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

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

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

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1126/science.8197455

Cites

0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Stat3: a STAT Family Member Activated by Tyrosine Phosphorylation in Response to Epidermal Growth Factor and Interleukin-6
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

Flagged first, then by citations

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).

Sorted by citations

Items 301–400 of 1,078

The Nucleocytoplasmic Rabies Virus P Protein Counteracts Interferon Signaling by Inhibiting both Nuclear Accumulation and DNA Binding of STAT1
Vidy, A., Bougrini, J. E., Chelbi-alix, M., & Blondel, D. (2007) · Journal of Virology · doi:10.1128/jvi.01930-06 · Cited by 162
“All the IFN-induced biological responses are believed to be mediated by ISG products that have been shown to display intrinsic antiviral activities (8, 24).”
Background
Elevated phosphorylation and activation of PDK-1/AKT pathway in human breast cancer
Lin, H.-J., Hsieh, F.-C., Song, H., & Lin, J. (2005) · British Journal of Cancer · doi:10.1038/sj.bjc.6602862 · Cited by 153
“Then activated Stat3 leads to dimer formation, nuclear localisation, and regulation of gene expression (Darnell et al, 1994; Zhong et al, 1994).”
Background
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
Effects of interferon-α, interferon-γ and cAMP on the transcriptional regulation of the serotonin transporter
Morikawa, O., Sakai, N., Obara, H., & Saito, N. (1998) · European Journal of Pharmacology · doi:10.1016/s0014-2999(98)00187-3 · Cited by 160
Varicella-Zoster Virus Pathogenesis and Immunobiology: New Concepts Emerging from Investigations with the SCIDhu Mouse Model
Ku, C., Besser, J., Abendroth, A., Grose, C. F., & Arvin, A. M. (2005) · Journal of Virology · doi:10.1128/jvi.79.5.2651-2658.2005 · Cited by 166
“phosphorylation of Stat1 phosphorylation by JAK kinases (14).”
Background
Selective blockade of the inhibitory Fcγ receptor (FcγRIIB) in human dendritic cells and monocytes induces a type I interferon response program
Dhodapkar, K. M., Banerjee, D. K., Connolly, J., Kukreja, A., Matayeva, E., Veri, M. C., Ravetch, J. V., Steinman, R. M., & Dhodapkar, M. V. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062545 · Cited by 141
“Type 1 IFN-mediated activation of its receptor activates Jak protein tyrosine kinases, which in turn phosphorylate STAT proteins, including STAT1 (16).”
Background
Fifty Years of Interferon Research: Aiming at a Moving Target
Vilček, J. (2006) · Immunity · doi:10.1016/j.immuni.2006.08.008 · Cited by 151
Crystal structure of PU. 1/IRF-4/DNA ternary complex
Escalante, C. R., Brass, A. L., Pongubala, J. M. R., Shatova, E., Shen, L., Singh, H., & Aggarwal, A. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00703-7 · Cited by 154
STAT3: a multifaceted oncoprotein
Guanizo, A. C., Fernando, C. D., Garama, D. J., & Gough, D. J. (2018) · Growth Factors · doi:10.1080/08977194.2018.1473393 · Cited by 179
“The accepted mechanism for STAT3 signalling is that STAT3 exists as a latent monomer in the cytosol until cytokines or growth factors bind to their cognate cell surface receptors (Figure 2(A)) (Darnell, 1997; Darnell et al., 1994).”
Background
Interferon regulatory factor family of transcription factors and regulation of oncogenesis
Takaoka, A., Tamura, T., & Taniguchi, T. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2007.00720.x · Cited by 152
Oncogenic signaling from the hematopoietic growth factor receptors c-Kit and Flt3
Masson, K., & Rönnstrand, L. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.06.002 · Cited by 137
“The signal transducers and activators of transcription (STATs) were originally described as ligand-induced transcription factors in interferon-treated cells [117].”
Herpes simplex type I (HSV-1) infection of the nervous system: Is an immune response a good thing?
Conrady, C. D., Drevets, D. A., & Carr, D. J. J. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.09.013 · Cited by 146
NK cells and interferons
Paolini, R., Bernardini, G., Molfetta, R., & Santoni, A. (2014) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.11.003 · Cited by 174
“STAT phosphorylation allows the formation of a transcriptional complex and the subsequent induction of several IFN-stimulated gene products endowed with antiviral activity [11].”
