Insights into Cytokine–Receptor Interactions from Cytokine Engineering

Cell Signaling by Receptor Tyrosine Kinases

Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929

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

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

Mechanisms of type-I- and type-II-interferon-mediated signalling

Platanias, L. C. (2005) · Nature reviews. Immunology · doi:10.1038/nri1604 · Cited by 3,631

Differentiation of Effector CD4 T Cell Populations

Zhu, J., Yamane, H., & Paul, W. E. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101212 · Cited by 3,452

Regulation of type I interferon responses

Ivashkiv, L. B., & Donlin, L. T. (2013) · Nature reviews. Immunology · doi:10.1038/nri3581 · Cited by 3,442

Principles of interleukin (IL)-6-type cytokine signalling and its regulation

HEINRICH, P. C., BEHRMANN, I., HAAN, S., HERMANNS, H. M., MÜLLER-NEWEN, G., & SCHAPER, F. (2003) · Biochemical Journal · doi:10.1042/bj20030407 · Cited by 3,272

STATs: transcriptional control and biological impact

Levy, D. E., & Darnell, J. E. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm909 · Cited by 3,201

Interferon-stimulated genes: A complex web of host defenses

Schneider, W. M., Chevillotte, M. D., & Rice, C. M. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120231 · Cited by 3,067

A diverse range of gene products are effectors of the type I interferon antiviral response

Schoggins, J. W., Wilson, S. J., Panis, M., Murphy, M. Y., Jones, C. T., Bieniasz, P. D., & Rice, C. M. (2011) · Nature · doi:10.1038/nature09907 · Cited by 2,412

Human Growth Hormone and Extracellular Domain of Its Receptor: Crystal Structure of the Complex

de Vos, A. M., Ultsch, M. H., & Kossiakoff, A. A. (1992) · Science · doi:10.1126/science.1549776 · Cited by 2,237

Structural design and molecular evolution of a cytokine receptor superfamily.

Bazán, J. F. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.6934 · Cited by 2,054

A Hot Spot of Binding Energy in a Hormone-Receptor Interface

Clackson, T., & Wells, J. A. (1995) · Science · doi:10.1126/science.7529940 · Cited by 1,987

Rapid evolution of a protein in vitro by DNA shuffling

Stemmer, W. P. C. (1994) · Nature · doi:10.1038/370389a0 · Cited by 1,932

Interferons, interferon‐like cytokines, and their receptors

Pestka, S., Krause, C. D., & Walter, M. R. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00204.x · Cited by 1,845

A function for interleukin 2 in Foxp3-expressing regulatory T cells

Fontenot, J. D., Rasmussen, J. P., Gavin, M. A., & Rudensky, A. Y. (2005) · Nature Immunology · doi:10.1038/ni1263 · Cited by 1,819

Yeast surface display for screening combinatorial polypeptide libraries

Boder, E. T., & Wittrup, K. D. (1997) · Nature Biotechnology · doi:10.1038/nbt0697-553 · Cited by 1,774

The role of interleukin-2 during homeostasis and activation of the immune system

Boyman, O., & Sprent, J. (2012) · Nature reviews. Immunology · doi:10.1038/nri3156 · Cited by 1,743

High-Resolution Epitope Mapping of hGH-Receptor Interactions by Alanine-Scanning Mutagenesis

Cunningham, B. C., & Wells, J. A. (1989) · Science · doi:10.1126/science.2471267 · Cited by 1,361

JAK-STAT Signaling: From Interferons to Cytokines

Schindler, C., Levy, D. E., & Decker, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.r700016200 · Cited by 1,287

DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution.

Stemmer, W. P. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10747 · Cited by 1,284

Potent and Selective Stimulation of Memory-Phenotype CD8+ T Cells In Vivo by IL-15

Zhang, X. M., Sun, S., Hwang, I., Tough, D. F., & Sprent, J. (1998) · Immunity · doi:10.1016/s1074-7613(00)80564-6 · Cited by 1,248

JAK and STAT Signaling Molecules in Immunoregulation and Immune-Mediated Disease

O’Shea, J. J., & Plenge, R. M. (2012) · Immunity · doi:10.1016/j.immuni.2012.03.014 · Cited by 1,186

The JAK-STAT Signaling Pathway: Input and Output Integration

Murray, P. J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.5.2623 · Cited by 1,179

The biology of interleukin-2 and interleukin-15: implications for cancer therapy and vaccine design

Waldmann, T. A. (2006) · Nature reviews. Immunology · doi:10.1038/nri1901 · Cited by 1,174

Interferons at age 50: past, current and future impact on biomedicine

Borden, E. C., Sen, G. C., Uze, G., Silverman, R. H., Ransohoff, R. M., Foster, G. R., & Stark, G. R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2422 · Cited by 1,154

Interleukin-2 at the Crossroads of Effector Responses, Tolerance, and Immunotherapy

Liao, W., Lin, J., & Leonard, W. J. (2013) · Immunity · doi:10.1016/j.immuni.2013.01.004 · Cited by 1,107

New insights into the regulation of T cells by γc family cytokines

Rochman, Y., Spolski, R. J., & Leonard, W. J. (2009) · Nature reviews. Immunology · doi:10.1038/nri2580 · Cited by 1,082

The Biology of Interleukin-2

Malek, T. R. (2008) · Annual Review of Immunology · doi:10.1146/annurev.immunol.26.021607.090357 · Cited by 1,079

Immunomodulatory functions of type I interferons

González-Navajas, J. M., Lee, J., David, M., & Raz, E. (2012) · Nature reviews. Immunology · doi:10.1038/nri3133 · Cited by 1,030

Interleukin 15: biology and relevance to human disease

Fehniger, T. A., & Caligiuri, M. A. (2001) · Blood · doi:10.1182/blood.v97.1.14 · Cited by 976

Selective Stimulation of T Cell Subsets with Antibody-Cytokine Immune Complexes

Boyman, O., Kovář, M., Rubinstein, M., Surh, C., & Sprent, J. (2006) · Science · doi:10.1126/science.1122927 · Cited by 940

Isolating and engineering human antibodies using yeast surface display

Chao, G., Lau, W. L., Hackel, B. J., Sazinsky, S. L., Lippow, S. M., & Wittrup, K. D. (2006) · Nature Protocols · doi:10.1038/nprot.2006.94 · Cited by 913

Dimerization of the Extracellular Domain of the Human Growth Hormone Receptor by a Single Hormone Molecule

Cunningham, B. C., Ultsch, M. H., de Vos, A. M., Mulkerrin, M. G., Clauser, K. R., & Wells, J. A. (1991) · Science · doi:10.1126/science.1948064 · Cited by 873

