The SOCS box—Adapting proteins for ubiquitination and proteasomal degradation

RING Domain E3 Ubiquitin Ligases

Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679 · see citing works

A family of cytokine-inducible inhibitors of signalling

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

SOCS proteins, cytokine signalling and immune regulation

Yoshimura, A., Naka, T., & Kubo, M. (2007) · Nature Reviews Immunology · doi:10.1038/nri2093 · Cited by 1,580 · see citing works

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507 · see citing works

SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2

Rui, L., Yuan, M., Frantz, D., Shoelson, S., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200444200 · Cited by 904 · see citing works

Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function

Stebbins, C. E., Kaelin, W. G., & Pavletich, N. P. (1999) · Science · doi:10.1126/science.284.5413.455 · Cited by 852 · see citing works

SOCS3 negatively regulates IL-6 signaling in vivo

Croker, B. A., Krebs, D. L., Zhang, J.-G., Wormald, S., Willson, T. A., Stanley, E. G., Robb, L., Greenhalgh, C. J., Förster, I., Clausen, B. E., et al. (2003) · Nature Immunology · doi:10.1038/ni931 · Cited by 840 · see citing works

The ankyrin repeat: a diversity of interactions on a common structural framework

Sedgwick, S. G., & Smerdon, S. J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01426-7 · Cited by 823 · see citing works

The emerging complexity of protein ubiquitination

Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821 · see citing works

TRIM proteins and cancer

Hatakeyama, S. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3139 · Cited by 805 · see citing works

Twenty proteins containing a C-terminal SOCS box form five structural classes

Hilton, D. J., Richardson, R. T., Alexander, W. S., Viney, E. M., Willson, T. A., Sprigg, N. S., Starr, R., Nicholson, S. E., Metcalf, D., & Nicola, N. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.1.114 · Cited by 728 · see citing works

Binding of the von Hippel-Lindau Tumor Suppressor Protein to Elongin B and C

Kibel, A. S., Iliopoulos, O., DeCaprio, J. A., & Kaelin, W. G. (1995) · Science · doi:10.1126/science.7660130 · Cited by 664 · see citing works

Regulation of NF-κB Signaling by Pin1-Dependent Prolyl Isomerization and Ubiquitin-Mediated Proteolysis of p65/RelA

Ryo, A., Suizu, F., Yoshida, Y., Perrem, K., Liou, Y., Wulf, G. M., Rottapel, R. K., Yamaoka, S., & Lu, K. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00490-8 · Cited by 632 · see citing works

The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation

Zhang, J., Farley, A., Nicholson, S. E., Willson, T. A., Zugaro, L. M., Simpson, R. J., Moritz, R. L., Cary, D., Richardson, R. T., Hausmann, G., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2071 · Cited by 626 · see citing works

Insights into SCF ubiquitin ligases from the structure of the Skp1–Skp2 complex

Schulman, B. A., Carrano, A. C., Jeffrey, P. D., Bowen, Z., Kinnucan, E., Finnin, M. S., Elledge, S. J., Harper, J. W., Pagano, M., & Pavletich, N. P. (2000) · Nature · doi:10.1038/35042620 · Cited by 610 · see citing works

SOCS regulation of the JAK/STAT signalling pathway

Croker, B. A., Kiu, H., & Nicholson, S. E. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.07.010 · Cited by 610 · see citing works

The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families

Kamura, T., Sato, S., Haque, D., Liu, L., Kaelin, W. G., Conaway, R. C., & Conaway, J. W. (1998) · Genes & Development · doi:10.1101/gad.12.24.3872 · Cited by 595 · see citing works

Hepatitis C Virus Down-Regulates Insulin Receptor Substrates 1 and 2 through Up-Regulation of Suppressor of Cytokine Signaling 3

Kawaguchi, T., Yoshida, T., Harada, M., Hisamoto, T., Nagao, Y., Ide, T., Taniguchi, E., Kumemura, H., Hanada, S., Maeyama, M., et al. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63408-6 · Cited by 534 · see citing works

