUNCTIONALITY OF THE MURINE INTERFERON-GAMMA RECEPTOR IN HUMAN-CELLS, CELL 76: 803 (1994). · DOI
IGARASHI, K, IN-VITRO ACTIVATION OF A TRANSCRIPTION FACTOR BY GAMMA-INTERFERON REQUIRES A MEMBRANE-ASSOCIATED TYROSINE KINASE AND IS MIMICKED BY VANADATE, MOLECULAR AND CELLULAR BIOLOGY 13: 3984 (1993).
Improta, T., Proceedings of the National Academy of Sciences of the United States of America 91: 4776 (1994).
JOHN, J, ISOLATION AND CHARACTERIZATION OF A NEW MUTANT HUMAN CELL-LINE UNRESPONSIVE TO ALPHA-INTERFERONS AND BETA-INTERFERONS, MOLECULAR AND CELLULAR BIOLOGY 11: 4189 (1991).
KAHN, K.D., PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 6806 (1993).
KANNO, Y, THE GENOMIC STRUCTURE OF THE MURINE ICSBP GENE REVEALS THE PRESENCE OF THE GAMMA INTERFERON-RESPONSIVE ELEMENT, TO WHICH AN ISGF3-ALPHA SUBUNIT (OR SIMILAR) MOLECULE BINDS, MOLECULAR AND CELLULAR BIOLOGY 13: 3951 (1993).
KESSLER, D.S., 2 INTERFERON-INDUCED NUCLEAR FACTORS BIND A SINGLE PROMOTER ELEMENT IN INTERFERON-STIMULATED GENES, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 85: 8521 (1988).
10.1126/science.1708916 · DOI
10.1126/science.7694370 · DOI
10.1126/science.8378773 · DOI
LARNER, A.C., TRANSCRIPTIONAL INDUCTION BY INTERFERON - NEW PROTEIN(S) DETERMINE THE EXTENT AND LENGTH OF THE INDUCTION, JOURNAL OF BIOLOGICAL CHEMISTRY 261: 453 (1986). · DOI
LARNER, A.C., TRANSCRIPTIONAL INDUCTION OF 2 GENES IN HUMAN-CELLS BY BETA-INTERFERON, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES 81: 6733 (1984).
LEE, T.H., ISOLATION AND CHARACTERIZATION OF 8 TUMOR NECROSIS FACTOR-INDUCED GENE-SEQUENCES FROM HUMAN FIBROBLASTS, MOLECULAR AND CELLULAR BIOLOGY 10: 1982 (1990).
LEVY, D, NEW BIOL 2: 923 (1990).
LEVY, D.E., SYNERGISTIC INTERACTION BETWEEN INTERFERON-ALPHA AND INTERFERON-GAMMA THROUGH INDUCED SYNTHESIS OF ONE SUBUNIT OF THE TRANSCRIPTION FACTOR ISGF3, EMBO JOURNAL 9: 1105 (1990). · DOI
LEVY, D.E., CYTOPLASMIC ACTIVATION OF ISGF3, THE POSITIVE REGULATOR OF INTERFERON-ALPHA-STIMULATED TRANSCRIPTION, RECONSTITUTED INVITRO, GENES & DEVELOPMENT 3: 1362 (1989). · DOI
LEVY, D.E., INTERFERON-INDUCED NUCLEAR FACTORS THAT BIND A SHARED PROMOTER ELEMENT CORRELATE WITH POSITIVE AND NEGATIVE TRANSCRIPTIONAL CONTROL, GENES & DEVELOPMENT 2: 383 (1988). · DOI
Levy, D. E., Interferon: Principles and Medical Applications: 161 (1992).
LEW, D.J., ALPHA-INTERFERON AND GAMMA INTERFERON STIMULATE TRANSCRIPTION OF A SINGLE GENE THROUGH DIFFERENT SIGNAL TRANSDUCTION PATHWAYS, MOLECULAR AND CELLULAR BIOLOGY 9: 5404 (1989).
LEW, D.J., OVERLAPPING ELEMENTS IN THE GUANYLATE-BINDING PROTEIN GENE PROMOTER MEDIATE TRANSCRIPTIONAL INDUCTION BY ALPHA AND GAMMA INTERFERONS, MOLECULAR AND CELLULAR BIOLOGY 11: 182 (1991).
LUSTER, A.D., GAMMA-INTERFERON TRANSCRIPTIONALLY REGULATES AN EARLY-RESPONSE GENE CONTAINING HOMOLOGY TO PLATELET PROTEINS, NATURE 315: 672 (1985). · DOI
MAO, C, MUTANT HUMAN-CELLS DEFECTIVE IN INDUCTION OF MAJOR HISTOCOMPATIBILITY COMPLEX CLASS-II GENES BY INTERFERON-GAMMA, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 2880 (1993).
MCKENDRY, R, HIGH-FREQUENCY MUTAGENESIS OF HUMAN-CELLS AND CHARACTERIZATION OF A MUTANT UNRESPONSIVE TO BOTH ALPHA INTERFERON AND GAMMA INTERFERON, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 88: 11455 (1991).