Tolerance, not immunity, crucially depends on IL-2

Malek, T. R., & Bayer, A. L. (2004) · Nature reviews. Immunology · doi:10.1038/nri1435 · Cited by 819

The IL-2/IL-2 receptor system: A current overview

Taniguchi, T. (1993) · Cell · doi:10.1016/0092-8674(93)90152-g · Cited by 775

IL-2 family cytokines: new insights into the complex roles of IL-2 as a broad regulator of T helper cell differentiation

Liao, W., Lin, J., & Leonard, W. J. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2011.08.003 · Cited by 768

Interleukin 15 Is Required for Proliferative Renewal of Virus-specific Memory CD8 T Cells

Becker, T. C., Wherry, E. J., Boone, D. L., Murali‐Krishna, K., Antia, R., Ma, A. I., & Ahmed, R. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020369 · Cited by 685

Interleukin‐13 in asthma pathogenesis

Wills‐Karp, M. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00215.x · Cited by 683

Hexameric Structure and Assembly of the Interleukin-6/IL-6 α-Receptor/gp130 Complex

Boulanger, M. J., Chow, D., Brevnova, E. E., & García, K. C. (2003) · Science · doi:10.1126/science.1083901 · Cited by 658

Haemopoietic receptors and helical cytokines

Bazán, J. F. (1990) · Immunology Today · doi:10.1016/0167-5699(90)90139-z · Cited by 633

Rational Design of Potent Antagonists to the Human Growth Hormone Receptor

Fuh, G., Cunningham, B. C., Fukunaga, R., Nagata, S., Goeddel, D. V., & Wells, J. A. (1992) · Science · doi:10.1126/science.256.5064.1677 · Cited by 631

Signaling Through the Hematopoietic Cytokine Receptors

Ihle, J. N., Witthuhn, B. A., Quelle, F. W., Yamamoto, K., & Silvennoinen, O. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002101 · Cited by 612

Crystallographic Evidence for Preformed Dimers of Erythropoietin Receptor Before Ligand Activation

Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K., & Wilson, I. A. (1999) · Science · doi:10.1126/science.283.5404.987 · Cited by 604

Effect of an interleukin-4 variant on late phase asthmatic response to allergen challenge in asthmatic patients: results of two phase 2a studies

Wenzel, S. E., Wilbraham, D., Fuller, R. W., Getz, E. B., & Longphre, M. V. (2007) · The Lancet · doi:10.1016/s0140-6736(07)61600-6 · Cited by 587

Exploiting a natural conformational switch to engineer an interleukin-2 ‘superkine’

Levin, A. M., Bates, D. L., Ring, A. M., Krieg, C., Lin, J. T., Su, L., Moraga, I., Raeber, M. E., Bowman, G. R., Novick, P. A., et al. (2012) · Nature · doi:10.1038/nature10975 · Cited by 562

Efficiency of signalling through cytokine receptors depends critically on receptor orientation

Syed, R. S., Reid, S. W., Li, C., Cheetham, J. C., Aoki, K. H., Liu, B., Zhan, H., Osslund, T. D., Chirino, A. J., Zhang, J., et al. (1998) · Nature · doi:10.1038/26773 · Cited by 551

A novel family of growth factor receptors: A common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and the p75 IL-2 receptor β-chain

Bazán, J. F. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91528-3 · Cited by 546

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

LaPorte, S. L., Juo, Z. S., Václavíková, J., Colf, L. A., Qi, X., Heller, N. M., Keegan, A. D., & García, K. C. (2008) · Cell · doi:10.1016/j.cell.2007.12.030 · Cited by 537

Complex modulation of cell type-specific signaling in response to type I interferons

van Boxel-Dezaire, A. H. H., Rani, M. R. S., & Stark, G. R. (2006) · Immunity · doi:10.1016/j.immuni.2006.08.014 · Cited by 530

Durability of Complete Responses in Patients With Metastatic Cancer Treated With High-Dose Interleukin-2

Rosenberg, S. A., Yang, J. C., White, D. E., & Steinberg, S. M. (1998) · Annals of Surgery · doi:10.1097/00000658-199809000-00004 · Cited by 486

Structure of the Quaternary Complex of Interleukin-2 with Its α, ß, and γ c Receptors

Wang, X., Rickert, M., & García, K. C. (2005) · Science · doi:10.1126/science.1117893 · Cited by 476

Receptors for interleukin‐13 and interleukin‐4 are complex and share a novel component that functions in signal transduction.

Zurawski, S., Vega, F., Huyghe, B. G., & Zurawski, G. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05927.x · Cited by 449

High‐dose interleukin‐2 for the treatment of metastatic renal cell carcinoma

Klapper, J. A., Downey, S. G., Smith, F. O., Yang, J. C., Hughes, M. S., Kammula, U. S., Sherry, R. M., Royal, R. E., Steinberg, S. M., & Rosenberg, S. A. (2008) · Cancer · doi:10.1002/cncr.23552 · Cited by 433

Mechanism of Activation of Protein Kinase JAK2 by the Growth Hormone Receptor

Brooks, A. J., Dai, W. H., O’Mara, M. L., Abankwa, D., Chhabra, Y., Pelekanos, R., Gardon, O., Tunny, K. A., Blucher, K. M., Morton, C. J., et al. (2014) · Science · doi:10.1126/science.1249783 · Cited by 421

Interleukin-4 and Interleukin-13 Signaling Connections Maps

Kelly-Welch, A. E., Hanson, E. M., Boothby, M. R., & Keegan, A. D. (2003) · Science · doi:10.1126/science.1085458 · Cited by 417

Structural Biology of Shared Cytokine Receptors

Wang, X., Lupardus, P. J., LaPorte, S. L., & García, K. C. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.24.021605.090616 · Cited by 417

Improved IL-2 immunotherapy by selective stimulation of IL-2 receptors on lymphocytes and endothelial cells

Krieg, C., Létourneau, S., Pantaleo, G., & Boyman, O. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002569107 · Cited by 394

Structural Linkage between Ligand Discrimination and Receptor Activation by Type I Interferons

Thomas, C., Moraga, I., Levin, D., Krutzik, P. O., Podoplelova, Y., Trejo, A., Lee, C.-H., Yarden, G., Vleck, S. E., Glenn, J. S., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.048 · Cited by 380

Crystal structure of a complex between interferon-γ and its soluble high-affinity receptor

Walter, M. R., Windsor, W. T., Nagabhushan, T. L., Lundell, D. J., Lunn, C. A., Zauodny, P. J., & Narula, S. K. (1995) · Nature · doi:10.1038/376230a0 · Cited by 360

Cytokine and Cytokine Receptor Pleiotropy and Redundancy

Ozaki, K., & Leonard, W. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r200003200 · Cited by 344