Identification of the von Hippel–Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex

Iwai, K., Yamanaka, K., Kamura, T., Minato, N., Conaway, R. C., Conaway, J. W., Klausner, R. D., & Pause, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12436 · Cited by 508 · see citing works

Gigantism in mice lacking suppressor of cytokine signalling-2

Metcalf, D., Greenhalgh, C. J., Viney, E. M., Willson, T. A., Starr, R., Nicola, N. A., Hilton, D. J., & Alexander, W. S. (2000) · Nature · doi:10.1038/35016611 · Cited by 490 · see citing works

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligasesPreprint

Kamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., & Nakayama, K. I. (2004) · Genes & Development · doi:10.1101/gad.1252404 · Cited by 476 · see citing works

Suppressor of cytokine signaling-3 preferentially binds to the SHP-2-binding site on the shared cytokine receptor subunit gp130

Nicholson, S. E., De Souza, D., Fabri, L. J., Corbin, J., Willson, T. A., Zhang, J.-G., Silva, A., Asimakis, M., Farley, A., Nash, A. D., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100135197 · Cited by 456 · see citing works

Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death

Vucic, D., Dixit, V. M., & Wertz, I. E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3143 · Cited by 451 · see citing works

The SOCS box: a tale of destruction and degradation

Kile, B. T., Schulman, B. A., Alexander, W. S., Nicola, N. A., Martin, H. M., & Hilton, D. J. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02085-6 · Cited by 433 · see citing works

Liver degeneration and lymphoid deficiencies in mice lacking suppressor of cytokine signaling-1

Starr, R., Metcalf, D., Elefanty, A. G., Brysha, M., Willson, T. A., Nicola, N. A., Hilton, D. J., & Alexander, W. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.24.14395 · Cited by 421 · see citing works

A census of protein repeats

Marcotte, E. M., Pellegrini, M. A., Yeates, T. O., & Eisenberg, D. S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3136 · Cited by 412 · see citing works

Cytokine‐inducible SH2 protein‐3 (CIS3/SOCS3) inhibits <i>Janus</i> tyrosine kinase by binding through the N‐terminal kinase inhibitory region as well as SH2 domain

Sasaki, A., Yasukawa, H., Suzuki, A., Kamizono, S., Syoda, T., Kinjyo, I., Sasaki, M., Johnston, J. A., & Yoshimura, A. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00263.x · Cited by 398 · see citing works

The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2

Kamizono, S., Hanada, T., Yasukawa, H., Minoguchi, S., Kato, R., Minoguchi, M., Hattori, K., Hatakeyama, S., Yada, M., Morita, S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010074200 · Cited by 311 · see citing works

Genetic analysis of von Hippel-Lindau disease

Nordstrom-O'Brien, M., van der Luijt, R. B., van Rooijen, E., van den Ouweland, A. M., Majoor‐Krakauer, D. F., Lolkema, M. P., van Brussel, A. S. A., Voest, E. E., & Giles, R. H. (2010) · Human Mutation · doi:10.1002/humu.21219 · Cited by 310 · see citing works

SOCS3 Is a Critical Physiological Negative Regulator of G-CSF Signaling and Emergency Granulopoiesis

Croker, B. A., Metcalf, D., Robb, L., Wei, W., Mifsud, S., DiRago, L., Cluse, L. A., Sutherland, K. D., Hartley, L., Williams, E., et al. (2004) · Immunity · doi:10.1016/s1074-7613(04)00022-6 · Cited by 285 · see citing works

SOCS2 negatively regulates growth hormone action in vitro and in vivo.