Background
Dissecting Interferon-Induced Transcriptional Programs in Human Peripheral Blood Cells
Waddell, S. J., Popper, S. J., Rubins, K., Griffiths, M. J., Brown, P. O., Levin, M., & Relman, D. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009753 · Cited by 148
“. Genes encoding proteins implicated in the major antiviral pathways initiated by interferon stimulation were consistently induced, including the dsRNA-dependent protein kinase pathway (PRKRA, EIF2AK2 (PRKR), PALM2-AKA1, EIF2B1), the 2-5A synthetase system (OAS1/2/3), and the Mx pathway (MX1/2). Genes involved in the…”
Background
Encephalomyocarditis Virus Disrupts Stress Granules, the Critical Platform for Triggering Antiviral Innate Immune Responses
Ng, C. S., Jogi, M., Yoo, J., Onomoto, K., Koike, S., Iwasaki, T., Yoneyama, M., Kato, H., & Fujita, T. (2013) · Journal of Virology · doi:10.1128/jvi.03248-12 · Cited by 146
“Secreted IFNs, in turn, activate a secondary JAK-STAT signaling cascade, which culminates in the activation of various interferon-stimulated genes (ISGs) (1, 2).”
Background
25 years of interferon-based treatment of chronic hepatitis C: an epoch coming to an end
Heim, M. H. (2013) · Nature reviews. Immunology · doi:10.1038/nri3463 · Cited by 161
Glucocorticoid modulation of cytokine signaling
Rogatsky, I., & Ivashkiv, L. B. (2006) · Tissue Antigens · doi:10.1111/j.1399-0039.2006.00599.x · Cited by 150
Human STAT1 Gain-of-Function Heterozygous Mutations: Chronic Mucocutaneous Candidiasis and Type I Interferonopathy
Okada, S., Asano, T., Moriya, K., Boisson‐Dupuis, S., Kobayashi, M., Casanova, J., & Puel, A. (2020) · Journal of Clinical Immunology · doi:10.1007/s10875-020-00847-x · Cited by 182
Targeting caspases in cancer therapeutics
Hensley, P. J., Mishra, M., & Kyprianou, N. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0128 · Cited by 148
Evolution of the Class 2 cytokines and receptors, and discovery of new friends and relatives
Krause, C. D., & Pestka, S. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.12.002 · Cited by 143
Role of Caspases in Cytokine-Induced Barrier Breakdown in Human Brain Endothelial Cells
Lopez‐Ramirez, M. A., Fischer, R., Torres-Badillo, C. C., Davies, H. A., Logan, K. E., Pfizenmaier, K., Male, D. K., Sharrack, B., & Romero, I. A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103460 · Cited by 140
“More recently, a study has proposed that primary cultures of human BECs are resistant to cell death mediated by TNF-a (18).”
BackgroundMethodInfluential
STAT1 and pathogens, not a friendly relationship
Najjar, I., & Fagard, R. (2010) · Biochimie · doi:10.1016/j.biochi.2010.02.009 · Cited by 147
“domain [12] and is phosphorylated on tyrosine 701 [13,14] (Fig.”
Negative feedback regulation of cellular antiviral signaling by RBCK1-mediated degradation of IRF3
Zhang, M., Tian, Y., Wang, R., Gao, D., Zhang, Y., Diao, F., Chen, D., Zhai, Z., & Shu, H. (2008) · Cell Research · doi:10.1038/cr.2008.277 · Cited by 144
The genetics of SLE: an update in the light of genome-wide association studies
Rhodes, B., & Vyse, T. J. (2008) · Rheumatology · doi:10.1093/rheumatology/ken247 · Cited by 151
Down-Regulation of the Interferon Signaling Pathway in T Lymphocytes from Patients with Metastatic Melanoma
Critchley-Thorne, R. J., Yan, N., Nacu, Ş., Weber, J. S., Holmes, S., & Lee, P. P. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040176 · Cited by 137
“Phosphorylated STAT1 homodimers bind to GAS (c-activated sequence) elements of ISG promoters [22].”
Background
Innate immunity and HCV
Heim, M. H. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.10.005 · Cited by 149
“Type I and III IFNs additionally induce the heterotrimeric transcription factor IFN-stimulated gene factor 3 (ISGF3) that consists of STAT1, STAT2, and IRF9 and binds to IFN-stimulated response elements (ISRE) [35,37,38] (Fig.”