Receptor and Antibody Epitopes in Human Growth Hormone Identified by Homolog-Scanning Mutagenesis

Cunningham, B. C., Jhurani, P., Ng, P. G., & Wells, J. A. (1989) · Science · doi:10.1126/science.2466339 · Cited by 342

Mature Dendritic Cells Derived from Human Monocytes Within 48 Hours: A Novel Strategy for Dendritic Cell Differentiation from Blood Precursors

Dauer, M., Obermaier, B., Herten, J., Haerle, C., Pohl, K., Rothenfußer, S., Schnurr, M. M., Endres, S., & Eigler, A. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.8.4069 · Cited by 325

Both integrated and differential regulation of components of the IL-2/IL-2 receptor system

Kim, H., Imbert, J., & Leonard, W. J. (2006) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2006.07.003 · Cited by 325

Direct Intracerebral Delivery of Cintredekin Besudotox (IL13-PE38QQR) in Recurrent Malignant Glioma: A Report by the Cintredekin Besudotox Intraparenchymal Study Group

Kunwar, S., Prados, M. D., Chang, S. M., Berger, M. S., Lang, F. F., Piepmeier, J. M., Sampson, J. H., Ram, Z., Gutin, P. H., Gibbons, R. D., et al. (2007) · Journal of Clinical Oncology · doi:10.1200/jco.2006.08.1117 · Cited by 325

The Structure of the GM-CSF Receptor Complex Reveals a Distinct Mode of Cytokine Receptor Activation

Hansen, G., Hercus, T. R., McClure, B. J., Stomski, F. C., Dottore, M., Powell, J. A., Ramshaw, H. S., Woodcock, J. M., Xu, Y., Guthridge, M. A., et al. (2008) · Cell · doi:10.1016/j.cell.2008.05.053 · Cited by 311

Soluble Interleukin-15 Receptor α (IL-15Rα)-sushi as a Selective and Potent Agonist of IL-15 Action through IL-15Rβ/γ

Mortier, E., Quéméner, A., Vusio, P., Lorenzen, I., Boublik, Y., Grötzinger, J., Plet, A., & Jacques, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508624200 · Cited by 308

HEMATOPOIETIC RECEPTOR COMPLEXES

Wells, J. A., & de Vos, A. M. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.003141 · Cited by 301

Crystal structure of the IL-2 signaling complex: Paradigm for a heterotrimeric cytokine receptor

Stauber, D. J., Debler, E., Horton, P. A., Smith, K. A., & Wilson, I. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511161103 · Cited by 288

Zinc Mediation of the Binding of Human Growth Hormone to the Human Prolactin Receptor

Cunningham, B. C., Bass, S., Fuh, G., & Wells, J. A. (1990) · Science · doi:10.1126/science.2270485 · Cited by 283

Cloning and Characterization of a Specific Interleukin (IL)-13 Binding Protein Structurally Related to the IL-5 Receptor α Chain

Caput, D., Laurent, P., Kaghad, M., Lélias, J.-M., Lefort, S., Vita, N., & Ferrara, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.28.16921 · Cited by 274

Structural basis of a unique interferon-β signaling axis mediated via the receptor IFNAR1

de Weerd, N. A., Vivian, J. P., Nguyen, T. K., Mangan, N. E., Gould, J. A., Braniff, S.-J., Zaker-Tabrizi, L., Fung, K. Y., Forster, S. C., Beddoe, T., et al. (2013) · Nature Immunology · doi:10.1038/ni.2667 · Cited by 267

Structure of an Extracellular gp130 Cytokine Receptor Signaling Complex

Chow, D., He, X. L., Snow, A. L., Rose‐John, S., & García, K. C. (2001) · Science · doi:10.1126/science.1058308 · Cited by 266

Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain

Constantinescu, S. N., Keren, T., Socolovsky, M., Nam, H.-S., Henis, Y. I., & Lodish, H. F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081069198 · Cited by 259

Cytokine structural taxonomy and mechanisms of receptor engagement

Sprang, S. R., & Bazán, J. F. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90144-a · Cited by 258

Discovery of a Potent Small Molecule IL-2 Inhibitor through Fragment Assembly

Braisted, A. C., Oslob, J. D., DeLano, W. L., Hyde, J., McDowell, R. S., Waal, N. D., Yu, C. H., Arkin, M. R., & Raimundo, B. C. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034247i · Cited by 256

Mechanistic and structural insight into the functional dichotomy between IL-2 and IL-15

Ring, A. M., Lin, J., Feng, D., Mitra, S., Rickert, M., Bowman, G. R., Pande, V. S., Li, P., Moraga, I., Spolski, R. J., et al. (2012) · Nature Immunology · doi:10.1038/ni.2449 · Cited by 252

Raising the Bar: The Curative Potential of Human Cancer Immunotherapy

Rosenberg, S. A. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003634 · Cited by 249

Treatment of Metastatic Melanoma Using Interleukin-2 Alone or in Conjunction with Vaccines

Smith, F. O., Downey, S. G., Klapper, J. A., Yang, J. C.-H., Sherry, R. M., Royal, R. E., Kammula, U. S., Hughes, M. S., Restifo, N. P., Levy, C. L., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-0116 · Cited by 239

Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation

Piehler, J., Thomas, C., Garcia, K. C., & Schreiber, G. (2012) · Immunological Reviews · doi:10.1111/imr.12001 · Cited by 230

The GM – CSF / IL‐3 / IL‐5 cytokine receptor family: from ligand recognition to initiation of signaling

Broughton, S. E., Dhagat, U., Hercus, T. R., Nero, T. L., Grimbaldeston, M. A., Bonder, C. S., Lopez, A. F., & Parker, M. W. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01164.x · Cited by 230

Affinity Maturation of Human Growth Hormone by Monovalent Phage Display

Lowman, H. B., & Wells, J. A. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1612 · Cited by 228

Inquiring into the Differential Action of Interferons (IFNs): an IFN-α2 Mutant with Enhanced Affinity to IFNAR1 Is Functionally Similar to IFN-β

Jaitin, D. A., Roisman, L. C., Jaks, E., Gavutis, M., Piehler, J., der Heyden, J. V., Uzé, G., & Schreiber, G. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1888-1897.2006 · Cited by 225

Differential Receptor Subunit Affinities of Type I Interferons Govern Differential Signal Activation

Jaks, E., Gavutis, M., Uzé, G., Martal, J., & Piehler, J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.053 · Cited by 224

IL-15:IL-15 receptor alpha superagonist complex: High-level co-expression in recombinant mammalian cells, purification and characterization

Han, K., Zhu, X., Liu, B., Jeng, E. K., Kong, L., Yovandich, J. L., Vyas, V. V., Marcus, W. D., Chavaillaz, P., Romero, C. A., et al. (2011) · Cytokine · doi:10.1016/j.cyto.2011.09.028 · Cited by 223

Endocytosis of interleukin 2 receptors in human T lymphocytes: distinct intracellular localization and fate of the receptor alpha, beta, and gamma chains.