MIRKOVITCH, J, MAPPING OF RNA-POLYMERASE ON MAMMALIAN GENES IN CELLS AND NUCLEI, MOLECULAR BIOLOGY OF THE CELL 3: 1085 (1992). · DOI
MIYAMOTO, M, REGULATED EXPRESSION OF A GENE ENCODING A NUCLEAR FACTOR, IRF-1, THAT SPECIFICALLY BINDS TO IFN-BETA-GENE REGULATORY ELEMENTS, CELL 54: 903 (1988). · DOI
MULLER, M, COMPLEMENTATION OF A MUTANT-CELL LINE - CENTRAL ROLE OF THE 91-KDA POLYPEPTIDE OF ISGF3 IN THE INTERFERON-ALPHA AND INTERFERON-GAMMA SIGNAL-TRANSDUCTION PATHWAYS, EMBO JOURNAL 12: 4221 (1993). · DOI · Paper page
MULLER, M, THE PROTEIN-TYROSINE KINASE JAK1 COMPLEMENTS DEFECTS IN INTERFERON-ALPHA/BETA AND INTERFERON-GAMMA SIGNAL-TRANSDUCTION, NATURE 366: 129 (1993). · DOI
MURDOCH, G.H., EPIDERMAL GROWTH-FACTOR RAPIDLY STIMULATES PROLACTIN GENE-TRANSCRIPTION, NATURE 300: 192 (1982). · DOI
OVERDUIN, M, 3-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY-2 DOMAIN OF C-ABL, CELL 70: 697 (1992). · DOI
PEARSE, R.N., INTERFERON-GAMMA-INDUCED TRANSCRIPTION OF THE HIGH-AFFINITY FC RECEPTOR FOR IGG REQUIRES ASSEMBLY OF A COMPLEX THAT INCLUDES THE 91-KDA SUBUNIT OF TRANSCRIPTION FACTOR ISGF3, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 4314 (1993).
PELLEGRINI, S, USE OF A SELECTABLE MARKER REGULATED BY ALPHA INTERFERON TO OBTAIN MUTATIONS IN THE SIGNALING PATHWAY, MOLECULAR AND CELLULAR BIOLOGY 9: 4605 (1989).
PINE, R, PURIFICATION AND CLONING OF INTERFERON-STIMULATED GENE FACTOR-2 (ISGF2) - ISGF2 (IRF-1) CAN BIND TO THE PROMOTERS OF BOTH BETA-INTERFERON-STIMULATED AND INTERFERON-STIMULATED GENES BUT IS NOT A PRIMARY TRANSCRIPTIONAL ACTIVATOR OF EITHER, MOLECULAR AND CELLULAR BIOLOGY 10: 2448 (1990).
PORTER, ACG, INTERFERON RESPONSE ELEMENT OF THE HUMAN GENE-6-16, EMBO JOURNAL 7: 85 (1988). · DOI
REICH, N, INTERFERON-INDUCED TRANSCRIPTION OF A GENE ENCODING A 15-KDA PROTEIN DEPENDS ON AN UPSTREAM ENHANCER ELEMENT, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 84: 6394 (1987).
10.1126/science.8378774 · DOI
RUTHERFORD, M.N., INTERFERON-INDUCED BINDING OF NUCLEAR FACTORS TO PROMOTER ELEMENTS OF THE 2-5A SYNTHETASE GENE, EMBO JOURNAL 7: 751 (1988). · DOI
10.1126/science.8397445 · DOI
SCHINDLER, C, PROTEINS OF TRANSCRIPTION FACTOR ISGF-3 - ONE GENE ENCODES THE 91-KDA AND 84-KDA ISGF-3 PROTEINS THAT ARE ACTIVATED BY INTERFERON-ALPHA, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 89: 7836 (1992).
10.1126/science.1496401 · DOI · Paper page
SHIRAYOSHI, Y, INTERFERON-INDUCED TRANSCRIPTION OF A MAJOR HISTOCOMPATIBILITY CLASS-I GENE ACCOMPANIES BINDING OF INDUCIBLE NUCLEAR FACTORS TO THE INTERFERON CONSENSUS SEQUENCE, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 85: 5884 (1988).
10.1016/0092-8674(94)90357-3 · DOI · Paper page
10.1126/science.1281555 · DOI
10.1126/science.7690989 · DOI · Paper page
SHUAL, K, POLYPEPTIDE SIGNALING TO THE NUCLEUS THROUGH TYROSINE PHOSPHORYLATION OF JAK AND STAT PROTEINS, NATURE 366: 580 (1993). · DOI
SILVENNOINEN, O, INTERFERON-INDUCED NUCLEAR SIGNALING BY JAK PROTEIN-TYROSINE KINASES, NATURE 366: 583 (1993). · DOI
SILVENNOINEN, O, STRUCTURE OF THE MURINE JAK2 PROTEIN-TYROSINE KINASE AND ITS ROLE IN INTERLEUKIN-3 SIGNAL-TRANSDUCTION, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 8429 (1993).
10.1126/science.8378775 · DOI
SIMS, S. H., MOLECULAR AND CELLULAR BIOLOGY 13: 690 (1993).
SOH, J, IDENTIFICATION AND SEQUENCE OF AN ACCESSORY FACTOR REQUIRED FOR ACTIVATION OF THE HUMAN INTERFERON-GAMMA RECEPTOR, CELL 76: 793 (1994). · DOI
UZE, G, GENETIC TRANSFER OF A FUNCTIONAL HUMAN INTERFERON-ALPHA RECEPTOR INTO MOUSE CELLS - CLONING AND EXPRESSION OF ITS CDNA, CELL 60: 225 (1990). · DOI
VEALS, S.A., SUBUNIT OF AN ALPHA-INTERFERON-RESPONSIVE TRANSCRIPTION FACTOR IS RELATED TO INTERFERON REGULATORY FACTOR AND MYB FAMILIES OF DNA-BINDING PROTEINS, MOLECULAR AND CELLULAR BIOLOGY 12: 3315 (1992).