BackgroundInfluential
The Ebola Virus Interferon Antagonist VP24 Directly Binds STAT1 and Has a Novel, Pyramidal Fold
Zhang, A. P. P., Bornholdt, Z. A., Liu, T., Abelson, D. M., Lee, D. E., Li, S., Woods, V. L., & Saphire, E. O. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002550 · Cited by 144
“Upon phosphorylation, P-STAT1 either dimerizes or forms a complex with IFN a/b-stimulated gene factor 3 (ISGF3) [18,29,30], and is subsequently transported to the nucleus via karyopherin a proteins where it regulates genes involved in the immune response [31–33].”
Background
Drosophila STAT is required for directly maintaining HP1 localization and heterochromatin stability
Shi, S., Larson, K., Guo, D., Lim, S. J., Dutta, P., Yan, S., & Li, W. X. (2008) · Nature Cell Biology · doi:10.1038/ncb1713 · Cited by 144
Macrophage Plasticity and Atherosclerosis Therapy
Lin, P. C., Ji, H., Li, Y., & Guo, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.679797 · Cited by 171
“For example, IFN-γ receptor interaction leads to the activation of kinases of the Jak family and then phosphorylation of STAT-1, which induces the expression of genes related to M1 phenotype (Darnell et al., 1994).”
Background
Targeted inhibition of STAT3 as a potential treatment strategy for atherosclerosis
Chen, Q., Lv, J., Yang, W., Xu, B., Wang, Z., Yu, Z., Wu, J., Yang, Y., & Han, Y. (2019) · Theranostics · doi:10.7150/thno.35528 · Cited by 174
“All four members range in size from 120-140 kDa, and each member has 7 conserved domains consisting of Janus homologies 1-7 (JH1-7) that can be mainly divided into three parts: 1) a C-terminal tyrosine kinase domain (JH1), which can activate JAKs; 2) a pseudokinase domain (JH2), which is necessary to maintain the JAK…”
Background
IL-21 Promotes Differentiation of Naive CD8 T Cells to a Unique Effector Phenotype
Casey, K. A., & Mescher, M. F. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.12.7640 · Cited by 114
“129S6 and STAT1 / mice were purchased from Taconic Farms.”
BackgroundInfluential
Treatment of hepatocellular carcinoma with major portal vein thrombosis by combined therapy with subcutaneous interferon-α and intra-arterial 5-fluorouracil; role of type 1 interferon receptor expression
Ôta, H., Nagano, H., Sakon, M., Eguchi, H., Kondo, M., Yamamoto, T., Nakamura, M., Damdinsuren, B., Wada, H., Marubashi, S., et al. (2005) · British Journal of Cancer · doi:10.1038/sj.bjc.6602742 · Cited by 145
The role of interferon-gamma on immune and allergic responses
Teixeira, L. K., Fonseca, B. P., Barboza, B. A., & Viola, J. P. B. (2005) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/s0074-02762005000900024 · Cited by 154
Molecular and cellular paradigms of multidrug resistance in cancer
Vaidya, F. U., Chhipa, A. S., Mishra, V., Gupta, V. K., Rawat, S. G., Kumar, A., & Pathak, C. (2020) · Cancer Reports · doi:10.1002/cnr2.1291 · Cited by 215
“tumor specific T-cell activation helps immune response escape mechanism in cancer cells apparently by inhibiting the expression of molecules associated with downstream IFN-γ signaling.(112) Recent clinical investigation showed that resistance to anti-CTLA4 molecule ipilimumab showed considerable mutations in Interfero…”
Background
Macrophage-specific inhibition of the histone demethylase JMJD3 decreases STING and pathologic inflammation in diabetic wound repair
Audu, C. O., Melvin, W. J., Joshi, A., Wolf, S., Moon, J. Y., Davis, F. M., Barrett, E. C., Mangum, K. D., Deng, H., Xing, X., et al. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00919-5 · Cited by 163
Janus kinases to jakinibs: from basic insights to clinical practice
Gadina, M., Le, M. T., Schwartz, D. M., Silvennoinen, O., Nakayamada, S., Yamaoka, K., & O’Shea, J. J. (2019) · Rheumatology · doi:10.1093/rheumatology/key432 · Cited by 159
The unique role of STAT2 in constitutive and IFN-induced transcription and antiviral responses
Błaszczyk, K., Nowicka, H., Kostyrko, K., Antonczyk, A., Wesoły, J., & Bluyssen, H. A. R. (2016) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.02.010 · Cited by 157
JAK Inhibitors for Treatment of Psoriasis: Focus on Selective TYK2 Inhibitors
Nogueira, M., Puig, L., & Torres, T. R. (2020) · Drugs · doi:10.1007/s40265-020-01261-8 · Cited by 167
“JAKi binds to the Adenosine Triphosphate (ATP)binding site on JAK, inhibiting the phosphorylation and activation of JAKs.”