Hémar, A., Subtil, A., Lieb, M., Morélon, E., Hellio, R., & Dautry‐Varsat, A. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.1.55 · Cited by 216

Human glioma cells overexpress receptors for interleukin 13 and are extremely sensitive to a novel chimeric protein composed of interleukin 13 and pseudomonas exotoxin.

Debinski, W., Obiri, N. I., Powers, S. K., Pastan, I. H., & Puri, R. K. (1995) · PubMed · Cited by 216

Crystal Structure of the IL-10/IL-10R1 Complex Reveals a Shared Receptor Binding Site

Josephson, K., Logsdon, N. J., & Walter, M. R. (2001) · Immunity · doi:10.1016/s1074-7613(01)00169-8 · Cited by 214

Receptor recognition by gp130 cytokines

Bravo, J., & Heath, J. K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.11.2399 · Cited by 214

Rational design of receptor-specific variants of human growth hormone.

Cunningham, B. C., & Wells, J. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3407 · Cited by 208

Diacylglycerol and Phosphatidate Generated by Phospholipases C and D, Respectively, Have Distinct Fatty Acid Compositions and Functions

Pettitt, T. R., Martin, A., Horton, T. J., Liossis, C., Lord, J. M., & Wakelam, M. J. O. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17354 · Cited by 203

CYTOKINE RECEPTOR SIGNAL TRANSDUCTION AND THE CONTROL OF HEMATOPOIETIC CELL DEVELOPMENT

Watowich, S. S., Wu, H., Socolovsky, M., Klingmüller, U., Constantinescu, S. N., & Lodish, H. F. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.91 · Cited by 200

Activation and inhibition of erythropoietin receptor function: role of receptor dimerization.

Watowich, S. S., Hilton, D. J., & Lodish, H. F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.3535 · Cited by 200

Dynamic expression profiling of type I and type III interferon-stimulated hepatocytes reveals a stable hierarchy of gene expression

Bolen, C. R., Ding, S., Robek, M. D., & Kleinstein, S. H. (2013) · Hepatology · doi:10.1002/hep.26657 · Cited by 195

Binding and activity of all human alpha interferon subtypes

Lavoie, T., Kalie, E., Crisafulli, S., Abramovich, R., DiGioia, G., Moolchan, K., Pestka, S., & Schreiber, G. (2011) · Cytokine · doi:10.1016/j.cyto.2011.07.019 · Cited by 194

Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain

Jones, B. C., Logsdon, N. J., & Walter, M. R. (2008) · Structure · doi:10.1016/j.str.2008.06.005 · Cited by 185

Conversion of human interleukin‐4 into a high affinity antagonist by a single amino acid replacement.

Kruse, N., Tony, H. P., & Sebald, W. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05401.x · Cited by 170

Transregulation of memory CD8 T-cell proliferation by IL-15Rα+ bone marrow–derived cells

Schluns, K. S., Klonowski, K. D., & Lefrançois, L. (2003) · Blood · doi:10.1182/blood-2003-08-2814 · Cited by 165

Antiproliferative Properties of Type I and Type II Interferon

Bekisz, J., Baron, S., Balinsky, C. A., Morrow, A., & Zoon, K. C. (2010) · Pharmaceuticals · doi:10.3390/ph3040994 · Cited by 164

IL-4 Receptor α Is an Important Modulator of IL-4 and IL-13 Receptor Binding: Implications for the Development of Therapeutic Targets

Andrews, A.-L., Holloway, J. W., Holgate, S. T., & Davies, D. E. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.12.7456 · Cited by 163

The Structure of Interleukin-23 Reveals the Molecular Basis of p40 Subunit Sharing with Interleukin-12

Lupardus, P. J., & García, K. C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.051 · Cited by 156

Novel Human Interleukin-15 Agonists

Zhu, X., Marcus, W. D., Xu, W. V., Lee, H.-I., Han, K., Egan, J. O., Yovandich, J. L., Rhode, P. R., & Wong, H. C. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901244 · Cited by 155

Convergent Mechanisms for Recognition of Divergent Cytokines by the Shared Signaling Receptor gp130

Boulanger, M. J., Bankovich, A. J., Kortemme, T., Baker, D. A., & García, K. C. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00365-4 · Cited by 154

Molecular Basis for Shared Cytokine Recognition Revealed in the Structure of an Unusually High Affinity Complex between IL-13 and IL-13Rα2

Lupardus, P. J., Birnbaum, M. E., & García, K. C. (2010) · Structure · doi:10.1016/j.str.2010.01.003 · Cited by 150

Tuning sensitivity to IL-4 and IL-13: differential expression of IL-4Rα, IL-13Rα1, and γc regulates relative cytokine sensitivity

Junttila, I., Mizukami, K., Dickensheets, H. L., Meier‐Schellersheim, M., Yamane, H., Donnelly, R. P., & Paul, W. E. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20080452 · Cited by 148

Signaling conformations of the tall cytokine receptor gp130 when in complex with IL-6 and IL-6 receptor

Skiniotis, G., Boulanger, M. J., García, K. C., & Walz, T. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb941 · Cited by 146

Potential use of IL-2/anti-IL-2 antibody immune complexes for the treatment of cancer and autoimmune disease

Boyman, O., Surh, C. D., & Sprent, J. (2006) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.6.12.1323 · Cited by 145

Hot-spot mimicry of a cytokine receptor by a small molecule

Thanos, C. D., DeLano, W. L., & Wells, J. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607058103 · Cited by 144

Fueling regulation: IL-2 keeps CD4+ Treg cells fit

Maloy, K. J., & Powrie, F. M. (2005) · Nature Immunology · doi:10.1038/ni1105-1071 · Cited by 137

Regulation of human Th9 differentiation by type I interferons and IL‐21

Wong, M. T., Ye, J. J., Alonso, M. N., Landrigan, A., Cheung, R. K., Engleman, E. G., & Utz, P. J. (2010) · Immunology and Cell Biology · doi:10.1038/icb.2010.53 · Cited by 136

Human IL-2 Mutein with Higher Antitumor Efficacy Than Wild Type IL-2

Carmenate, T., Pacios-Michelena, A., Enamorado, M., Moreno, E., García‐Martínez, K., Fuente, D., & León, K. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201895 · Cited by 136

Differential Functions of IL-4 Receptor Types I and II for Dendritic Cell Maturation and IL-12 Production and Their Dependency on GM-CSF