10.1016/0092-8674(92)90105-L · DOI
Wakao, H., EMBO J. 13: 2182 (1994). · DOI
WATLING, D, COMPLEMENTATION BY THE PROTEIN-TYROSINE KINASE JAK2 OF A MUTANT-CELL LINE DEFECTIVE IN THE INTERFERON-GAMMA SIGNAL-TRANSDUCTION PATHWAY, NATURE 366: 166 (1993). · DOI
WILKS, A.F., 2 NOVEL PROTEIN-TYROSINE KINASES, EACH WITH A 2ND PHOSPHOTRANSFERASE-RELATED CATALYTIC DOMAIN, DEFINE A NEW CLASS OF PROTEIN-KINASE, MOLECULAR AND CELLULAR BIOLOGY 11: 2057 (1991).
WILKS, A.F., 2 PUTATIVE PROTEIN-TYROSINE KINASES IDENTIFIED BY APPLICATION OF THE POLYMERASE CHAIN-REACTION, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 86: 1603 (1989).
WITTHUHN, B.A., JAK2 ASSOCIATES WITH THE ERYTHROPOIETIN RECEPTOR AND IS TYROSINE-PHOSPHORYLATED AND ACTIVATED FOLLOWING STIMULATION WITH ERYTHROPOIETIN, CELL 74: 227 (1993). · DOI
Yamamato K. Molecular and Cellular Biology in press.
Zhong, Z., Proceedings of the National Academy of Sciences of the United States of America 91: 4806 (1994).

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Background
Virus-Activated Interferon Regulatory Factor 7 Upregulates Expression of the Interferon-Regulated BST2 Gene Independently of Interferon Signaling
Bego, M. G., Mercier, J., & Cohen, É. A. (2012) · Journal of Virology · doi:10.1128/jvi.06971-11 · Cited by 70
“As controls, we used STAT1-expressing parental 2fTGH cells, U3A-R, a rescue cell line in which expression of STAT1 was stably reestablished through introduction of a construct encoding STAT1 under the control of a human cytomegalovirus immediate-early gene promoter, as well as U3A-701 cells, which express a phosphoryl…”
BackgroundMethodInfluential
Rac1 is required for oncolytic NDV replication in human cancer cells and establishes a link between tumorigenesis and sensitivity to oncolytic virus
Puhlmann, J., Puehler, F., Mumberg, D., Boukamp, P., & Beier, R. (2010) · Oncogene · doi:10.1038/onc.2009.507 · Cited by 63
“To further analyze the IFN pathway in these cells, we studied the activation and induction of STAT1 and 2 which are components of the JAK-STAT pathway and are activated as a consequence of IFN binding to its cell surface receptor (Darnell et al., 1994).”
IL-4 protein expression and basal activation of Erk in vivo in follicular lymphoma
Calvo, K. R., Dabir, B., Kovach, A. E., Devor, C. B., Bandle, R., Bond, A., Shih, J. H., & Jaffe, E. S. (2008) · Blood · doi:10.1182/blood-2008-02-138933 · Cited by 64
Osteoclast activation in inflammatory periodontal diseases
Wiebe, S. H., Hafezi, M., Sandhu, H., Sims, S. M., & Dixon, S. J. (1996) · Oral Diseases · doi:10.1111/j.1601-0825.1996.tb00218.x · Cited by 66
Diesel exhaust particulate-induced activation of Stat3 requires activities of EGFR and Src in airway epithelial cells
Cao, D., Tal, T. L., Graves, L. M., GILMOUR, I. J., Linak, W. P., REED, W. A., Bromberg, P. A., & Samet, J. M. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00204.2006 · Cited by 68
“STATs are a family of cytoplasmic transcription factors identified as being key mediators of physiological signaling by cytokines and growth factors (5, 6, 24).”
Background
Central Role of ULK1 in Type I Interferon Signaling
Saleiro, D., Mehrotra, S., Kroczynska, B., Beauchamp, E. M., Lisowski, P., Majchrzak-Kita, B., Bhagat, T. D., Stein, B. L., McMahon, B., Altman, J. K., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.056 · Cited by 74
“No significant differences in IFNdependent Isg15, Isg54, and Irf9 mRNA expression were observed between control cells and cells in which ATG5 was knocked down (Figures 4A–4D).”
BackgroundInfluential
The Ubiquitin Ligase TRAF6 Negatively Regulates the JAK-STAT Signaling Pathway by Binding to STAT3 and Mediating Its Ubiquitination
Wei, J., Yuan, Y., Jin, C., Chen, H., Leng, L., He, F., & Wang, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049567 · Cited by 65
“Both of the NF-kB and the JAK-STAT signaling pathways have a central role in the immune response, but the cross-talk between the two signaling pathways is not very clear [1] [11].”
Background
STAT1 gene expression is enhanced by nuclear EGFR and HER2 via cooperation With STAT3
Han, W., Carpenter, R. L., Cao, X., & Lo, H. (2012) · Molecular Carcinogenesis · doi:10.1002/mc.21936 · Cited by 68
“To this end, we focused our efforts on signal transducer and activator of transcription 1 (STAT1), a transcription factor that responds to inflammatory signals and regulates genes involved in inflammatory response [37,38].”
Inhibiting aberrant Stat3 function with molecular therapeutics: a progress report
Haftchenary, S., Avadisian, M., & Gunning, P. (2011) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e328341185b · Cited by 68
Rinderpest Virus Blocks Type I and Type II Interferon Action: Role of Structural and Nonstructural Proteins
Nanda, S. K., & Baron, M. D. (2006) · Journal of Virology · doi:10.1128/jvi.02720-05 · Cited by 64
“The type I IFNs mediate their biological function by binding to the IFN- receptor on the target cells, resulting in the autophosphorylation and activation of the receptor-associated Janus kinases (JAKs), JAK1 and tyrosine kinase 2 (TYK2), and then the phosphorylation of the signaling molecules STAT1 and STAT2 (13, 29).”