BackgroundInfluential
Hypoxia and STAT3 signalling interactions regulate pro-inflammatory pathways in rheumatoid arthritis
Gao, W., McCormick, J., Connolly, M., Balogh, E., Veale, D. J., & Fearon, U. (2014) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2013-204105 · Cited by 154
Mechanisms linking obesity and cancer
Louie, S. M., Roberts, L. S., & Nomura, D. K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.02.008 · Cited by 152
Docosahexaenoic acid changes lipid composition and interleukin-2 receptor signaling in membrane rafts
Li, Q., Wang, M., Tan, L., Wang, C., Ma, J., Li, N., Li, Y., Xu, G., & Li, J. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m500033-jlr200 · Cited by 142
IFITM1 plays an essential role in the antiproliferative action of interferon-γ
Yang, G., Xu, Y., Chen, X., & Hu, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209807 · Cited by 129
“Activated JAK1 and JAK2 phosphorylate signal transducers and activators of transcription 1 (STAT1), which forms a homodimer and translocates into the nucleus to activate the transcription of IFN-g -responsive elements (Darnell et al., 1994).”
Background
Innate Immune Responses to Dengue Virus
Navarro-Sánchez, E., Desprès, P., & Cedillo‐Barrón, L. (2005) · Archives of Medical Research · doi:10.1016/j.arcmed.2005.04.007 · Cited by 140
Inhibition of p300 Histone Acetyltransferase by Viral Interferon Regulatory Factor
Li, M., Damania, B., Alvarez, X., Ogryzko, V., Ozato, K., & Jung, J. U. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.21.8254-8263.2000 · Cited by 142
Challenges in Immunotherapy Presented by the Glioblastoma Multiforme Microenvironment
Jackson, C. M., Ruzevick, J., Phallen, J. A., Belcaid, Z., & Lim, M. K. (2011) · Clinical and Developmental Immunology · doi:10.1155/2011/732413 · Cited by 144
“The phosphorylated receptor then recruits STAT1 and STAT3 via the Src homology 2 (SH2) domain of the STAT protein [214, 215].”
Background
A novel small molecule inhibits STAT3 phosphorylation and DNA binding activity and exhibits potent growth suppressive activity in human cancer cells
Lin, L., Deangelis, S., Foust, E., Fuchs, J. R., Li, C., Li, P., Schwartz, E. B., Lesinski, G. B., Benson, D., Lü, J., et al. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-217 · Cited by 152
“After activated by some cell surface cytokines, such as IL-6, IFN-g, JAK2 phosphorylates and activates cytoplasmic STAT3 protein to an active dimer, which translocates to the nucleus and induce the transcription of specific target genes [14,15].”
Osteoblasts secrete Cxcl9 to regulate angiogenesis in bone
Huang, B., Wang, W., Li, Q., Wang, Z., Yan, B., Zhang, Z., Wang, L., Huang, M., Jia, C., Lu, J., et al. (2016) · Nature Communications · doi:10.1038/ncomms13885 · Cited by 146
A meta-analysis of genome-wide association studies identifies novel variants associated with osteoarthritis of the hip
Εvangelou, Ε., Kerkhof, H. J. M., Styrkársdóttir, U., Ntzani, E., Bos, S. D., Esko, T., Evans, D. S., Metrustry, S., Panoutsopoulou, K., Ramos, Y. F., et al. (2013) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2012-203114 · Cited by 124
Identification of target genes and a unique cis element regulated by IRF-8 in developing macrophages
Tamura, T., Thotakura, P., Tanaka, T. S., Ko, M. S. H., & Ozato, K. (2005) · Blood · doi:10.1182/blood-2005-01-0080 · Cited by 135
Porcine reproductive and respiratory syndrome (PRRS): an immune dysregulatory pandemic
Butler, J. E., Lager, K. M., Golde, W. T., Faaberg, K. S., Šinkora, M., Loving, C. L., & Zhang, Y. (2014) · Immunologic Research · doi:10.1007/s12026-014-8549-5 · Cited by 159
“IFNs bind to their receptors on cell surface and activate JAK/STAT signaling, resulting in the expression of IFN-stimulated genes (ISGs) [83] .”