Greenhalgh, C., Rico-Bautista, E., Lorentzon, M., Thaus, A. L., Morgan, P., Willson, T., Zervoudakis, P., Metcalf, D., Street, I. H., Nicola, N., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22710 · Cited by 269 · see citing works

Deubiquitinases in the regulation of NF-κB signaling

Harhaj, E. W., & Dixit, V. M. (2010) · Cell Research · doi:10.1038/cr.2010.166 · Cited by 261 · see citing works

Regulation of Jak2 through the Ubiquitin-Proteasome Pathway Involves Phosphorylation of Jak2 on Y1007 and Interaction with SOCS-1

Ungureanu, D., Saharinen, P., Junttila, I., Hilton, D. J., & Silvennoinen, O. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3316-3326.2002 · Cited by 260 · see citing works

SOCS2 negatively regulates growth hormone action in vitro and in vivo

Greenhalgh, C. J., Rico-Bautista, E., Lorentzon, M., Thaus, A. L., Morgan, P. O., Willson, T. A., Zervoudakis, P., Metcalf, D., Street, I. P., Nicola, N. A., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci200522710 · Cited by 257 · see citing works

The ANK repeat: a ubiquitous motif involved in macromolecular recognition

Michaely, P., & Bennett, V. (1992) · Trends in Cell Biology · doi:10.1016/0962-8924(92)90084-z · Cited by 232 · see citing works

The Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid hormone activation and PTHrP secretion in the developing growth plate

Dentice, M., Bandyopadhyay, A., Gereben, B., Callebaut, I., Christoffolete, M. A., Kim, B. W., Nissim, S., Mornon, J.-P., Zavacki, A. M., Zeöld, A., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1272 · Cited by 227 · see citing works

Structural assembly of cullin-RING ubiquitin ligase complexes

Zimmerman, E. S., Schulman, B. A., & Zheng, N. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.010 · Cited by 227 · see citing works

Socs-1 Inhibits TEL-JAK2-Mediated Transformation of Hematopoietic Cells through Inhibition of JAK2 Kinase Activity and Induction of Proteasome-Mediated Degradation

Frantsve‐Hawley, J., Schwaller, J., Sternberg, D., Kutok, J. L., & Gilliland, D. G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3547-3557.2001 · Cited by 171 · see citing works

Suppressor of Cytokine Signaling-1 Inhibits VAV Function through Protein Degradation

Sepulveda, P. D., Ilangumaran, S., & Rottapel, R. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000106200 · Cited by 167 · see citing works

Crystal structure of the SOCS2–elongin C–elongin B complex defines a prototypical SOCS box ubiquitin ligase

Bullock, A. N., Debreczeni, J. E., Edwards, A. M., Sundström, M., & Knapp, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601638103 · Cited by 165 · see citing works

The Structure of SOCS3 Reveals the Basis of the Extended SH2 Domain Function and Identifies an Unstructured Insertion That Regulates Stability

Babon, J. J., McManus, E. J., Yao, S., DeSouza, D. P., Mielke, L. A., Sprigg, N. S., Willson, T. A., Hilton, D. J., Nicola, N. A., Baca, M., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.024 · Cited by 163 · see citing works

Suppressor of Cytokine Signaling (SOCS) 1 Inhibits Type I Interferon (IFN) Signaling via the Interferon α Receptor (IFNAR1)-associated Tyrosine Kinase Tyk2

Piganis, R., de Weerd, N. A., Gould, J. A., Schindler, C., Mansell, A. S., Nicholson, S. E., & Hertzog, P. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.270207 · Cited by 159 · see citing works

The SOCS box of suppressor of cytokine signaling-1 is important for inhibition of cytokine action in vivo

Zhang, J., Metcalf, D., Rakar, S., Asimakis, M., Greenhalgh, C. J., Willson, T. A., Starr, R., Nicholson, S. E., Carter, W., Alexander, W. S., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231486498 · Cited by 155 · see citing works

SOCS-6 Binds to Insulin Receptor Substrate 4, and Mice Lacking the SOCS-6 Gene Exhibit Mild Growth Retardation

Krebs, D. L., Uren, R. T., Metcalf, D., Rakar, S., Zhang, J., Starr, R., Souza, D. P. D., Hanzinikolas, K., Eyles, J. L., Connolly, L., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4567-4578.2002 · Cited by 150 · see citing works

The SOCS Box Encodes a Hierarchy of Affinities for Cullin5: Implications for Ubiquitin Ligase Formation and Cytokine Signalling Suppression