Background
Physical and Functional Interactions between STAP-2/BKS and STAT5
Sekine, Y., Yamamoto, T., Yumioka, T., Sugiyama, K., Tsuji, S., Oritani, K., Shimoda, K., Minoguchi, M., Yoshimura, A., & Matsuda, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411692200 · Cited by 59
MiR-122 modulates type I interferon expression through blocking suppressor of cytokine signaling 1
Li, A., Song, W., Qian, J., Li, Y., He, J., Zhang, Q., Li, W., Zhai, A., Kao, W., Hu, Y., et al. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.01.008 · Cited by 67
The IFN signature and STAT1 expression in RA synovial fluid macrophages are induced by TNFα and counter-regulated by synovial fluid microenvironment
Gordon, R. A., Grigoriev, G., Lee, A., Kalliolias, G., & Ivashkiv, L. (2012) · Arthritis & Rheumatism · doi:10.1002/art.34544 · Cited by 67
“The discovery of the JAK/STAT signaling pathway clarified that most of the “IFN -inducible genes” expressed in RA synovium are targets of STAT-1 (4).”
Background
Withaferin A down-regulates lipopolysaccharide-induced cyclooxygenase-2 expression and PGE2 production through the inhibition of STAT1/3 activation in microglial cells
Min, K., Choi, K.-H., & Kwon, T. K. (2011) · International Immunopharmacology · doi:10.1016/j.intimp.2011.02.029 · Cited by 62
“BV2 cells were transiently transfected with luciferase reporter plasmids containing 8 GAS elements and stimulated with 100 ng/ml LPS either in the presence or absence of withaferin A. LPS dramatically enhanced GAS luciferase activity by approximately 5.7-fold, but GAS luciferase activity was reduced by withaferin A in…”
BackgroundInfluential
S‐glutathionylation of IRF3 regulates IRF3–CBP interaction and activation of the IFNβ pathway
Prinarakis, E., Chantzoura, E., Thanos, D., & Spyrou, G. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.28 · Cited by 77
“…present on the cell surface and by doing so activate the JAK–STAT signalling pathway eliciting their effects through the transcriptional activation of target genes bearing specific DNA-binding recognition sites (ISREs) within their promoters (Darnell et al, 1994; Ihle, 1996; Stark et al, 1998).”
Background
Molecular mechanisms of immunotherapy resistance in triple-negative breast cancer
Zheng, Y., Li, S., Tang, H., Meng, X., & Zheng, Q. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1153990 · Cited by 68
Hypoxia as a Modulator of Inflammation and Immune Response in Cancer
Castillo‐Rodríguez, R. A., Trejo‐Solís, C., Cabrera‐Cano, A., Gómez‐Manzo, S., & Dávila‐Borja, V. M. (2022) · Cancers · doi:10.3390/cancers14092291 · Cited by 70
Neoadjuvant Immunotherapy for High-Risk, Resectable Malignancies: Scientific Rationale and Clinical Challenges
Krishnamoorthy, M., Lenehan, J. G., & Vareki, S. M. (2020) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djaa216 · Cited by 75
“Both JAK1 and JAK2 are required for sensitivity to IFNc, which has antiproliferative effects (54,55).”
Background
Cannabidiol as a Novel Therapeutic for Immune Modulation
Peyravian, N., Deo, S. K., Daunert, S., & Jimenez, J. J. (2020) · ImmunoTargets and Therapy · doi:10.2147/itt.s263690 · Cited by 79
Epstein–Barr Virus and Innate Immunity: Friends or Foes?
Jangra, S., Yuen, K., Botelho, M. G., & Jin, D. (2019) · Microorganisms · doi:10.3390/microorganisms7060183 · Cited by 74
“These kinases phosphorylate and activate STAT1 to form homodimers, also known as GAF [118].”
Background
MiR‐16 regulates mouse peritoneal macrophage polarization and affects T‐cell activation
Jia, X., Li, X., Shen, Y., Miao, J., Liu, H., Li, G., & Wang, Z. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12882 · Cited by 71
“found that the signal transducers and activators of transcription 1 (STAT1) homodimers induced by IFN-c engages the cis elements within the promoter region of target genes including iNOS and IL-12, promotes target gene expression and drives the M1 differentiation of macrophages [24].”
Background
Targeted Therapies in Liver Fibrosis: Combining the Best Parts of Platelet-Derived Growth Factor BB and Interferon Gamma
van Dijk, F., Olinga, P., Poelstra, K., & Beljaars, L. (2015) · Frontiers in Medicine · doi:10.3389/fmed.2015.00072 · Cited by 60
WHSC1 links transcription elongation to HIRA‐mediated histone H3.3 deposition
Sarai, N., Nimura, K., Tamura, T., Kanno, T., Patel, M. C., Heightman, T. D., Ura, K., & Ozato, K. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.176 · Cited by 73
“Whsc1 (cid:2) / (cid:2) and WT cells were stimulated with IFN b (hereafter IFN) at 100U/ml, an optimal concentration for ISG induction (Darnell et al , 1994).”
Nuclear Localization of Signal Transducer and Activator of Transcription 3 in Head and Neck Squamous Cell Carcinoma Is Associated with a Better Prognosis
Pectasides, E., Egloff, A. M., Sasaki, C. T., Kountourakis, P., Burtness, B. A., Fountzilas, G., Dafni, U. G., Zaramboukas, T., Rampias, T. N., Rimm, D. L., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-2658 · Cited by 65
“After activation, STAT proteins dimerize and translocate to the nucleus, where they bind to DNA-response elements and alter the transcription of genes controlling normal cell functions such as growth, apoptosis, and differentiation (2).”