Lutz, M. B., Schnare, M., Menges, M., Rößner, S., Röllinghoff, M., Schuler, G., & Gessner, A. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.7.3574 · Cited by 135

A T-cell-selective interleukin 2 mutein exhibits potent antitumor activity and is well tolerated in vivo

Shanafelt, A. B., Lin, Y., Shanafelt, M.-C., Forte, C. P., Dubois‐Stringfellow, N., Carter, C., Gibbons, J. A., Cheng, S.-L., Delaria, K. A., Fleischer, R., et al. (2000) · Nature Biotechnology · doi:10.1038/81199 · Cited by 135

Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation 1 1Edited by J. Karn

Frisch, C., Schreiber, G., Johnson, C. M., & Fersht, A. R. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0892 · Cited by 133

Targeting IL-15 Receptor-Bearing Cells with an Antagonist Mutant IL-15/Fc Protein Prevents Disease Development and Progression in Murine Collagen-Induced Arthritis

Ferrari‐Lacraz, S., Zanelli, E. H., Neuberg, M., Donskoy, E., Kim, Y. S., Zheng, X. X., Hancock, W. W., Maśliński, W., Li, X. C., Strom, T. B., et al. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.9.5818 · Cited by 130

Evolution of a cytokine using DNA family shuffling

Chang, C.-C. J., Chen, T. T., Cox, B. W., Dawes, G. N., Stemmer, W. P. C., Punnonen, J., & Patten, P. A. (1999) · Nature Biotechnology · doi:10.1038/11737 · Cited by 128

The Stability of the Ternary Interferon-Receptor Complex Rather than the Affinity to the Individual Subunits Dictates Differential Biological Activities

Kalie, E., Jaitin, D. A., Podoplelova, Y., Piehler, J., & Schreiber, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806019200 · Cited by 127

Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex

Tamada, T., Honjo, E., Maeda, Y., Okamoto, T., Ishibashi, M., Tokunaga, M., & Kuroki, R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511264103 · Cited by 119

Durability of Complete Responses in Patients With Metastatic Cancer Treated With High-Dose Interleukin-2. Identification of the Antigens Mediating Response

Rosenberg, S. A., Yang, J., White, D. E., & Steinberg, S. M. (1999) · The Journal of Urology · doi:10.1016/s0022-5347(05)68669-7 · Cited by 116

Optimizing the affinity and specificity of proteins with molecular display

Levin, A. M., & Weiss, G. A. (2005) · Molecular BioSystems · doi:10.1039/b511782h · Cited by 114

Structure-Function Studies of Interleukin 15 using Site-specific Mutagenesis, Polyethylene Glycol Conjugation, and Homology Modeling

Pettit, D. K., Bonnert, T. P., Eisenman, J. R., Srinivasan, S., Paxton, R., Beers, C., Lynch, D., Miller, B., Yost, J., Grabstein, K. H., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2312 · Cited by 113

Structural Organization of a Full-Length gp130/LIF-R Cytokine Receptor Transmembrane Complex

Skiniotis, G., Lupardus, P. J., Martick, M. M., Walz, T., & García, K. C. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.011 · Cited by 112

Crystal structure of the IL-15–IL-15Rα complex, a cytokine-receptor unit presented in trans

Chirifu, M., Hayashi, C., Nakamura, T., Toma, Š., Shuto, T., Kai, H., Yamagata, Y., Davis, S. J., & Ikemizu, S. (2007) · Nature Immunology · doi:10.1038/ni1492 · Cited by 110

Multifaceted Activities of Type I Interferon Are Revealed by a Receptor Antagonist

Levin, D., Schneider, W. M., Hoffmann, H.-H., Yarden, G., Busetto, A. G., Manor, O., Sharma, N., Rice, C. M., & Schreiber, G. (2014) · Science Signaling · doi:10.1126/scisignal.2004998 · Cited by 109

Engineering Human Prolactin to Bind to the Human Growth Hormone Receptor

Cunningham, B. C., Henner, D. J., & Wells, J. A. (1990) · Science · doi:10.1126/science.2321008 · Cited by 108

Novel anti–brain tumor cytotoxins specific for cancer cells

Debinski, W., Gibo, D. M., Obiri, N. I., Kealiher, A., & Puri, R. K. (1998) · Nature Biotechnology · doi:10.1038/nbt0598-449 · Cited by 107

Emerging families of cytokines and receptors

Bazán, J. F. (1993) · Current Biology · doi:10.1016/0960-9822(93)90009-d · Cited by 106

Interleukin-13 in asthma pathogenesis

Wills-Karp, M. A. (2004) · Current Allergy and Asthma Reports · doi:10.1007/s11882-004-0057-6 · Cited by 104

Mechanistic Diversity of Cytokine Receptor Signaling Across Cell Membranes

Stroud, R. M., & Wells, J. A. (2004) · Science s STKE · doi:10.1126/stke.2312004re7 · Cited by 103

Structure of the Complete Extracellular Domain of the Common β Subunit of the Human GM-CSF, IL-3, and IL-5 Receptors Reveals a Novel Dimer Configuration

Carr, P. D., Gustin, S. E., Church, A. P., Murphy, J. M., Ford, S. C., Mann, D. A., Woltring, D., Walker, I. G., Ollis, D. L., & Young, I. G. (2001) · Cell · doi:10.1016/s0092-8674(01)00213-6 · Cited by 103

Receptor Recognition Sites of Cytokines Are Organized as Exchangeable Modules

Kallen, K., Grötzinger, J., Lelièvre, E., Vollmer, P., Aasland, D., Renné, C., Müllberg, J., Büschenfelde, K. M. Z., Gascan, H., & Rose‐John, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.11859 · Cited by 102

Crystal Structure of the Entire Ectodomain of gp130

Xu, Y., Kershaw, N. J., Luo, C. S., Soo, P., Pocock, M. J., Czabotar, P. E., Hilton, D. J., Nicola, N. A., Garrett, T., & Zhang, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.129502 · Cited by 100

Receptor Density Is Key to the Alpha2/Beta Interferon Differential Activities

Moraga, I., Harari, D., Schreiber, G., Uzé, G., & Pellegrini, S. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01808-08 · Cited by 100

An Interferon α2 Mutant Optimized by Phage Display for IFNAR1 Binding Confers Specifically Enhanced Antitumor Activities

Kalie, E., Jaitin, D. A., Abramovich, R., & Schreiber, G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610115200 · Cited by 98

Signalling by the βc family of cytokines

Hercus, T. R., Dhagat, U., Kan, W. L., Broughton, S. E., Nero, T. L., Perugini, M., Sandow, J. J., D’Andrea, R. J., Ekert, P. G., Hughes, T. P., et al. (2013) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2013.03.002 · Cited by 97