Babon, J. J., Sabo, J. K., Zhang, J., Nicola, N. A., & Norton, R. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.024 · Cited by 143 · see citing works

Structure of the SOCS4-ElonginB/C Complex Reveals a Distinct SOCS Box Interface and the Molecular Basis for SOCS-Dependent EGFR Degradation

Bullock, A. N., Rodríguez, M. C., Debreczeni, J. E., Songyang, Z., & Knapp, S. (2007) · Structure · doi:10.1016/j.str.2007.09.016 · Cited by 127 · see citing works

Tyrosine Phosphorylation Disrupts Elongin Interaction and Accelerates SOCS3 Degradation

Haan, S., FERGUSON, P. W., Sommer, U., Hiremath, M. M., McVicar, D. W., Heinrich, P. C., Johnston, J. A., & Cacalano, N. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303170200 · Cited by 119 · see citing works

ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes

Kohroki, J., Nishiyama, T., Nakamura, T., & Masuho, Y. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.016 · Cited by 117 · see citing works

Suppressors of cytokine signaling (SOCS): negative regulators of signal transduction

Alexander, W. S., Starr, R., Metcalf, D., Nicholson, S. E., Farley, A., Elefanty, A. G., Brysha, M., Kile, B. T., Richardson, R. T., Baca, M., et al. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.66.4.588 · Cited by 116 · see citing works

Deletion of SOCS7 leads to enhanced insulin action and enlarged islets of Langerhans

Banks, A. S., Li, J., McKeag, L., Hribal, M. L., Kashiwada, M., Accili, D., & Rothman, P. B. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23853 · Cited by 104 · see citing works

The SOCS Box Domain of SOCS3: Structure and Interaction with the ElonginBC-Cullin5 Ubiquitin Ligase

Babon, J. J., Sabo, J. K., Soetopo, A., Yao, S., Bailey, M. F., Zhang, J., Nicola, N. A., & Norton, R. S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.038 · Cited by 103 · see citing works

Ubiquitination and Degradation of Homeodomain-interacting Protein Kinase 2 by WD40 Repeat/SOCS Box Protein WSB-1

Choi, D. W., Seo, Y.-M., Kim, E.-A. L., Sung, K. S., Ahn, J. W., Park, S., Lee, S.-R., & Choi, C. Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708873200 · Cited by 101 · see citing works

The SPRY domain–containing SOCS box protein SPSB2 targets iNOS for proteasomal degradation

Kuang, Z., Lewis, R. S., Curtis, J., Zhan, Y., Saunders, B. M., Babon, J. J., Kolesnik, T. B., Low, A., Masters, S. L., Willson, T. A., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200912087 · Cited by 101 · see citing works

The SOCS2 Ubiquitin Ligase Complex Regulates Growth Hormone Receptor Levels

Vesterlund, M., Zadjali, F., Persson, T., Nielsen, M. L., Kessler, B. M., Norstedt, G., & Flores‐Morales, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025358 · Cited by 98 · see citing works

ASB2 targets filamins A and B to proteasomal degradation

Heuzé, M. L., Lamsoul, I., Baldassarre, M., Lad, Y., Lévêque, S., Razinia, Z., Moog‐Lutz, C., Calderwood, D., & Lutz, P. G. (2008) · Blood · doi:10.1182/blood-2007-12-128744 · Cited by 90 · see citing works

Suppressor of cytokine signaling 3 controls lysosomal routing of G‐CSF receptor

Irandoust, M. I., Aarts, L. H. J., Roovers, O., Gits, J., Erkeland, S. J., & Touw, I. P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601640 · Cited by 89 · see citing works

Suppressor of Cytokine Signaling 6 Associates with KIT and Regulates KIT Receptor Signaling

Bayle, J., Letard, S., Frank, R., Dubreuil, P. C., & Sepulveda, P. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313381200 · Cited by 86 · see citing works

c-Cbl-Dependent Monoubiquitination and Lysosomal Degradation of gp130

Tanaka, Y., Tanaka, N., Saeki, Y., Tanaka, K., Murakami, M., Hirano, T., Ishii, N., & Sugamura, K. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01784-07 · Cited by 82 · see citing works