Background
Synthetic DNA Vaccines: Improved Vaccine Potency by Electroporation and Co-Delivered Genetic Adjuvants
Flingai, S., Czerwonko, M. E., Goodman, J., Kudchodkar, S. B., Muthumani, K., & Weiner, D. B. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00354 · Cited by 149
“IFN-γ, one of the primary proteins responsible for this effect, is secreted to inhibit the propagation of viruses by inducing transcriptional repressors that downregulate viral replication (49).”
Background
Innate Immunity Evasion by Dengue Virus
Morrison, J., Aguirre, S., & Fernández-Sesma, A. (2012) · Viruses · doi:10.3390/v4030397 · Cited by 142
Exploiting the Ref-1-APE1 node in cancer signaling and other diseases: from bench to clinic
Shah, F., Logsdon, D. P., Messmann, R. A., Fehrenbacher, J. C., Fishel, M. L., & Kelley, M. R. (2017) · npj Precision Oncology · doi:10.1038/s41698-017-0023-0 · Cited by 155
Leptin-Induced JAK/STAT Signaling and Cancer Growth
Mullen, M., & Gonzalez-Perez, R. R. (2016) · Vaccines · doi:10.3390/vaccines4030026 · Cited by 154
Regulation of PD-1/PD-L1 pathway and resistance to PD-1/PD-L1 blockade
Bai, J., Gao, Z., Li, X., Dong, L., Han, W., & Nie, J. (2017) · Oncotarget · doi:10.18632/oncotarget.22690 · Cited by 159
“One mechanism by which cancer cells could escape the effects of IFN-γ is by decreasing the expression or mutations in molecules in IFN-γ signaling pathway, which goes through the IFN-γ receptors JAK1 and/or JAK2 and the signal transducer and activators of transcription (STATs) [86].”
Background
Quantitative Multicolor Super-Resolution Microscopy Reveals Tetherin HIV-1 Interaction
Lehmann, M., Rocha, S., Mangeat, B., Blanchet, F. P., Uji‐i, H., Hofkens, J., & Piguet, V. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002456 · Cited by 133
Polycystin-1 regulates STAT activity by a dual mechanism
Talbot, J., Shillingford, J., Vasanth, S., Doerr, N., Mukherjee, S., Kinter, M., Watnick, T. J., & Weimbs, T. (2011) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1103816108 · Cited by 140
Toll-like Receptor-dependent and -independent Viperin Gene Expression and Counter-regulation by PRDI-binding Factor-1/BLIMP1
Severa, M., Coccia, E. M., & Fitzgerald, K. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604516200 · Cited by 127
Polyfunctional analysis of human t cell responses: importance in vaccine immunogenicity and natural infection
Makedonas, G., & Betts, M. R. (2006) · Springer Seminars in Immunopathology · doi:10.1007/s00281-006-0025-4 · Cited by 126
“This may result from the fact that IFN-γ signalling upregulates NFκ-B activity [87], which could increase the activation state of the cell, thereby making it a prime target for HIV infection.”