An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor

Huyton, T., Zhang, J., Luo, C. S., Lou, M.-Z., Hilton, D. J., Nicola, N. A., & Garrett, T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705577104 · Cited by 94

Shared Cytokine Signaling Receptors: Structural Insights from the Gp130 System

Boulanger, M. J., & García, K. C. (2004) · Advances in protein chemistry · doi:10.1016/s0065-3233(04)68004-1 · Cited by 91

Application of IL-2 and other cytokines in renal cancer

McDermott, D. F., & Atkins, M. B. (2004) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.4.4.455 · Cited by 90

Gene therapy-mediated delivery of targeted cytotoxins for glioma therapeutics

Candolfi, M., Xiong, W., Yagiz, K., Liu, C., Muhammad, A. K. M. G., Puntel, M., Foulad, D. S., Zadmehr, A., Ahlzadeh, G. E., Kroeger, K. M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008261107 · Cited by 87

Redirecting cell-type specific cytokine responses with engineered interleukin-4 superkines

Junttila, I., Creusot, R. J., Moraga, I., Bates, D. L., Wong, M. T., Alonso, M. N., Suhoski, M. M., Lupardus, P. J., Meier‐Schellersheim, M., Engleman, E. G., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1096 · Cited by 85

Receptor for Interleukin (IL) 13 Does Not Interact with IL4 but Receptor for IL4 Interacts with IL13 on Human Glioma Cells

Debinski, W., Miner, R., Leland, P., Obiri, N. I., & Puri, R. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22428 · Cited by 83

Differential recognition of the type I interferon receptor by interferons tau and alpha is responsible for their disparate cytotoxicities.

Subramaniam, P. S., Khan, S., Pontzer, C. H., & Johnson, H. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12270 · Cited by 81

Interferon: Current Status and Future Prospects in Cancer Therapy

Wang, B. X., Rahbar, R., & Fish, E. N. (2011) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2010.0158 · Cited by 81

Mutational Analysis of the IFNAR1 Binding Site on IFNα2 Reveals the Architecture of a Weak Ligand–Receptor Binding-site

Roisman, L. C., Jaitin, D. A., Baker, D. P., & Schreiber, G. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.042 · Cited by 80

Compensatory Energetic Mechanisms Mediating the Assembly of Signaling Complexes Between Interleukin-2 and its α, β, and γc Receptors

Rickert, M., Boulanger, M. J., Goriatcheva, N., & García, K. C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.038 · Cited by 80

The Dynamics of Signal Triggering in a gp130-Receptor Complex

Matadeen, R., Hon, W., Heath, J. K., Jones, E. Y., & Fuller, S. (2007) · Structure · doi:10.1016/j.str.2007.02.006 · Cited by 80

The IL-15-based superagonist ALT-803 promotes the antigen-independent conversion of memory CD8+T cells into innate-like effector cells with antitumor activity

Wong, H. C., Jeng, E. K., & Rhode, P. R. (2013) · OncoImmunology · doi:10.4161/onci.26442 · Cited by 80

Multifarious Determinants of Cytokine Receptor Signaling Specificity

Moraga, I., Spangler, J. B., Mendoza, J. L., & García, K. C. (2014) · Advances in immunology · doi:10.1016/b978-0-12-800100-4.00001-5 · Cited by 79

An Antagonist IL-15/Fc Protein Prevents Costimulation Blockade-Resistant Rejection

Ferrari‐Lacraz, S., Zheng, X. X., Kim, Y. S., Li, Y., Maśliński, W., Li, X. C., & Strom, T. B. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.6.3478 · Cited by 74

The ppp(A2′p)nA and Protein Kinase Systems in Wild‐Type and Interferon‐Resistant Daudi Cells

Silverman, R. H., Watling, D., Balkwill, F. R., Trowsdale, J., & Kerr, I. M. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06783.x · Cited by 72

Interleukin-13 sensitivity and receptor phenotypes of human glial cell lines: non-neoplastic glia and low-grade astrocytoma differ from malignant glioma

Liu, H., Jacobs, B., Liu, J., Prayson, R. A., Estes, M. L., Barnett, G. H., & Barna, B. P. (2000) · Cancer Immunology Immunotherapy · doi:10.1007/s002620000110 · Cited by 71

Molecular Mechanisms for Viral Mimicry of a Human Cytokine: Activation of gp130 by HHV-8 Interleukin-6

Boulanger, M. J., Chow, D., Brevnova, E. E., Martick, M. M., Sandford, G. R., Nicholas, J., & García, K. C. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.070 · Cited by 69

High-Affinity CD25-Binding IL-2 Mutants Potently Stimulate Persistent T Cell Growth

Rao, B. M., Driver, I. H., Lauffenburger, D. A., & Wittrup, K. D. (2005) · Biochemistry · doi:10.1021/bi050436x · Cited by 69

Interleukin-2 mutants with enhanced -receptor subunit binding affinity

Rao, B. M., Girvin, A. T., Ciardelli, T. L., Lauffenburger, D. A., & Wittrup, K. D. (2003) · Protein Engineering Design and Selection · doi:10.1093/protein/gzg111 · Cited by 67

Comparison of Gene Expression Patterns Induced by Treatment of Human Umbilical Vein Endothelial Cells with IFN- α 2b vs. IFN- β 1a: Understanding the Functional Relationship Between Distinct Type I Interferons That Act Through a Common Receptor

da Silva, A. J., Brickelmaier, M., Majeau, G. R., Lukashin, A. V., Peyman, J. A., Whitty, A., & Hochman, P. S. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753536149 · Cited by 66

Cytokine–receptor interactions as drug targets

Schreiber, G., & Walter, M. R. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.06.165 · Cited by 64

The Basis of Distinctive IL-2– and IL-15–Dependent Signaling: Weak CD122-Dependent Signaling Favors CD8+ T Central-Memory Cell Survival but Not T Effector-Memory Cell Development

Castro, I., Yu, A., Dee, M. J., & Malek, T. R. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003961 · Cited by 64

Partial agonist/antagonist mouse interleukin‐2 proteins indicate that a third component of the receptor complex functions in signal transduction.