The E3 ubiquitin ligase specificity subunit ASB2β is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation

Bello, N. F., Lamsoul, I., Heuzé, M. L., Métais, A., Moreaux, G., Calderwood, D., Duprez, D., Moog‐Lutz, C., & Lutz, P. G. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.27 · Cited by 75 · see citing works

Ankyrin Repeat and SOCS Box 3 (ASB3) Mediates Ubiquitination and Degradation of Tumor Necrosis Factor Receptor II

Chung, A. S., Guan, Y. A., Yuan, Z., Albina, J. E., & Chin, Y. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.11.4716-4726.2005 · Cited by 75 · see citing works

The SOCS box of suppressor of cytokine signaling-3 contributes to the control of G-CSF responsiveness in vivo

Boyle, K., Egan, P. J., Rakar, S., Willson, T. A., Wicks, I. P., Metcalf, D., Hilton, D. J., Nicola, N. A., Alexander, W. S., Roberts, A. W., et al. (2007) · Blood · doi:10.1182/blood-2007-03-079178 · Cited by 72 · see citing works

Regulation of Inducible Nitric-oxide Synthase by the SPRY Domain- and SOCS Box-containing Proteins

Nishiya, T., Matsumoto, K., Maekawa, S., Kajita, E., Horinouchi, T., Fujimuro, M., Ogasawara, K., Uehara, T., & Miwa, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190678 · Cited by 72 · see citing works

ASB2 Is an Elongin BC-interacting Protein That Can Assemble with Cullin 5 and Rbx1 to Reconstitute an E3 Ubiquitin Ligase Complex

Heuzé, M. L., Guibal, F. C., Banks, C. A. S., Conaway, J. W., Conaway, R. C., Cayre, Y. E., Benecke, A., & Lutz, P. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413040200 · Cited by 72 · see citing works

Structural Basis for c-KIT Inhibition by the Suppressor of Cytokine Signaling 6 (SOCS6) Ubiquitin Ligase

Zadjali, F., Pike, A. C. W., Vesterlund, M., Sun, J., Wu, C., Li, S. S. ‐., Rönnstrand, L., Knapp, S., Bullock, A. N., & Flores‐Morales, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173526 · Cited by 70 · see citing works

Deletion of the SOCS box of suppressor of cytokine signaling 3 (SOCS3) in embryonic stem cells reveals SOCS box-dependent regulation of JAK but not STAT phosphorylation

Boyle, K., Zhang, J., Nicholson, S. E., Trounson, E., Babon, J. J., McManus, E. J., Nicola, N. A., & Robb, L. G. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.11.002 · Cited by 65 · see citing works

ASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial function

Kwon, S., Kim, D., Rhee, J. W., Park, J. A., Kim, D., Kim, D.-S., Lee, Y., & Kwon, H. (2010) · BMC Biology · doi:10.1186/1741-7007-8-23 · Cited by 60 · see citing works

ECSASB2 mediates MLL degradation during hematopoietic differentiation

Wang, J., Muntean, A. G., & Hess, J. L. (2011) · Blood · doi:10.1182/blood-2011-06-362079 · Cited by 57 · see citing works

TLR Regulation of SPSB1 Controls Inducible Nitric Oxide Synthase Induction

Lewis, R. S., Kolesnik, T. B., Kuang, Z., D’Cruz, A. A., Blewitt, M. E., Masters, S. L., Low, A., Willson, T. A., Norton, R. S., & Nicholson, S. E. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002993 · Cited by 57 · see citing works

Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes

Nie, L., Zhao, Y., Wu, W., Yang, Y.-Z., Wang, H.-C., & Sun, X.-H. (2010) · Cell Research · doi:10.1038/cr.2010.165 · Cited by 50 · see citing works

Suppressor of Cytokine Signaling 2 Regulates IL-15–Primed Human NK Cell Function via Control of Phosphorylated Pyk2