Background
IL-6 induces neuroendocrine dedifferentiation and cell proliferation in non-small cell lung cancer cells
Chang, K.-T., Tsai, C., Chiou, Y.-C., Chiu, C., Jeng, K.-S., & Huang, C. F. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00089.2005 · Cited by 68
“Subsequently, activated STATs form dimers and translocate to the nucleus where they bind specific promoter elements of target genes and regulate their transcription (12, 13, 20, 21).”
Background
Neutralizing antibodies and efficacy of interferon β-1a
Kappos, L., Clanet, M., Sandberg-wollheim, M., Radue, E., Hartung, H., Hohlfeld, R., Xu, J., Bennett, D., Sandrock, A., & Goelz, S. (2005) · Neurology · doi:10.1212/01.wnl.0000171747.59767.5c · Cited by 65
JAK/STAT signaling in insect innate immunity
Bang, I. S. (2019) · Entomological Research · doi:10.1111/1748-5967.12384 · Cited by 83
STAT3: A Potential Drug Target for Tumor and Inflammation
Hu, Y. S., Han, X., & Liu, X. H. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190620145052 · Cited by 81
Identification of Cyanamide-Based Janus Kinase 3 (JAK3) Covalent Inhibitors
Casimiro‐Garcia, A., Trujillo, J. I., Vajdos, F. F., Juba, B. M., Banker, M. E., AULABAUGH, A. E., Balbo, P., Bauman, J. N., Chrencik, J., Coe, J. W., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01308 · Cited by 85
Non‐canonical Stat3 signaling in cancer
Srivastava, J., & DiGiovanni, J. (2015) · Molecular Carcinogenesis · doi:10.1002/mc.22438 · Cited by 64
Minireview: Nuclear Receptor Coregulators of the p160 Family: Insights into Inflammation and Metabolism
Rollins, D. A., Coppo, M., & Rogatsky, I. (2015) · Molecular Endocrinology · doi:10.1210/me.2015-1005 · Cited by 66
Harnessing Mechanistic Knowledge on Beneficial Versus Deleterious IFN-I Effects to Design Innovative Immunotherapies Targeting Cytokine Activity to Specific Cell Types
Tomasello, E., Pollet, É., Manh, T. V., Uzé, G., & Dalod, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00526 · Cited by 91
“IFNAR is composed of two distinct subunits, IFNAR1 and IFNAR2, which are constitutively associated with members of the JAK family, tyrosine kinase 2 (TYK2) and JAK1, respectively (186) .”
Background
A Critical Role for Interferon Regulatory Factor 9 in Cerebral Ischemic Stroke
Chen, H., Guo, S., Li, Z.-Z., Lu, Y., Jiang, D.-S., Zhang, R., Lei, H. C., Gao, L., Zhang, X., Zhang, Y., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1545-14.2014 · Cited by 66
Platycodon grandiflorum root-derived saponins attenuate atopic dermatitis-like skin lesions via suppression of NF-κB and STAT1 and activation of Nrf2/ARE-mediated heme oxygenase-1.
Choi, J. H., Jin, S.-W., Han, E., Park, B., Kim, H. G., Khanal, T., Hwang, Y., Do, M. T., Lee, H.-S., Chung, Y., et al. (2014) · Phytomedicine · doi:10.1016/j.phymed.2014.04.011 · Cited by 65
Mechanism of the inhibition of the STAT3 signaling pathway by EGCG
Wang, Y., Ren, X., Deng, C., YANG, L., Yan, E., GUO, T., Li, Y., & Xu, M. X. (2013) · Oncology Reports · doi:10.3892/or.2013.2743 · Cited by 65
“In addition, human tumor xenograft studies in mice have repeatedly demonstrated that inhibition of STAT3 signaling results in decreased tumor growth and improved animal survival by inducing apoptosis in tumor cells, inhibiting angiogenesis (4), and enhancing antitumor immune-mediated cytotoxicity (1,5).”
Ubiquitin-Specific Proteases 25 Negatively Regulates Virus-Induced Type I Interferon Signaling
Zhong, H., Wang, D., Fang, L., Zhang, H., Luo, R., Shang, M., Ouyang, C., Ouyang, H., Chen, H., & Xiao, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080976 · Cited by 65
“The type I IFN signal is then transducted by the activation of Janus kinase (JAK) family protein kinases and the signal transducers and activators of transcription (STAT) family of proteins [2] , resulting in the generation of the transcriptional activator, IFN-stimulated gene factor 3 (ISGF3).”
Background
Kaposi's Sarcoma-Associated Herpesvirus Kaposin B Induces Unique Monophosphorylation of STAT3 at Serine 727 and MK2-Mediated Inactivation of the STAT3 Transcriptional Repressor TRIM28
King, C. A. (2013) · Journal of Virology · doi:10.1128/jvi.02976-12 · Cited by 71
“leading to the formation of dimers through reciprocal phosphotyrosine-SH2 domain interactions (31, 32).”