Zurawski, S., Imler, J. L., & Zurawski, G. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07610.x · Cited by 64

A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor

Kraich, M., Klein, M., Patiño, E., Harrer, H., Nickel, J., Sebald, W., & Mueller, T. D. (2006) · BMC Biology · doi:10.1186/1741-7007-4-13 · Cited by 61

Activation and Inhibition of Erythropoietin Receptor Function: Role of Receptor Dimerization

Watowich, S. S., Hilton, D. J., & Lodish, H. F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.3535-3549.1994 · Cited by 59

Structural Basis for Cytokine Hormone-Receptor Recognition and Receptor Activation

Kossiakoff, A. A., & de Vos, A. M. (1998) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60433-7 · Cited by 58

New and experimental therapies for HCV

Pereira, A. A., & Jacobson, I. M. (2009) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2009.92 · Cited by 58

The high-affinity interaction of human IL-4 and the receptor α chain is constituted by two independent binding clusters

Zhang, J.-L., Simeonowa, I., Wang, Y., & Sebald, W. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5243 · Cited by 57

Phase I Trial of BAY 50-4798, an Interleukin-2–Specific Agonist in Advanced Melanoma and Renal Cancer

Margolin, K. A., Atkins, M. B., Dutcher, J. P., Ernstoff, M. S., Smith, J. W., Clark, J. I., Baar, J., Sosman, J. A., Weber, J. S., Lathia, C. D., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1341 · Cited by 56

Crystal Structures of the Pro-Inflammatory Cytokine Interleukin-23 and Its Complex with a High-Affinity Neutralizing Antibody

Beyer, B. M., Ingram, R. N., Ramanathan, L., Reichert, P., Le, H. V., Madison, V., & Orth, P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.001 · Cited by 56

A phase I dose-escalation study of the immunocytokine EMD 521873 (Selectikine) in patients with advanced solid tumours

Gillessen, S., Gnad-Vogt, U., Gallerani, E., Beck, J., Sessa, C., Omlin, A. G., Mattiacci, M. R., Liedert, B., Kramer, D., Laurent, J., et al. (2012) · European Journal of Cancer · doi:10.1016/j.ejca.2012.07.015 · Cited by 54

Adjuvants targeting innate and adaptive immunity synergize to enhance tumor immunotherapy

Verdeil, G., Marquardt, K., Surh, C. D., & Sherman, L. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805054105 · Cited by 52

Rational design of a GCN4-derived mimetic of interleukin-4.

Oschkinat, H., Serrano, L. G., Domingues, H., Cregut, D., & Sebald, W. (1999) · Nature Structural Biology · doi:10.1038/10706 · Cited by 50

Structure Analysis of the IL-5 Ligand-Receptor Complex Reveals a Wrench-like Architecture for IL-5Rα

Patiño, E., Kotzsch, A., Saremba, S., Nickel, J., Schmitz, W., Sebald, W., & Mueller, T. D. (2011) · Structure · doi:10.1016/j.str.2011.08.015 · Cited by 48

A phase I trial of continuous infusion interleukin-4 (IL-4) alone and following interleukin-2 (IL-2) in cancer patients

Sosman, J. A., Kefer, C., Fisher, R. I., Ellis, T. M., & Fisher, S. G. (1994) · Annals of Oncology · doi:10.1093/oxfordjournals.annonc.a058878 · Cited by 47

Increased Endosomal Sorting of Ligand to Recycling Enhances Potency of an Interleukin-2 Analog

Fallon, E. M., Liparoto, S. F., Lee, K. J., Ciardelli, T. L., & Lauffenburger, D. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.6790 · Cited by 47

Clathrin-lndependent endocytosis and signalling of interleukin 2 receptors IL-2R endocytosis and signalling.

Gesbert, F., Sauvonnet, N., & Dautry‐Varsat, A. (2004) · PubMed · Cited by 46

Receptor antagonist and selective agonist derivatives of mouse interleukin‐2.

Zurawski, S., & Zurawski, G. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05483.x · Cited by 45

Structural Analysis of IL-10 and Type I Interferon Family Members and their Complexes with Receptor

Walter, M. R. (2004) · Advances in protein chemistry · doi:10.1016/s0065-3233(04)68006-5 · Cited by 45

Interleukin 13 Mutants of Enhanced Avidity Toward the Glioma-Associated Receptor, IL13Rα2

Madhankumar, A. B., Mintz, A., & Debinski, W. (2004) · Neoplasia · doi:10.1016/s1476-5586(04)80049-6 · Cited by 45

Combination treatment with IL-2 and anti-IL-2 mAbs reduces tumor metastasis via NK cell activation

Jin, G.-H., Hirano, T., & Murakami, M. (2008) · International Immunology · doi:10.1093/intimm/dxn036 · Cited by 45

Engineered Interleukin-2 Antagonists for the Inhibition of Regulatory T Cells

Liu, D. V., Maier, L. M., Hafler, D. A., & Wittrup, K. D. (2009) · Journal of Immunotherapy · doi:10.1097/cji.0b013e3181b528da · Cited by 44

Antiproliferative Effects of Interferons on Human Melanoma Cells in the Human Tumor Colony-Forming Assay

Schiller, J. H., Willson, J. K. V., Bittner, G., Wolberg, W. H., Hawkins, M., & Borden, E. C. (1986) · Journal of Interferon Research · doi:10.1089/jir.1986.6.615 · Cited by 43

Prolonged STAT1 activation related to the growth arrest of malignant lymphoma cells by interferon-alpha.

Grimley, P., Fang, H., Rui, H., Petricoin, E. F., Ray, S., Dong, F., Fields, K., Hu, R., Zoon, K., Audet, S., et al. (1998) · Blood · doi:10.1182/blood.v91.8.3017.3017_3017_3027 · Cited by 42

The interleukin‐4 site‐2 epitope determining binding of the common receptor γ chain

Letzelter, F., Wang, Y., & Sebald, W. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2570011.x · Cited by 42

IN VIVO EXPRESSION OF THE INTERLEUKIN 4 RECEPTOR ALPHA BY ASTROCYTES IN EPILEPSY CEREBRAL CORTEX

Liu, H., Prayson, R. A., Estes, M. L., Drazba, J. A., Barnett, G. H., Bingaman, W. E., Liu, J., Jacobs, B., & Barna, B. P. (2000) · Cytokine · doi:10.1006/cyto.2000.0773 · Cited by 41

An immune cell-selective interleukin 4 agonist

Shanafelt, A. B., Forte, C. P., Kasper, J. J., Sanchez-Pescador, L., Wetzel, M., Gundel, R. H., & Greve, J. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9454 · Cited by 41

General Classes and Functions of Four-Helix Bundle Cytokines

Nicola, N. A., & Hilton, D. J. (1998) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60432-5 · Cited by 37

Expressed Gene Clusters Associated with Cellular Sensitivity and Resistance Towards Anti-viral and Anti-proliferative Actions of Interferon

Khabar, K. S. A., Al‐Haj, L., Al-Zoghaibi, F., Marie, M., Dhalla, M., Polyak, S. J., & Williams, B. R. G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.065 · Cited by 37

Fighting cancers from within: augmenting tumor immunity with cytokine therapy

Pellegrini, M., Mak, T. W., & Ohashi, P. S. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.05.003 · Cited by 35