Background
STAT3 and its targeting inhibitors in osteosarcoma
Liu, Y., Liao, S., Bennett, S., Tang, H., Song, D., Wood, D., Zhan, X., & Xu, J. (2020) · Cell Proliferation · doi:10.1111/cpr.12974 · Cited by 163
Activation of endoplasmic reticulum stress response by hepatitis viruses up‐regulates protein phosphatase 2A
Christen, V., Treves, S., Duong, F., & Heim, M. (2007) · Hepatology · doi:10.1002/hep.21611 · Cited by 139
Splicing factor YBX1 mediates persistence of JAK2-mutated neoplasms
Jayavelu, A. K., Schnoeder, T. M., Perner, F., Herzog, C., Meiler, A., Krishnamoorthy, G., Huber, N., Mohr, J., Edelmann-Stephan, B., Austin, R. J., et al. (2020) · Nature · doi:10.1038/s41586-020-2968-3 · Cited by 155
The potential of activator protein 1 (AP-1) in cancer targeted therapy
Song, D., Lian, Y., & Zhang, L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1224892 · Cited by 153
MicroRNA Involvement in Signaling Pathways During Viral Infection
Barbu, M. G., Condrat, C. E., Thompson, D. C., Bugnar, O. L., Crețoiu, D., Toader, O. D., Suciu, N., & Voinea, S. C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00143 · Cited by 151
Translational and clinical advances in JAK-STAT biology: The present and future of jakinibs
Gadina, M., Johnson, C., Schwartz, D. M., Bonelli, M. M., Hasni, S., Kanno, Y., Changelian, P. S., Laurence, A. D. J., & O’Shea, J. J. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.5ri0218-084r · Cited by 162
The Erythropoietin Receptor: Molecular Structure and Hematopoietic Signaling Pathways
Watowich, S. S. (2011) · Journal of Investigative Medicine · doi:10.2310/jim.0b013e31820fb28c · Cited by 114
Transcription Factor Redundancy Ensures Induction of the Antiviral State
Schmid, S., Mordstein, M., Kochs, G., García‐Sastre, A., & tenOever, B. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.165936 · Cited by 122
Paradigm shifts in the cell biology of STAT signaling
Sehgal, P. B. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.07.003 · Cited by 135
The pathogenicity and virulence of Toxoplasma gondii
Sanchez, S. G., & Besteiro, S. (2021) · Virulence · doi:10.1080/21505594.2021.2012346 · Cited by 151
“transcription (JAK/STAT) signaling pathway, which can lead to the transcriptional modulation of hundreds of IFN-regulated genes [136,137].”
Disruption of Type I Interferon Signaling by the Nonstructural Protein of Severe Fever with Thrombocytopenia Syndrome Virus via the Hijacking of STAT2 and STAT1 into Inclusion Bodies
Ning, Y., Feng, K., Min, Y., Cao, W., Wang, M., Dèng, F., Hú, Z., & Wáng, H. (2015) · Journal of Virology · doi:10.1128/jvi.00154-15 · Cited by 144
Stat3 contributes to keloid pathogenesis via promoting collagen production, cell proliferation and migration
Lim, C. P., Phan, T.-T., Lim, I. J., & Cao, X. (2006) · Oncogene · doi:10.1038/sj.onc.1209531 · Cited by 135
“Stat3 can homodimerize, or heterodimerize with Stat1, and the dimer then translocates to the nucleus, binds to target DNA sequences and regulates the transcription of target genes (Darnell et al., 1994).”
Background
Progestins Induce Transcriptional Activation of Signal Transducer and Activator of Transcription 3 (Stat3) via a Jak- and Src-Dependent Mechanism in Breast Cancer Cells
Proietti, C. J., Salatino, M., Rosemblit, C., Carnevale, R. P., Pecci, A., Kornblihtt, A. R., Molinolo, A., Frahm, I., Charreau, E. H., Schillaci, R., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.12.4826-4840.2005 · Cited by 130
“Cytoplasmic Stats were found to be recruited to and activated either by tyrosine kinase receptors (RTKs), after binding of GFs (38, 42, 50), or by soluble tyrosine kinases of the Janus (JAK) and Src kinase families, after binding of cytokines to their receptors (16, 52).”