Background
Inhibition of the JAK-STAT3 Signaling Pathway by Ganoderic Acid A Enhances Chemosensitivity of HepG2 Cells to Cisplatin
Yao, X.-Y., Li, G.-L., Xu, H., & Lu, C.-T. (2012) · Planta Medica · doi:10.1055/s-0032-1315303 · Cited by 65
The Role of MAPK in Drug-Induced Kidney Injury
Cassidy, H., Radford, R., Slyne, J., O’Connell, S., Slattery, C., Ryan, M. P., & McMorrow, T. (2012) · Journal of Signal Transduction · doi:10.1155/2012/463617 · Cited by 71
“Vancomycin is a cationic glycopeptide antibiotic used in the treatment of penicillin-resistant Gram-positive infections, methicillin-resistant Staphylococcus aureus infections, and Clostridium difficile infections, which has seen a resurgence in use due to the emergence of β-lactam-resistant Gram-positive organism-ass…”
Background
(−)-Epigallocatechin Gallate Induces Fas/CD95-Mediated Apoptosis through Inhibiting Constitutive and IL-6-Induced JAK/STAT3 Signaling in Head and Neck Squamous Cell Carcinoma Cells
Lin, H.-Y., Hou, S.-C., Chen, S.-C., Kao, M., Yu, C.-C., Funayama, S., Ho, C., & Way, T. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf204362n · Cited by 66
Interferon type I responses in primary and secondary infections
Alsharifi, M., Müllbacher, A., & Regner, M. (2008) · Immunology and Cell Biology · doi:10.1038/sj.icb.7100159 · Cited by 62
Dual Role of the Jak1 FERM and Kinase Domains in Cytokine Receptor Binding and in Stimulation-Dependent Jak Activation
Haan, S., Margue, C., Engrand, A., Rolvering, C., de Leur, H. S.-V., Heinrich, P. C., Behrmann, I., & Haan, C. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.2.998 · Cited by 63
“The STAT transcription factors are then tyrosine phosphorylated and translocate to the nucleus where they bind to specific DNA sequences in the promoter regions of their respective target genes (2, 3).”
Background
Responses of cancer cells with wild-type or tyrosine kinase domain-mutated epidermal growth factor receptor (EGFR) to EGFR-targeted therapy are linked to downregulation of hypoxia-inducible factor-1α
Lü, Y., Liang, K., Li, X., & Fan, Z. (2007) · Molecular Cancer · doi:10.1186/1476-4598-6-63 · Cited by 63
“Even more divergent results were found in the levels of STAT3 phosphorylation after cetuximab and gefitinib treatment: levels of Tyr705-phosphorylated STAT3, which is regulated primarily via the JAK or Src kinase pathway [ 26 ], were markedly increased in A431 and H3255 cells; essentially unchanged or modestly increas…”
Result
IFN-α-Induced Signal Transduction, Gene Expression, and Antitumor Activity of Immune Effector Cells Are Negatively Regulated by Suppressor of Cytokine Signaling Proteins
Zimmerer, J. M., Lesinski, G. B., Kondadasula, S. V., Karpa, V. I., Lehman, A., Ray‐Chaudhury, A., Becknell, B., & Carson, W. E. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.8.4832 · Cited by 62
“The prototypical IFN- -signaling reaction results in the formation of IFN-stimulated gene factor 3, a DNA-binding complex that consists of STAT1 (or STAT1 ), STAT2, and IFN regulatory factor 9 (14).”
Background
Hepatitis C Infection and Alcohol Use: A Dangerous Mix for the Liver and Antiviral Immunity
Szabó, G., Aloman, C., Polyak, S. J., Weinman, S. A., Wands, J. R., & Zakhari, S. (2006) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2006.00083.x · Cited by 66
COX-2 Inhibitors Modulate IL-12 Signaling Through JAK-STAT Pathway Leading to Th1 Response in Experimental Allergic Encephalomyelitis
Muthian, G., Raikwar, H. P., Johnson, C., Rajasingh, J., Kalgutkar, A., Marnett, L., & Bright, J. (2006) · Journal of Clinical Immunology · doi:10.1007/s10875-006-8787-y · Cited by 65
Stat3 isoforms, α and β, demonstrate distinct intracellular dynamics with prolonged nuclear retention of Stat3β mapping to its unique C-terminal end
Huang, Y., Qiu, J., Dong, S., Redell, M. S., Poli, V., Mancini, M. A., & Tweardy, D. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704548200 · Cited by 65
The YXXQ motif in gp 130 is crucial for STAT3 phosphorylation at Ser727 through an H7-sensitive kinase pathway
Abe, K., Hirai, M., Mizuno, K., Higashi, N., Sekimoto, T., Miki, T., Hirano, T., & Nakajima, K. (2001) · Oncogene · doi:10.1038/sj.onc.1204461 · Cited by 65
Interferon Regulatory Factors and TFIIB Cooperatively Regulate Interferon-Responsive Promoter Activity In Vivo and In Vitro
Wang, I.-M., Blanco, J. C. G., Tsai, S. Y., Tsai, M.-J., & Ozato, K. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.6313 · Cited by 64
Tetrahedral Framework Nucleic Acid Promotes the Treatment of Bisphosphonate-Related Osteonecrosis of the Jaws by Promoting Angiogenesis and M2 Polarization
Zhao, D., Cui, W., Liu, M., Li, J., Sun, Y., Shi, S., Lin, S., & Lin, Y. (2020) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.0c13839 · Cited by 82
MicroRNA gga-miR-130b Suppresses Infectious Bursal Disease Virus Replication via Targeting of the Viral Genome and Cellular Suppressors of Cytokine Signaling 5
Fu, M., Wang, B., Chen, X., He, Z., Wang, Y., Li, X., Cao, H., & Zheng, S. J. (2017) · Journal of Virology · doi:10.1128/jvi.01646-17 · Cited by 72
PLA2R1: Expression and function in cancer
Bernard, D., & Vindrieux, D. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.03.003 · Cited by 75
Elevated levels of serum IL-5 are associated with an increased likelihood of major depressive disorder
Elomaa, A.-P., NISKANEN, L. K., Herzig, K., Viinamäki, H. T., Hintikka, J. J., Koivumaa-Honkanen, H. T., Honkalampi, K. M., Valkonen‐Korhonen, M., Harvima, I. T., & Lehto, S. M. (2012) · BMC Psychiatry · doi:10.1186/1471-244x-12-2 · Cited by 65
“IFN-a and -g have also been shown to activate JAK family kinases and consequently phosphorylate STATs [48], and further induce depressive symptoms [49].”