Directed evolution of gene-shuffled IFN-α molecules with activity profiles tailored for treatment of chronic viral diseases

Brideau-Andersen, A. D., Huang, X., Sun, S.-C. C., Chen, T. T., Stark, D. M., Sas, I. J., Zadik, L., Dawes, G. N., Guptill, D. R., McCord, R., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609001104 · Cited by 35

Cytokine receptor activation at the cell surface

Broughton, S. E., Hercus, T. R., Lopez, A. F., & Parker, M. W. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.03.015 · Cited by 35

Mutation of the IFNAR-1 Receptor Binding Site of Human IFN-α2 Generates Type I IFN Competitive Antagonists

Pan, M., Kalie, E., Scaglione, B. J., Raveche, E. S., Schreiber, G., & Langer, J. A. (2008) · Biochemistry · doi:10.1021/bi801588g · Cited by 34

T-cell activation by treatment of cancer patients with EMD 521873 (Selectikine), an IL-2/anti-DNA fusion protein

Laurent, J., Touvrey, C., Gillessen, S., Joffraud, M., Vicari, M., Bertrand, C., Ongarello, S., Liedert, B., Gallerani, E., Beck, J., et al. (2013) · Journal of Translational Medicine · doi:10.1186/1479-5876-11-5 · Cited by 33

Affinity Maturation of Leukemia Inhibitory Factor and Conversion to Potent Antagonists of Signaling

Fairlie, W. D., Uboldi, A. D., McCoubrie, J. E., Wang, C. C., Lee, E. F., Yao, S., Souza, D. P. D., Mifsud, S., Metcalf, D., Nicola, N. A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310103200 · Cited by 32

Intramolecular Cooperativity in a Protein Binding Site Assessed by Combinatorial Shotgun Scanning Mutagenesis

Pál, G., Ultsch, M. H., Clark, K. P., Currell, B., Kossiakoff, A. A., & Sidhu, S. S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.040 · Cited by 28

A Point Mutation in Interleukin-2 That Alters Ligand Internalization

Chang, D. Z., Wu, Z., & Ciardelli, T. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13349 · Cited by 27

Mutagenic Analysis of a Receptor Contact Site on Interleukin-2: Preparation of an IL-2 Analog with Increased Potency

Berndt, W. G., Chang, D. Z., Smith, K. A., & Ciardelli, T. L. (1994) · Biochemistry · doi:10.1021/bi00187a026 · Cited by 26

Systemic Delivery of Tumor-Targeted p53 Gene Therapy Results in Chemo/Radiosensitization

Chang, E. H. (1999) · Nature Biotechnology · doi:10.1038/70147 · Cited by 26

Receptor binding and internalization of mouse interleukin-2 derivatives that are partial agonists.

Imler, J. L., & Zurawski, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42192-8 · Cited by 24

De novo design of an IL-4 antagonist and its structure at 1.9 Å

LaPorte, S. L., Forsyth, C. M., Cunningham, B. C., Miercke, L. J. W., Akhavan, D., & Stroud, R. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408890102 · Cited by 23

New perspectives on the design of cytokines and growth factors

Kallen, K.-J., Grötzinger, J., & Rose‐John, S. (2000) · Trends in biotechnology · doi:10.1016/s0167-7799(00)01492-x · Cited by 23

Chimera of IL-2 Linked to Light Chain of anti-IL-2 mAb Mimics IL-2/anti-IL-2 mAb Complexes Both Structurally and Functionally

Tomala, J., Kovářová, J., Kabešová, M., Votavová, P., Chmelova, H., Dvořáková, B., Řı́hová, B., & Kovář, M. (2013) · ACS Chemical Biology · doi:10.1021/cb3007242 · Cited by 18

Targeted Toxins for Glioblastoma Multiforme: Pre-Clinical Studies and Clinical Implementation

Candolfi, M., Kroeger, K. M., Xiong, W., Liu, C., Puntel, M., Yagiz, K., Muhammad, A. G., Mineharu, Y., Foulad, D. S., Wibowo, M., et al. (2011) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152011797378689 · Cited by 18

Rational Design of Interleukin-21 Antagonist through Selective Elimination of the γC Binding Epitope

Kang, L., Bondensgaard, K., Li, T., Hartmann, R., & Hjorth, S. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101444 · Cited by 15

Therapeutic Enhancement of IL-2 Through Molecular Design

Cassell, D. J., Choudhri, S., Humphrey, R. W., Martell, R. E., Reynolds, T., & Shanafelt, A. B. (2002) · Current Pharmaceutical Design · doi:10.2174/1381612023393260 · Cited by 15

Mechanisms and consequences of Jak–STAT signaling in the immune system

Villarino, A. V., Kanno, Y., & O'Shea, J. J. (2017) · Nature Immunology · doi:10.1038/ni.3691 · Cited by 1,221

The molecular details of cytokine signaling via the JAK/STAT pathway

Morris, R., Kershaw, N. J., & Babon, J. J. (2018) · Protein Science · doi:10.1002/pro.3519 · Cited by 943

Interleukin-6 Family CytokinesPreprint

Rose‐John, S. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028415 · Cited by 846

The JAK-STAT pathway at 30: Much learned, much more to do

Philips, R. L., Wang, Y., Cheon, H., Kanno, Y., Gadina, M., Sartorelli, V., Horvath, C. M., Darnell, J. E., Jr., Stark, G. R., & O’Shea, J. J. (2022) · Cell · doi:10.1016/j.cell.2022.09.023 · Cited by 755

Atopic dermatitis: an expanding therapeutic pipeline for a complex disease

Bieber, T. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00266-6 · Cited by 623

Cytokine engineering for targeted immunotherapy

Bakhshi, P., Ho, J. Q., Zaer, N., Webster, T. J., & Zanganeh, S. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-21521-6.00011-9

Recent and future perspectives on engineering interferons and other cytokines as therapeutics

Aung, T., Grubbe, W. S., Nusbaum, R. J., & Mendoza, J. L. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.09.005 · Cited by 34

The use of supercytokines, immunocytokines, engager cytokines, and other synthetic cytokines in immunotherapy

Zheng, X., Wu, Y., Bi, J., Huang, Y., Cheng, Y., Li, Y., Wu, Y., Cao, G., & Tian, Z. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-021-00786-6 · Cited by 157

Emerging principles of cytokine pharmacology and therapeutics

Saxton, R. A., Glassman, C. R., & García, K. C. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00557-6 · Cited by 223

Engineering cytokine receptors to control cellular functions

Kawahara, M., Ueda, H., & Nagamune, T. (2009) · Biochemical Engineering Journal · doi:10.1016/j.bej.2009.09.010 · Cited by 24