Lee, S. H., Yun, S., Piao, Z.-H., Jeong, M., Kim, D. O., Jung, H., Lee, J., Kim, M. J., Kim, M. S., Chung, J. W., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000784 · Cited by 50 · see citing works

Ankyrin Repeat and Suppressors of Cytokine Signaling Box Protein Asb-9 Targets Creatine Kinase B for Degradation

Debrincat, M. A., Zhang, J., Willson, T. A., Silke, J., Connolly, L., Simpson, R. J., Alexander, W. S., Nicola, N. A., Kile, B. T., & Hilton, D. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609164200 · Cited by 47 · see citing works

Regulation of Drosophila Vasa In Vivo through Paralogous Cullin-RING E3 Ligase Specificity Receptors

Kugler, J., Woo, J., Oh, B., & Lasko, P. F. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01100-09 · Cited by 38 · see citing works

The TEL-Jak2 oncoprotein induces Socs1 expression and altered cytokine response in Ba/F3 cells

Monni, R., Santos, S. C. R., Mauchauffé, M., Berger, R., Ghysdael, J., Gouilleux, F., Gisselbrecht, S., Bernard, O., & Penard‐Lacronique, V. (2001) · Oncogene · doi:10.1038/sj.onc.1204201 · Cited by 38 · see citing works

SOCS-6 Negatively Regulates T Cell Activation through Targeting p56 to Proteasomal Degradation

Choi, Y. B., Son, M., Park, M., Shin, J., & Yun, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.073726 · Cited by 37 · see citing works

The novel gene asb11: a regulator of the size of the neural progenitor compartment

Diks, S. H., Bink, R. J., van de Water, S., Joore, J., van Rooijen, C., Verbeek, F. J., den Hertog, J., Peppelenbosch, M. P., & Živković, D. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601081 · Cited by 34 · see citing works

Site‐Specific Ubiquitination Determines Lysosomal Sorting and Signal Attenuation of the Granulocyte Colony‐Stimulating Factor Receptor

Wölfler, A., Irandoust, M. I., Meenhuis, A., Gits, J., Roovers, O., & Touw, I. P. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00928.x · Cited by 33 · see citing works

Ankyrin repeat and SOCS box containing protein 4 (Asb-4) colocalizes with insulin receptor substrate 4 (IRS4) in the hypothalamic neurons and mediates IRS4 degradation

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SOCS1 and SOCS3 as key checkpoint molecules in the immune responses associated to skin inflammation and malignant transformation

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Small GTPase Rab40c Associates with Lipid Droplets and Modulates the Biogenesis of Lipid Droplets

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Fat-regulated adaptor protein Dlish binds the growth suppressor Expanded and controls its stability and ubiquitination

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WD repeat and SOCS box containing protein 2 in the proliferation, cycle progression, and migration of melanoma cells

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Natural Sesquiterpene Lactones Enhance Chemosensitivity of Tumor Cells through Redox Regulation of STAT3 Signaling

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SOCS3 is a suppressor of γc cytokine signaling and constrains generation of murine Foxp3 + regulatory T cells

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Growth hormone (GH)/STAT5 signaling during the growth period in liver of mice overexpressing GH

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Downregulation of miR-122 by porcine reproductive and respiratory syndrome virus promotes viral replication by targeting SOCS3

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Elevated levels of exogenous prolactin promote inflammation at the maternal-fetal interface via the JAK2/STAT5B signaling axis

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Suppression of Interferon-α Treatment Response by Host Negative Factors in Hepatitis B Virus Infection

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Longitudinal Analysis of Serum Autoantibody-Reactivities in Patients with Primary Open Angle Glaucoma and Optic Disc Hemorrhage

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ASB1 inhibits prostate cancer progression by destabilizing CHCHD3 via K48-linked ubiquitination

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The Neglected Suppressor of Cytokine Signalling (SOCS): SOCS4-7

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Cullin-5 controls the number of megakaryocyte-committed stem cells to prevent thrombocytosis in mice

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