Background
Targeting Cancer Cell Ferroptosis to Reverse Immune Checkpoint Inhibitor Therapy Resistance
Deng, J., Zhou, M. L., Liao, T., Kuang, W., Xia, H., Yin, Z., Tan, Q., Li, Y., Song, S., Zhou, E., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.818453 · Cited by 63
The LIM protein AJUBA promotes colorectal cancer cell survival through suppression of JAK1/STAT1/IFIT2 network
Jia, H., Song, L., Cong, Q., Wang, J.-L., Xu, H., Chu, Y., Li, Q., Zhang, Y., Zou, X., Zhang, C.-M., et al. (2017) · Oncogene · doi:10.1038/onc.2016.418 · Cited by 63
Stat3/Cdc25a-dependent cell proliferation promotes embryonic axis extension during zebrafish gastrulation
Liu, Y., Sepich, D. S., & Solnica‐Krezel, L. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006564 · Cited by 58
“Signal transducer and activator of transcription 3 (STAT3) is an essential mediator of cytokine and growth factor signaling involved in animal development, homeostasis and disease [1, 2].”
Background
Brain-derived neurotrophic factor promotes nerve regeneration by activating the JAK/STAT pathway in Schwann cells
Lin, G., Zhang, H., Sun, F., Lu, Z., Reed-Maldonado, A., Lee, Y.-C., Wang, G.-F., Banie, L., & Lue, T. (2016) · Translational Andrology and Urology · doi:10.21037/tau.2016.02.03 · Cited by 63
“Transected peripheral nerves demonstrate elevated levels of JAK2, STAT1, and most importantly STAT3 (23).”
Background
Innate immune regulation by STAT ‐mediated transcriptional mechanisms
Li, H. S., & Watowich, S. S. (2014) · Immunological Reviews · doi:10.1111/imr.12198 · Cited by 72
“iNOS, IL-12, and CIITA) by direct binding to the gamma-activated sequence (GAS, a STAT consensus binding element) in their proximal promoters (117).”
Background
Pharmacological Properties of Guggulsterones, the Major Active Components of Gum Guggul
Shah, R., Gulati, V., & Palombo, E. A. (2012) · Phytotherapy Research · doi:10.1002/ptr.4647 · Cited by 63
“26: 1594–1605 (2012) the transcription process (Darnell et al., 1994).”
Discovery and Optimization of C-2 Methyl Imidazopyrrolopyridines as Potent and Orally Bioavailable JAK1 Inhibitors with Selectivity over JAK2
Zak, M., Mendonca, R. V., Balázs, M., Barrett, K., Bergeron, P., Blair, W. S., Chang, C., Deshmukh, G., DeVoss, J., Dragovich, P. S., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300628c · Cited by 68
Alcohol Metabolism Increases the Replication of Hepatitis C Virus and Attenuates the Antiviral Action of Interferon
McCartney, E. M., Semendric, L., Helbig, K. J., Hinze, S. J., Jones, B., Weinman, S. A., & Beard, M. R. (2008) · The Journal of Infectious Diseases · doi:10.1086/593216 · Cited by 63
“The binding of IFN- to its cognate receptor results in the activation of the Jak/Stat signaling pathway [32], culminating in the expression of IFN-stimulated genes (ISGs) that act to limit HCV replication.”
Background
IFN‐γ‐induced IDO and WRS expression in microglia is differentially regulated by IL‐4
Yadav, M. C., Burudi, E. M. E., Alirezaei, M., Flynn, C. C., Watry, D. D., Lanigan, C. M. S., & Fox, H. S. (2007) · Glia · doi:10.1002/glia.20544 · Cited by 76
“Consequently, STAT-1 homodimers are formed and bind to IFN-g-inducible promoters (Darnell et al., 1994).”
Background
Neuroinflammation in retinitis pigmentosa: Therapies targeting the innate immune system
Zhao, L., Hou, C., & Yan, N. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1059947 · Cited by 65
The Role of Indoleamine 2, 3-Dioxygenase 1 in Regulating Tumor Microenvironment
Huang, X., Zhang, F., Wang, X., & Liu, K. (2022) · Cancers · doi:10.3390/cancers14112756 · Cited by 69
Tackling Chronic Inflammation with Withanolide Phytochemicals—A Withaferin A Perspective
Logie, E., & Berghe, W. V. (2020) · Antioxidants · doi:10.3390/antiox9111107 · Cited by 67
Pharmacological targets of metabolism in disease: Opportunities from macrophages
Castegna, A., Gissi, R., Menga, A., Montopoli, M., Favia, M., Viola, A., & Canton, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107521 · Cited by 75
Kaempferol 7-O-β-D-glucoside isolated from the leaves of Cudrania tricuspidata inhibits LPS-induced expression of pro-inflammatory mediators through inactivation of NF-κB, AP-1, and JAK-STAT in RAW 264.7 macrophages
Lee, S.-B., Shin, J., Han, H.-S., Lee, H., Park, J. C., & Lee, K. (2018) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2018.02.022 · Cited by 67
Antagonizing cytokine-mediated JAK-STAT signaling by porcine reproductive and respiratory syndrome virus
Yang, L., & Zhang, Y. (2016) · Veterinary Microbiology · doi:10.1016/j.vetmic.2016.12.036 · Cited by 65
“PRRSV blocks the nuclear translocation of the IFNinduced ISGF3 complex via nsp1b (Chen et al., 2010; Patel et al., 2010).”