Background
The pleiotropic role of transcription factor STAT3 in oncogenesis and its targeting through natural products for cancer prevention and therapy
Garg, M., Shanmugam, M. K., Bhardwaj, V., Goel, A., Gupta, R., Sharma, A., Baligar, P., Kumar, A. P., Goh, B. C., Wang, L., et al. (2020) · Medicinal Research Reviews · doi:10.1002/med.21761 · Cited by 143
“The Janus kinase–signal transducer and activator of transcription (JAK–STAT) signaling pathway was originally reported as a downstream phosphorylation cascade initiated by interferon‐α (IFNα) and interleukin‐6 (IL‐6).(1,2) To date, seven members of the STAT protein family: STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, S…”
Background
Porcine Deltacoronavirus nsp5 Antagonizes Type I Interferon Signaling by Cleaving STAT2
Zhu, X.-Y., Wang, D., Zhou, J., Pan, T., Chen, J.-Y., Yang, Y., Lv, M., Ye, X., Peng, G., Fang, L.-R., et al. (2017) · Journal of Virology · doi:10.1128/jvi.00003-17 · Cited by 132
Genetic susceptibility to Candida infections
Smeekens, S. P., van de Veerdonk, F. L., Kullberg, B. J., & Netea, M. G. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201201678 · Cited by 119
“Mutations in the CC-domain of STAT1 , a signaling molecule downstream of the type I and type II IFN receptor (Darnell et al, 1994), but also IL-23 and IL-12 receptors (as heterodimer with STAT3 or STAT4), have recently been demonstrated to be the main cause of autosomal-dominant CMC (van de…”
Hypoxia induces chemoresistance in ovarian cancer cells by activation of signal transducer and activator of transcription 3
Selvendiran, K., Bratasz, A., Kuppusamy, M. L., Tazi, M., Rivera, B. K., & Kuppusamy, P. (2009) · International Journal of Cancer · doi:10.1002/ijc.24601 · Cited by 123
“STAT3 is activated by phosphorylation at the Tyr705 residue, which induces dimerization, nuclear translocation and DNA binding.(11) The resulting signal-transduction pathways permit them to”
Background
A Novel Platinum Compound Inhibits Constitutive Stat3 Signaling and Induces Cell Cycle Arrest and Apoptosis of Malignant Cells
Turkson, J., Zhang, S., Mora, L. B., Burns, A. C., Sebti, S. M., & Jove, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502694200 · Cited by 153
Gene regulatory network modeling of macrophage differentiation corroborates the continuum hypothesis of polarization states
Palma, A., Jarrah, A. S., Tieri, P., Cesareni, G., & Castiglione, F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01659 · Cited by 122
Glucocorticoids and the innate immune system: crosstalk with the toll-like receptor signaling network
Chinenov, Y., & Rogatsky, I. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.04.014 · Cited by 133
Influenza A Virus Polymerase Inhibits Type I Interferon Induction by Binding to Interferon β Promoter Stimulator 1
Iwai, A., Shiozaki, T., Kawai, T., Akira, S., Kawaoka, Y., Takada, A., Kida, H., & Miyazaki, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.112458 · Cited by 125
Expressional screening of interferon‐stimulated genes for antiviral activity against hepatitis C virus replication
Itsui, Y., Sakamoto, N., Kurosaki, M., Kanazawa, N., Tanabe, Y., Koyama, T., Takeda, Y., Nakagawa, M., Kakinuma, S., Sekine, Y., et al. (2006) · Journal of Viral Hepatitis · doi:10.1111/j.1365-2893.2006.00732.x · Cited by 131
1,25 dihydroxyvitamin‐D3 modulates JAK–STAT pathway in IL‐12/IFNγ axis leading to Th1 response in experimental allergic encephalomyelitis
Muthian, G., Raikwar, H. P., Rajasingh, J., & Bright, J. J. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20826 · Cited by 134
“…gene expression through activation of NF-jB signaling pathway (Murphy et al., 1995; Zhang and Ghosh, 2000; Du et al., 2001), IFNg augments IL-12 production through activation of JAK–STAT pathway in macrophage, microglia and dendritic cells (Darnell et al., 1994; Ma et al., 1997; Wang et al., 2000).”
Background
A Novel Inhibitor of STAT3 Homodimerization Selectively Suppresses STAT3 Activity and Malignant Transformation
Zhang, X., Sun, Y., Pireddu, R., Yang, H., Urlam, M. K., Lawrence, H. R., Guida, W. C., Lawrence, N. J., & Sebti, S. M. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3175 · Cited by 146
“STAT3 is an important regulator of many biological processes including proliferation, survival, inflammation, and immune responses (1, 2).”
BackgroundInfluential
The genetics of systemic lupus erythematosus and implications for targeted therapy
Sestak, A. L., Fürnrohr, B. G., Harley, J. B., Merrill, J. T., & Namjou, B. (2011) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2010.138057 · Cited by 125
Actions of neurotrophic factors and their signaling pathways in neuronal survival and axonal regeneration
Cui, Q. (2006) · Molecular Neurobiology · doi:10.1385/mn:33:2:155 · Cited by 130
Regulation of PTX3, a key component of humoral innate immunity in human dendritic cells: stimulation by IL-10 and inhibition by IFN-γ
Doni, A., Mosca, M., Bottazzi, B., Peri, G., Valentino, S., Polentarutti, N., Garlanda, C., & Mantovani, A. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0905493 · Cited by 115
Secretory phospholipase A2 of group IIA: Is it an offensive or a defensive player during atherosclerosis and other inflammatory diseases?