BackgroundInfluential
Targeted inhibition of STATs and IRFs as a potential treatment strategy in cardiovascular disease
Szeląg, M., Piaszyk-Borychowska, A., Plens-Gałąska, M., Wesoły, J., & Bluyssen, H. A. R. (2016) · Oncotarget · doi:10.18632/oncotarget.9195 · Cited by 66
“Each IRF-DBD has the fold of a ‘helix-turn-helix’ and recognizes a similar DNA motifIFN regulatory element (IRE, NAANNGAAA) [25], that is present in the regulatory regions of IFNs and ISGs or binds to its tandem-repeat form called the IFN-stimulated response element (ISRE, A/GNGAAANNGAAACT) [26].”
Background
STAT1 deficiency redirects IFN signalling toward suppression of TLR response through a feedback activation of STAT3
Kim, H. S., Kim, D. C., Kim, H.-M., Kwon, H., Kwon, S. J., Kang, S., Kim, S. C., & Choi, G.-E. (2015) · Scientific Reports · doi:10.1038/srep13414 · Cited by 60
VX-509 (Decernotinib) Is a Potent and Selective Janus Kinase 3 Inhibitor That Attenuates Inflammation in Animal Models of Autoimmune Disease
Mahajan, S., Hogan, J. K., Shlyakhter, D., Oh, L., Salituro, F. G., Farmer, L. J., & Hoock, T. C. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.221176 · Cited by 64
“At the 10 mg/kg dose level in the CIA model, VX-509 produced significant inhibition of the immune-mediated pathology with exposure levels above the IC50 point for JAK3 while below the IC50 points for the JAK2/ JAK1/TYK2 assays.”
BackgroundMethodInfluential
A Novel Small Molecular STAT3 Inhibitor, LY5, Inhibits Cell Viability, Cell Migration, and Angiogenesis in Medulloblastoma Cells
Xiao, H., Bid, H. K., Jou, D., Wu, X., Yu, W., Li, C., Houghton, P. J., & Lin, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616748 · Cited by 64
“Many drivers of STAT3 activation, including the anti-inflammatory IL-10, pro-inflammatory IL-6, and type I and II interferons (IFNs), ensure constitutive Stat3 activation, which may account for the fact that STAT3 can mediate both anti-inflammatory and pro-inflammatory responses (4, 25, 26).”
Background
microRNA control of interferons and interferon induced anti-viral activity
Sedger, L. M. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2013.07.009 · Cited by 66
Molecular pathways controlling inhibitory receptor expression
Grabenstatter, H. L., Russek, S. J., & Brooks‐Kayal, A. R. (2012) · Epilepsia · doi:10.1111/epi.12036 · Cited by 64
“Phosphorylated STAT proteins (pSTATs) dimerize and translocate to the nucleus where they bind specific STAT DNA regulatory elements in the promoters of target genes to alter their transcription (Darnell et al., 1994; Schindler & Darnell, 1995; Ihle, 1996; Levy & Darnell, 2002).”
MER41 Repeat Sequences Contain Inducible STAT1 Binding Sites
Schmid, C. D., & Bücher, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011425 · Cited by 67
“relatively few binding sequences defined a consensus sequence TCCNNNGAA of the IFN-c-activated site (GAS [13]).”
BackgroundMethodInfluential
Clinical, Pathological and Molecular Determinants in Squamous Cell Carcinoma of the Oral Cavity
Al-Swiahb, J. N., Chen, C., Chuang, H., Fang, F., Tasi, H.-T., & Chien, C. (2010) · Future Oncology · doi:10.2217/fon.10.35 · Cited by 59
“STAT family members are latent cytoplasmic transcription factors activated by extracellular proteins, including growth factors, cytokines, hormones and peptides [82,83].”
Background
Transcriptional analysis of host responses to Marek's disease virus infection in genetically resistant and susceptible chickens.
Sarson, A., Parvizi, P., Lepp, D., Quinton, M., & Sharif, S. (2008) · Animal Genetics · doi:10.1111/j.1365-2052.2008.01710.x · Cited by 62

Authors: Darnell, J. E., Kerr, L. M., & Stark, G. R.
Affiliations: Rockefeller University (US)
Case Comprehensive Cancer Center (US)
ORCID: Stark, George R.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1994-06-03
Volume: 264
Issue: 5164
Pages: 1415-1421
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.8197455
OpenAlex: W2029275361
Cited by: 6,080
References: 85
Citations by year: 2026: 84 · 2025: 139 · 2024: 175 · 2023: 170 · 2022: 183 · 2021: 177 · 2020: 162 · 2019: 155 · 2018: 121 · 2017: 166 · 2016: 148 · 2015: 152 · 2014: 160 · 2013: 207 · 2012: 188
FWCI: 28.59
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: JAK/STAT signaling, interferon-alpha, interferon-gamma, signal transduction, STAT proteins, transcriptional activation, JAK kinases, interferon receptor, nuclear translocation, DNA binding
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cell Line, DNA-Binding Proteins, Genes, Genetic Complementation Test, Humans, Interferon-gamma, Molecular Sequence Data, Mutation, Protein-Tyrosine Kinases, Regulatory Sequences, Nucleic Acid, Transcription Factors, Signal Transduction, Transcriptional Activation, Interferon-alpha, Interferon-Stimulated Gene Factor 3, Interferon-Stimulated Gene Factor 3, gamma Subunit

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

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