Menschikowski, M., Hagelgans, A., & Siegert, G. (2005) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2005.10.005 · Cited by 117
STAT proteins: a kaleidoscope of canonical and non-canonical functions in immunity and cancer
Awasthi, N. P., Liongue, C., & Ward, A. C. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01214-y · Cited by 155
“This creates docking sites for downstream signaling proteins containing SH2 domains, including uSTAT molecules [2, 31, 38].”
Background
The JAK/STAT Pathway in Skeletal Muscle Pathophysiology
Moresi, V., Adamo, S., & Berghella, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00500 · Cited by 145
Collagen Membrane and Immune Response in Guided Bone Regeneration: Recent Progress and Perspectives
Chu, C., Deng, J., Sun, X., Qu, Y., & Man, Y. (2017) · Tissue Engineering Part B Reviews · doi:10.1089/ten.teb.2016.0463 · Cited by 140
STAT2 and IRF9
Fink, K., & Grandvaux, N. (2013) · JAK-STAT · doi:10.4161/jkst.27521 · Cited by 122
Molecular mechanisms of liver regeneration and protection for treatment of liver dysfunction and diseases
Fujiyoshi, M., & Ozaki, M. (2010) · Journal of Hepato-Biliary-Pancreatic Sciences · doi:10.1007/s00534-010-0304-2 · Cited by 129
“The IL-6/STAT3 signaling is transmitted in the following manner [32–34].”
Background
Immune cell-specific amplification of interferon signaling by the IRF-4/8-PU. 1 complex
Kanno, Y., Levi, B.-Z., Tamura, T., & Ozato, K. (2005) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2005.25.770 · Cited by 128
“14,24 GAS has a characteristic dyad symmetry consisting of an inverted GAA repeat with spacing of 2–4 nt TTCN(2–4)GAA 25 (Fig.1).”
Activation of Stat3 Signaling in AgRP Neurons Promotes Locomotor Activity
Mesaros, A., Koralov, S. B., Rother, E., Wunderlich, F. T., Ernst, M. B., Barsh, G. S., Rajewsky, K., & Brüning, J. C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.01.007 · Cited by 128
Virus Control of Cell Metabolism for Replication and Evasion of Host Immune Responses
Moreno‐Altamirano, M. M. B., Kolstoe, S. E., & Sánchez-García, F. J. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00095 · Cited by 136
“Both IFN-α and IFN-β activate the expression of interferonstimulated genes (ISGs) through the Janus kinase-signal transducer and activator of transcription (JAK-STAT) signaling pathway, leading to the inhibition of viral replication and assembly (Darnell et al., 1994; Seth et al., 2005).”
Background
Bacterial and fungal pattern recognition receptors in homologous innate signaling pathways of insects and mammals
Stokes, B., Yadav, S., Shokal, U., Smith, L., & Eleftherianos, I. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00019 · Cited by 127
Suppression of Stat3 promotes neurogenesis in cultured neural stem cells
Gu, F., Hata, R., Ma, Y., Tanaka, J., Mitsuda, N., Kumon, Y., Hanakawa, Y., Hashimoto, K., Nakajima, K., & Sakanaka, M. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20561 · Cited by 117
“…Inc. Key words: Stat3; neural stem cell; neurogenesis; astrogliogenesis Investigations of signal transduction from interferon (IFN) receptors led to the discovery of the first member of the signal transducer and activator of transcription (Stat) protein family, Stat1 (Darnell et al., 1994).”
Background
STAT signaling in mammary gland differentiation, cell survival and tumorigenesis
Haricharan, S., & Li, Y. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.03.014 · Cited by 135
“A specific STAT is then recruited to the particular receptor-Jak complex formed, which subsequently phosphorylates and activates the STAT (Darnell et al., 1994).”
Background
Inhibition of the JAK-STAT3 pathway by andrographolide enhances chemosensitivity of cancer cells to doxorubicin
Zhou, J., Ong, C. N., Hur, G. M., & Shen, H. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.12.014 · Cited by 128
The Role of Metabolic Remodeling in Macrophage Polarization and Its Effect on Skeletal Muscle Regeneration
Santa, F. D., Vitiello, L., Torcinaro, A., & Ferraro, E. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7420 · Cited by 157
“3) (66).”

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Metadata

Record

About these checks